|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-214 |
2.82e-110 |
|
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: 317.60 E-value: 2.82e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSGMFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-ENTKEIRNMVGYLPQD 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlKQPQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:cd03264 81 FGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497584106 164 LDPEERIRFRNLLCEIANDRIVILSTHIVGDIEATCENVAILNSGKVIYNG 214
Cdd:cd03264 161 LDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-228 |
3.67e-95 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 280.41 E-value: 3.67e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-ENTKEIRNMVGYLPQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGeIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVaRDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 DFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTA 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 163 GLDPEERIRFRNLLCEIAND-RIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEALAKLAEEKVY 228
Cdd:COG1131 161 GLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVF 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-245 |
1.96e-73 |
|
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: 225.12 E-value: 1.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-ENTKEIRNMVGYLPQ 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGeITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 DFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTA 162
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 163 GLDPEERIRFRNLLCEIAN-DRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEALAKLAEEkvysievdkkdiENIK 241
Cdd:COG4555 162 GLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE------------ENLE 229
|
....
gi 497584106 242 SRFI 245
Cdd:COG4555 230 DAFV 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-266 |
1.76e-71 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 222.29 E-value: 1.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIenTKEIRNMVGYLPQD 83
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGeIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL--DPEDRRRIGYLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:COG4152 80 RGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 164 LDPEERIRFRNLLCE-IANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEALAKLAEEKVYSIEVDkKDIENIKS 242
Cdd:COG4152 160 LDPVNVELLKDVIRElAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEAD-GDAGWLRA 238
|
250 260
....*....|....*....|....
gi 497584106 243 RFIVIGMLTHGGKAILRIISDDKP 266
Cdd:COG4152 239 LPGVTVVEEDGDGAELKLEDGADA 262
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-210 |
2.43e-68 |
|
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: 209.95 E-value: 2.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-ENTKEIRNMVGYLPQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGeIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 DFSMYPNMTVykamdylavlsdiplrkrrkiiakllskvnltnYQNVKvksLSGGMNRRLGIAQSLIHNPRVLIVDEPTA 162
Cdd:cd03230 81 EPSLYENLTV---------------------------------RENLK---LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497584106 163 GLDPEERIRFRNLLCEIAND-RIVILSTHIVGDIEATCENVAILNSGKV 210
Cdd:cd03230 125 GLDPESRREFWELLRELKKEgKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
3-263 |
7.83e-61 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 194.99 E-value: 7.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-ENTKEIRNMVGYL 80
Cdd:TIGR03522 1 MSIRVSSLTKLYGTQNALDEVSFEAQKGrIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVlQNPKEVQRNIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:TIGR03522 81 PEHNPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 161 TAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEALAKLAEEKVYSIEVDKK-DIEN 239
Cdd:TIGR03522 161 TTGLDPNQLVEIRNVIKNIGKDKTIILSTHIMQEVEAICDRVIIINKGKIVADKKLDELSAANKKQVIEVEFEEQiDLQL 240
|
250 260
....*....|....*....|....*
gi 497584106 240 IKS-RFIVIGMLTHGGKAILRIISD 263
Cdd:TIGR03522 241 FETlEEISSVKNTGGNTWKLTFETP 265
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-216 |
6.37e-59 |
|
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: 187.33 E-value: 6.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQ--ALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-ENTKEIRNMVGYLPQ 82
Cdd:cd03263 3 IRNLTKTYKKGTkpAVDDLSLNVYKGeIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYCPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 DFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTA 162
Cdd:cd03263 83 FDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497584106 163 GLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGST 216
Cdd:cd03263 163 GLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-219 |
3.86e-56 |
|
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: 180.26 E-value: 3.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-ENTKEIRNMVGYLPQ 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGeIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 DFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTA 162
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 163 GLDPEERIRFRNLLCEI--ANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-214 |
6.31e-56 |
|
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: 179.40 E-value: 6.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIenTKEIRNMVGYLPQD 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGeIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL--DIAARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497584106 164 LDPEERIRFRNLLCEIA-NDRIVILSTHIVGDIEATCENVAILNSGKVIYNG 214
Cdd:cd03269 159 LDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-214 |
2.56e-55 |
|
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: 177.79 E-value: 2.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGYLPQD 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGeIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSMYPNMTVYKAMDYLAVLsdipLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARL----LGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497584106 164 LDPEERIRFRNLLCEIANDRI-VILSTHIVGDIEATCENVAILNSGKVIYNG 214
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGItVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-263 |
7.52e-52 |
|
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: 171.80 E-value: 7.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 12 KRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-ENTKEIRNMVGYLPQDFSMYPN 89
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGeVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 90 MTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEER 169
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 170 IRFRNLLCEIANDRI-VILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL-AKLAEEKVYSIEVDKKDIENIKSRFIVI 247
Cdd:TIGR01188 161 RAIWDYIRALKEEGVtILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELkRRLGKDTLESRPRDIQSLKVEVSMLIAE 240
|
250
....*....|....*.
