|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
21-252 |
2.49e-101 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 294.66 E-value: 2.49e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY-RELQTPTQRIGVSLD 99
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVaRDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 100 GGAFVGGRTGRGHLRCYAPAAGCSP----ERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSN 175
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRkearERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 176 GLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQgeRLESAFMRLTQAGE 252
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR--LLEDVFLELTGEEA 235
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
21-228 |
3.27e-94 |
|
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: 275.63 E-value: 3.27e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSLDG 100
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 101 GAFVGGRTGRGHLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPE 180
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2155196442 181 GMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03268 161 GIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
20-247 |
6.48e-80 |
|
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: 240.53 E-value: 6.48e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYREL-QTPTQRIGVSL 98
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEpREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 DGGAFVGGRTGRGHLRCYAPAAGCSPE----RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPS 174
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEelkkRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 175 NGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLL--TQGERLESAFMRL 247
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELReeIGEENLEDAFVAL 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
21-224 |
1.35e-70 |
|
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: 214.18 E-value: 1.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPT-QRIGVSLD 99
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 100 GGAFVGGRTGRGHLRcyapaagcsperldrllaetglaeaadrpvsgYSTGMKQRLSLAAALLGDPELLILDEPSNGLDP 179
Cdd:cd03230 81 EPSLYENLTVRENLK--------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2155196442 180 EGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:cd03230 129 ESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-233 |
3.55e-66 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 207.27 E-value: 3.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRelQTPTQRIG---- 95
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--PEDRRRIGylpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 --------------VSLdggafvggrtgrGHLRCYAPAAgcSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAAL 161
Cdd:COG4152 79 erglypkmkvgeqlVYL------------ARLKGLSKAE--AKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 162 LGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHL 233
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
21-248 |
1.66e-60 |
|
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: 190.30 E-value: 1.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY--RELQtptqRIGVSL 98
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWtrKDLH----KIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 DGGAFVGGRTGRGHLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLD 178
Cdd:TIGR03740 77 ESPPLYENLTARENLKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 179 PEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDhlltQGERLESAFMRLT 248
Cdd:TIGR03740 157 PIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKIN----KSENLEKLFVEVV 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-233 |
3.96e-58 |
|
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: 184.25 E-value: 3.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRG--RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYR-ELQTPTQRIGVS 97
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 98 LDGGAFVGGRTGRGHLRCYAPAAGCS----PERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEP 173
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPkseiKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 174 SNGLDPEG--MLWlrTFLRRfAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHL 233
Cdd:cd03263 161 TSGLDPASrrAIW--DLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
21-233 |
5.36e-58 |
|
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: 183.73 E-value: 5.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHP-YRELQTPTQRIGVSLD 99
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 100 GGAFVGGRTGRGHLRCYAPAAGCS----PERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSN 175
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPgaerRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 176 GLDPEGM--LW--LRTFLRRFaasGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHL 233
Cdd:cd03265 161 GLDPQTRahVWeyIEKLKEEF---GMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
28-228 |
1.68e-54 |
|
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: 177.58 E-value: 1.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 28 KKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY-RELQTPTQRIGVSLDGGAFVGG 106
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 107 RTGRGHLRCYAPAAGCS----PERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGM 182
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPkdeaEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2155196442 183 LWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEG 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-228 |
1.84e-53 |
|
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: 172.17 E-value: 1.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRT----AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGhpYRELQTP---TQR 93
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPaeaRRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 94 IGVSLDGGAFVGGRTGRGHLRCYAPAAGCSPE----RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLI 169
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDeltaRLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 170 LDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-210 |
2.31e-53 |
|
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: 171.51 E-value: 2.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 19 PVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYREL-QTPTQRIGVS 97
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDArEDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 98 LDGGAFVGGRTGRGHLRCYAPAAGC--SPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSN 175
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLraDREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2155196442 176 GLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEME 210
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA 195
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-244 |
5.09e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 171.81 E-value: 5.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 16 DNSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRElqtPTQRIG 95
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 -----VSLDGG------AFVG-GRTGRGHLRCYAPAAGCspERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLG 163
Cdd:COG1121 79 yvpqrAEVDWDfpitvrDVVLmGRYGRRGLFRRPSRADR--EAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 164 DPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGkLLSSGPLDHLLTQgERLESA 243
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTP-ENLSRA 234
|
.
gi 2155196442 244 F 244
Cdd:COG1121 235 Y 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
21-223 |
2.03e-52 |
|
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: 169.38 E-value: 2.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqtPTQRIGVSLDG 100
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA--ARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 101 GAFVGGRTGRGHLRCYAPAAGCSPE----RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNG 176
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEearrRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2155196442 177 LDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGK 223
Cdd:cd03269 159 LDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
21-228 |
1.72e-51 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 166.98 E-value: 1.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGrVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRE-LQTPTQRIGVSLD 99
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKqPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 100 GGAFVGGRTGRGHLRCYAPAAGCSP----ERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSN 175
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSkevkARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 176 GLDPEGMLWLRTFLRRFAAsGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
21-242 |
3.04e-50 |
|
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: 164.43 E-value: 3.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFR-GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPT--QRIG-- 95
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGlv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 ------------VSLDggafVggrtgrghlrCYAPAA-GCSPE----RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLA 158
Cdd:COG1122 81 fqnpddqlfaptVEED----V----------AFGPENlGLPREeireRVEEALELVGLEHLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 159 AALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQGE 238
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
....
gi 2155196442 239 RLES 242
Cdd:COG1122 227 LLEE 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-236 |
4.18e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 153.70 E-value: 4.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGR---------------------TAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTAL 78
Cdd:COG4586 1 IIEVENLSKTYRVYekepglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 79 LWGH-PYRELQTPTQRIGVsldggafVGGRtgRGHLRCYAPAA----------GCSP----ERLDRLLAETGLAEAADRP 143
Cdd:COG4586 81 VLGYvPFKRRKEFARRIGV-------VFGQ--RSQLWWDLPAIdsfrllkaiyRIPDaeykKRLDELVELLDLGELLDTP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 144 VSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRF-AASGRTVLLSSHLLSEMEQTVDDVLLMHHG 222
Cdd:COG4586 152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
250
....*....|....
gi 2155196442 223 KLLSSGPLDHLLTQ 236
Cdd:COG4586 232 RIIYDGSLEELKER 245
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
22-223 |
9.95e-45 |
|
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: 147.78 E-value: 9.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 22 EVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSLdgg 101
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 102 afvggrtgrghlrcyapaagcsperldrllaetglaeaadrpVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEG 181
Cdd:cd00267 78 ------------------------------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2155196442 182 MLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGK 223
Cdd:cd00267 116 RERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-232 |
4.38e-43 |
|
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: 146.04 E-value: 4.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH------PY--------RE 86
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglpPHeiarlgigRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 87 LQTPTQ----------RIGVSLDGGAFVGGRTGRGHLRcyapAAgcsPERLDRLLAETGLAEAADRPVSGYSTGMKQRLS 156
Cdd:cd03219 81 FQIPRLfpeltvlenvMVAAQARTGSGLLLARARREER----EA---RERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 157 LAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDH 232
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
20-244 |
1.30e-42 |
|
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: 145.57 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPT--QRIGV- 96
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 ----SLDGGAFVG-----GRTgrGHLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPEL 167
Cdd:COG1120 81 pqepPAPFGLTVRelvalGRY--PHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 168 LILDEPSNGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQgERLESAF 244
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTP-ELLEEVY 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-228 |
1.60e-42 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 143.83 E-value: 1.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 22 EVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQT-----PtQRIGV 96
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKrigyvP-QRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 S----LDGGAFVG-GRTGRGHLRCYAPAAGCspERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILD 171
Cdd:cd03235 80 DrdfpISVRDVVLmGLYGHKGLFRRLSKADK--AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 172 EPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHgKLLSSG 228
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-228 |
2.40e-42 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 146.10 E-value: 2.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 19 PVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY-RELQTPTQRIGVS 97
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 98 LDGGAFVGGRTGRGHLRCYA-----PAAGCSpERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDE 172
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGryfglSAAAAR-ALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 173 PSNGLDPEG--MLWLRtfLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:PRK13537 165 PTTGLDPQArhLMWER--LRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
27-228 |
4.05e-42 |
|
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: 143.63 E-value: 4.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 27 RKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH-PYRELQTPTQRIGVSLdggafvG 105
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRKKFLRRIGVVF------G 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 106 GRTG-----------RGHLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPS 174
Cdd:cd03267 102 QKTQlwwdlpvidsfYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 175 NGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
16-235 |
1.09e-41 |
|
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: 142.43 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 16 DNSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY-----RELQTP 90
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglseKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 91 TQRIGVSLDGGA-F----VGGRTG---RGHLRCyapaagcSPERLDRL----LAETGLAEAADRPVSGYSTGMKQRLSLA 158
Cdd:COG1127 81 RRRIGMLFQGGAlFdsltVFENVAfplREHTDL-------SEAEIRELvlekLELVGLPGAADKMPSELSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 159 AALLGDPELLILDEPSNGLDPEGMlwlRTF------LRRfaASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDH 232
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITS---AVIdelireLRD--ELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEE 228
|
...
gi 2155196442 233 LLT 235
Cdd:COG1127 229 LLA 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
17-229 |
2.89e-41 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 142.10 E-value: 2.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 17 NSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH------PY------ 84
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpPHriarlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 85 --RELQTPT----------------QRIGVSLDGGAFVGGRTGRGHLRCYapaagcspERLDRLLAETGLAEAADRPVSG 146
Cdd:COG0411 81 iaRTFQNPRlfpeltvlenvlvaahARLGRGLLAALLRLPRARREEREAR--------ERAEELLERVGLADRADEPAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 147 YSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAA-SGRTVLLSSHLLSEMEQTVDDVLLMHHGKLL 225
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
....
gi 2155196442 226 SSGP 229
Cdd:COG0411 233 AEGT 236
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
31-223 |
3.18e-41 |
|
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: 140.68 E-value: 3.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTP--TQRIGVSL---------- 98
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKelRRKVGLVFqnpddqffgp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 ---DGGAFvggrtGRGHLrcyapaaGCSPE----RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILD 171
Cdd:cd03225 92 tveEEVAF-----GLENL-------GLPEEeieeRVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 172 EPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGK 223
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-228 |
1.22e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 142.66 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 11 TTPVKDNSPV-IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY-RELQ 88
Cdd:PRK13536 31 ASIPGSMSTVaIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 89 TPTQRIGVSLDGGAFVGGRTGRGHLRCYAPAAGCSPERLD----RLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGD 164
Cdd:PRK13536 111 LARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEavipSLLEFARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 165 PELLILDEPSNGLDPEG--MLWLRtfLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:PRK13536 191 PQLLILDEPTTGLDPHArhLIWER--LRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-256 |
2.18e-40 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 147.96 E-value: 2.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 12 TPVKDNSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY--RELQT 89
Cdd:NF033858 258 PADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIAT 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 90 pTQRIG-----VSLDGGAFVggrtgRG----HLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAA 160
Cdd:NF033858 338 -RRRVGymsqaFSLYGELTV-----RQnlelHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 161 LLGDPELLILDEPSNGLDPEG--MLW--LRTFLRRfaaSGRTVLLSSHLLSEMEQtVDDVLLMHHGKLLSSGPLDHLLTQ 236
Cdd:NF033858 412 VIHKPELLILDEPTSGVDPVArdMFWrlLIELSRE---DGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAA 487
|
250 260
....*....|....*....|...
gi 2155196442 237 --GERLESAFMR-LTQAGEGTQT 256
Cdd:NF033858 488 rgAATLEEAFIAyLEEAAGAAAA 510
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
9-236 |
2.47e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 145.43 E-value: 2.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 9 ERTTPVKDNSPVIEVCGLRKKFRGR-----TAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHP 83
Cdd:COG1123 249 RAAPAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 84 ------------YRELQ----------TPTQRIGVSLDGGAFVGGRTGRGHLRcyapaagcspERLDRLLAETGL-AEAA 140
Cdd:COG1123 329 ltklsrrslrelRRRVQmvfqdpysslNPRMTVGDIIAEPLRLHGLLSRAERR----------ERVAELLERVGLpPDLA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 141 DRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDP---EGMLwlrTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDV 216
Cdd:COG1123 399 DRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVsvqAQIL---NLLRDLQRElGLTYLFISHDLAVVRYIADRV 475
|
250 260
....*....|....*....|
gi 2155196442 217 LLMHHGKLLSSGPLDHLLTQ 236
Cdd:COG1123 476 AVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
22-228 |
3.41e-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: 3.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 22 EVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQtptqrigvsldgg 101
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 102 afvggRTGRGHLRCYAPAAgcsperldrlLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEG 181
Cdd:cd03214 68 -----PKELARKIAYVPQA----------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2155196442 182 MLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03214 133 QIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
18-244 |
5.85e-40 |
|
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: 138.29 E-value: 5.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 18 SPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEG-TALLWGHPY-----RELQtpt 91
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRggedvWELR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 92 QRIGVSldggafvggrTGRGHLRCYAPAAG-----------------CSPE---RLDRLLAETGLAEAADRPVSGYSTGM 151
Cdd:COG1119 78 KRIGLV----------SPALQLRFPRDETVldvvlsgffdsiglyrePTDEqreRARELLELLGLAHLADRPFGTLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 152 KQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASG-RTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPL 230
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPK 227
|
250
....*....|....
gi 2155196442 231 DHLLTqGERLESAF 244
Cdd:COG1119 228 EEVLT-SENLSEAF 240
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
21-235 |
7.81e-40 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 137.63 E-value: 7.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYR-----ELQTPTQRIG 95
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseaELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 VSLDGGAF-----VGGRTG---RGHLRcyapaagCSPERLDRL----LAETGLAEAADRPVSGYSTGMKQRLSLAAALLG 163
Cdd:cd03261 81 MLFQSGALfdsltVFENVAfplREHTR-------LSEEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 164 DPELLILDEPSNGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLT 235
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
27-231 |
2.28e-39 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 136.75 E-value: 2.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 27 RKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGhpyrelqtptqRIGVSLD-GGAFVG 105
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-----------RVSALLElGAGFHP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 106 GRTGRGHLRCYAPAAGCSPERLDRLLAE----TGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEpsngldpeg 181
Cdd:COG1134 102 ELTGRENIYLNGRLLGLSRKEIDEKFDEivefAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE--------- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2155196442 182 mlWL-----------RTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLD 231
Cdd:COG1134 173 --VLavgdaafqkkcLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
32-237 |
3.64e-38 |
|
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: 139.89 E-value: 3.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSLdggafVGGR---- 107
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAW-----VPQNpylf 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 108 --TGRGHLRCYAPAAgcSPERLDRLLAETGLAEAADRPVSGYST-----------GMKQRLSLAAALLGDPELLILDEPS 174
Cdd:COG4988 424 agTIRENLRLGRPDA--SDEELEAALEAAGLDEFVAALPDGLDTplgeggrglsgGQAQRLALARALLRDAPLLLLDEPT 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 175 NGLDPEGMLWLRTFLRRFAAsGRTVLLSSHLLSEMEQtVDDVLLMHHGKLLSSGPLDHLLTQG 237
Cdd:COG4988 502 AHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-243 |
1.27e-37 |
|
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: 138.11 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 18 SPVIEVCGLRKKFRG--RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPT---EGTALLWGHPYREL--QTP 90
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELseALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 91 TQRIG-VSLDGGAFVGGRTGRGHLRCYAPAAGCSP----ERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDP 165
Cdd:COG1123 82 GRRIGmVFQDPMTQLNPVTVGDQIAEALENLGLSRaearARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 166 ELLILDEPSNGLDPEGMLWLRTFLRRFAA-SGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQGERLESA 243
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAV 240
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
21-228 |
1.76e-36 |
|
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: 128.41 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqtPTQRIGVSL-- 98
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPERRNIGMvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 -DGGAFvggrtgrGHLR-----CYAPAAGCSPE-----RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPEL 167
Cdd:cd03259 79 qDYALF-------PHLTvaeniAFGLKLRGVPKaeiraRVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 168 LILDEPSNGLDPEGMLWLRTFLRR-FAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-228 |
1.53e-35 |
|
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: 126.11 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 24 CGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGhpyrelqTPTQRIGVsldGGAF 103
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------RVSSLLGL---GGGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 104 VGGRTGRGHLRCYAPAAGCSPERLDRLLAE----TGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDP 179
Cdd:cd03220 96 NPELTGRENIYLNGRLLGLSRKEIDEKIDEiiefSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2155196442 180 EGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03220 176 AFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
31-224 |
1.11e-34 |
|
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: 123.52 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTaLLWGHPYRELQTPTQRIG-VSLDGGAFVGGRTG 109
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGS-ILLNGKPIKAKERRKSIGyVMQDVDYQLFTDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 110 RGHLRCYAPAAGCSPERLDRLLAETGLAEAADR-PVSgYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTF 188
Cdd:cd03226 90 REELLLGLKELDAGNEQAETVLKDLDLYALKERhPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGEL 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 2155196442 189 LRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:cd03226 169 IRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
36-175 |
6.17e-34 |
|
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: 119.67 E-value: 6.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 36 VDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHP--YRELQTPTQRIGV-----SLDGGAFVGGRT 108
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltDDERKSLRKEIGYvfqdpQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2155196442 109 GRGhLRCYAPAAGCSPERLDRLLAETGLAEAADRPV----SGYSTGMKQRLSLAAALLGDPELLILDEPSN 175
Cdd:pfam00005 81 RLG-LLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
21-223 |
2.30e-33 |
|
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: 119.21 E-value: 2.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHP----YRELQTPTQRIGV 96
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdlEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 SLDGGAFVGGRTgrghlrcyapaagcsperldrllaetglaeAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNG 176
Cdd:cd03229 81 VFQDFALFPHLT------------------------------VLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2155196442 177 LDPEGMLWLRTFLRR-FAASGRTVLLSSHLLSEMEQTVDDVLLMHHGK 223
Cdd:cd03229 131 LDPITRREVRALLKSlQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
20-234 |
2.92e-33 |
|
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: 120.84 E-value: 2.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqtPTQ---RIGV 96
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHL--PMHeraRLGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 S-LDGGAFV-GGRTGRGHLRC-----YAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLI 169
Cdd:TIGR04406 79 GyLPQEASIfRKLTVEENIMAvleirKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 170 LDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLL 234
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-224 |
1.08e-32 |
|
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: 117.14 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYrELQTPT--QRIGVSL 98
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-SFASPRdaRRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 dggafvggrtgrghlrcyapaagcsperldrllaetglaeaadrpVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLD 178
Cdd:cd03216 80 ---------------------------------------------VYQLSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2155196442 179 PEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
17-204 |
1.23e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 119.81 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 17 NSPVIEVCGLRKKFR----GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRElqtPTQ 92
Cdd:COG1116 4 AAPALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG---PGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 93 RIGVsldggAF--------------VG-GRTGRGHLRCYAPaagcspERLDRLLAETGLAEAADR-P--VSGystGMKQR 154
Cdd:COG1116 81 DRGV-----VFqepallpwltvldnVAlGLELRGVPKAERR------ERARELLELVGLAGFEDAyPhqLSG---GMRQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2155196442 155 LSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRR-FAASGRTVLLSSH 204
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlWQETGKTVLFVTH 197
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-239 |
1.24e-32 |
|
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: 125.33 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRT--AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPT--QRIGV 96
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 SL-DGGAFVGgrTGRGHLRCYAPAAgcSPERLDRLLAETGLAEAADRPVSGY-----------STGMKQRLSLAAALLGD 164
Cdd:COG2274 554 VLqDVFLFSG--TIRENITLGDPDA--TDEEIIEAARLAGLHDFIEALPMGYdtvvgeggsnlSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 165 PELLILDEPSNGLDPEGMLWLRTFLRRFAAsGRTVLLSSHLLSEMEQtVDDVLLMHHGKLLSSGPLDHLLTQGER 239
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGL 702
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
21-248 |
1.45e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 121.41 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGhpyRELQT--PTQRIGVsl 98
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG---RDLFTnlPPRERRV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 dggAFV------------------GgrtgrghLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAA 160
Cdd:COG1118 78 ---GFVfqhyalfphmtvaeniafG-------LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 161 LLGDPELLILDEPSNGLD----PEGMLWLRTFLRRFaasGRTVLLSSHLLSE-MEqtV-DDVLLMHHGKLLSSGPLDHLL 234
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL---GGTTVFVTHDQEEaLE--LaDRVVVMNQGRIEQVGTPDEVY 222
|
250
....*....|....*
gi 2155196442 235 tqgERLESAF-MRLT 248
Cdd:COG1118 223 ---DRPATPFvARFL 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
21-228 |
2.70e-32 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 118.03 E-value: 2.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWG------HPYRElqtptQRI 94
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklPMHKR-----ARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 95 GVS-LDGGAFVGGR-TGRGHLRCYAPAAGCSP----ERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELL 168
Cdd:cd03218 76 GIGyLPQEASIFRKlTVEENILAVLEIRGLSKkereEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 169 ILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEG 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
21-224 |
2.72e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.22 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPT--QRIG-VS 97
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAyVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 98 LDggAFVGGRTGRGHL------RCYAPaagcSPERLDRLLAETGLAEAA-DRPVSGYSTGMKQRLSLAAALLGDPELLIL 170
Cdd:COG4619 81 QE--PALWGGTVRDNLpfpfqlRERKF----DRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 171 DEPSNGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-228 |
2.86e-32 |
|
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: 117.76 E-value: 2.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 27 RKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRP---TEGTALLWGHPyRELQTPTQRIGVSLDGGAF 103
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQP-RKPDQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 104 VGGRTGRGHLRCYAPAAG--CSPERLDRLLAE-TGLAEAADRPVSGY-----STGMKQRLSLAAALLGDPELLILDEPSN 175
Cdd:cd03234 93 LPGLTVRETLTYTAILRLprKSSDAIRKKRVEdVLLRDLALTRIGGNlvkgiSGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2155196442 176 GLDPEGMLWLRTFLRRFAASGRTVLLSSHL-LSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
20-234 |
3.59e-32 |
|
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: 117.68 E-value: 3.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGR----TAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH-----PYRELQTP 90
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 91 TQRIGVSLDGGAFVGGRTGRGHLRCYAPAAGCS----PERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPE 166
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPkaeiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 167 LLILDEPSNGLDPE---GML-WLRTFLRRFaasGRTVLLSSHllsEME---QTVDDVLLMHHGKLLSSGPLDHLL 234
Cdd:cd03258 161 VLLCDEATSALDPEttqSILaLLRDINREL---GLTIVLITH---EMEvvkRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
19-234 |
7.23e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 117.05 E-value: 7.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 19 PVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHP------YRElqtptQ 92
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlpmHKR-----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 93 RIGVSL---DGGAFvGGRTGRGHLRCYAPAAGCSP----ERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDP 165
Cdd:COG1137 77 RLGIGYlpqEASIF-RKLTVEDNILAVLELRKLSKkereERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 166 ELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLL 234
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
11-239 |
1.49e-31 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 121.80 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 11 TTPVKDNSPVIEVCGLRKKFRG--RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQ 88
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 89 TPT--QRIGVSLDGGAFVGGrTGRGHLRCYAPAAgcSPERLDRLLAETGLAEAADRPVSGYST-----------GMKQRL 155
Cdd:COG4987 404 EDDlrRRIAVVPQRPHLFDT-TLRENLRLARPDA--TDEELWAALERVGLGDWLAALPDGLDTwlgeggrrlsgGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 156 SLAAALLGDPELLILDEPSNGLDPE-GMLWLRTFLRrfAASGRTVLLSSHLLSEMEQtVDDVLLMHHGKLLSSGPLDHLL 234
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAAtEQALLADLLE--ALAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELL 557
|
....*
gi 2155196442 235 TQGER 239
Cdd:COG4987 558 AQNGR 562
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
31-223 |
1.61e-31 |
|
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: 114.02 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPT--QRIGVSLDggafvggrt 108
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAYVPQ--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 109 grghlrcyapaagcSPERLDRLLAETGLaeaadrpvsgySTGMKQRLSLAAALLGDPELLILDEPSNGLDPEG-MLWLRT 187
Cdd:cd03228 84 --------------DPFLFSGTIRENIL-----------SGGQRQRIAIARALLRDPPILILDEATSALDPETeALILEA 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 2155196442 188 FLRRFAasGRTVLLSSHLLSEMEQtVDDVLLMHHGK 223
Cdd:cd03228 139 LRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-224 |
4.58e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 119.75 E-value: 4.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 19 PVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYReLQTPTQ----RI 94
Cdd:COG3845 4 PALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRSPRDaialGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 95 G-------------------VSLDGGAfvGGRTGRGHLRcyapaagcspERLDRLLAETGLAEAADRPVSGYSTGMKQRL 155
Cdd:COG3845 83 GmvhqhfmlvpnltvaenivLGLEPTK--GGRLDRKAAR----------ARIRELSERYGLDVDPDAKVEDLSVGEQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 156 SLAAALLGDPELLILDEPSNGLDP---EGMLwlrTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLTPqeaDELF---EILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-244 |
4.98e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 115.25 E-value: 4.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 19 PVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPT--QRIGV 96
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 -----SLdggAF-------VG-GRTGRGHLRCYAPAAgcsperLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALL- 162
Cdd:PRK13548 81 lpqhsSL---SFpftveevVAmGRAPHGLSRAEDDAL------VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 163 -----GDPELLILDEPSNGLDPEGMLWLRTFLRRFA-ASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQ 236
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTP 231
|
....*...