gi 497584106 248 GMLTHGGKAILRIISD 263
Cdd:TIGR01188 241 LGETGLGLLAVTVDSD 256
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-219 |
1.21e-48 |
|
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: 161.35 E-value: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF-GKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI--ENTKEIRNMVGYL 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFvAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItkKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDfsmyP-----NMTVYKamdylavlsDI---------PLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQ 146
Cdd:COG1122 81 FQN----PddqlfAPTVEE---------DVafgpenlglPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497584106 147 SLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRI-VILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKtVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-211 |
5.30e-48 |
|
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: 159.22 E-value: 5.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 9 NLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGYLPQDFSMY 87
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGeFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQDYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 88 PNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPE 167
Cdd:cd03259 85 PHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497584106 168 ERIRFRNLLCEI--ANDRIVILSTHIVGDIEATCENVAILNSGKVI 211
Cdd:cd03259 165 LREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-217 |
2.86e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 158.33 E-value: 2.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIentKEIRNMVGY 79
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGeFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP---RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSMYPN--MTV--------YKAMDYLAVLSdiplRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLI 149
Cdd:COG1121 80 VPQRAEVDWDfpITVrdvvlmgrYGRRGLFRRPS----RADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 150 HNPRVLIVDEPTAGLDPEERIRFRNLLCEI-ANDRIVILSTHIVGDIEATCENVAILNsGKVIYNGSTE 217
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPE 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-198 |
7.22e-46 |
|
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: 153.40 E-value: 7.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE-IRNMVGYL 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGeALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRkiIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 497584106 161 TAGLDPEERIRFRNLLCE-IANDRIVILSTHIVGDIEAT 198
Cdd:COG4133 159 FTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAA 197
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-196 |
1.06e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.86 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRF----GKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEntkEIRN 75
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFvALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT---GPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 76 MVGYLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVL 155
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497584106 156 IVDEPTAGLDPEERIRFRNLLCEI--ANDRIVILSTHivgDIE 196
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTH---DVD 200
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-246 |
1.10e-45 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 154.43 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN--TKEIRNMVGYLP 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVtALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 QDFSMYPNMTVYkamDYLAvLSDIPLRKR--------RKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPR 153
Cdd:COG1120 82 QEPPAPFGLTVR---ELVA-LGRYPHLGLfgrpsaedREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 154 VLIVDEPTAGLDPEERIRFRNLLCEIAND--RIVILSTHivgDIE---ATCENVAILNSGKVIYNGSTEALakLAEE--- 225
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLH---DLNlaaRYADRLVLLKDGRIVAQGPPEEV--LTPElle 232
|
250 260
....*....|....*....|.
gi 497584106 226 KVYSIEVDKKDIENIKSRFIV 246
Cdd:COG1120 233 EVYGVEARVIEDPVTGRPLVL 253
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-190 |
1.87e-45 |
|
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: 152.64 E-value: 1.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFG----KKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEI------ 73
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFvAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 74 RNMVGYLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPR 153
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 497584106 154 VLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTH 190
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTH 199
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-219 |
1.03e-44 |
|
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: 158.14 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF-----GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-----ENTKEI 73
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGeTLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklsrRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 74 RNMVGYLPQD-FSMY-PNMTVYKAMDY-LAVLSDIPLRKRRKIIAKLLSKVNL-TNYQNVKVKSLSGGMNRRLGIAQSLI 149
Cdd:COG1123 341 RRRVQMVFQDpYSSLnPRMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497584106 150 HNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR----IVIlsTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELgltyLFI--SHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-209 |
1.16e-44 |
|
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: 149.26 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI----ENTKEIRNMVGY 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGeIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdleDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSMYPNMTVykamdylavlsdiplrkrrkiiakllskvnltnYQNVkVKSLSGGMNRRLGIAQSLIHNPRVLIVDE 159
Cdd:cd03229 81 VFQDFALFPHLTV---------------------------------LENI-ALGLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497584106 160 PTAGLDPEERIRFRNLLCEI-ANDRI-VILSTHIVGDIEATCENVAILNSGK 209
Cdd:cd03229 127 PTSALDPITRREVRALLKSLqAQLGItVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-209 |
3.99e-44 |
|
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: 149.15 E-value: 3.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRF--GKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI--ENTKEIRNMVGYLP 81
Cdd:cd03225 2 LKNLSFSYpdGARPALDDISLTIKKGEFvLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtkLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 QD-FSMYPNMTVYkamDYLA---VLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIV 157
Cdd:cd03225 82 QNpDDQFFGPTVE---EEVAfglENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497584106 158 DEPTAGLDPEERIRFRNLLCEIANDRI-VILSTHIVGDIEATCENVAILNSGK 209
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-214 |
1.56e-43 |
|
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: 147.68 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTkeiRNMVGYLPQDFS 85
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFlAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE---RKRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 86 M---YPnMTVYK----AMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVD 158
Cdd:cd03235 79 IdrdFP-ISVRDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 159 EPTAGLDPEERIRFRNLLCEI-ANDRIVILSTHIVGDIEATCENVAILNsGKVIYNG 214
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-219 |
3.30e-43 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 149.57 E-value: 3.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSGM-FGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-ENTKEIRNMVGYLPQ 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGEcFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 DFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTA 162
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497584106 163 GLDPEER----IRFRNLLceiANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK13537 168 GLDPQARhlmwERLRSLL---ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-227 |
7.40e-43 |
|
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: 146.66 E-value: 7.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENT-----KEIR 74
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGeILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLsekelYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 75 NMVGYLPQD---FSmypNMTVYkamDYLAV----LSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQS 147
Cdd:COG1127 82 RRIGMLFQGgalFD---SLTVF---ENVAFplreHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 148 LIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIaNDRI---VILSTHIVGDIEATCENVAILNSGKVIYNGSTEALAKLAE 224
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIREL-RDELgltSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDD 234
|
...
gi 497584106 225 EKV 227
Cdd:COG1127 235 PWV 237
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-219 |
9.60e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 146.74 E-value: 9.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF-GKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNM---V 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFvALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTalRGRALRRLrrrI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 78 GYLPQDFSMYPNMTVYK-----AMDYL----AVLSDIPLRKRRKIIAkLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSL 148
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTnvlagRLGRTstwrSLLGLFPPEDRERALE-ALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497584106 149 IHNPRVLIVDEPTAGLDPE--ERIrfRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:COG3638 162 VQEPKLILADEPVASLDPKtaRQV--MDLLRRIAREDgiTVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-214 |
1.07e-42 |
|
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: 145.59 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKK----QALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-ENTKEIRNMVG 78
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGeVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 79 YLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVD 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 159 EPTAGLDPEERIRFRNLLCEI-ANDRIVILSTHIVGDIEATCENVAILNSGKVIYNG 214
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-228 |
3.23e-42 |
|
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: 145.02 E-value: 3.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFG-KKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN--TKEIRNM---V 77
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGeFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkGKALRQLrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 78 GYLPQDFSMYPNMTVYK--------AMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLI 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLEnvlsgrlgRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 150 HNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKVIYNGSTEALAKLAEEKV 227
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDEI 240
|
.
gi 497584106 228 Y 228
Cdd:cd03256 241 Y 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-190 |
5.90e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 144.03 E-value: 5.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKK----QALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE--- 72
Cdd:COG1136 1 MSPLLELRNLTKSYGTGegevTALRGVSLSIEAGEFvAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 73 --IRN-MVGYLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLI 149
Cdd:COG1136 81 arLRRrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497584106 150 HNPRVLIVDEPTAGLDPEERIRFRNLLCEIAND--RIVILSTH 190
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTH 203
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-196 |
1.67e-41 |
|
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: 142.61 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFG----KKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIentKEIRNMVGY 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFvALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV---TGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 497584106 160 PTAGLDPEERIRFRNLLCEI--ANDRIVILSTHivgDIE 196
Cdd:cd03293 158 PFSALDALTREQLQEELLDIwrETGKTVLLVTH---DID 193
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
7-215 |
2.17e-41 |
|
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: 142.54 E-value: 2.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIeNTKEIRNmVGYLPQDFS 85
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNsVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW-TRKDLHK-IGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 86 MYPNMTVYKAMDYLAVLSDIPLRKrrkiIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLD 165
Cdd:TIGR03740 81 LYENLTARENLKVHTTLLGLPDSR----IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497584106 166 PEERIRFRNLLCEIANDRI-VILSTHIVGDIEATCENVAILNSGKVIYNGS 215
Cdd:TIGR03740 157 PIGIQELRELIRSFPEQGItVILSSHILSEVQQLADHIGIISEGVLGYQGK 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-209 |
2.27e-41 |
|
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: 140.07 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN--TKEIRNMVGYLPQd 83
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGeIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlpLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 fsmypnmtvykamdylavlsdiplrkrrkiiakllskvnltnyqnvkvksLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497584106 164 LDPEERIRFRNLLCEIAND-RIVILSTHIVGDIEATCENVAILNSGK 209
Cdd:cd00267 111 LDPASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-221 |
1.69e-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: 140.33 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE-----IRNMVG 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGeILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelyrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 79 YLPQDFSMYPNMTVYKAMDY-LAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIV 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFpLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 158 DEPTAGLDP------EERIrfRNLLCEIANDRIVIlsTHIVGDIEATCENVAILNSGKVIYNGSTEALAK 221
Cdd:cd03261 161 DEPTAGLDPiasgviDDLI--RSLKKELGLTSIMV--THDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-214 |
2.09e-39 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 136.03 E-value: 2.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 6 AVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN--TKEIRNMVGYLPQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGeIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlsPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 dfsmypnmtvykAMDYLAVLSdipLRKRRkiiakllskvnltnyqnvkVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTA 162