gi 2155196442 237 gERLESAF 244
Cdd:PRK13548 232 -ETLRRVY 238
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-224 |
5.87e-31 |
|
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: 114.53 E-value: 5.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGR----TAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY----------- 84
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 85 -RELQ----------TPTQRIGVSLdggafvgGRTGRGHLRCYAPAAgcSPERLDRLLAETGLAEA-ADRPVSGYSTGMK 152
Cdd:cd03257 81 rKEIQmvfqdpmsslNPRMTIGEQI-------AEPLRIHGKLSKKEA--RKEAVLLLLVGVGLPEEvLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 153 QRLSLAAALLGDPELLILDEPSNGLDP---EGMLWLrtfLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVsvqAQILDL---LKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-244 |
2.95e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 113.29 E-value: 2.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqTPTQ---RIGV- 96
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAW-SPWElarRRAVl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 ----SLdggAF-------VG-GRTGrghlrcYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALL-- 162
Cdd:COG4559 81 pqhsSL---AFpftveevVAlGRAP------HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAql 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 163 -----GDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQg 237
Cdd:COG4559 152 wepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTD- 230
|
....*..
gi 2155196442 238 ERLESAF 244
Cdd:COG4559 231 ELLERVY 237
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
21-208 |
3.03e-30 |
|
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: 112.18 E-value: 3.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGR----TAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPyreLQTPTQRIGV 96
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP---VTGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 SLDGGAFVGGRTGRGHLRCYAPAAGCSP----ERLDRLLAETGLAEAADR-P--VSGystGMKQRLSLAAALLGDPELLI 169
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKaearERAEELLELVGLSGFENAyPhqLSG---GMRQRVALARALAVDPDVLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2155196442 170 LDEPSNGLDP---EGM-LWLRTFLRRfaaSGRTVLLSSHLLSE 208
Cdd:cd03293 155 LDEPFSALDAltrEQLqEELLDIWRE---TGKTVLLVTHDIDE 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
25-224 |
4.11e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.47 E-value: 4.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 25 GLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGT--------------------------AL 78
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEvsipkglrigylpqeppldddltvldTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 79 LWGH-PYRELQTPTQRIGVSLDGGAFVGGRTGRGHLRcYAPAAGCSPE-RLDRLLAETGLAEA-ADRPVSGYSTGMKQRL 155
Cdd:COG0488 83 LDGDaELRALEAELEELEAKLAEPDEDLERLAELQEE-FEALGGWEAEaRAEEILSGLGFPEEdLDRPVSELSGGWRRRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 156 SLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAAsgrTVLLSSH---LLsemEQTVDDVLLMHHGKL 224
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG---TVLVVSHdryFL---DRVATRILELDRGKL 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
21-224 |
4.96e-30 |
|
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: 112.43 E-value: 4.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHpyRELQTPTQRIGVSL-- 98
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQERNVGFvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 ------------DGGAFvGGRTGRGHLRcyaPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPE 166
Cdd:cd03296 81 qhyalfrhmtvfDNVAF-GLRVKPRSER---PPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 167 LLILDEPSNGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-233 |
5.15e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.04 E-value: 5.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 19 PVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYReLQTPT--QRIGV 96
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSPRdaQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 sldggAFV------------------------GGRTGRGHLRcyapaagcspERLDRLLAETGLAEAADRPVSGYSTGMK 152
Cdd:COG1129 82 -----AIIhqelnlvpnlsvaeniflgreprrGGLIDWRAMR----------RRARELLARLGLDIDPDTPVGDLSVAQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 153 QRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDH 232
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAE 226
|
.
gi 2155196442 233 L 233
Cdd:COG1129 227 L 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-230 |
5.60e-30 |
|
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: 118.19 E-value: 5.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 19 PVIEVCGLRKKFR--GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYR-ELQTPTQRIG 95
Cdd:TIGR01257 927 PGVCVKNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 VSLDGGAFVGGRTGRGHLRCYAPAAGCSPE----RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILD 171
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEeaqlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 172 EPSNGLDPEGMLWLRTFLRRFaASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG-PL 230
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGtPL 1145
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-247 |
1.53e-29 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 116.76 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTtlrmLLGLI----RPTEGTALLWGHP-----YRELQTP 90
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIagarKIQQGRVEVLGGDmadarHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 91 tqRIgvsldggAFV--G-GRT--------------GR--GHlrcyapAAGCSPERLDRLLAETGLAEAADRPVSGYSTGM 151
Cdd:NF033858 77 --RI-------AYMpqGlGKNlyptlsvfenldffGRlfGQ------DAAERRRRIDELLRATGLAPFADRPAGKLSGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 152 KQRLSLAAALLGDPELLILDEPSNGLDPegmLWLRTF------LRRfAASGRTVLLSSHLLSEMEQtVDDVLLMHHGKLL 225
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPTTGVDP---LSRRQFwelidrIRA-ERPGMSVLVATAYMEEAER-FDWLVAMDAGRVL 216
|
250 260
....*....|....*....|....
gi 2155196442 226 SSGPLDHLL--TQGERLESAFMRL 247
Cdd:NF033858 217 ATGTPAELLarTGADTLEAAFIAL 240
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
19-244 |
2.22e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 114.17 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 19 PVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY---------RELQT 89
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaraasRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 90 PTQRIGVSLDGGAFVGGRTGRG-HLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELL 168
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGRTpHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 169 ILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTqGERLESAF 244
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT-ADTLRAAF 236
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
32-204 |
3.78e-29 |
|
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: 108.66 E-value: 3.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY----RELQTPTQRIGVSLDG------G 101
Cdd:TIGR01166 4 GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysrKGLLERRQRVGLVFQDpddqlfA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 102 AFVGGRTGRGHLRCYAPAAGCSpERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEG 181
Cdd:TIGR01166 84 ADVDQDVAFGPLNLGLSEAEVE-RRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|...
gi 2155196442 182 MLWLRTFLRRFAASGRTVLLSSH 204
Cdd:TIGR01166 163 REQMLAILRRLRAEGMTVVISTH 185
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
36-244 |
4.46e-29 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 109.93 E-value: 4.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 36 VDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIrPTEGTALLWGHPYRELQTPTQRigvsldggafvggrtgrgHLRC 115
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELA------------------RHRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 116 YAP-------------------AAGCSPERLDRLLAET----GLAEAADRPVSGYSTGMKQRLSLAAALL-----GDPE- 166
Cdd:COG4138 73 YLSqqqsppfampvfqylalhqPAGASSEAVEQLLAQLaealGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEg 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 167 -LLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQgERLESAF 244
Cdd:COG4138 153 qLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTP-ENLSEVF 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-228 |
5.80e-29 |
|
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: 108.92 E-value: 5.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 23 VCGLRKKFRGRTAvdGISFDVPAGrVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRE----LQTPTQ--RIGV 96
Cdd:cd03297 3 CVDIEKRLPDFTL--KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQqrKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 SLDGGAFVGGRTGRGHLRCYAPAAGCSPERL--DRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPS 174
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGLKRKRNREDRIsvDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 175 NGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-237 |
9.75e-29 |
|
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: 111.36 E-value: 9.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 26 LRKKFRGR---TAVDgISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALL----WGHPYRELQTPTQ--RIG- 95
Cdd:TIGR02142 1 LSARFSKRlgdFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtLFDSRKGIFLPPEkrRIGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 VSLDGGAF----VGGRTGRGHLRCYAPAAGCSPERLDRLLaetGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILD 171
Cdd:TIGR02142 80 VFQEARLFphlsVRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 172 EPSNGLDPEGMLWLRTFLRRFAASGRT-VLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQG 237
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
21-233 |
1.03e-28 |
|
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: 108.42 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLI-----RPTEGTALLWGHPYRELQTPT---- 91
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 92 QRIG----------------VSLdgGAFVGGRTGRGHLRcyapaagcspERLDRLLAETGL-AEAADRP-VSGYSTGMKQ 153
Cdd:cd03260 81 RRVGmvfqkpnpfpgsiydnVAY--GLRLHGIKLKEELD----------ERVEEALRKAALwDEVKDRLhALGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 154 RLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASgRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHL 233
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
19-204 |
1.15e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 108.99 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 19 PVIEVCGLRKKFR-GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY-----RELQTPTQ 92
Cdd:COG3638 1 PMLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalrgRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 93 RIGVSLDGGAFVG-------------GRTG--RGHLRCYAPAagcSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSL 157
Cdd:COG3638 81 RIGMIFQQFNLVPrlsvltnvlagrlGRTStwRSLLGLFPPE---DRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 158 AAALLGDPELLILDEPSNGLDPEG----MlwlrTFLRRFAAS-GRTVLLSSH 204
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTarqvM----DLLRRIAREdGITVVVNLH 205
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-233 |
2.93e-28 |
|
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: 113.18 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 9 ERTTPVKDNSPVIEVCGLRKKFRGRT--AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHP-YR 85
Cdd:TIGR01257 1926 QRIISGGNKTDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLT 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 86 ELQTPTQRIGVSLDGGAFVGGRTGRGHLRCYAPAAGCSPERLDRL----LAETGLAEAADRPVSGYSTGMKQRLSLAAAL 161
Cdd:TIGR01257 2006 NISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 162 LGDPELLILDEPSNGLDPEG--MLW--LRTFLRRfaasGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHL 233
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQArrMLWntIVSIIRE----GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
21-224 |
9.62e-28 |
|
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: 105.65 E-value: 9.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRG----RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqTPTQR--- 93
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKL-SEKELaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 94 ----IG-----------------VSLdgGAFVGGRTGRGHlrcyapaagcsPERLDRLLAETGLAEAADRPVSGYSTGMK 152
Cdd:cd03255 80 rrrhIGfvfqsfnllpdltalenVEL--PLLLAGVPKKER-----------RERAEELLERVGLGDRLNHYPSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 153 QRLSLAAALLGDPELLILDEPSNGLDPE-GMLWLRTFLRRFAASGRTVLLSSHLLsEMEQTVDDVLLMHHGKL 224
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSEtGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-224 |
1.01e-27 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 104.22 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTA--VDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTallwghpyrelqtptqrigVSL 98
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGR-------------------VRL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 DGGAFvgGRTGRGHLRcyaPAAGCSPERlDRLLAETglaeAADRPVSGystGMKQRLSLAAALLGDPELLILDEPSNGLD 178
Cdd:cd03246 62 DGADI--SQWDPNELG---DHVGYLPQD-DELFSGS----IAENILSG---GQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2155196442 179 PEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQtVDDVLLMHHGKL 224
Cdd:cd03246 129 VEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
32-239 |
1.14e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.02 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPT--QRIG-VSLDggAFVGGRT 108
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGvVPQD--TFLFSGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 109 GRGHLRCYAPAAgcSPERLDRLLAETGLAEAADRPVSGYST-----------GMKQRLSLAAALLGDPELLILDEPSNGL 177
Cdd:COG1132 430 IRENIRYGRPDA--TDEEVEEAAKAAQAHEFIEALPDGYDTvvgergvnlsgGQRQRIAIARALLKDPPILILDEATSAL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 178 DPEGMLWLRTFLRRFAAsGRTVLLSSHLLSemeqTV---DDVLLMHHGKLLSSGPLDHLLTQGER 239
Cdd:COG1132 508 DTETEALIQEALERLMK-GRTTIVIAHRLS----TIrnaDRILVLDDGRIVEQGTHEELLARGGL 567
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-234 |
1.29e-27 |
|
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: 105.59 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqtPTQRIgvSLDG 100
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGL--PPHER--ARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 101 GAFV-GGR------TGRGHLR--CYAPAAGCSPERLDRLLAE-TGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLIL 170
Cdd:cd03224 77 IGYVpEGRrifpelTVEENLLlgAYARRRAKRKARLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 171 DEPSNGLDP---EGMLwlrTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLL 234
Cdd:cd03224 157 DEPSEGLAPkivEEIF---EAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
33-250 |
1.58e-27 |
|
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: 106.77 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 33 RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTAL-----LWGHPYRELQTPTQRIGVsldggAF---- 103
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTidgrdITAKKKKKLKDLRKKVGL-----VFqfpe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 104 -----------VggrtgrghlrCYAPAA-GCSP----ERLDRLLAETGLAEA-ADRP---VSGystGMKQRLSLAAALLG 163
Cdd:TIGR04521 93 hqlfeetvykdI----------AFGPKNlGLSEeeaeERVKEALELVGLDEEyLERSpfeLSG---GQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 164 DPELLILDEPSNGLDPEG---MlwLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQGERL 240
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGrkeI--LDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDEL 237
|
250
....*....|
gi 2155196442 241 ESAFMRLTQA 250
Cdd:TIGR04521 238 EKIGLDVPEI 247
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
17-229 |
2.26e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 107.88 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 17 NSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqTPTQR-IG 95
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-PPEKRnVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 -VSLDGGAFvggrtgrGHL------------RCYAPAAgcSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALL 162
Cdd:COG3842 81 mVFQDYALF-------PHLtvaenvafglrmRGVPKAE--IRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 163 GDPELLILDEPSNGLDP---EGM-LWLRTFLRRFaasGRTVLLSSHLLSE-MeqTV-DDVLLMHHGKLLSSGP 229
Cdd:COG3842 152 PEPRVLLLDEPLSALDAklrEEMrEELRRLQREL---GITFIYVTHDQEEaL--ALaDRIAVMNDGRIEQVGT 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
21-223 |
2.27e-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: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTaLLWGhpyrelqtPTQRIGVsldg 100
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-VTWG--------STVKIGY---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 101 gafvggrtgrghlrcyapaagcsperLDRLlaetglaeaadrpvSGystGMKQRLSLAAALLGDPELLILDEPSNGLDPE 180
Cdd:cd03221 68 --------------------------FEQL--------------SG---GEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2155196442 181 GMLWLRTFLRRFAasgRTVLLSSHLLSEMEQTVDDVLLMHHGK 223
Cdd:cd03221 105 SIEALEEALKEYP---GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-214 |
2.51e-27 |
|
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: 109.68 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 18 SPVIEVCGLRKKFRGRT-AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGV 96
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 sldggAFVGGR------TGRGHLRCYAPAAgcSPERLDRLLAETGLAEA-ADRPV----------SGYSTGMKQRLSLAA 159
Cdd:TIGR02857 399 -----AWVPQHpflfagTIAENIRLARPDA--SDAEIREALERAGLDEFvAALPQgldtpigeggAGLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 160 ALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFaASGRTVLLSSH---LLSEMEQTVD 214
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHrlaLAALADRIVV 528
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
21-229 |
3.30e-27 |
|
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: 104.96 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKF-RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH-----PYRELQTPTQRI 94
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 95 GVSLDGGAFVG----------GR-----TGRGHLRCYAPAagcspERLD--RLLAETGLAEAADRPVSGYSTGMKQRLSL 157
Cdd:cd03256 81 GMIFQQFNLIErlsvlenvlsGRlgrrsTWRSLFGLFPKE-----EKQRalAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 158 AAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGP 229
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGP 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
31-229 |
4.67e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.98 E-value: 4.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAGRVTgFL-GPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYREL---QTPT--QRIGVSL-DGG-- 101
Cdd:COG2884 13 GGREALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYlrRRIGVVFqDFRll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 102 ---------AFVggrtgrghLRcyapAAGCSP----ERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELL 168
Cdd:COG2884 92 pdrtvyenvALP--------LR----VTGKSRkeirRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2155196442 169 ILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSH---LLSEMEQTvddVLLMHHGKLLSSGP 229
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHdleLVDRMPKR---VLELEDGRLVRDEA 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
39-244 |
9.99e-27 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 103.86 E-value: 9.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 39 ISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIrPTEGTALLWGHPYRELQTPTQrigvsldggafvggrtgrGHLRCY-- 116
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAEL------------------ARHRAYls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 117 ---------------------APAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALL-----GDPE--LL 168
Cdd:PRK03695 76 qqqtppfampvfqyltlhqpdKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 169 ILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQgERLESAF 244
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTP-ENLAQVF 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
21-235 |
1.63e-26 |
|
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: 103.15 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRG-RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRElQTPTQ---RIGV 96
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE-QDPVElrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 SLDGGAFVGGRTGRGHLRCYAPAAGCSPE----RLDRLLAETGL--AEAADRPVSGYSTGMKQRLSLAAALLGDPELLIL 170
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEkireRADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 171 DEPSNGLDPEGMLWL-RTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLT 235
Cdd:cd03295 160 DEPFGALDPITRDQLqEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
32-251 |
1.69e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY----RELQTPTQRIGVSLDG------G 101
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKLRESVGMVFQDpdnqlfS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 102 AFVGGRTGRGHLRCYAPAAGCSpERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEG 181
Cdd:PRK13636 98 ASVYQDVSFGAVNLKLPEDEVR-KRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2155196442 182 MLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQGERLESAFMRLTQAG 251
Cdd:PRK13636 177 VSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNLRLPRIG 247
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
31-237 |
3.46e-26 |
|
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: 101.92 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQR--IGVSL-DGGAFVGgr 107
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRsmIGVVLqDTFLFSG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 108 TGRGHLRCYAPAAgcSPERLDRLLAETGLAEAADRPVSGY-----------STGMKQRLSLAAALLGDPELLILDEPSNG 176
Cdd:cd03254 92 TIMENIRLGRPNA--TDEEVIEAAKEAGAHDFIMKLPNGYdtvlgenggnlSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2155196442 177 LDPEGMLWLRTFLRRFaASGRTVLLSSHLLSEMeQTVDDVLLMHHGKLLSSGPLDHLLTQG 237
Cdd:cd03254 170 IDTETEKLIQEALEKL-MKGRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
35-228 |
5.00e-26 |
|
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: 101.13 E-value: 5.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 35 AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYREL--QTPTQRIG-VSLDGGAFVGgrTGRG 111
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLdpADLRRNIGyVPQDVTLFYG--TLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 112 HLRCYAPAAgcSPERLDRLLAETGLAEAADRPVSGY-----------STGMKQRLSLAAALLGDPELLILDEPSNGLDPE 180
Cdd:cd03245 97 NITLGAPLA--DDERILRAAELAGVTDFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDPPILLLDEPTSAMDMN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2155196442 181 GMLWLRTFLRRFAAsGRTVLLSSHLLSeMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03245 175 SEERLKERLRQLLG-DKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-232 |
5.64e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 101.73 E-value: 5.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 17 NSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY------------ 84
Cdd:COG4674 7 HGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLtgldeheiarlg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 85 --RELQTPT--------QRIGVSLDggafvGGRTGRGHLRcyAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQR 154
Cdd:COG4674 87 igRKFQKPTvfeeltvfENLELALK-----GDRGVFASLF--ARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 155 LSLAAALLGDPELLILDEPSNGLDPEGMlwLRT--FLRRfAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDH 232
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVAGMTDAET--ERTaeLLKS-LAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDE 236
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
21-231 |
6.61e-26 |
|
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: 101.16 E-value: 6.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSLDG 100
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 101 GAFVggrtgrGHLRCYAPAA------GCSP----ERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLIL 170
Cdd:cd03300 81 YALF------PHLTVFENIAfglrlkKLPKaeikERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 171 DEPSNGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG-PLD 231
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGtPEE 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
21-236 |
8.10e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 103.23 E-value: 8.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGR----TAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH-----PYRELQTPT 91
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltalSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 92 QRIGV---------SldggafvggRTGRGH----LRCyapaAGCSP----ERLDRLLAETGLAEAADRPVSGYSTGMKQR 154
Cdd:COG1135 82 RKIGMifqhfnllsS---------RTVAENvalpLEI----AGVPKaeirKRVAELLELVGLSDKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 155 LSLAAALLGDPELLILDEPSNGLDPEGM-----LwLRTFLRRFaasGRTVLLSSHllsEME---QTVDDVLLMHHGKLLS 226
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTrsildL-LKDINREL---GLTIVLITH---EMDvvrRICDRVAVLENGRIVE 221
|
250
....*....|
gi 2155196442 227 SGPLDHLLTQ 236
Cdd:COG1135 222 QGPVLDVFAN 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-249 |
8.88e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 102.01 E-value: 8.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 25 GLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHP--YRE-------------LQT 89
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldYSKrgllalrqqvatvFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 90 PTQRIGVS-LDGG-AFvggrtgrgHLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPEL 167
Cdd:PRK13638 86 PEQQIFYTdIDSDiAF--------SLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 168 LILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQGERLESAfmRL 247
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQA--GL 235
|
..
gi 2155196442 248 TQ 249
Cdd:PRK13638 236 TQ 237
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
33-237 |
9.43e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 101.24 E-value: 9.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 33 RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY-----REL--------QTPTQRIGVSLD 99
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsmlssRQLarrlallpQHHLTPEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 100 ggAFVG-GRTGrgHLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLD 178
Cdd:PRK11231 95 --ELVAyGRSP--WLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 179 PEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQG 237
Cdd:PRK11231 171 INHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
8-236 |
1.81e-25 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 102.51 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 8 MERTTPVKDNSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTlRMLLGLIRPTEGTallwgHPYREL 87
Cdd:NF000106 1 MTRKTISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR-----RPWRF* 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 88 QTPTQRIGVSLDGGAFVGGRTGR-----GHLRCYAPAAGC------SPERLDRLLAETGLAEAADRPVSGYSTGMKQRLS 156
Cdd:NF000106 75 TWCANRRALRRTIG*HRPVR*GRresfsGRENLYMIGR*LdlsrkdARARADELLERFSLTEAAGRAAAKYSGGMRRRLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 157 LAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQ 236
Cdd:NF000106 155 LAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
31-231 |
1.86e-25 |
|
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: 104.44 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqTPTQRigvsldgGAFVGgrtgr 110
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW-DREEL-------GRHIG----- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 111 ghlrcYAP------------------------------AAGCS------PERLDRLLAETGlaeaadRPVSGystGMKQR 154
Cdd:COG4618 410 -----YLPqdvelfdgtiaeniarfgdadpekvvaaakLAGVHemilrlPDGYDTRIGEGG------ARLSG---GQRQR 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 155 LSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMeQTVDDVLLMHHGKLLSSGPLD 231
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLL-AAVDKLLVLRDGRVQAFGPRD 551
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-236 |
2.13e-25 |
|
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: 101.67 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGR----TAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRP---TEGTAL-----LWGHPYREL 87
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILfdgedLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 88 QT------------------PTQRIGVSLdggafvgGRTGRGHLRCYAPAAgcsPERLDRLLAETGLAEAADR----P-- 143
Cdd:COG0444 81 RKirgreiqmifqdpmtslnPVMTVGDQI-------AEPLRIHGGLSKAEA---RERAIELLERVGLPDPERRldryPhe 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 144 VSGystGMKQRLSLAAALLGDPELLILDEPSNGLDP----EGMLWLRTFLRRFaasGRTVLLSSHLLSEMEQTVDDVLLM 219
Cdd:COG0444 151 LSG---GMRQRVMIARALALEPKLLIADEPTTALDVtiqaQILNLLKDLQREL---GLAILFITHDLGVVAEIADRVAVM 224
|
250
....*....|....*..
gi 2155196442 220 HHGKLLSSGPLDHLLTQ 236
Cdd:COG0444 225 YAGRIVEEGPVEELFEN 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
32-224 |
2.94e-25 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 99.02 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHP---YRELQTPTQR--IGVSLDGGAFVGG 106
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYLRrkIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 107 RTGRGH----LRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGM 182
Cdd:cd03292 93 RNVYENvafaLEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2155196442 183 LWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:cd03292 173 WEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-243 |
5.49e-25 |
|
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: 99.81 E-value: 5.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRG--RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRE------------ 86
Cdd:TIGR04520 1 IEVENVSFSYPEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDeenlweirkkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 87 --LQTP-TQRIGVSL-DGGAFvggrtgrghlrcyapaagcSPE-----------RLDRLLAETGLAEAADRPVSGYSTGM 151
Cdd:TIGR04520 81 mvFQNPdNQFVGATVeDDVAF-------------------GLEnlgvpreemrkRVDEALKLVGMEDFRDREPHLLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 152 KQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTvDDVLLMHHGKLLSSGPL 230
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVLA-DRVIVMNKGKIVAEGTP 220
|
250
....*....|...
gi 2155196442 231 DHLLTQGERLESA 243
Cdd:TIGR04520 221 REIFSQVELLKEI 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-224 |
6.03e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.84 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 19 PVIEVCGLRKKFRGRTAVDGISFDVPAG-RVtGFLGPNGAGKTTTLRMLLGLIRPTEGTaLLWGHpyrelqtpTQRIG-V 96
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGdRI-GLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGE--------TVKIGyF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 SLDGGAFVGGRTGRGHLRCYAPaaGCSPERLDRLLAETGLA-EAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSN 175
Cdd:COG0488 384 DQHQEELDPDKTVLDELRDGAP--GGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 176 GLDPEGMLWLRTFLRRFAasGrTVLLSSH---LLsemEQTVDDVLLMHHGKL 224
Cdd:COG0488 462 HLDIETLEALEEALDDFP--G-TVLLVSHdryFL---DRVATRILEFEDGGV 507
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
32-204 |
1.31e-24 |
|
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: 97.04 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQT-PTQRIgvsldggAFVGGRTG- 109
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENI-------LYLGHLPGl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 110 ------RGHLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGML 183
Cdd:TIGR01189 85 kpelsaLENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|.
gi 2155196442 184 WLRTFLRRFAASGRTVLLSSH 204
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTH 185
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-247 |
1.34e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.00 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKF-RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY----RELQTPTQRI 94
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 95 GVSL---DGGAF---VGGRTGRGHLRCYAPAAGCSpERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELL 168
Cdd:PRK13639 81 GIVFqnpDDQLFaptVEEDVAFGPLNLGLSKEEVE-KRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 169 ILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQGERLESAFMRL 247
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKANLRL 238
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
21-224 |
2.97e-24 |
|
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: 96.44 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWG----HPYRELQTPTQRIG- 95
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltDDKKNINELRQKVGm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 ----------------VSLdggafvGGRTGRGHLRCYAPaagcspERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAA 159
Cdd:cd03262 81 vfqqfnlfphltvlenITL------APIKVKGMSKAEAE------ERALELLEKVGLADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2155196442 160 ALLGDPELLILDEPSNGLDPEgmlWLRTFL---RRFAASGRTVLLSSHllsEM---EQTVDDVLLMHHGKL 224
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPE---LVGEVLdvmKDLAEEGMTMVVVTH---EMgfaREVADRVIFMDDGRI 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
18-226 |
3.45e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 96.65 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 18 SPVIEVCGLRKKFR----GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqTPTQR 93
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSL-SEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 94 -------IG-----------------VSLdgGAFVGGRTGRGhlrcyapaagcSPERLDRLLAETGLAEAADRPVSGYST 149
Cdd:COG1136 81 arlrrrhIGfvfqffnllpeltalenVAL--PLLLAGVSRKE-----------RRERARELLERVGLGDRLDHRPSQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 150 GMKQRLSLAAALLGDPELLILDEPSNGLDPE-GMLWLRTFLRRFAASGRTVLLSSH---LLSEMeqtvDDVLLMHHGKLL 225
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKtGEEVLELLRELNRELGTTIVMVTHdpeLAARA----DRVIRLRDGRIV 223
|
.
gi 2155196442 226 S 226
Cdd:COG1136 224 S 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
21-224 |
3.61e-24 |
|
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: 96.17 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSLDG 100
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 101 GAFVGGRTGRGHLRCYAPAAGCSPERLDRLLAET----GLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNG 176
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVaellQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2155196442 177 LDPEGMLWLRTFLRRF-AASGRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:cd03301 161 LDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
31-236 |
4.95e-24 |
|
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: 100.56 E-value: 4.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSL--------DGGA 102
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALvsqdvvlfNDTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 103 FVGGRTGRGhlrcyapaAGCSPERLDRLLAETGLAEAADRPVSGYST-----------GMKQRLSLAAALLGDPELLILD 171
Cdd:TIGR02203 423 ANNIAYGRT--------EQADRAEIERALAAAYAQDFVDKLPLGLDTpigengvllsgGQRQRLAIARALLKDAPILILD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 172 EPSNGLDPEGMLWLRTFLRRFaASGRTVLLSSHLLSEMEQTvDDVLLMHHGKLLSSGPLDHLLTQ 236
Cdd:TIGR02203 495 EATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEKA-DRIVVMDDGRIVERGTHNELLAR 557
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-236 |
5.00e-24 |
|
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: 98.63 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDgISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY----RELQTPTQ--RIG-VSLDGGAF 103
Cdd:COG4148 11 RGGFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsaRGIFLPPHrrRIGyVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 104 ----VGGRTGRGHLRCYAPAagcSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDP 179
Cdd:COG4148 90 phlsVRGNLLYGRKRAPRAE---RRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 180 EGMLWLRTFLRRFAASGRT-VLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQ 236
Cdd:COG4148 167 ARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-224 |
8.68e-24 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 94.42 E-value: 8.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 19 PVIEVCGLRkkfrGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqTPTQRIGvsl 98
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR-SPRDAIR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 DGGAFVggrtgrghlrcyapaagcsPErlDRLlaETGLaeAADRPV-------SGYSTGMKQRLSLAAALLGDPELLILD 171
Cdd:cd03215 75 AGIAYV-------------------PE--DRK--REGL--VLDLSVaenialsSLLSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 172 EPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-241 |
1.10e-23 |
|
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: 95.43 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 18 SPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGhpyRELQ-TPTQRI-- 94
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG---EDITgLPPHRIar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 95 -GVSL---DGGAF----------VGGRTGRGHLRcyapaagcSPERLDRLLA---EtgLAEAADRPVSGYSTGMKQRLSL 157
Cdd:COG0410 78 lGIGYvpeGRRIFpsltveenllLGAYARRDRAE--------VRADLERVYElfpR--LKERRRQRAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 158 AAALLGDPELLILDEPSNGLDPegMLWLRTF--LRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLT 235
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLAP--LIVEEIFeiIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
....*.
gi 2155196442 236 QGERLE 241
Cdd:COG0410 226 DPEVRE 231
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
37-204 |
1.18e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 94.49 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 37 DGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRigvSLdggAFVGGRTG------- 109
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ---DL---LYLGHQPGiktelta 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 110 RGHLRCYAPAAGC-SPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTF 188
Cdd:PRK13538 92 LENLRFYQRLHGPgDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAL 171
|
170
....*....|....*.
gi 2155196442 189 LRRFAASGRTVLLSSH 204
Cdd:PRK13538 172 LAQHAEQGGMVILTTH 187
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
20-247 |
1.26e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.41 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRG-RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRigvsl 98
Cdd:PRK13652 3 LIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 dggAFVGGRTGRGHLRCYAPAA-----------GCSPE----RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLG 163
Cdd:PRK13652 78 ---KFVGLVFQNPDDQIFSPTVeqdiafgpinlGLDEEtvahRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 164 DPELLILDEPSNGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQGERLES 242
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLAR 234
|
....*
gi 2155196442 243 AFMRL 247
Cdd:PRK13652 235 VHLDL 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
21-239 |
1.73e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 95.20 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGT----------ALLWGHPYRELQTP 90
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTirvgditidtARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 91 TQRIGVSLDGGAFVGGRTG-----RGHLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDP 165
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVleniiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 166 ELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLT--QGER 239
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAdpQQPR 239
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-205 |
1.91e-23 |
|
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: 94.10 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSLDGGAFVGGR-TGR 110
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTlSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 111 GHLRCYAPAagCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLR 190
Cdd:cd03231 92 ENLRFWHAD--HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....*
gi 2155196442 191 RFAASGRTVLLSSHL 205
Cdd:cd03231 170 GHCARGGMVVLTTHQ 184
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
31-237 |
2.79e-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: 94.22 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQR--IG-VSLDGGAFVG-- 105
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRrqIGlVSQDVFLFNDtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 106 ------GRTG--RGHLRCYAPAAGC------SPERLDRLLAETGlaeaadrpvSGYSTGMKQRLSLAAALLGDPELLILD 171
Cdd:cd03251 93 aeniayGRPGatREEVEEAARAANAhefimeLPEGYDTVIGERG---------VKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 172 EPSNGLDPEGMLWLRTFLRRFAAsGRTVLLSSHLLSEMEQTvDDVLLMHHGKLLSSGPLDHLLTQG 237
Cdd:cd03251 164 EATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLAQG 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-247 |
3.99e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.80 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFR-GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWG---HPYRE--------- 86
Cdd:PRK13647 4 IIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGrevNAENEkwvrskvgl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 87 -LQTPTQRI--GVSLDGGAF--VGGRTGRGHLRcyapaagcspERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAAL 161
Cdd:PRK13647 84 vFQDPDDQVfsSTVWDDVAFgpVNMGLDKDEVE----------RRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 162 LGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPlDHLLTQGERLE 241
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD-KSLLTDEDIVE 232
|
....*.
gi 2155196442 242 SAFMRL 247
Cdd:PRK13647 233 QAGLRL 238
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
17-228 |
5.07e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 94.29 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 17 NSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqtPTQRI-- 94
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL--PGHQIar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 95 -GV-------------------------SLDGGAFVGGRTGRGHLRCYAPAAGCSPERLDRLlaetGLAEAADRPVSGYS 148
Cdd:PRK11300 80 mGVvrtfqhvrlfremtvienllvaqhqQLKTGLFSGLLKTPAFRRAESEALDRAATWLERV----GLLEHANRQAGNLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 149 TGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTF---LRRfaASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLL 225
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELiaeLRN--EHNVTVLLIEHDMKLVMGISDRIYVVNQGTPL 233
|
...
gi 2155196442 226 SSG 228
Cdd:PRK11300 234 ANG 236
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
35-206 |
1.12e-22 |
|
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: 96.28 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 35 AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSL-DGGAFVGGRTGRGHL 113
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVcAQDAHLFDTTVRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 114 RCYAPaaGCSPERLDRLLAETGLAEAADRPVSGYST-----------GMKQRLSLAAALLGDPELLILDEPSNGLDPEGM 182
Cdd:TIGR02868 430 RLARP--DATDEELWAALERVGLADWLRALPDGLDTvlgeggarlsgGERQRLALARALLADAPILLLDEPTEHLDAETA 507
|
170 180
....*....|....*....|....
gi 2155196442 183 LWLRTFLRRfAASGRTVLLSSHLL 206
Cdd:TIGR02868 508 DELLEDLLA-ALSGRTVVLITHHL 530
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
20-240 |
1.90e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 92.36 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY----RELQTPTQRIG 95
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 V-----SLdggaFvggrtgrGHLR-----CYAP--AAGCSP----ERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAA 159
Cdd:COG1126 81 MvfqqfNL----F-------PHLTvlenvTLAPikVKKMSKaeaeERAMELLERVGLADKADAYPAQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 160 ALLGDPELLILDEPSNGLDPE---GMLwlrTFLRRFAASGRTVLLSSHllsEME--QTV-DDVLLMHHGKLLSSGPLDHL 233
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPElvgEVL---DVMRDLAKEGMTMVVVTH---EMGfaREVaDRVVFMDGGRIVEEGPPEEF 223
|
....*....
gi 2155196442 234 LT--QGERL 240
Cdd:COG1126 224 FEnpQHERT 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-241 |
3.44e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.39 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 18 SPVIEVCGLRKKFRG--RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRE--------- 86
Cdd:PRK13635 3 EEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetvwdvrrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 87 ----LQTP-TQRIGVSL-DGGAFvgGRTGRGHLRCYAPaagcspERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAA 160
Cdd:PRK13635 83 vgmvFQNPdNQFVGATVqDDVAF--GLENIGVPREEMV------ERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 161 LLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGR-TVLLSSHLLSEMEQTvDDVLLMHHGKLLSSGPLDHLLTQGER 239
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQA-DRVIVMNKGEILEEGTPEEIFKSGHM 233
|
..
gi 2155196442 240 LE 241
Cdd:PRK13635 234 LQ 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
15-243 |
1.17e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 90.82 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 15 KDNSPVIEVCGLRKKFRG--RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWG-----HPYREL 87
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 88 --------QTP-TQRIGVSL-DGGAFvggrtgrgHL--RCYAPAAgcSPERLDRLLAETGLAEAADRPVSGYSTGMKQRL 155
Cdd:PRK13632 82 rkkigiifQNPdNQFIGATVeDDIAF--------GLenKKVPPKK--MKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 156 SLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLS-SHllsEMEQTV--DDVLLMHHGKLLSSGPLDH 232
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTH---DMDEAIlaDKVIVFSEGKLIAQGKPKE 228
|
250
....*....|.
gi 2155196442 233 LLTQGERLESA 243
Cdd:PRK13632 229 ILNNKEILEKA 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
21-229 |
1.25e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.06 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTaLLWGHpyREL-QTPTQRIGVSL- 98
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGE-ILIGG--RDVtDLPPKDRNIAMv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 -------------DGGAFvggrtgrgHLRcyapAAGCSPERLDRLLAET----GLAEAADRPVSGYSTGMKQRLSLAAAL 161
Cdd:COG3839 81 fqsyalyphmtvyENIAF--------PLK----LRKVPKAEIDRRVREAaellGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 162 LGDPELLILDEP-SNgLDPEGMLWLRTFLRRF-AASGRTVLLSSHllsemEQT-----VDDVLLMHHGKLLSSGP 229
Cdd:COG3839 149 VREPKVFLLDEPlSN-LDAKLRVEMRAEIKRLhRRLGTTTIYVTH-----DQVeamtlADRIAVMNDGRIQQVGT 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
32-235 |
1.33e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWG---HPYRELQTPTQRIGVSLDG--GAFVGg 106
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKLQGIRKLVGIVFQNpeTQFVG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 107 RTGRGHLrCYAPAAGCSP-----ERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEG 181
Cdd:PRK13644 93 RTVEEDL-AFGPENLCLPpieirKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2155196442 182 MLWLRTFLRRFAASGRTVLLSSHLLSEMeQTVDDVLLMHHGKLLSSGPLDHLLT 235
Cdd:PRK13644 172 GIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
34-228 |
1.66e-21 |
|
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: 88.14 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 34 TAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQ-TPTQRIGVsLDGGAFvggrtgrgh 112
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEkALSSLISV-LNQRPY--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 113 lrcyapaagcsperldrlLAETGLAEAADRPVSGystGMKQRLSLAAALLGDPELLILDEPSNGLDP--EGMLwLRTFLR 190
Cdd:cd03247 86 ------------------LFDTTLRNNLGRRFSG---GERQRLALARILLQDAPIVLLDEPTVGLDPitERQL-LSLIFE 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 2155196442 191 rfAASGRTVLLSSHLLSEMEQtVDDVLLMHHGKLLSSG 228
Cdd:cd03247 144 --VLKDKTLIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
32-228 |
2.74e-21 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 87.99 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRP--TEGTALLWGHPyRELQTPTQRIGvsldggaFVggrtg 109
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRP-LDKRSFRKIIG-------YV----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 110 rghlrcyapaagcspERLDRLLAETGLAEAADRPV--SGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRT 187
Cdd:cd03213 88 ---------------PQDDILHPTLTVRETLMFAAklRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2155196442 188 FLRRFAASGRTVLLSSH-LLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03213 153 LLRRLADTGRTIICSIHqPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
21-224 |
6.14e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 90.14 E-value: 6.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFrGRTAV-DGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIG---- 95
Cdd:PRK10851 3 IEIANIKKSF-GRTQVlNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGfvfq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 --------VSLDGGAF---VGGRTGRghlrcyaPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGD 164
Cdd:PRK10851 82 hyalfrhmTVFDNIAFgltVLPRRER-------PNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2155196442 165 PELLILDEPSNGLDPEGMLWLRTFLRRFAASGR-TVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-243 |
7.77e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.61 E-value: 7.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 18 SPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPT-----EGTALLWGHP---YRELQT 89
Cdd:PRK14271 19 APAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVsgyrySGDVLLGGRSifnYRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 90 PTQRIG----------VSLDGGAFVGGRTG----RGHLRCYAPAAgcsperldrlLAETGLAEA-----ADRPVSgYSTG 150
Cdd:PRK14271 99 FRRRVGmlfqrpnpfpMSIMDNVLAGVRAHklvpRKEFRGVAQAR----------LTEVGLWDAvkdrlSDSPFR-LSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 151 MKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASgRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPL 230
Cdd:PRK14271 168 QQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPT 246
|
250
....*....|...
gi 2155196442 231 DHLLTQGERLESA 243
Cdd:PRK14271 247 EQLFSSPKHAETA 259
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
20-229 |
1.10e-20 |
|
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: 87.74 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKF-RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY-----RELQTPTQR 93
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrgKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 94 IGVSLDGGAFVG----------GRTG-----RGHLRCYAPAagcSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLA 158
Cdd:TIGR02315 81 IGMIFQHYNLIErltvlenvlhGRLGykptwRSLLGRFSEE---DKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 159 AALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGP 229
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGA 229
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-237 |
1.65e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.29 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 11 TTPVKDNSPV-IEVCGLR-KKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIrPTEGTALLWGHPYRELQ 88
Cdd:PRK11174 339 EKELASNDPVtIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 89 TPTQRIGVsldggAFVGGR------TGRGHLRCYAPAAgcSPERLDRLLAETGLAE-------AADRPVS----GYSTGM 151
Cdd:PRK11174 418 PESWRKHL-----SWVGQNpqlphgTLRDNVLLGNPDA--SDEQLQQALENAWVSEflpllpqGLDTPIGdqaaGLSVGQ 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 152 KQRLSLAAALLGDPELLILDEPSNGLDPEG----MLWLRTflrrfAASGRTVLLSSHLLSEMEQtVDDVLLMHHGKLLSS 227
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLDAHSeqlvMQALNA-----ASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQ 564
|
250
....*....|
gi 2155196442 228 GPLDHLLTQG 237
Cdd:PRK11174 565 GDYAELSQAG 574
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
33-251 |
1.66e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.41 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 33 RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQR--IGVSL-DGGAFvgGRTG 109
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRrnIAVVFqDAGLF--NRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 110 RGHLRCYAPAAgcSPERLdRLLAEtgLAEAAD---RPVSGYST-----------GMKQRLSLAAALLGDPELLILDEPSN 175
Cdd:PRK13657 426 EDNIRVGRPDA--TDEEM-RAAAE--RAQAHDfieRKPDGYDTvvgergrqlsgGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 176 GLDPEgmlwlrTFLRRFAA-----SGRTVLLSSHLLSemeqTV---DDVLLMHHGKLLSSGPLDHLLTQGERlesaFMRL 247
Cdd:PRK13657 501 ALDVE------TEAKVKAAldelmKGRTTFIIAHRLS----TVrnaDRILVFDNGRVVESGSFDELVARGGR----FAAL 566
|
....
gi 2155196442 248 TQAG 251
Cdd:PRK13657 567 LRAQ 570
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
16-245 |
3.04e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 88.24 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 16 DNSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIG 95
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 VSLDGGAF-----VGGRTGRGhLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLIL 170
Cdd:PRK11432 82 MVFQSYALfphmsLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 171 DEPSNGLDPEgmlwLRTFLR--------RFaasGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQ-GERLE 241
Cdd:PRK11432 161 DEPLSNLDAN----LRRSMRekirelqqQF---NITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQpASRFM 233
|
....
gi 2155196442 242 SAFM 245
Cdd:PRK11432 234 ASFM 237
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
31-247 |
3.59e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.11 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHP---YRELQ------TPTQRIGVsldgg 101
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiadYSEAAlrqaisVVSQRVHL----- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 102 aFVGgrTGRGHLRCYAPAAgcSPERLDRLLAETGLAEAAD-------------RPVSGystGMKQRLSLAAALLGDPELL 168
Cdd:PRK11160 426 -FSA--TLRDNLLLAAPNA--SDEALIEVLQQVGLEKLLEddkglnawlgeggRQLSG---GEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 169 ILDEPSNGLDPEG---MLWLrtfLRRFAAsGRTVLLSSHLLSEMEQtVDDVLLMHHGKLLSSGPLDHLLTQGERLESAFM 245
Cdd:PRK11160 498 LLDEPTEGLDAETerqILEL---LAEHAQ-NKTVLMITHRLTGLEQ-FDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
..
gi 2155196442 246 RL 247
Cdd:PRK11160 573 RL 574
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
32-237 |
6.04e-20 |
|
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: 85.36 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQR--IG-VSLDGGAF---VG 105
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRraIGvVPQDTVLFndtIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 106 -----GRTGRGHLRCYAPAAGC--------SPERLDRLLAETGLAeaadrpVSGystGMKQRLSLAAALLGDPELLILDE 172
Cdd:cd03253 93 yniryGRPDATDEEVIEAAKAAqihdkimrFPDGYDTIVGERGLK------LSG---GEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 173 PSNGLDPEG-MLWLRTFLRrfAASGRTVLLSSHLLSEMEQTvDDVLLMHHGKLLSSGPLDHLLTQG 237
Cdd:cd03253 164 ATSALDTHTeREIQAALRD--VSKGRTTIVIAHRLSTIVNA-DKIIVLKDGRIVERGTHEELLAKG 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-244 |
1.03e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.70 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 18 SPVIEVCGLRKKFR-GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRE------LQTP 90
Cdd:PRK15056 4 QAGIVVNDVTVTWRnGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQalqknlVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 91 TQRIGVSLDGGAFVGG--RTGR-GHLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPEL 167
Cdd:PRK15056 84 PQSEEVDWSFPVLVEDvvMMGRyGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 168 LILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVdDVLLMHHGKLLSSGPLDHLLTqGERLESAF 244
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFC-DYTVMVKGTVLASGPTETTFT-AENLELAF 238
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
39-234 |
1.05e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.81 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 39 ISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqTPTQRiGVSL---DGGAFvggrtgrGHLRC 115
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL-PPAER-PVSMlfqENNLF-------PHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 116 YAPAA-GCSP---------ERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDP---EGM 182
Cdd:COG3840 89 AQNIGlGLRPglkltaeqrAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 183 LWLRTFLRRfaASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLL 234
Cdd:COG3840 169 LDLVDELCR--ERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
21-252 |
1.12e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.14 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPyreLQTPTQRIGVSLDG 100
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP---VEGPGAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 101 GAFVGGRTGRGHLRCYAPAAGCS-PERLDR---LLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNG 176
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEkMQRLEIahqMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 177 LDP---EGMLWLrtFLRRFAASGRTVLLSSHLLSEMeqtvddVLLMHHGKLLSSGPLDHLltqgERLESAFMRLTQAGE 252
Cdd:PRK11248 159 LDAftrEQMQTL--LLKLWQETGKQVLLITHDIEEA------VFMATELVLLSPGPGRVV----ERLPLNFARRFVAGE 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
32-204 |
1.41e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.77 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQrigvsldgGAFVGGR---- 107
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA--------CHYLGHRnamk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 108 ---TGRGHLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLW 184
Cdd:PRK13539 86 palTVAENLEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|
gi 2155196442 185 LRTFLRRFAASGRTVLLSSH 204
Cdd:PRK13539 166 FAELIRAHLAQGGIVIAATH 185
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
25-224 |
1.72e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 84.73 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 25 GLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQ------------ 92
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRlmfqdarllpwk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 93 ----RIGVSLdggafvggrtgRGHLRCYAPAAgcsperldrlLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELL 168
Cdd:PRK11247 97 kvidNVGLGL-----------KGQWRDAALQA----------LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 169 ILDEPSNGLDPEGMLWLRTFLRR-FAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESlWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
27-237 |
1.90e-19 |
|
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: 84.07 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 27 RKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQR--IGVSLDGGAFV 104
Cdd:cd03252 9 RYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRrqVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 105 G---------GRTGRGHLRCYAPA--AGCS------PERLDRLLAETGlaeaadrpvSGYSTGMKQRLSLAAALLGDPEL 167
Cdd:cd03252 89 NrsirdnialADPGMSMERVIEAAklAGAHdfiselPEGYDTIVGEQG---------AGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 168 LILDEPSNGLDPEGMLWLRTFLRRFAAsGRTVLLSSHLLSEMeQTVDDVLLMHHGKLLSSGPLDHLLTQG 237
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-228 |
2.18e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 19 PVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqTPT------- 91
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHKlaaqlgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 92 ----QRIGV----SLDGGAFVGGRTGRGhlRCYAPAAGCSP--ERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAAL 161
Cdd:PRK09700 83 giiyQELSVidelTVLENLYIGRHLTKK--VCGVNIIDWREmrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 162 LGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
21-244 |
3.10e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.98 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH-----PYREL-------- 87
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattPSRELakrlailr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 88 QTP--TQRIGVSlDGGAFvgGR--TGRGHLrcyapaagcSPE---RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAA 160
Cdd:COG4604 82 QENhiNSRLTVR-ELVAF--GRfpYSKGRL---------TAEdreIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 161 LLGDPELLILDEPSNGLDPE---GMLWLrtfLRRFA-ASGRTVLL--------SSHllsemeqtVDDVLLMHHGKLLSSG 228
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKhsvQMMKL---LRRLAdELGKTVVIvlhdinfaSCY--------ADHIVAMKDGRVVAQG 218
|
250
....*....|....*.
gi 2155196442 229 PLDHLLTqGERLESAF 244
Cdd:COG4604 219 TPEEIIT-PEVLSDIY 233
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-236 |
3.28e-19 |
|
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: 84.23 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 26 LRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHP--------YRELQTptQRIGVS 97
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaamsrkeLRELRR--KKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 98 LDGGAFVGGRTGRGHLRCYAPAAGCSP-ERLDR---LLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEP 173
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRaEREERaaeALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 174 SNGLDPegmlWLRT-----FLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQ 236
Cdd:cd03294 188 FSALDP----LIRRemqdeLLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
37-239 |
3.34e-19 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 83.36 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 37 DGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQR--IG-VSLDGGAFVG-------- 105
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRsqIGlVSQEPVLFDGtiaeniry 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 106 GRTGRG--HLRCYAPAAGCS------PERLDRLLAETGlaeaadrpvSGYSTGMKQRLSLAAALLGDPELLILDEPSNGL 177
Cdd:cd03249 100 GKPDATdeEVEEAAKKANIHdfimslPDGYDTLVGERG---------SQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 178 DPEGMLWLRTFLRRfAASGRTVLLSSHLLSEMeQTVDDVLLMHHGKLLSSGPLDHLLTQGER 239
Cdd:cd03249 171 DAESEKLVQEALDR-AMKGRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-242 |
4.69e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 83.65 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 16 DNSPVIEVCGLRKKFRGRTA--VDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY--RELQTPT 91
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItdDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 92 QRIGVSLDG--GAFVGGRTGrghlrcYAPAAGCS---------PERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAA 160
Cdd:PRK13648 83 KHIGIVFQNpdNQFVGSIVK------YDVAFGLEnhavpydemHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 161 LLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLS-SHLLSE-MEQtvDDVLLMHHGKLLSSGPLDHLLTQGE 238
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDLSEaMEA--DHVIVMNKGTVYKEGTPTEIFDHAE 234
|
....
gi 2155196442 239 RLES 242
Cdd:PRK13648 235 ELTR 238
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
30-228 |
5.84e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.01 E-value: 5.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 30 FRGRTAVDgISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTA------LLWGHPYRELQTPTQRIGVSLDggaF 103
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivVSSTSKQKEIKPVRKKVGVVFQ---F 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 104 VGGRTGRGHLR---CYAPAA-GCSPERLDRLLAE----TGLA-EAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPS 174
Cdd:PRK13643 93 PESQLFEETVLkdvAFGPQNfGIPKEKAEKIAAEklemVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2155196442 175 NGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
20-229 |
9.04e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 84.08 E-value: 9.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGR----TAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEG---------TALlwghPYRE 86
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGrvlvdgqdlTAL----SEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 87 LQTPTQRIGVSLDGGAFVGGRTGRGH----LRcyapAAGCSPE----RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLA 158
Cdd:PRK11153 77 LRKARRQIGMIFQHFNLLSSRTVFDNvalpLE----LAGTPKAeikaRVTELLELVGLSDKADRYPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 159 AALLGDPELLILDEPSNGLDPE---GML-WLRTFLRRFaasGRTVLLSSHllsEME---QTVDDVLLMHHGKLLSSGP 229
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPAttrSILeLLKDINREL---GLTIVLITH---EMDvvkRICDRVAVIDAGRLVEQGT 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
38-237 |
1.08e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.16 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 38 GISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYREL-------------QTPTQRIGVSLDGGAFV 104
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYdhhylhrqvalvgQEPVLFSGSVRENIAYG 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 105 GGRTGRGHLRCYAPAAGCS------PERLDRLLAETGlaeaadrpvSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLD 178
Cdd:TIGR00958 579 LTDTPDEEIMAAAKAANAHdfimefPNGYDTEVGEKG---------SQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 179 PEGMlwlRTFLRRFAASGRTVLLSSHLLSEMEQtVDDVLLMHHGKLLSSGPLDHLLTQG 237
Cdd:TIGR00958 650 AECE---QLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-224 |
1.57e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.30 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 8 MERTTPVKDNSPVIEVCGLRkkfrGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYReL 87
Cdd:COG1129 244 LFPKRAAAPGEVVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-I 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 88 QTPTQRI--GVsldggAFV-GGRTGRG--------------HLRCYAPAAGCSPERLDRLLAEtgLAEA-------ADRP 143
Cdd:COG1129 319 RSPRDAIraGI-----AYVpEDRKGEGlvldlsirenitlaSLDRLSRGGLLDRRRERALAEE--YIKRlriktpsPEQP 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 144 VSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDP----EgmlwLRTFLRRFAASGRTVLLSShllSEMEQTV---DDV 216
Cdd:COG1129 392 VGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVgakaE----IYRLIRELAAEGKAVIVIS---SELPELLglsDRI 464
|
....*...
gi 2155196442 217 LLMHHGKL 224
Cdd:COG1129 465 LVMREGRI 472
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
26-234 |
1.77e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.48 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 26 LRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQrigvsldggafvg 105
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHAR------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 106 GRTGRGHLRCYAP---------------------AAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGD 164
Cdd:PRK10895 76 ARRGIGYLPQEASifrrlsvydnlmavlqirddlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 165 PELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLL 234
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-236 |
1.87e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.94 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSlDG 100
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVA-DK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 101 GAFVGGRTGRG----HLRCY-----------APAA--GCSP----ERLDRLLAETGLAEAA-DRPVSGYSTGMKQRLSLA 158
Cdd:PRK10619 85 NQLRLLRTRLTmvfqHFNLWshmtvlenvmeAPIQvlGLSKqearERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 159 AALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQ 236
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-240 |
2.04e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 81.29 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWG----HPYRELQTPTQRIG 95
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvnDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 V------------SLDGGAFvGGRTGRGHLRCYApaagcspERLDR-LLAETGLAEAADRPVSGYSTGMKQRLSLAAALL 162
Cdd:PRK09493 81 MvfqqfylfphltALENVMF-GPLRVRGASKEEA-------EKQAReLLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 163 GDPELLILDEPSNGLDPEgmlwLR----TFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQ-- 236
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPE----LRhevlKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNpp 228
|
....
gi 2155196442 237 GERL 240
Cdd:PRK09493 229 SQRL 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-242 |
2.27e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.09 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKF---RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRE---------- 86
Cdd:PRK13650 4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenvwdirhki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 87 ---LQTP-TQRIGVSL-DGGAFVGGRTGRGHLRCYapaagcspERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAAL 161
Cdd:PRK13650 84 gmvFQNPdNQFVGATVeDDVAFGLENKGIPHEEMK--------ERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 162 LGDPELLILDEPSNGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTvDDVLLMHHGKLLSSGPLDHLLTQGERL 240
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALS-DRVLVMKNGQVESTSTPRELFSRGNDL 234
|
..
gi 2155196442 241 ES 242
Cdd:PRK13650 235 LQ 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-236 |
3.19e-18 |
|
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: 83.58 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 16 DNSPVIEVCGLRKKFRGR-----------TAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIrPTEGTALLWGHP- 83
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKrglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDl 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 84 ----YRELQTPTQRIGV-------SLDGGAFVGGRTGRGhLRCYAPAAGcSPERLDR---LLAETGL-AEAADRPVSGYS 148
Cdd:COG4172 350 dglsRRALRPLRRRMQVvfqdpfgSLSPRMTVGQIIAEG-LRVHGPGLS-AAERRARvaeALEEVGLdPAARHRYPHEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 149 TGMKQRLSLAAALLGDPELLILDEPSNGLDpegmlwlRT-------FLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMH 220
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALD-------VSvqaqildLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMK 500
|
250
....*....|....*.
gi 2155196442 221 HGKLLSSGPLDHLLTQ 236
Cdd:COG4172 501 DGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
33-228 |
3.54e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.38 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 33 RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTE---------GTAL----LWGhpYRE-----LQTP-TQR 93
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnskitvdGITLtaktVWD--IREkvgivFQNPdNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 94 IGVSL-DGGAFvgGRTGRGHLRcyapaagcsPERL---DRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLI 169
Cdd:PRK13640 98 VGATVgDDVAF--GLENRAVPR---------PEMIkivRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 170 LDEPSNGLDPEGMLWLRTFLRRFAA-SGRTVLLSSHLLSEMEQTvDDVLLMHHGKLLSSG 228
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEANMA-DQVLVLDDGKLLAQG 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-236 |
4.26e-18 |
|
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: 82.93 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 3 EQQECMERTTPVKDNSPVIEVCGLRKKF----RGRT-AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTA 77
Cdd:TIGR03269 262 EGVSEVEKECEVEVGEPIIKVRNVSKRYisvdRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 78 -LLWGHPYRELQTP--------TQRIGVSLDGGAFVGGRTGRGHLrcyAPAAGCS-PERLDRLLA----------ETGLA 137
Cdd:TIGR03269 342 nVRVGDEWVDMTKPgpdgrgraKRYIGILHQEYDLYPHRTVLDNL---TEAIGLElPDELARMKAvitlkmvgfdEEKAE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 138 EAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWL-RTFLRRFAASGRTVLLSSHLLSEMEQTVDDV 216
Cdd:TIGR03269 419 EILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVtHSILKAREEMEQTFIIVSHDMDFVLDVCDRA 498
|
250 260
....*....|....*....|
gi 2155196442 217 LLMHHGKLLSSGPLDHLLTQ 236
Cdd:TIGR03269 499 ALMRDGKIVKIGDPEEIVEE 518
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
12-234 |
4.56e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.17 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 12 TPVKDNSPVIEVCGLRKKFRgRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRP---TEGTALLWGHPyRELQ 88
Cdd:TIGR00955 18 GSWKQLVSRLRGCFCRERPR-KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMP-IDAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 89 TPTQRIGVSLDGGAFVGGRTGRGHLRCYA----PAAGCSPERLDR---LLAETGLAEAAD------RPVSGYSTGMKQRL 155
Cdd:TIGR00955 96 EMRAISAYVQQDDLFIPTLTVREHLMFQAhlrmPRRVTKKEKRERvdeVLQALGLRKCANtrigvpGRVKGLSGGERKRL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 156 SLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHL-LSEMEQTVDDVLLMHHGKLLSSGPLDHLL 234
Cdd:TIGR00955 176 AFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
21-233 |
8.36e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 79.67 E-value: 8.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSLDG 100
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 101 GafVGGRTGRGHLRCY---------AP--AAGCSP----ERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDP 165
Cdd:COG4161 83 K--VGMVFQQYNLWPHltvmenlieAPckVLGLSKeqarEKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 166 ELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHL 233
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
38-224 |
9.94e-18 |
|
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: 79.44 E-value: 9.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 38 GISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSLDGGAFV-GGRTGRGHLrCY 116
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVlFARSLQDNI-AY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 117 ApAAGCSPERLDRL-----------LAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWL 185
Cdd:cd03248 111 G-LQSCSFECVKEAaqkahahsfisELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 2155196442 186 RTFLRRfAASGRTVLLSSHLLSEMEQTvDDVLLMHHGKL 224
Cdd:cd03248 190 QQALYD-WPERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-233 |
1.10e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 18 SPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqTPTQ--RIG 95
Cdd:PRK15439 9 PPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-TPAKahQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 VSL--DGGAFVGGRTGRGHLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEP 173
Cdd:PRK15439 88 IYLvpQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 174 SNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHL 233
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
18-178 |
1.53e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.03 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 18 SPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqTPTQR-IGV 96
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-PPYQRpINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 SLDGGAFVGGRTGRGHLrcyapAAGCSPERLDR---------LLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPEL 167
Cdd:PRK11607 96 MFQSYALFPHMTVEQNI-----AFGLKQDKLPKaeiasrvneMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170
....*....|.
gi 2155196442 168 LILDEPSNGLD 178
Cdd:PRK11607 171 LLLDEPMGALD 181
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-228 |
1.60e-17 |
|
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: 78.92 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFrGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSLDG 100
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 101 GAFVGGRT-------GRGHLRCYAPAAgcsPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEP 173
Cdd:cd03299 80 YALFPHMTvykniayGLKKRKVDKKEI---ERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 174 SNGLDPEGMLWLRTFLRRF-AASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03299 157 FSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-208 |
1.78e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.11 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 18 SPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHP-------------- 83
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfasttaalaagv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 84 ---YRELQT-PTQRIGVSLDGGAF--VGGRTGRGHLRcyapaagcspERLDRLLAETGLAEAADRPVSGYSTGMKQRLSL 157
Cdd:PRK11288 82 aiiYQELHLvPEMTVAENLYLGQLphKGGIVNRRLLN----------YEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2155196442 158 AAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSE 208
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEE 202
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
30-229 |
4.73e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 30 FRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTAllwghpyreLQTPTQRIG-----VSLDGG-AF 103
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGyvpqkLYLDTTlPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 104 VGGRTGRghLRCYAPAAGCSPErLDRLLAetglAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGML 183
Cdd:PRK09544 85 TVNRFLR--LRPGTKKEDILPA-LKRVQA----GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2155196442 184 WLRTF---LRRFAASGrtVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGP 229
Cdd:PRK09544 158 ALYDLidqLRRELDCA--VLMVSHDLHLVMAKTDEVLCLNHHICCSGTP 204
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
11-204 |
5.57e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.31 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 11 TTPVKDNSPVIEVC---GLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLI--RPTEGTALLWGHPYR 85
Cdd:COG2401 18 SSVLDLSERVAIVLeafGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 86 ELQTPTQRIGVSLDGGAFVggrtgrghlrcyapaagcsperldRLLAETGLAEAAD--RPVSGYSTGMKQRLSLAAALLG 163
Cdd:COG2401 98 REASLIDAIGRKGDFKDAV------------------------ELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2155196442 164 DPELLILDEPSNGLDPE----GMLWLRTFLRRFaasGRTVLLSSH 204
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQtakrVARNLQKLARRA---GITLVVATH 195
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-235 |
6.54e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.80 E-value: 6.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 25 GLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRI------GVSL 98
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiqMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 DG-GAFVGGRTGRG-------HLRCYAPAAgcSPERLDRLLAETGLA-EAADRPVSGYSTGMKQRLSLAAALLGDPELLI 169
Cdd:PRK10419 97 DSiSAVNPRKTVREiireplrHLLSLDKAE--RLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 170 LDEPSNGLD---PEGMLWLRTFLRRfaASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLT 235
Cdd:PRK10419 175 LDEAVSNLDlvlQAGVIRLLKKLQQ--QFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
30-242 |
7.42e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.86 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 30 FRGRtAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY------RELQTPTQRIGVS------ 97
Cdd:PRK13649 18 FEGR-ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsknKDIKQIRKKVGLVfqfpes 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 98 -------LDGGAFvggrtgrghlrcyAPAA-GCSPERLDRL----LAETGLAEAA-DRPVSGYSTGMKQRLSLAAALLGD 164
Cdd:PRK13649 97 qlfeetvLKDVAF-------------GPQNfGVSQEEAEALarekLALVGISESLfEKNPFELSGGQMRRVAIAGILAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 165 PELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQGERLES 242
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLEE 241
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-231 |
1.19e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 76.64 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 22 EVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGliRP----TEGTALLWGHPYRELqTPTQRI--G 95
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG--HPkyevTSGSILLDGEDILEL-SPDERAraG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 VSLdggAF-----VGG-------RTGRGHLRCYAPAAGCSPERLDRLLAETGLAEA-ADRPV-SGYSTGMKQRLSLAAAL 161
Cdd:COG0396 79 IFL---AFqypveIPGvsvsnflRTALNARRGEELSAREFLKLLKEKMKELGLDEDfLDRYVnEGFSGGEKKRNEILQML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 162 LGDPELLILDEPSNGLDpegmLW-LRT---FLRRFAASGRTVLLSSH---LLSEMEqtVDDVLLMHHGKLLSSGPLD 231
Cdd:COG0396 156 LLEPKLAILDETDSGLD----IDaLRIvaeGVNKLRSPDRGILIITHyqrILDYIK--PDFVHVLVDGRIVKSGGKE 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-235 |
2.21e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.10 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIR-----PTEGTALLWGH-----PYRELQT 89
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQdifkmDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 90 PTQRI--------GVSLDGGAFVGGRTGRghlrcYAPAAGCSPERLDRLLAETGL-AEAADR---PVSGYSTGMKQRLSL 157
Cdd:PRK14247 83 RVQMVfqipnpipNLSIFENVALGLKLNR-----LVKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 158 AAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASgRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLT 235
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
12-228 |
2.48e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.81 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 12 TPVKDNSpVIEVCGLRKKFRGRT-----AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTallwghpyre 86
Cdd:PRK13631 14 NPLSDDI-ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGT---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 87 LQTPTQRIGVSLDGGAFVGGRTGRG-----HLR-----------------------CYAPAA-GCSPERLDRL----LAE 133
Cdd:PRK13631 83 IQVGDIYIGDKKNNHELITNPYSKKiknfkELRrrvsmvfqfpeyqlfkdtiekdiMFGPVAlGVKKSEAKKLakfyLNK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 134 TGLAEA-ADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQT 212
Cdd:PRK13631 163 MGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEV 242
|
250
....*....|....*.
gi 2155196442 213 VDDVLLMHHGKLLSSG 228
Cdd:PRK13631 243 ADEVIVMDKGKILKTG 258
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-231 |
2.55e-16 |
|
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: 74.87 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGL--IRPTEGTALLWGHPYRELqTPTQR--IGV 96
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDL-PPEERarLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 SLdggAFVggrtgrghlrcyapaagcSPERLDRLLAETGLaeaadRPVS-GYSTGMKQRLSLAAALLGDPELLILDEPSN 175
Cdd:cd03217 80 FL---AFQ------------------YPPEIPGVKNADFL-----RYVNeGFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 176 GLDPEGMLWLRTFLRRFAASGRTVLLSSH---LLSEMEqtVDDVLLMHHGKLLSSGPLD 231
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVLIITHyqrLLDYIK--PDRVHVLYDGRIVKSGDKE 190
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
36-246 |
2.79e-16 |
|
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: 75.58 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 36 VDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGhpyRELQTPTQRIGVSLDGGAFVGGRTGRGHL-- 113
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG---KQITEPGPDRMVVFQNYSLLPWLTVRENIal 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 114 --RCYAPAAGCSPER--LDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFL 189
Cdd:TIGR01184 78 avDRVLPDLSKSERRaiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 190 RRFAASGR-TVLLSSHLLSEMEQTVDDVLLMhhgkllSSGPLDHLltqGERLESAFMR 246
Cdd:TIGR01184 158 MQIWEEHRvTVLMVTHDVDEALLLSDRVVML------TNGPAANI---GQILEVPFPR 206
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-204 |
4.29e-16 |
|
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: 77.28 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGT-------ALLWGHPYRELQTPTQ 92
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTieigetvKLAYVDQSRDALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 93 RIGVSLDGGA---FVGGRTGRGhlRCYAPAAGCSperldrllaetglaeAAD--RPVSGYSTGMKQRLSLAAALLGDPEL 167
Cdd:TIGR03719 402 TVWEEISGGLdiiKLGKREIPS--RAYVGRFNFK---------------GSDqqKKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170 180 190
....*....|....*....|....*....|....*..
gi 2155196442 168 LILDEPSNGLDPEGMLWLRTFLRRFAASgrtVLLSSH 204
Cdd:TIGR03719 465 LLLDEPTNDLDVETLRALEEALLNFAGC---AVVISH 498
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
11-204 |
4.73e-16 |
|
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: 77.13 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 11 TTPVKDNSPVIEVCGLRKKFrgrtavDGISFDVPAGR-----VTGFLGPNGAGKTTTLRMLLGLIRPTEGtallwghpyr 85
Cdd:COG1245 332 PRREKEEETLVEYPDLTKSY------GGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEG---------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 86 ELQT-------PtQRIGVSLDGgafvggrTGRGHLR-CYAPAAGCS--------PERLDRLLaetglaeaaDRPVSGYST 149
Cdd:COG1245 396 EVDEdlkisykP-QYISPDYDG-------TVEEFLRsANTDDFGSSyykteiikPLGLEKLL---------DKNVKDLSG 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 150 GMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAAS-GRTVLLSSH 204
Cdd:COG1245 459 GELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDH 514
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
33-242 |
5.77e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.47 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 33 RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWG--------------------HPYRELQTPTQ 92
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkkvglvFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 93 RIGVSLdggAFvggrtGRGHLrcyapaaGCSPE----RLDRLLAETGLA--EAADRPVSGYSTGMKQRLSLAAALLGDPE 166
Cdd:PRK13637 100 TIEKDI---AF-----GPINL-------GLSEEeienRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 167 LLILDEPSNGLDPEG---MLWLRTFLRRfaASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQGERLES 242
Cdd:PRK13637 165 ILILDEPTAGLDPKGrdeILNKIKELHK--EYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLES 241
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
35-229 |
6.86e-16 |
|
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: 74.07 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 35 AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRE--LQTPTQRIG-VSLDGGAFVGgrTGRG 111
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKigLHDLRSRISiIPQDPVLFSG--TIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 112 HLrcyAPAAGCSPERLDRLLAETGLAEAADRPVSG-----------YSTGMKQRLSLAAALLGDPELLILDEPSNGLDPE 180
Cdd:cd03244 97 NL---DPFGEYSDEELWQALERVGLKEFVESLPGGldtvveeggenLSVGQRQLLCLARALLRKSKILVLDEATASVDPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 181 GMLWLRTFLRRfAASGRTVLLSSHLLsemeQTVDD---VLLMHHGKLLSSGP 229
Cdd:cd03244 174 TDALIQKTIRE-AFKDCTVLTIAHRL----DTIIDsdrILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
36-225 |
9.50e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.87 E-value: 9.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 36 VDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHpYRELQTPTQ-----RIGVSLdggAFvggRTGR 110
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGY-HITPETGNKnlkklRKKVSL---VF---QFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 111 GHL-------------RCYAPAAGCSPERLDRLLAETGLAEA-ADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNG 176
Cdd:PRK13641 96 AQLfentvlkdvefgpKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2155196442 177 LDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLL 225
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
32-237 |
9.57e-16 |
|
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: 76.32 E-value: 9.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYREL-------------QTPTQRIGVSL 98
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIdrhtlrqfinylpQEPYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 DGgAFVGGRtgrghlrcyapaAGCSPERLDRL--LAE-------------TGLAEAAdrpvSGYSTGMKQRLSLAAALLG 163
Cdd:TIGR01193 566 EN-LLLGAK------------ENVSQDEIWAAceIAEikddienmplgyqTELSEEG----SSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 164 DPELLILDEPSNGLDpegMLWLRTFLRRFA-ASGRTVLLSSHLLSEMEQTvDDVLLMHHGKLLSSGPLDHLLTQG 237
Cdd:TIGR01193 629 DSKVLILDESTSNLD---TITEKKIVNNLLnLQDKTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLDRN 699
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-250 |
1.53e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 17 NSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPyRELQTP--TQRI 94
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE-VTFNGPksSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 95 GVSLD------------------GGAFVgGRTGR-GHLRCYAPAagcsperlDRLLAETGLAEAADRPVSGYSTGMKQRL 155
Cdd:PRK10762 80 GIGIIhqelnlipqltiaeniflGREFV-NRFGRiDWKKMYAEA--------DKLLARLNLRFSSDKLVGELSIGEQQMV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 156 SLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHL-- 233
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLte 230
|
250 260
....*....|....*....|..
gi 2155196442 234 -----LTQGERLESAFMRLTQA 250
Cdd:PRK10762 231 dslieMMVGRKLEDQYPRLDKA 252
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-233 |
1.73e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 17 NSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGL---------------------IRPTE- 74
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyegeiifegeelqasnIRDTEr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 75 -GTALLwghpYRELQTPTQrigVSLDGGAFVGGRTGRGHLRCYAPAAgcspERLDRLLAETGLAEAADRPVSGYSTGMKQ 153
Cdd:PRK13549 82 aGIAII----HQELALVKE---LSVLENIFLGNEITPGGIMDYDAMY----LRAQKLLAQLKLDINPATPVGNLGLGQQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 154 RLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHL 233
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-232 |
1.90e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.51 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSLdg 100
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIREL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 101 gafvggRTGRG----------HLRCY-----AP--AAGCSPE----RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAA 159
Cdd:PRK11124 81 ------RRNVGmvfqqynlwpHLTVQqnlieAPcrVLGLSKDqalaRAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 160 ALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDH 232
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-233 |
2.13e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 73.65 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH-----PYRELQTPTQRI 94
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 95 GVSLDGGAFVGGRTG--------RGHLRCyapaagcsPERLDRL-----LAETGLAEAADRPVSGYSTGMKQRLSLAAAL 161
Cdd:PRK11831 87 SMLFQSGALFTDMNVfdnvayplREHTQL--------PAPLLHStvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 162 LGDPELLILDEPSNGLDPEGMLWLRTFLRRF-AASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHL 233
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-236 |
2.57e-15 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 74.72 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 16 DNSPVIEVCGLRKKFRG----RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGL-----IRPT-----EGTALLwG 81
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpaAHPSgsilfDGQDLL-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 82 HPYRELQT------------------PTQRIG------VSLDGGafVGGRTGRghlrcyapaagcspERLDRLLAETGLA 137
Cdd:COG4172 81 LSERELRRirgnriamifqepmtslnPLHTIGkqiaevLRLHRG--LSGAAAR--------------ARALELLERVGIP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 138 EAAdRPVSGY----STGMKQRLSLAAALLGDPELLILDEPSNGLDP----EGMLWLRTFLRRFaasGRTVLLSSHLLSEM 209
Cdd:COG4172 145 DPE-RRLDAYphqlSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqaQILDLLKDLQREL---GMALLLITHDLGVV 220
|
250 260
....*....|....*....|....*..
gi 2155196442 210 EQTVDDVLLMHHGKLLSSGPLDHLLTQ 236
Cdd:COG4172 221 RRFADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
43-228 |
2.91e-15 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 72.14 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 43 VPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqtPTQRIGVSL---DGGAF--------VG-GRTGR 110
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA--PPADRPVSMlfqENNLFahltveqnVGlGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 111 GHLRcyapaaGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDP---EGMLWLRT 187
Cdd:cd03298 99 LKLT------AEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPalrAEMLDLVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2155196442 188 FLRRfaASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03298 173 DLHA--ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-204 |
2.96e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.84 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 9 ERTTPVKDNSPV-IEVCGLRKKFrgrtavDGISFDVPAG-----RVTGFLGPNGAGKTTTLRMLLGLIRPTEGTallwgh 82
Cdd:PRK13409 328 ERPPRDESERETlVEYPDLTKKL------GDFSLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE------ 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 83 PYRELQT---PtQRIGVSLDGgafvggrTGRGHLRCYAPAAGCS--------PERLDRLLaetglaeaaDRPVSGYSTGM 151
Cdd:PRK13409 396 VDPELKIsykP-QYIKPDYDG-------TVEDLLRSITDDLGSSyykseiikPLQLERLL---------DKNVKDLSGGE 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2155196442 152 KQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAA-SGRTVLLSSH 204
Cdd:PRK13409 459 LQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEeREATALVVDH 512
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
31-243 |
3.36e-15 |
|
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: 74.48 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPT-EGTALLWGHPYrELQTPTQRI--------------G 95
Cdd:TIGR02633 271 PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPV-DIRNPAQAIragiamvpedrkrhG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 VSLDGGafVGGRTGRGHLRCY--------APAAGCSPERLDRLLAETGlaeAADRPVSGYSTGMKQRLSLAAALLGDPEL 167
Cdd:TIGR02633 350 IVPILG--VGKNITLSVLKSFcfkmridaAAELQIIGSAIQRLKVKTA---SPFLPIGRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 168 LILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSgPLDHLLTQGERLESA 243
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD-FVNHALTQEQVLAAA 499
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
17-178 |
5.34e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.44 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 17 NSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHpyRELQTPTQRIGV 96
Cdd:PRK09452 11 LSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ--DITHVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 S--------------LDGGAFvggrtgrgHLRCY-APAAGCSPeRLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAAL 161
Cdd:PRK09452 89 NtvfqsyalfphmtvFENVAF--------GLRMQkTPAAEITP-RVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170
....*....|....*..
gi 2155196442 162 LGDPELLILDEPSNGLD 178
Cdd:PRK09452 160 VNKPKVLLLDESLSALD 176
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
32-241 |
5.79e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.51 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHP--------------YRELQTPtQRIGVS 97
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarkvaYLPQQLP-AAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 98 LDGGAFVGGRTGRGHLRCYAPAagcSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGL 177
Cdd:PRK10575 102 VRELVAIGRYPWHGALGRFGAA---DREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 178 DPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLtQGERLE 241
Cdd:PRK10575 179 DIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM-RGETLE 242
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
42-230 |
7.05e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.98 E-value: 7.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 42 DVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH----PYRELQTPTQ--RIG-VSLDGGAFVGGRTgRGHLR 114
Cdd:PRK11144 20 TLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdAEKGICLPPEkrRIGyVFQDARLFPHYKV-RGNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 115 cYapaaGCS---PERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRR 191
Cdd:PRK11144 99 -Y----GMAksmVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2155196442 192 FAASGRT-VLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPL 230
Cdd:PRK11144 174 LAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
35-236 |
7.09e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 73.77 E-value: 7.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 35 AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGhpyrelQTPTQRIGVSLDGGAfvggrTGRGHLR 114
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGLNGQL-----TGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 115 CYAPAAGCSPERLDRLLAEtgLAEAAD------RPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDpegmlwlRTF 188
Cdd:PRK13545 108 LKGLMMGLTKEKIKEIIPE--IIEFADigkfiyQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD-------QTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 189 LRR-------FAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQ 236
Cdd:PRK13545 179 TKKcldkmneFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
23-228 |
8.45e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.38 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 23 VCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIG-VSLDGG 101
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGfVTQDDI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 102 AFvggrtgrGHLRCYAPAAGCSPERL-------------DRLLAETGLAEAADRPVS-----GYSTGMKQRLSLAAALLG 163
Cdd:PLN03211 151 LY-------PHLTVRETLVFCSLLRLpksltkqekilvaESVISELGLTKCENTIIGnsfirGISGGERKRVSIAHEMLI 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 164 DPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHL-LSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-204 |
1.13e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.36 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY-RELQTPTQRIgvsl 98
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 dggAFVGGRTGRG---HLR--CYAPAAGCSPE-RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDE 172
Cdd:PRK13540 77 ---CFVGHRSGINpylTLRenCLYDIHFSPGAvGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 2155196442 173 PSNGLDPEGMLWLRTFLRRFAASGRTVLLSSH 204
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
46-193 |
1.22e-14 |
|
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: 71.29 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 46 GRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLwghPYRELQTPTQRIGVSLDGG--AFVGGRTGRGHLRCYAPAAGCS 123
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---ELDTVSYKPQYIKADYEGTvrDLLSSITKDFYTHPYFKTEIAK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 124 PERLDRLLaetglaeaaDRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFA 193
Cdd:cd03237 102 PLQIEQIL---------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
16-234 |
1.25e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.50 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 16 DNSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTAL--LWGHPYREL------ 87
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrMRDGQLRDLyalsea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 88 --------------QTPTQ--RIGVSldGGAFVGGR---TGR---GHLRCYApaagcsPERLDRLlaETGLAEAADRPvS 145
Cdd:PRK11701 82 errrllrtewgfvhQHPRDglRMQVS--AGGNIGERlmaVGArhyGDIRATA------GDWLERV--EIDAARIDDLP-T 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 146 GYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250
....*....|
gi 2155196442 225 LSSGPLDHLL 234
Cdd:PRK11701 231 VESGLTDQVL 240
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
30-242 |
1.75e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.20 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 30 FRGRTAVDgISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLW------GHPYRELQTPTQRIG-------- 95
Cdd:PRK13634 18 FERRALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitaGKKNKKLKPLRKKVGivfqfpeh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 ------VSLDggafvggrtgrghlRCYAPAA-GCSPE----RLDRLLAETGLAEAA-DRPVSGYSTGMKQRLSLAAALLG 163
Cdd:PRK13634 97 qlfeetVEKD--------------ICFGPMNfGVSEEdakqKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 164 DPELLILDEPSNGLDPEGML-WLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQGERLES 242
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKeMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEA 242
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-178 |
2.24e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.13 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 15 KDNSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRI 94
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 95 GVSLDGGAFV-GGRTGRGHL------RCYAPaagcSPERLDRLLAETGLAEAA-DRPVSGYSTGMKQRLSLAAALLGDPE 166
Cdd:PRK10247 82 QVSYCAQTPTlFGDTVYDNLifpwqiRNQQP----DPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170
....*....|..
gi 2155196442 167 LLILDEPSNGLD 178
Cdd:PRK10247 158 VLLLDEITSALD 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-233 |
2.46e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.16 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGlIRPT---EGTALLWGHPYRELQ-TPTQRIG 95
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNiRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 V-------------SLDGGAFVGGR-TGRGHLRCYAPAAgcspERLDRLLAETGLAEAAD-RPVSGYSTGMKQRLSLAAA 160
Cdd:TIGR02633 80 IviihqeltlvpelSVAENIFLGNEiTLPGGRMAYNAMY----LRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 161 LLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHL 233
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
33-222 |
3.02e-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: 69.19 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 33 RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRML-----LGLIrptEGTALLWGHPYRElqTPTQRIGVSLDGGAFVGGR 107
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVI---TGEILINGRPLDK--NFQRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 108 TGRGHLRCYAPAAGCSPERldrllaetglaeaadrpvsgystgmKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRT 187
Cdd:cd03232 95 TVREALRFSALLRGLSVEQ-------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 2155196442 188 FLRRFAASGRTVLLSSHLLSE--MEQtVDDVLLMHHG 222
Cdd:cd03232 150 FLKKLADSGQAILCTIHQPSAsiFEK-FDRLLLLKRG 185
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
32-224 |
3.35e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.52 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY-----RELQTPTQRIGVSLDGGAFVGG 106
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlknREVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 107 RTGRGHLRCYAPAAGCSPE----RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLD---P 179
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDdirrRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2155196442 180 EGMLWLrtfLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:PRK10908 174 EGILRL---FEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
20-255 |
4.09e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLI---RPTEGTALLWGHPyrelqtpTQRIGv 96
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRT-------VQREG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 SLDGGAfvggRTGRGHLRC-----------------YAPAAGCSP--------------ERLDRLLAETGLAEAADRPVS 145
Cdd:PRK09984 76 RLARDI----RKSRANTGYifqqfnlvnrlsvlenvLIGALGSTPfwrtcfswftreqkQRALQALTRVGMVHFAHQRVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 146 GYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
250 260 270
....*....|....*....|....*....|.
gi 2155196442 225 LSSGPLDHLltQGERLESAFMRLTQAGEGTQ 255
Cdd:PRK09984 232 FYDGSSQQF--DNERFDHLYRSINRVEENAK 260
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
20-76 |
4.74e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.30 E-value: 4.74e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGT 76
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT 380
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-224 |
4.92e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 19 PVIEVCGLRkkfrGRTAVDgISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPT------- 91
Cdd:PRK15439 267 PVLTVEDLT----GEGFRN-ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlarglv 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 92 ------QRIGVSLDG------GAFVGGRTGRgHLRCYAPAAgcspeRLDRLLAETGLA-EAADRPVSGYSTGMKQRLSLA 158
Cdd:PRK15439 342 ylpedrQSSGLYLDAplawnvCALTHNRRGF-WIKPARENA-----VLERYRRALNIKfNHAEQAARTLSGGNQQKVLIA 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 159 AALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:PRK15439 416 KCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-228 |
5.11e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.82 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRT---------AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHP------- 83
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlhfgdys 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 84 YRELQ------------TPTQRIGVSLDGGafvggrtgrghLRCYAPAAGCSPE-RLDRLLAETGL-AEAADRPVSGYST 149
Cdd:PRK15112 84 YRSQRirmifqdpstslNPRQRISQILDFP-----------LRLNTDLEPEQREkQIIETLRQVGLlPDHASYYPHMLAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 150 GMKQRLSLAAALLGDPELLILDEPSNGLDpegmLWLRT-----FLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLD----MSMRSqlinlMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
....
gi 2155196442 225 LSSG 228
Cdd:PRK15112 229 VERG 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-228 |
5.55e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.11 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRT-----AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTaLLWGHPYRELQTPTQRIG 95
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGT-IEWIFKDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 VSLDggAFVGGRTGRGHLR-----------------------------CYAPAA-GCSPERLDRLLAE----TGLAEA-A 140
Cdd:PRK13651 82 KVLE--KLVIQKTRFKKIKkikeirrrvgvvfqfaeyqlfeqtiekdiIFGPVSmGVSKEEAKKRAAKyielVGLDESyL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 141 DRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMH 220
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
....*...
gi 2155196442 221 HGKLLSSG 228
Cdd:PRK13651 240 DGKIIKDG 247
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
33-236 |
5.62e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.90 E-value: 5.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 33 RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSLDGGA-FVGGRTGRG 111
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTpFLFSDTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 112 HLRCYAPAAgcSPERLDRLLAETGLAEAADRPVSGYST-----------GMKQRLSLAAALLGDPELLILDEPSNGLDPE 180
Cdd:PRK10789 408 NIALGRPDA--TQQEIEHVARLASVHDDILRLPQGYDTevgergvmlsgGQKQRISIARALLLNAEILILDDALSAVDGR 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 181 GMLWLRTFLRRFAAsGRTVLLSSHLLSEMEQTvDDVLLMHHGKLLSSGPLDHLLTQ 236
Cdd:PRK10789 486 TEHQILHNLRQWGE-GRTVIISAHRLSALTEA-SEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
36-233 |
6.10e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.34 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 36 VDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGL----IRPTEGTALLWGHPYRELQTPTQRIGVSLDG--GAFVGGRTG 109
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 110 RGHLR--CYAPAAGCSPERLDRLLAETGLAEAAdRPVSGY----STGMKQRLSLAAALLGDPELLILDEPSNGLDPEGML 183
Cdd:PRK10418 99 HTHARetCLALGKPADDATLTAALEAVGLENAA-RVLKLYpfemSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2155196442 184 WLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHL 233
Cdd:PRK10418 178 RILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-244 |
7.33e-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: 71.09 E-value: 7.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFR--GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRpTEGTALLWGHPYRE--LQTPTQRIGV 96
Cdd:TIGR01271 1218 MDVQGLTAKYTeaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSvtLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 sLDGGAFVGGRTGRGHLRcyaPAAGCSPERLDRLLAETGLAEAADR---------PVSGY--STGMKQRLSLAAALLGDP 165
Cdd:TIGR01271 1297 -IPQKVFIFSGTFRKNLD---PYEQWSDEEIWKVAEEVGLKSVIEQfpdkldfvlVDGGYvlSNGHKQLMCLARSILSKA 1372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 166 ELLILDEPSNGLDPEGMLWLRTFLRRfAASGRTVLLSSHLLSEMEQtVDDVLLMHHGKLLSSGPLDHLLTQGERLESAF 244
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-219 |
7.41e-14 |
|
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: 68.61 E-value: 7.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 18 SPVIEVCGLRKKFR-----GRT--AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGtALLWGHPYR--ELQ 88
Cdd:COG4778 2 TTLLEVENLSKTFTlhlqgGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSG-SILVRHDGGwvDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 89 TPTQR---------IG-VSldggafvggrtgrGHLRC----------YAP--AAGCSPE----RLDRLLAETGLAEA-AD 141
Cdd:COG4778 81 QASPReilalrrrtIGyVS-------------QFLRViprvsaldvvAEPllERGVDREearaRARELLARLNLPERlWD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 142 RPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLM 219
Cdd:COG4778 148 LPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-231 |
7.76e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.44 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 9 ERTTPVKDNSPVIEVCGLR-KKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYREL 87
Cdd:COG3845 246 VEKAPAEPGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 88 qTPTQRI--GVsldggAFV-GGRTGRG----------------HLRCYAPAAGCSPERLDRLLAEtgLAEA-------AD 141
Cdd:COG3845 326 -SPRERRrlGV-----AYIpEDRLGRGlvpdmsvaenlilgryRRPPFSRGGFLDRKAIRAFAEE--LIEEfdvrtpgPD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 142 RPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHH 221
Cdd:COG3845 398 TPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYE 477
|
250
....*....|
gi 2155196442 222 GKLlsSGPLD 231
Cdd:COG3845 478 GRI--VGEVP 485
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-204 |
9.17e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.34 E-value: 9.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDG-ISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTpTQRIGVSLDGGAFVGGRTG 109
Cdd:PRK13543 21 RNEEPVFGpLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR-SRFMAYLGHLPGLKADLST 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 110 RGHLRCYAPAAGCSPERL-DRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTF 188
Cdd:PRK13543 100 LENLHFLCGLHGRRAKQMpGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
|
170
....*....|....*.
gi 2155196442 189 LRRFAASGRTVLLSSH 204
Cdd:PRK13543 180 ISAHLRGGGAALVTTH 195
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
33-237 |
1.36e-13 |
|
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: 69.85 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 33 RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELqtpTQR-----IGVsldggafVG-- 105
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV---TQAslraaIGI-------VPqd 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 106 --------------GRTG--RGHLRCYAPAAGCS------PERLDRLLAETGLAeaadrpVSGystGMKQRLSLAAALLG 163
Cdd:COG5265 441 tvlfndtiayniayGRPDasEEEVEAAARAAQIHdfieslPDGYDTRVGERGLK------LSG---GEKQRVAIARTLLK 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 164 DPELLILDEPSNGLDPEGMLWLRTFLRRfAASGRTVLLSSHLLSemeqTV---DDVLLMHHGKLLSSGPLDHLLTQG 237
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALRE-VARGRTTLVIAHRLS----TIvdaDEILVLEAGRIVERGTHAELLAQG 583
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
15-240 |
1.97e-13 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 67.90 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 15 KDNSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPT--- 91
Cdd:COG4598 3 DTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgel 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 92 --------QRIGVSLdGGAF---------------------VGGRtgrghlrcyaPAAGCSpERLDRLLAETGLAEAADR 142
Cdd:COG4598 83 vpadrrqlQRIRTRL-GMVFqsfnlwshmtvlenvieapvhVLGR----------PKAEAI-ERAEALLAKVGLADKRDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 143 PVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPE--GMLwLRTfLRRFAASGRTVLLSSHllsEME---QTVDDVL 217
Cdd:COG4598 151 YPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPElvGEV-LKV-MRDLAEEGRTMLVVTH---EMGfarDVSSHVV 225
|
250 260
....*....|....*....|....*
gi 2155196442 218 LMHHGKLLSSGPLDHLLT--QGERL 240
Cdd:COG4598 226 FLHQGRIEEQGPPAEVFGnpKSERL 250
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
35-228 |
2.09e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.50 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 35 AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPY-------RELQTPTQRIGVSLD-------- 99
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkiKEVKRLRKEIGLVFQfpeyqlfq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 100 -----GGAFVGGRTGRGHLRCYAPAagcsPERLDRLLAETGLAEAADRPVSGystGMKQRLSLAAALLGDPELLILDEPS 174
Cdd:PRK13645 106 etiekDIAFGPVNLGENKQEAYKKV----PELLKLVQLPEDYVKRSPFELSG---GQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 175 NGLDPEGML-WLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:PRK13645 179 GGLDPKGEEdFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
33-228 |
3.28e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.81 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 33 RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTAL-----------LWGHPYRE---LQTPTQRIGVSL 98
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYvdgldtsdeenLWDIRNKAgmvFQNPDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 --DGGAFvggrtGRGHLrcyapaaGCSPE----RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDE 172
Cdd:PRK13633 103 veEDVAF-----GPENL-------GIPPEeireRVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 173 PSNGLDPEGML-WLRTFLRRFAASGRTVLLSSHLLSEMEQTvDDVLLMHHGKLLSSG 228
Cdd:PRK13633 171 PTAMLDPSGRReVVNTIKELNKKYGITIILITHYMEEAVEA-DRIIVMDSGKVVMEG 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
31-217 |
4.54e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 68.27 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RG-RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGT-------ALLW-------------------GHP 83
Cdd:PRK10636 11 RGvRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSytfpgnwQLAWvnqetpalpqpaleyvidgDRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 84 YRELQTPTQRIGVSLDGGAFVggrTGRGHLRcyAPAAGCSPERLDRLLAETGLA-EAADRPVSGYSTGMKQRLSLAAALL 162
Cdd:PRK10636 91 YRQLEAQLHDANERNDGHAIA---TIHGKLD--AIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 163 GDPELLILDEPSNGLDPEGMLWLRTFLRRFAAsgrTVLLSSHLLSEMEQTVDDVL 217
Cdd:PRK10636 166 CRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKII 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-204 |
4.85e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 68.04 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 25 GLRKKF-RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLwghpyrelqTPTQRIGV-----SL 98
Cdd:TIGR03719 9 RVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP---------QPGIKVGYlpqepQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 DGGAFVGGRT--GRGHLR--------CYApAAGCSPERLDRLLAETG-----------------LAEAA--------DRP 143
Cdd:TIGR03719 80 DPTKTVRENVeeGVAEIKdaldrfneISA-KYAEPDADFDKLAAEQAelqeiidaadawdldsqLEIAMdalrcppwDAD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2155196442 144 VSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAAsgrTVLLSSH 204
Cdd:TIGR03719 159 VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTH 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-235 |
9.72e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.42 E-value: 9.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 16 DNSPVIEVCGLRKKFRGR-----------TAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRpTEGTALLWGHPY 84
Cdd:PRK15134 271 PASPLLDVEQLQVAFPIRkgilkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 85 ------------RELQTPTQRIGVSLDGGAFVGGRTGRGhLRCYAPA--AGCSPERLDRLLAETGL-AEAADRPVSGYST 149
Cdd:PRK15134 350 hnlnrrqllpvrHRIQVVFQDPNSSLNPRLNVLQIIEEG-LRVHQPTlsAAQREQQVIAVMEEVGLdPETRHRYPAEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 150 GMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGR-TVLLSSHLLSEMEQTVDDVLLMHHGKLLSSG 228
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
....*..
gi 2155196442 229 PLDHLLT 235
Cdd:PRK15134 509 DCERVFA 515
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
35-250 |
1.10e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.99 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 35 AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHpyrelqtptqrIGVSLDGGAFVGGRTGRGHLR 114
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 115 CYAPAAGCSPERLDRLLAE----TGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDpegmlwlRTFLR 190
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKiiefSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD-------QTFAQ 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 191 R-------FAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQGERLESAFMRLTQA 250
Cdd:PRK13546 181 KcldkiyeFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKSKA 247
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-236 |
1.24e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 65.83 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 11 TTPVKDNSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTL----RM--LLGLIRpTEGTALLWGHP- 83
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMndLIPGAR-VEGEILLDGEDi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 84 YRELQTPTQ---RIG----------------VSLdgGAFVGGRTGRGHLRcyapaagcspERLDRLLAETGL-AEAADR- 142
Cdd:COG1117 81 YDPDVDVVElrrRVGmvfqkpnpfpksiydnVAY--GLRLHGIKSKSELD----------EIVEESLRKAALwDEVKDRl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 143 --PVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDP-------EGMLWLRtflRRFaasgrTVLLSSHLlseMEQTV 213
Cdd:COG1117 149 kkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPistakieELILELK---KDY-----TIVIVTHN---MQQAA 217
|
250 260
....*....|....*....|....*.
gi 2155196442 214 ---DDVLLMHHGKLLSSGPLDHLLTQ 236
Cdd:COG1117 218 rvsDYTAFFYLGELVEFGPTEQIFTN 243
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
46-204 |
1.33e-12 |
|
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: 67.12 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 46 GRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTallWGHP---------YR--ELQTPTQRIgvsLDGGA------------ 102
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGD---YDEEpswdevlkrFRgtELQDYFKKL---ANGEIkvahkpqyvdli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 103 --FVGGRTG--------RGhlrcyapaagcspeRLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDE 172
Cdd:COG1245 173 pkVFKGTVRellekvdeRG--------------KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|..
gi 2155196442 173 PSNGLDPEGMLWLRTFLRRFAASGRTVLLSSH 204
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-240 |
1.57e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.88 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVD---GISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH--PYRELQTPTQRI 94
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNqlnGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEllTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 95 GVSLDG--GAFVGGrTGRGHLRCYAPAAGCSPE----RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELL 168
Cdd:PRK13642 84 GMVFQNpdNQFVGA-TVEDDVAFGMENQGIPREemikRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 169 ILDEPSNGLDPEGMLWLRTFLRRFAASGR-TVLLSSHLLSEMEQTvDDVLLMHHGKLLSSGPLDHLLTQGERL 240
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASS-DRILVMKAGEIIKEAAPSELFATSEDM 234
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-204 |
1.89e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEG-----TAL--LWGHPYRELQTPTQRIGVSLDGG--- 101
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGrihcgTKLevAYFDQHRAELDPEKTVMDNLAEGkqe 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 102 AFVGGRTgRgHLRCYAPAAGCSPERldrllaetglaeaADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEG 181
Cdd:PRK11147 411 VMVNGRP-R-HVLGYLQDFLFHPKR-------------AMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
|
170 180
....*....|....*....|...
gi 2155196442 182 MLWLRTFLRRFAAsgrTVLLSSH 204
Cdd:PRK11147 476 LELLEELLDSYQG---TVLLVSH 495
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-229 |
2.11e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.76 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 16 DNSPVIEVCGLRKKF---RG-----RT--AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH--- 82
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkRGlfkpeRLvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 83 --------------------PYRELQtPTQRIGVSLDGGAFVGGRTGRGHLRcyapaagcspERLDRLLAETGL-AEAAD 141
Cdd:PRK11308 81 kadpeaqkllrqkiqivfqnPYGSLN-PRKKVGQILEEPLLINTSLSAAERR----------EKALAMMAKVGLrPEHYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 142 RPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLD---PEGMLWLRTFLRRfaASGRTVLLSSHLLSEMEQTVDDVLL 218
Cdd:PRK11308 150 RYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDvsvQAQVLNLMMDLQQ--ELGLSYVFISHDLSVVEHIADEVMV 227
|
250
....*....|.
gi 2155196442 219 MHHGKLLSSGP 229
Cdd:PRK11308 228 MYLGRCVEKGT 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-228 |
2.79e-12 |
|
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: 65.98 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGL--IRPTEGTAL-------------------- 78
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 79 ---------------LWGHPYRELQTPTQRIGVSLDGG-AFVGGRTGRGHLRCYAPAAGCS-PERLDR---LLAETGLAE 138
Cdd:TIGR03269 81 pcpvcggtlepeevdFWNLSDKLRRRIRKRIAIMLQRTfALYGDDTVLDNVLEALEEIGYEgKEAVGRavdLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 139 AADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFA-ASGRTVLLSSHLLSEMEQTVDDVL 217
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|.
gi 2155196442 218 LMHHGKLLSSG 228
Cdd:TIGR03269 241 WLENGEIKEEG 251
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
35-234 |
3.51e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.44 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 35 AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYREL------QTPTQRIGVSLDGGAF----- 103
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelrEVRRKKIAMVFQSFALmphmt 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 104 VGGRTGRGHLRCYAPAAGCSPERLDRLlAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGML 183
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDAL-RQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 184 WLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLL 234
Cdd:PRK10070 202 EMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-222 |
4.26e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.90 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 33 RTAVDGISFDVPAGRVTGFLGPNGAGKTTTL-----RMLLGLIrpTEGTALLWGHPyreLQTPTQR-IGVSLDGGAFVGG 106
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVI--TGGDRLVNGRP---LDSSFQRsIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 107 RTGRGHLRCYA----PAAGCSPERLD------RLLAETGLAEA-ADRPVSGYSTGMKQRLSLAAALLGDPELLI-LDEPS 174
Cdd:TIGR00956 851 STVRESLRFSAylrqPKSVSKSEKMEyveeviKLLEMESYADAvVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPT 930
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2155196442 175 NGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSE--MEQtVDDVLLMHHG 222
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAilFEE-FDRLLLLQKG 979
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-178 |
5.82e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 46 GRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTalLWGHP--------YR--ELQTPTQRIgvsLDGGA------------- 102
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEPswdevlkrFRgtELQNYFKKL---YNGEIkvvhkpqyvdlip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 103 -FVGGRTG--------RGhlrcyapaagcspeRLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEP 173
Cdd:PRK13409 174 kVFKGKVRellkkvdeRG--------------KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
....*
gi 2155196442 174 SNGLD 178
Cdd:PRK13409 240 TSYLD 244
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
33-235 |
6.33e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 6.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 33 RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTP--TQRIGV-----SLDGGAFVG 105
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKevARRIGLlaqnaTTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 106 GRTGRG---HLRCYAPAAGCSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPE-- 180
Cdd:PRK10253 100 ELVARGrypHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIShq 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 181 -GMLWLRTFLRRfaASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLT 235
Cdd:PRK10253 180 iDLLELLSELNR--EKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
17-252 |
7.56e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.74 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 17 NSPVIEVCGLRKKFR-GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIG 95
Cdd:PRK10790 337 QSGRIDIDNVSFAYRdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 VS--------LDGGAFVGGRTGRghlrcyapaaGCSPERLDRLLAETGLAEAADRPVSG-----------YSTGMKQRLS 156
Cdd:PRK10790 417 VAmvqqdpvvLADTFLANVTLGR----------DISEEQVWQALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 157 LAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRrfAASGRTVLLS-SHLLSEMEQTvDDVLLMHHGKLLSSGPLDHLLT 235
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALA--AVREHTTLVViAHRLSTIVEA-DTILVLHRGQAVEQGTHQQLLA 563
|
250
....*....|....*..
gi 2155196442 236 QGERLESAFmRLTQAGE 252
Cdd:PRK10790 564 AQGRYWQMY-QLQLAGE 579
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
38-223 |
8.95e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 62.49 E-value: 8.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 38 GISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH-------PYreLQTPTQR--I--GVSLDggafvgg 106
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiayvsqePW--IQNGTIRenIlfGKPFD------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 107 rtgrghlrcyapaagcsPERLDR------------LLAETGLAEAADRPVSgYSTGMKQRLSLAAALLGDPELLILDEPS 174
Cdd:cd03250 94 -----------------EERYEKvikacalepdleILPDGDLTEIGEKGIN-LSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 175 NGLDPEGMLWLrtF---LRRFAASGRTVLLSSHLLSEMEQtVDDVLLMHHGK 223
Cdd:cd03250 156 SAVDAHVGRHI--FencILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-226 |
1.14e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.11 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLR-MLLGLIR--PT----------------------------------E 74
Cdd:PLN03073 189 GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRyMAMHAIDgiPKncqilhveqevvgddttalqcvlntdiertqlleE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 75 GTALLWGHPYRELQTPTQRIGVSLDGGA---FVGGRTGRGHLRCYAPAAGCSPERLDRLLAetGLAEAAD---RPVSGYS 148
Cdd:PLN03073 269 EAQLVAQQRELEFETETGKGKGANKDGVdkdAVSQRLEEIYKRLELIDAYTAEARAASILA--GLSFTPEmqvKATKTFS 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 149 TGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAasgRTVLLSSHLLSEMEQTVDDVLLMHHGKLLS 226
Cdd:PLN03073 347 GGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSHAREFLNTVVTDILHLHGQKLVT 421
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
50-204 |
1.19e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 50 GFLGPNGAGKTTTLRMLLGLIRPTEGTALLwghpyrelqTPTQRIGV-----SLDGGAFVGG--RTGRGHLR-------- 114
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARP---------APGIKVGYlpqepQLDPEKTVREnvEEGVAEVKaaldrfne 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 115 CYApAAGCSPERLDRLLAETG-----------------LAEAAD--R------PVSGYSTGMKQRLSLAAALLGDPELLI 169
Cdd:PRK11819 108 IYA-AYAEPDADFDALAAEQGelqeiidaadawdldsqLEIAMDalRcppwdaKVTKLSGGERRRVALCRLLLEKPDMLL 186
|
170 180 190
....*....|....*....|....*....|....*
gi 2155196442 170 LDEPSNGLDPEGMLWLRTFLRRFAAsgrTVLLSSH 204
Cdd:PRK11819 187 LDEPTNHLDAESVAWLEQFLHDYPG---TVVAVTH 218
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
35-236 |
2.41e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.11 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 35 AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSL---------DGGA--- 102
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALvsqnvhlfnDTIAnni 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 103 --FVGGRTGRGHLRCYAPAAGCS------PERLDRLLAETGLAeaadrpVSGystGMKQRLSLAAALLGDPELLILDEPS 174
Cdd:PRK11176 438 ayARTEQYSREQIEEAARMAYAMdfinkmDNGLDTVIGENGVL------LSG---GQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 175 NGLDPEGMLWLRTFLRRFAASgRTVLLSSHLLSEMEQTvDDVLLMHHGKLLSSGPLDHLLTQ 236
Cdd:PRK11176 509 SALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEKA-DEILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
35-222 |
4.43e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.03 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 35 AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH--------PYRELQTPTQRIG----VSLDGGA 102
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdllgmkddEWRAVRSDIQMIFqdplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 103 FVGGRTGRGhLRCYAP--AAGCSPERLDRLLAETGLAE-AADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDP 179
Cdd:PRK15079 116 TIGEIIAEP-LRTYHPklSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2155196442 180 EGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHG 222
Cdd:PRK15079 195 SIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-229 |
4.46e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.43 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 18 SPVIEVCGLRKKFR-GRTAVD---GISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTallwghpYRelqTPTQR 93
Cdd:PRK10535 2 TALLELKDIRRSYPsGEEQVEvlkGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGT-------YR---VAGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 94 IgVSLDGGAFVGGRT-------GRGHLRCYAPA----------AGCS-PERLDR---LLAETGLAEAADRPVSGYSTGMK 152
Cdd:PRK10535 72 V-ATLDADALAQLRRehfgfifQRYHLLSHLTAaqnvevpavyAGLErKQRLLRaqeLLQRLGLEDRVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 153 QRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHlLSEMEQTVDDVLLMHHGKLLSSGP 229
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH-DPQVAAQAERVIEIRDGEIVRNPP 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
36-234 |
6.24e-11 |
|
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: 62.27 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 36 VDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH-PYRELQTPTQRigVSLDGGAFVGGRTGRGHLR 114
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvAYVPQQAWIQN--DSLRENILFGKALNEKYYQ 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 115 CYAPAagCSperldrLLAETGLAEAADRPVSG-----YSTGMKQRLSLAAALLGDPELLILDEPSNGLD----------- 178
Cdd:TIGR00957 732 QVLEA--CA------LLPDLEILPSGDRTEIGekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhifehv 803
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 179 --PEGMLwlrtflrrfaaSGRTVLLSSHLLSEMEQtVDDVLLMHHGKLLSSGPLDHLL 234
Cdd:TIGR00957 804 igPEGVL-----------KNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELL 849
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
43-207 |
6.83e-11 |
|
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: 60.84 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 43 VPA-GRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTallWGHP---------YR--ELQTPTQRIgvsLDGG--------- 101
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPpdwdeildeFRgsELQNYFTKL---LEGDvkvivkpqy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 102 -----AFVGGRTG----RGHLRcyapaagcspERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDE 172
Cdd:cd03236 96 vdlipKAVKGKVGellkKKDER----------GKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190
....*....|....*....|....*....|....*
gi 2155196442 173 PSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLS 207
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
32-243 |
7.99e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 60.64 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 32 GRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRpTEGTALLWGHPYRE--LQTPTQRIGVsLDGGAFVGGRTG 109
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvpLQKWRKAFGV-IPQKVFIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 110 RGHLRCYapaaGC-SPERLDRLLAETGLAEAADR---------PVSGY--STGMKQRLSLAAALLGDPELLILDEPSNGL 177
Cdd:cd03289 94 RKNLDPY----GKwSDEEIWKVAEEVGLKSVIEQfpgqldfvlVDGGCvlSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 178 DPEGMLWLRTFLRRfAASGRTVLLSSHLLSEMEQtVDDVLLMHHGKLLSSGPLDHLLTQGERLESA 243
Cdd:cd03289 170 DPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNEKSHFKQA 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-224 |
1.36e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 8 MERTTPVKDNSPVIEVCGLRKKFRGRtaVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWG------ 81
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdispr 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 82 HPYRELQ------TPTQR---------------IGVSLDGGAFVGgrtgrghlrcyapAAGCSPERLDRLLAETGLAEAA 140
Cdd:PRK09700 331 SPLDAVKkgmayiTESRRdngffpnfsiaqnmaISRSLKDGGYKG-------------AMGLFHEVDEQRTAENQRELLA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 141 ------DRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVD 214
Cdd:PRK09700 398 lkchsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCD 477
|
250
....*....|
gi 2155196442 215 DVLLMHHGKL 224
Cdd:PRK09700 478 RIAVFCEGRL 487
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
35-241 |
1.66e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.79 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 35 AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWG----HPYR--ELQTPTQRIGV------------ 96
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKdkYIRPVRKRIGMvfqfpesqlfed 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 SLDGGAFVGGRTGRGHLRCyapaagcSPERLDRLLAETGLA----EAADRPVSGystGMKQRLSLAAALLGDPELLILDE 172
Cdd:PRK13646 102 TVEREIIFGPKNFKMNLDE-------VKNYAHRLLMDLGFSrdvmSQSPFQMSG---GQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 173 PSNGLDPEGMLWLRTFLRRFAA-SGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQGERLE 241
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLA 241
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-256 |
2.58e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.74 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 17 NSPVIEVCGLRKKFRGR----TAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRP---TEGTALLWGH-----PY 84
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPdgdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGReilnlPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 85 REL------------QTPTqrigVSLDGGAFVGGR--------TGRGHLRCYAPAAgcsperldRLLAETGLAEAADR-- 142
Cdd:PRK09473 89 KELnklraeqismifQDPM----TSLNPYMRVGEQlmevlmlhKGMSKAEAFEESV--------RMLDAVKMPEARKRmk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 143 --PvSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLD----PEGMLWLRTFLRRFaasGRTVLLSSHLLSEMEQTVDDV 216
Cdd:PRK09473 157 myP-HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREF---NTAIIMITHDLGVVAGICDKV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2155196442 217 LLMHHGKLLSSGPLDHLLTQ-----GERLESAFMRLTQAGEGTQT 256
Cdd:PRK09473 233 LVMYAGRTMEYGNARDVFYQpshpySIGLLNAVPRLDAEGESLLT 277
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-229 |
3.25e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.70 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIR-----PTEGTALLWGHP-YRELQTPtqrI 94
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNiYSPDVDP---I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 95 GVSLDGGAFVGGRTGRGHLRCYAPAA------------GCSPERLDRLLAETGLAEAA-----DRPvSGYSTGMKQRLSL 157
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHLTIYDNVAigvklnglvkskKELDERVEWALKKAALWDEVkdrlnDYP-SNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 158 AAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASgRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGP 229
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-235 |
3.50e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.91 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 39 ISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIR------PTEGTALLWGHPYRELQTPTQRIGVsldgGAFVGGRTGRGH 112
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEV----GMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 113 LRCYAPAA------GCSPER-----LDRLLAETGL-AEAADR---PVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGL 177
Cdd:PRK14246 105 LSIYDNIAyplkshGIKEKReikkiVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2155196442 178 D---PEGMLWLRTFLRRfaasGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLT 235
Cdd:PRK14246 185 DivnSQAIEKLITELKN----EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
46-230 |
8.36e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.70 E-value: 8.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 46 GRVTGFLGPNGAGKTTTLRMLLGliRPT----EGTALLWGHPYRE--------------LQTPTQRIGVSLDGGAFvggr 107
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKKQetfarisgyceqndIHSPQVTVRESLIYSAF---- 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 108 tgrghLRCyaPAAGCSPERL---DRLLAETGLAEAADRPV-----SGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDP 179
Cdd:PLN03140 980 -----LRL--PKEVSKEEKMmfvDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 180 EGMLWLRTFLRRFAASGRTVLLSSHLLS-EMEQTVDDVLLMHH-GKLLSSGPL 230
Cdd:PLN03140 1053 RAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRgGQVIYSGPL 1105
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
31-243 |
8.38e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 8.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIR-PTEGTALLWGHPYReLQTPTQRI--------------G 95
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVK-IRNPQQAIaqgiamvpedrkrdG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 VSLDGG-------AFVGGRTGRGHLRcYAPAAGCSPERLDRLLAETGLAEAadrPVSGYSTGMKQRLSLAAALLGDPELL 168
Cdd:PRK13549 352 IVPVMGvgknitlAALDRFTGGSRID-DAAELKTILESIQRLKVKTASPEL---AIARLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 169 ILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHlLTQGERLESA 243
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHN-LTQEQVMEAA 501
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
27-228 |
1.82e-09 |
|
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: 55.73 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 27 RKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPT---EGTALLWGHPYRELqtptqrigvsldggaf 103
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEF---------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 104 vggrtgrgHLRCYAPAAGCS------PERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGL 177
Cdd:cd03233 78 --------AEKYPGEIIYVSeedvhfPTLTVRETLDFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2155196442 178 DPEGMLWLRTFLRRFAASGRTVLLSShLLS---EMEQTVDDVLLMHHGKLLSSG 228
Cdd:cd03233 150 DSSTALEILKCIRTMADVLKTTTFVS-LYQasdEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-179 |
2.16e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 56.25 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKF-RG----RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGH------PYRElqt 89
Cdd:COG1101 2 LELKNLSKTFnPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklpEYKR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 90 pTQRIG-V---SLDGGAfvGGRT---------GRGHLRCYAPaaGCSPERLDR---LLAET--GLAEAADRPVSGYSTGM 151
Cdd:COG1101 79 -AKYIGrVfqdPMMGTA--PSMTieenlalayRRGKRRGLRR--GLTKKRRELfreLLATLglGLENRLDTKVGLLSGGQ 153
|
170 180
....*....|....*....|....*...
gi 2155196442 152 KQRLSLAAALLGDPELLILDEPSNGLDP 179
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDP 181
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
40-236 |
2.31e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 40 SFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIrptegtALLWGHPYRELQTPT-------QRI-----------GVSLDGG 101
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGEL------PLLSGERQSQFSHITrlsfeqlQKLvsdewqrnntdMLSPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 102 AFvgGRTGRGHLRCYAPAagcsPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEG 181
Cdd:PRK10938 97 DT--GRTTAEIIQDEVKD----PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 182 MLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQ 236
Cdd:PRK10938 171 RQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-216 |
2.58e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.11 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 20 VIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGlIRPT---EGTALLWGHP--YRELQTpTQRI 94
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVcrFKDIRD-SEAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 95 GV-------------SLDGGAFVGGRTGRGHL----RCYAPAAgcsperldRLLAETGLAEAADRPVSGYSTGMKQRLSL 157
Cdd:NF040905 79 GIviihqelalipylSIAENIFLGNERAKRGVidwnETNRRAR--------ELLAKVGLDESPDTLVTDIGVGKQQLVEI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2155196442 158 AAALLGDPELLILDEPSNGL---DPEGMLWLrtfLRRFAASGRTVLLSSHLLSEMEQTVDDV 216
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALneeDSAALLDL---LLELKAQGITSIIISHKLNEIRRVADSI 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-229 |
3.12e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 3 EQQECMERTTPVKDNSPVIEVCGLRKKFRGRT-----------AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIR 71
Cdd:PRK10261 296 AKQEPPIEQDTVVDGEPILQVRNLVTRFPLRSgllnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 72 PTEGTALLWGHPY------------RELQTPTQRIGVSLDGGAFVGGRTGRGhLRCYAPAAG-CSPERLDRLLAETGL-A 137
Cdd:PRK10261 376 SQGGEIIFNGQRIdtlspgklqalrRDIQFIFQDPYASLDPRQTVGDSIMEP-LRVHGLLPGkAAAARVAWLLERVGLlP 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 138 EAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPE---GMLWLRTFLRRfaASGRTVLLSSHLLSEMEQTVD 214
Cdd:PRK10261 455 EHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSirgQIINLLLDLQR--DFGIAYLFISHDMAVVERISH 532
|
250
....*....|....*
gi 2155196442 215 DVLLMHHGKLLSSGP 229
Cdd:PRK10261 533 RVAVMYLGQIVEIGP 547
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
126-195 |
3.70e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 3.70e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 126 RLDRLLAETGLAeaADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAAS 195
Cdd:PRK11147 138 RINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGS 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
40-245 |
4.29e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 55.36 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 40 SFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRElQTPTQR--------------------IGVSLD 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT-TPPSRRpvsmlfqennlfshltvaqnIGLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 100 GGafvggrtgrghLRCYAPaagcSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDP 179
Cdd:PRK10771 98 PG-----------LKLNAA----QREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 180 ---EGMLwlrTFLRRFAASGR-TVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTqGERLESAFM 245
Cdd:PRK10771 163 alrQEML---TLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS-GKASASALL 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
35-179 |
5.53e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.17 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 35 AVDGISFDVPAGRVTGFLGPNGAGKTTTLR---MLLGLIRP--TEGTALLWGHP-YRELQTPTQ---RIGV--------- 96
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGfrVEGKVTFHGKNlYAPDVDPVEvrrRIGMvfqkpnpfp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 -----SLDGGAFVGGRTGrghlrcyapaagcspeRLDRLLaETGLAEAA------DR-PVSG--YSTGMKQRLSLAAALL 162
Cdd:PRK14243 105 ksiydNIAYGARINGYKG----------------DMDELV-ERSLRQAAlwdevkDKlKQSGlsLSGGQQQRLCIARAIA 167
|
170
....*....|....*..
gi 2155196442 163 GDPELLILDEPSNGLDP 179
Cdd:PRK14243 168 VQPEVILMDEPCSALDP 184
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-220 |
6.57e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.04 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 19 PVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTL----RM--LLGLIRpTEGTALLWGHPYRELQTPTQ 92
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnRMneLESEVR-VEGRVEFFNQNIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 93 RIGVSLdggAFVGGRTGRGHLRCYAPAA------GCSPE-RLDRLLaETGLAEAA---------DRPVSGYSTGMKQRLS 156
Cdd:PRK14258 85 RLRRQV---SMVHPKPNLFPMSVYDNVAygvkivGWRPKlEIDDIV-ESALKDADlwdeikhkiHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 157 LAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFA-ASGRTVLLSSHLLSEMEQTVDDVLLMH 220
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFK 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-178 |
7.93e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.44 E-value: 7.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 17 NSPVIEVCGLRKKFR-GRTAVD---GISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPT- 91
Cdd:PRK11629 2 NKILLQCDNLCKRYQeGSVQTDvlhNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 92 -----QRIG------------VSLDGGA---FVGGRtgrghlrcyAPAAgcSPERLDRLLAETGLAEAADRPVSGYSTGM 151
Cdd:PRK11629 82 aelrnQKLGfiyqfhhllpdfTALENVAmplLIGKK---------KPAE--INSRALEMLAAVGLEHRANHRPSELSGGE 150
|
170 180
....*....|....*....|....*..
gi 2155196442 152 KQRLSLAAALLGDPELLILDEPSNGLD 178
Cdd:PRK11629 151 RQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
31-180 |
9.60e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 55.20 E-value: 9.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAG-RVtgfL--GPNGAGKTTTLRMLLGL--------IRPTEGTAL-LWGHPYrelqtptqrigvsl 98
Cdd:COG4178 374 DGRPLLEDLSLSLKPGeRL---LitGPSGSGKSTLLRAIAGLwpygsgriARPAGARVLfLPQRPY-------------- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 99 dggaFVGGRtgrghLR---CY-APAAGCSPERLDRLLAETGLAEAADRP---------VSGystGMKQRLSLAAALLGDP 165
Cdd:COG4178 437 ----LPLGT-----LRealLYpATAEAFSDAELREALEAVGLGHLAERLdeeadwdqvLSL---GEQQRLAFARLLLHKP 504
|
170
....*....|....*
gi 2155196442 166 ELLILDEPSNGLDPE 180
Cdd:COG4178 505 DWLFLDEATSALDEE 519
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-233 |
1.02e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 25 GLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHP-----------------YREL 87
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfksskealengismvHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 88 QTPTQR-------IGVSLDGGAFVggrtgrGHLRCYapaagcspERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAA 160
Cdd:PRK10982 83 NLVLQRsvmdnmwLGRYPTKGMFV------DQDKMY--------RDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 161 LLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHL 233
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
35-245 |
1.17e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.11 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 35 AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPT---QRIGVSLDGGAFVGGRTGRG 111
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 112 HLRCYAPAAGCSP--ERLDRLLAE-TGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTF 188
Cdd:PRK11614 100 NLAMGGFFAERDQfqERIKWVYELfPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 189 LRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQgERLESAFM 245
Cdd:PRK11614 180 IEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN-EAVRSAYL 235
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-204 |
1.84e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEG------------------------- 75
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGtvkwsenanigyyaqdhaydfendl 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 76 TALLWGHPYRELQTPTQRIgvsldggafvggrtgRGhlrcyapaagcspeRLDRLLAEtglAEAADRPVSGYSTGMKQRL 155
Cdd:PRK15064 400 TLFDWMSQWRQEGDDEQAV---------------RG--------------TLGRLLFS---QDDIKKSVKVLSGGEKGRM 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2155196442 156 SLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAAsgrTVLLSSH 204
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG---TLIFVSH 493
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
33-224 |
2.05e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 33 RTAVDGISFD-VPAGRVtGFLGPNGAGKTTTLRMLLGLIRPTEGT-ALLWG--------HPYREL---QTPTQrigvsld 99
Cdd:PRK10636 325 RIILDSIKLNlVPGSRI-GLLGRNGAGKSTLIKLLAGELAPVSGEiGLAKGiklgyfaqHQLEFLradESPLQ------- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 100 ggafvggrtgrgHLRCYAPAAgcSPERLDRLLAETGL-AEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLD 178
Cdd:PRK10636 397 ------------HLARLAPQE--LEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2155196442 179 PEGMLWLRTFLRRFAASGRTVLLSSHLLsemEQTVDDVLLMHHGKL 224
Cdd:PRK10636 463 LDMRQALTEALIDFEGALVVVSHDRHLL---RSTTDDLYLVHDGKV 505
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
42-204 |
2.07e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.57 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 42 DVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTallwghpyrelqtptqrigVSLDGGAFVggrtgrghlrcyapaag 121
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN-------------------DEWDGITPV----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 122 CSPERLDrllaetglaeaadrpvsgYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASG-RTVL 200
Cdd:cd03222 65 YKPQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTAL 126
|
....
gi 2155196442 201 LSSH 204
Cdd:cd03222 127 VVEH 130
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
39-232 |
2.22e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 39 ISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYReLQTPTQRI--GVSL-------DGgaFVGGRTG 109
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-IRSPRDAIraGIMLcpedrkaEG--IIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 110 RGHL-----RCYAPAAGCSPERLDRLLAETGLAE------AADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLD 178
Cdd:PRK11288 349 ADNInisarRHHLRAGCLINNRWEAENADRFIRSlniktpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2155196442 179 PEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLlsSGPLDH 232
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI--AGELAR 480
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
36-224 |
2.44e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 36 VDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGhpyRELQTPTQRIGvsLDGG-AFVG-GRTGRG-- 111
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG---HEVVTRSPQDG--LANGiVYISeDRKRDGlv 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 112 ------------HLRCYAPAAGcspeRLDRLlAETGLAE-----------AADRPVSGYSTGMKQRLSLAAALLGDPELL 168
Cdd:PRK10762 343 lgmsvkenmsltALRYFSRAGG----SLKHA-DEQQAVSdfirlfniktpSMEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 169 ILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSShllSEMEQTV---DDVLLMHHGKL 224
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVS---SEMPEVLgmsDRILVMHEGRI 473
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
46-208 |
4.90e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 46 GRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLwghpyrelqtptqrigvsldggafvggrtgrghlrcyapaagCSPE 125
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY------------------------------------------IDGE 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 126 RLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEG------MLWLRTFLRRFAASGRTV 199
Cdd:smart00382 40 DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllLEELRLLLLLKSEKNLTV 119
|
....*....
gi 2155196442 200 LLSSHLLSE 208
Cdd:smart00382 120 ILTTNDEKD 128
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
52-224 |
7.89e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.55 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 52 LGPNGAGKTTTLRMLLGLIRPTEGTALlwghpyrelQTPTQRIGV----SLDGgAFVGGRTGRGHLRCYApaaGCSPERL 127
Cdd:PLN03073 541 VGPNGIGKSTILKLISGELQPSSGTVF---------RSAKVRMAVfsqhHVDG-LDLSSNPLLYMMRCFP---GVPEQKL 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 128 DRLLAETGLA-EAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASgrtVLLSSHLL 206
Cdd:PLN03073 608 RAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG---VLMVSHDE 684
|
170
....*....|....*...
gi 2155196442 207 SEMEQTVDDVLLMHHGKL 224
Cdd:PLN03073 685 HLISGSVDELWVVSEGKV 702
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
143-210 |
8.90e-08 |
|
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: 52.01 E-value: 8.90e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2155196442 143 PVSGYSTGMKQRLSLAAALLGDPE---LLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEME 210
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
35-235 |
1.15e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.73 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 35 AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIR---------------------PTEGTALLwGHP----YRELQT 89
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrvtadrmrfddidllrlsPRERRKLV-GHNvsmiFQEPQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 90 ---PTQRIGV----SLDGGAFVGGRTGRGHLRcyapaagcsPERLDRLLAETGLAEAADRPVS---GYSTGMKQRLSLAA 159
Cdd:PRK15093 101 cldPSERVGRqlmqNIPGWTYKGRWWQRFGWR---------KRRAIELLHRVGIKDHKDAMRSfpyELTEGECQKVMIAI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2155196442 160 ALLGDPELLILDEPSNGLDPEGMLWLRTFLRRF-AASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLT 235
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-228 |
1.29e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 17 NSPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGliRP----TEGTALLWGHPYRELqTPTQ 92
Cdd:CHL00131 4 NKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDL-EPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 93 R--IGVSLdggAF-----VGGRTGRGHLRcyapaAGCSPERLDRLLAE----------------TGLAEA-ADRPVS-GY 147
Cdd:CHL00131 81 RahLGIFL---AFqypieIPGVSNADFLR-----LAYNSKRKFQGLPEldplefleiineklklVGMDPSfLSRNVNeGF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 148 STGMKQRLS-LAAALLgDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDD-VLLMHHGKLL 225
Cdd:CHL00131 153 SGGEKKRNEiLQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDyVHVMQNGKII 231
|
...
gi 2155196442 226 SSG 228
Cdd:CHL00131 232 KTG 234
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
127-204 |
1.80e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 127 LDRLlaetGLAEA-ADRPVSGYSTGmKQRLSLAA-ALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLL-SS 203
Cdd:PRK10938 385 LDIL----GIDKRtADAPFHSLSWG-QQRLALIVrALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVS 459
|
.
gi 2155196442 204 H 204
Cdd:PRK10938 460 H 460
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
39-238 |
2.71e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 39 ISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTAL-LWGHPYRELQTP-----TQRIGVsLDGGAFVGGRTGRgh 112
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVvIRGSVAYVPQVSwifnaTVRENI-LFGSDFESERYWR-- 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 113 lrcyAPAAGCSPERLDrLLAETGLAEAADRPVSgYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRF 192
Cdd:PLN03232 713 ----AIDVTALQHDLD-LLPGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKD 786
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2155196442 193 AASGRTVLLSSHLLSEMEQtVDDVLLMHHGKLLSSGPLDHLLTQGE 238
Cdd:PLN03232 787 ELKGKTRVLVTNQLHFLPL-MDRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
39-239 |
2.83e-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: 51.06 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 39 ISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTPTQRIGVSLDGGAFvgGRTgRGHLRCYAP 118
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIF--GLS-YDEYRYTSV 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 119 AAGCSPERLDRLLAETGLAEAADRPVSgYSTGMKQRLSLAAALLGDPELLILDEPSNGLD--PEGMLWLRTFLRRFAASG 196
Cdd:TIGR01271 522 IKACQLEEDIALFPEKDKTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFTHLDvvTEKEIFESCLCKLMSNKT 600
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2155196442 197 RtVLLSSHLlsEMEQTVDDVLLMHHGKLLSSGPLDHLltQGER 239
Cdd:TIGR01271 601 R-ILVTSKL--EHLKKADKILLLHEGVCYFYGTFSEL--QAKR 638
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
53-207 |
3.28e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 53 GPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYRELQTP-----TQRIGVSLDGGAFvggrtgrGHLRCYAPAAGcSPERL 127
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPyctyiGHNLGLKLEMTVF-------ENLKFWSEIYN-SAETL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 128 DRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLS 207
Cdd:PRK13541 105 YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLES 184
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-179 |
3.33e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.77 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 18 SPVIEVCGLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRML--LGLIRP---TEGTALLWGHPYRELQTPT- 91
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYSPRTDTv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 92 ---QRIGV----------SLDGGAFVGGRTGRGHlrcyapaagcSPERLDRLLaETGLAEAA------DR---PVSGYST 149
Cdd:PRK14239 83 dlrKEIGMvfqqpnpfpmSIYENVVYGLRLKGIK----------DKQVLDEAV-EKSLKGASiwdevkDRlhdSALGLSG 151
|
170 180 190
....*....|....*....|....*....|
gi 2155196442 150 GMKQRLSLAAALLGDPELLILDEPSNGLDP 179
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDP 181
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
141-231 |
3.46e-07 |
|
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: 48.86 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 141 DRPVSGYSTGMKQRLSLAAALLGDPE--LLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLsEMEQTVDDVLL 218
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL-DVLSSADWIID 160
|
90
....*....|...
gi 2155196442 219 MHHGKLLSSGPLD 231
Cdd:cd03238 161 FGPGSGKSGGKVV 173
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
148-236 |
5.11e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.90 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 148 STGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLW-LRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKLLS 226
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQiFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVE 239
|
90
....*....|
gi 2155196442 227 SGPLDHLLTQ 236
Cdd:COG4170 240 SGPTEQILKS 249
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-224 |
8.59e-07 |
|
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: 48.18 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 21 IEVCGLRKKFRGR--TAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYR--ELQTPTQRIG- 95
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIStiPLEDLRSSLTi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 96 VSLDGGAFVGgrTGRGHLRCYApaagcspERLDR-LLAETGLAEAAdrpvSGYSTGMKQRLSLAAALLGDPELLILDEPS 174
Cdd:cd03369 87 IPQDPTLFSG--TIRSNLDPFD-------EYSDEeIYGALRVSEGG----LNLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2155196442 175 NGLDPEG-MLWLRTFLRRFaaSGRTVLLSSHLLsemeQTV---DDVLLMHHGKL 224
Cdd:cd03369 154 ASIDYATdALIQKTIREEF--TNSTILTIAHRL----RTIidyDKILVMDAGEV 201
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-238 |
9.75e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 33 RTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTallwghpyrelqtptqriGVSLDGG-AFVG------ 105
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA------------------SVVIRGTvAYVPqvswif 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 106 GRTGRGHLRCYAPAagcSPERLDR------------LLAETGLAEAADRPVSgYSTGMKQRLSLAAALLGDPELLILDEP 173
Cdd:PLN03130 692 NATVRDNILFGSPF---DPERYERaidvtalqhdldLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2155196442 174 SNGLDPE-GMLWLRTFLRRfAASGRTVLLSS---HLLSEmeqtVDDVLLMHHGKLLSSGPLDHLLTQGE 238
Cdd:PLN03130 768 LSALDAHvGRQVFDKCIKD-ELRGKTRVLVTnqlHFLSQ----VDRIILVHEGMIKEEGTYEELSNNGP 831
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
44-206 |
1.60e-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: 46.97 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 44 PAGRVTGFLGPNGAGKTTTLRmllglirptegtALLWGhpyrelqtptqrigvsLDGGAFVGGRTGRGHLRCYAPAagcs 123
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTILD------------AIGLA----------------LGGAQSATRRRSGVKAGCIVAA---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 124 pERLDRLLAETGLaeaadrpvsgySTGMKQRLSLA-----AALLGDPeLLILDEPSNGLDPEGMLWLRTFLRRFAASGRT 198
Cdd:cd03227 67 -VSAELIFTRLQL-----------SGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKGAQ 133
|
....*...
gi 2155196442 199 VLLSSHLL 206
Cdd:cd03227 134 VIVITHLP 141
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
38-250 |
1.97e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 38 GISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYREL-------------QTP-----TQRIGV--- 96
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFgltdlrrvlsiipQSPvlfsgTVRFNIdpf 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 97 SLDGGAFVGGRTGRGHLRcyaPAAGCSPERLDRLLAETGlaeaadrpvSGYSTGMKQRLSLAAALLGDPELLILDEPSNG 176
Cdd:PLN03232 1334 SEHNDADLWEALERAHIK---DVIDRNPFGLDAEVSEGG---------ENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2155196442 177 LDPE-GMLWLRTFLRRFAASgrTVLLSSHLLSEMEQtVDDVLLMHHGKLLSSGPLDHLLTqgeRLESAFMRLTQA 250
Cdd:PLN03232 1402 VDVRtDSLIQRTIREEFKSC--TMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS---RDTSAFFRMVHS 1470
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
50-189 |
2.51e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 50 GFLGPNGAGKTTTLRMLLGLIRPTEGTALLwghpyrelqTPTQRIGV-SLDGGAF----VGGRTGRGHL----------R 114
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSL---------DPNERLGKlRQDQFAFeeftVLDTVIMGHTelwevkqerdR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 115 CYA-PAA-------------------GCSPE-RLDRLLAETGLA-EAADRPVSGYSTGMKQRLSLAAALLGDPELLILDE 172
Cdd:PRK15064 102 IYAlPEMseedgmkvadlevkfaemdGYTAEaRAGELLLGVGIPeEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDE 181
|
170
....*....|....*..
gi 2155196442 173 PSNGLDPEGMLWLRTFL 189
Cdd:PRK15064 182 PTNNLDINTIRWLEDVL 198
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
31-204 |
4.77e-06 |
|
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: 45.61 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGL--------IRPT-EGTALLWGHPYrelqtptqrigvsldgg 101
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwpwgsgriGMPEgEDLLFLPQRPY----------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 102 afvggrTGRGHLR---CYApaagcsperLDRLLaetglaeaadrpvsgySTGMKQRLSLAAALLGDPELLILDEPSNGLD 178
Cdd:cd03223 75 ------LPLGTLReqlIYP---------WDDVL----------------SGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180
....*....|....*....|....*.
gi 2155196442 179 PEGmlwLRTFLRRFAASGRTVLLSSH 204
Cdd:cd03223 124 EES---EDRLYQLLKELGITVISVGH 146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
31-224 |
5.12e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTtLRMLL-----GliRPTEGTALLWGHPYReLQTPTQRIGvslDGGAFVG 105
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTE-LAMSVfgrsyG--RNISGTVFKDGKEVD-VSTVSDAID---AGLAYVT 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 106 -GRTGRG-----HLRCYAPAAGcsperLDRL--------LAETGLAE-----------AADRPVSGYSTGMKQRLSLAAA 160
Cdd:NF040905 344 eDRKGYGlnlidDIKRNITLAN-----LGKVsrrgvideNEEIKVAEeyrkkmniktpSVFQKVGNLSGGNQQKVVLSKW 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2155196442 161 LLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
38-178 |
8.58e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.54 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 38 GISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYREL------QTPTQRIGVSLDGGAFVGGRTGRG 111
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeearaKLRAKHVGFVFQSFMLIPTLNALE 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2155196442 112 HLRCYAPAAG----CSPERLDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLD 178
Cdd:PRK10584 108 NVELPALLRGessrQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-223 |
9.51e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 25 GLRKKFRGRTAVDGISFDVPAGRVTGFLGPNGAGKTTT----LRML----------------LGLIRPTEGT-------- 76
Cdd:PRK15134 14 AFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTalsiLRLLpsppvvypsgdirfhgESLLHASEQTlrgvrgnk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 77 -ALLWGHPYRELQtPTQRIG------VSLDGGafVGGRTGRGH-LRCyapaagcsperLDRllaeTGLAEAADRpVSGY- 147
Cdd:PRK15134 94 iAMIFQEPMVSLN-PLHTLEkqlyevLSLHRG--MRREAARGEiLNC-----------LDR----VGIRQAAKR-LTDYp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 148 ---STGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAAS-GRTVLLSSHLLSEMEQTVDDVLLMHHGK 223
Cdd:PRK15134 155 hqlSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
31-254 |
1.03e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.59 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 31 RGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLG-LIRPTE-------GTALLWGHPYRELQTP--TQRIGVSLDG 100
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPrlARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 101 G--AFVGGRTGRGHLRCY--APAAGCSPER----LDRLLAETGLAEAADRPVSGYSTGMKQRLSLAAAL---------LG 163
Cdd:PRK13547 92 AqpAFAFSAREIVLLGRYphARRAGALTHRdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 164 DPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRT-VLLSSHLLSEMEQTVDDVLLMHHGKLLSSGPLDHLLTQG--ERL 240
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAhiARC 251
|
250
....*....|....
gi 2155196442 241 ESAFMRLTQAGEGT 254
Cdd:PRK13547 252 YGFAVRLVDAGDGV 265
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
141-238 |
1.09e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 45.69 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 141 DRPVSGY--STGMKQRLSLAAALL--GDPELLILDEPSNGLDPEgmlWLRTFLRRFA-ASGRT-VLLSSH---LLSEMEq 211
Cdd:COG4637 251 DRPFPARelSDGTLRFLALLAALLspRPPPLLCIEEPENGLHPD---LLPALAELLReASERTqVIVTTHspaLLDALE- 326
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2155196442 212 tVDDVLLMHHG----------------KLLSSGPLDHLLTQGE 238
Cdd:COG4637 327 -PEEVLVLEREddgetrirrlsdlelpEWLEGYSLGELWARGL 368
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
39-239 |
1.52e-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: 45.23 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 39 ISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEG-----------TALLWGHPyrelQTPTQRI--GVSLDggafvg 105
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGkikhsgrisfsSQFSWIMP----GTIKENIifGVSYD------ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 106 grtgrgHLRCYAPAAGCS--------PERLDRLLAETGLAeaadrpvsgYSTGMKQRLSLAAALLGDPELLILDEPSNGL 177
Cdd:cd03291 126 ------EYRYKSVVKACQleeditkfPEKDNTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2155196442 178 D--PEGMLWLRTFLRRFAASGRtVLLSSHLlsEMEQTVDDVLLMHHGKLLSSGPLDHLltQGER 239
Cdd:cd03291 191 DvfTEKEIFESCVCKLMANKTR-ILVTSKM--EHLKKADKILILHEGSSYFYGTFSEL--QSLR 249
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
35-178 |
1.96e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.12 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 35 AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIR-PTEGTALLWGHPYRELQTPTQRIGVSLDGGA----FVGGRTG 109
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAEKLEFNGQDLQRISEKERRNLVGAEvamiFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 110 RGhlRCY-----------APAAGCSPERLDR---LLAETGLAEAADRpVSGY----STGMKQRLSLAAALLGDPELLILD 171
Cdd:PRK11022 102 LN--PCYtvgfqimeaikVHQGGNKKTRRQRaidLLNQVGIPDPASR-LDVYphqlSGGMSQRVMIAMAIACRPKLLIAD 178
|
....*..
gi 2155196442 172 EPSNGLD 178
Cdd:PRK11022 179 EPTTALD 185
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
25-76 |
4.36e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.06 E-value: 4.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2155196442 25 GLRKKFRGRT-AVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGT 76
Cdd:PRK11650 8 AVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGE 60
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-235 |
4.46e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 28 KKFRGRTAVDGIsfdVPAGRVTGFLGPNGAGKTTTLRMLLGLI----RPTEGTALLWGHP-------YR---------EL 87
Cdd:TIGR00956 72 KTFDILKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITpeeikkhYRgdvvynaetDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 88 QTPTQRIGVSLDGGAfvggrtgrghlRCYAPaaGCSPERLDRL----------LAETGLAEAADRPVS-----GYSTGMK 152
Cdd:TIGR00956 149 HFPHLTVGETLDFAA-----------RCKTP--QNRPDGVSREeyakhiadvyMATYGLSHTRNTKVGndfvrGVSGGER 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 153 QRLSLAAALLGDPELLILDEPSNGLDPEGMLwlrTFLRRFAASGR----TVLLSSHLLSE-MEQTVDDVLLMHHGKLLSS 227
Cdd:TIGR00956 216 KRVSIAEASLGGAKIQCWDNATRGLDSATAL---EFIRALKTSANildtTPLVAIYQCSQdAYELFDKVIVLYEGYQIYF 292
|
....*...
gi 2155196442 228 GPLDHLLT 235
Cdd:TIGR00956 293 GPADKAKQ 300
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
141-235 |
1.12e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 141 DRPVSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFA-ASGRTVLLSshLLSEMEQT---VDDV 216
Cdd:PLN03140 331 DEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVhLTEATVLMS--LLQPAPETfdlFDDI 408
|
90
....*....|....*....
gi 2155196442 217 LLMHHGKLLSSGPLDHLLT 235
Cdd:PLN03140 409 ILLSEGQIVYQGPRDHILE 427
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
148-233 |
1.69e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.54 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 148 STGMKQRLSLAAALLGDPELLILDEPSNGLD---PEGMLWLRTFLRRFAASGrtVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiQAQILQLIKVLQKEMSMG--VIFITHDMGVVAEIADRVLVMYQGEA 247
|
....*....
gi 2155196442 225 LSSGPLDHL 233
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-246 |
2.51e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 141 DRPVSGYSTGMKQRLSLA----AALLGdpELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHlLSEMEQTVDDV 216
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLAtqigSGLTG--VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEH-DEDTIRAADYV 559
|
90 100 110
....*....|....*....|....*....|....*.
gi 2155196442 217 LLM------HHGKLLSSGPLDHLLTQGERLESAFMR 246
Cdd:TIGR00630 560 IDIgpgageHGGEVVASGTPEEILANPDSLTGQYLS 595
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
136-223 |
2.54e-04 |
|
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: 41.53 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 136 LAEAADRPVSGYSTGMKQRLSLAAALL-------GDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSH---L 205
Cdd:COG3593 152 IEDGKELPLDRLGSGFQRLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHsphL 231
|
90
....*....|....*...
gi 2155196442 206 LSEMEqtVDDVLLMHHGK 223
Cdd:COG3593 232 LSEVP--LENIRRLRRDS 247
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
38-250 |
2.69e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 38 GISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWGHPYREL-------------QTPTQRIGV---SLD-- 99
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFglmdlrkvlgiipQAPVLFSGTvrfNLDpf 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 100 ---GGAFVGGRTGRGHLRcyaPAAGCSPERLDRLLAETGlaeaadrpvSGYSTGMKQRLSLAAALLGDPELLILDEPSNG 176
Cdd:PLN03130 1337 nehNDADLWESLERAHLK---DVIRRNSLGLDAEVSEAG---------ENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 177 LD-PEGMLWLRTFLRRFAASgrTVLLSSHLLSemeqTV---DDVLLMHHGKLLSSGPLDHLLTQGerlESAFMRLTQA 250
Cdd:PLN03130 1405 VDvRTDALIQKTIREEFKSC--TMLIIAHRLN----TIidcDRILVLDAGRVVEFDTPENLLSNE---GSAFSKMVQS 1473
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
51-224 |
3.47e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.50 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 51 FL-GPNGAGKTTTLRMLLGLIRPTEGTALLWGHP--------YRELQTptqriGVSLDGGAFVGGRTGRGHlrcyaPAAg 121
Cdd:PRK10522 353 FLiGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPvtaeqpedYRKLFS-----AVFTDFHLFDQLLGPEGK-----PAN- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 122 csPERLDRLLAETGLA---EAADRPVSG--YSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEgmlWLRTF----LRRF 192
Cdd:PRK10522 422 --PALVEKWLERLKMAhklELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPH---FRREFyqvlLPLL 496
|
170 180 190
....*....|....*....|....*....|..
gi 2155196442 193 AASGRTVLLSSHLLSEMEQTvDDVLLMHHGKL 224
Cdd:PRK10522 497 QEMGKTIFAISHDDHYFIHA-DRLLEMRNGQL 527
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-204 |
4.17e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2155196442 142 RPVSGYSTGMKQRLSLAAALLG---DPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSH 204
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
145-178 |
6.90e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 6.90e-04
10 20 30
....*....|....*....|....*....|....
gi 2155196442 145 SGYSTGMKQRLSLAAALLGDPELLILDEPSNGLD 178
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
13-224 |
8.92e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.10 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 13 PVKDNSP---VIEVCGLRKKfrGRTAVDGISFDVPAGRVTGFLGPNGAGKTTTLRMLLGLIRPTEGTALLWG-----HPY 84
Cdd:PRK10982 240 PDKENKPgevILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkinnHNA 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 85 RE-------LQTPTQR---IGVSLDggafVGGRTGRGHLRCYAPAAGCSPERldRLLAETGLAEAADR--------PVSG 146
Cdd:PRK10982 318 NEainhgfaLVTEERRstgIYAYLD----IGFNSLISNIRNYKNKVGLLDNS--RMKSDTQWVIDSMRvktpghrtQIGS 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 147 YSTGMKQRLSLAAALLGDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLLSEMEQTVDDVLLMHHGKL 224
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
148-249 |
1.17e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 148 STGMKQRLSLAAALLGDPELLILDEPSNGLDPEG-MLWLRTFLRRFAASGRTVLLSSHLLSEMEQTvDDVLLMHH----G 222
Cdd:PTZ00265 1360 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSeKLIEKTIVDIKDKADKTIITIAHRIASIKRS-DKIVVFNNpdrtG 1438
|
90 100
....*....|....*....|....*...
gi 2155196442 223 KLLSS-GPLDHLLTQGERLESAFMRLTQ 249
Cdd:PTZ00265 1439 SFVQAhGTHEELLSVQDGVYKKYVKLAK 1466
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
124-246 |
1.93e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 38.74 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 124 PERLDRLLAETGlaeaadrpvSGYSTGMKQRLSLAAALLGDPELLILDEPSNGLD--PEGMLWlRTFLRRFAasGRTVLL 201
Cdd:cd03288 143 PGGLDAVVTEGG---------ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDmaTENILQ-KVVMTAFA--DRTVVT 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2155196442 202 SSHLLSEMeQTVDDVLLMHHGKLLSSGPLDHLLTQGERLESAFMR 246
Cdd:cd03288 211 IAHRVSTI-LDADLVLVLSRGILVECDTPENLLAQEDGVFASLVR 254
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
142-206 |
2.51e-03 |
|
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: 38.36 E-value: 2.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 142 RPVSGYSTGMKQRLSLAAALL---GDPELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLL 206
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNL 232
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-204 |
6.45e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 6.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 141 DRPVSGYSTGMKQRLSLAAALLGdpELL----ILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSH 204
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGA--ELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH 536
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
40-192 |
6.67e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.22 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 40 SFDVPAGRVTGFLGPNGAGKTT---TLRMLLGLIR-------PTEGTA--LLWGHPyrELQTPTQRIGVSLDGGafvGGR 107
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNlldALRFLSDAARgglqdalARRGGLeeLLWRGP--RTITEPIRLELEFAEE---DER 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 108 TGRGHLRCYAPAAGCSP----ERLDRLLAETGLAEAADRPVSGYSTGMKQRLSlaaallgDPELLILDEPSNGLDPEgML 183
Cdd:COG4637 90 DLRYELELGLPEPGGRPevkeERLWLKRGSGGRPFLDFRPKGRAVGGEPERLD-------SPESLLSQLGDPERFPE-LR 161
|
....*....
gi 2155196442 184 WLRTFLRRF 192
Cdd:COG4637 162 ALREALRSW 170
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
125-204 |
6.95e-03 |
|
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: 36.85 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2155196442 125 ERLdRLLAETGLAE-AADRPVSGYSTGMKQRLSLA----AALLGdpELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTV 199
Cdd:cd03270 116 ERL-GFLVDVGLGYlTLSRSAPTLSGGEAQRIRLAtqigSGLTG--VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTV 192
|
....*
gi 2155196442 200 LLSSH 204
Cdd:cd03270 193 LVVEH 197
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-206 |
9.55e-03 |
|
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: 37.30 E-value: 9.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2155196442 142 RPVSGYSTGMKQRLSLAAALLGD---PELLILDEPSNGLDPEGMLWLRTFLRRFAASGRTVLLSSHLL 206
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| |