Cdd:cd03214 81 ------------ALELLGLAH---LADRP-------------------FNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 163 GLDPEERIRFRNLLCEIANDR--IVILSTHivgDIEAT---CENVAILNSGKVIYNG 214
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERgkTVVMVLH---DLNLAaryADRVILLKDGRIVAQG 180
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-219 |
2.23e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 140.35 E-value: 2.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-ENTKEIRNMVGYL 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGeCFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497584106 161 TAGLDPEER----IRFRNLLceiANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK13536 200 TTGLDPHARhliwERLRSLL---ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-219 |
1.16e-38 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 144.50 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 9 NLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE-NTKEIRNMVGYLPQDFSM 86
Cdd:NF033858 271 GLTMRFGDFTAVDHVSFRIRRGeIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDaGDIATRRRVGYMSQAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 87 YPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDP 166
Cdd:NF033858 351 YGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 167 EERIRFRNLLCEIA-NDRIVI-LSTHIVGdiEAT-CENVAILNSGKVIYNGSTEAL 219
Cdd:NF033858 431 VARDMFWRLLIELSrEDGVTIfISTHFMN--EAErCDRISLMHAGRVLASDTPAAL 484
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-227 |
1.18e-38 |
|
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: 135.64 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK--EIRNM-VGYL 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGeIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPphEIARLgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDFSMYPNMTVYKAMDyLAV--------LSDIPLRKRRKIIAK---LLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLI 149
Cdd:cd03219 81 FQIPRLFPELTVLENVM-VAAqartgsglLLARARREEREARERaeeLLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 150 HNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRI-VILSTHIVGDIEATCENVAILNSGKVIYNGSTEALakLAEEKV 227
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV--RNNPRV 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-227 |
1.30e-38 |
|
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: 135.36 E-value: 1.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENT---KEIRNMVGYL 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmhKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDFSMYPNMTVykAMDYLAVLSDIPLRK--RRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVD 158
Cdd:cd03218 81 PQEASIFRKLTV--EENILAVLEIRGLSKkeREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 159 EPTAGLDPEERIRFRNLLCEIANDRIVILST-HIVGDIEATCENVAILNSGKVIYNGSTEALAklAEEKV 227
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA--ANELV 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-225 |
2.57e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 136.04 E-value: 2.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGK-----KQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-----ENTKEI 73
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFvAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakkkKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 74 RNMVGYLPQdfsmYPNM-----TVYKamdylavlsDI---------PLRKRRKIIAKLLSKVNLTnyQNVKVKS---LSG 136
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYK---------DIafgpknlglSEEEAEERVKEALELVGLD--EEYLERSpfeLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 137 GMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEI--ANDRIVILSTHIVGDIEATCENVAILNSGKVIYNG 214
Cdd:TIGR04521 146 GQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
250
....*....|.
gi 497584106 215 STEALAKLAEE 225
Cdd:TIGR04521 226 TPREVFSDVDE 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-228 |
4.83e-38 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 134.39 E-value: 4.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 2 EMKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN---TKEIRNMV 77
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 78 GYLPQDFSMYPNMTVYKAMdyLAVL--SDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVL 155
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNI--LAVLelRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497584106 156 IVDEPTAGLDPEERIRFRNLLCEIANDRIVILST-HIVGDIEATCENVAILNSGKVIYNGSTEALAKLAE-EKVY 228
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLvRKVY 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-214 |
2.72e-37 |
|
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: 131.86 E-value: 2.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF----GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN-----TKEIR 74
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGeTLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 75 NMVGYLPQD--FSMYPNMTVYKAMD--YLAVLSDIPLRKRRKIIAKLLSKVNL-TNYQNVKVKSLSGGMNRRLGIAQSLI 149
Cdd:cd03257 82 KEIQMVFQDpmSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 150 HNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKVIYNG 214
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-219 |
3.24e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 135.23 E-value: 3.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMK-IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK-EIRNmV 77
Cdd:COG3842 1 MAMPaLELENVSKRYGDVTALDDVSLSIEPGeFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpEKRN-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 78 GYLPQDFSMYPNMTVY-------KAMDylavlsdIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIH 150
Cdd:COG3842 80 GMVFQDYALFPHLTVAenvafglRMRG-------VPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497584106 151 NPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR-I-VILSTHivgDIE---ATCENVAILNSGKVIYNGSTEAL 219
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELgItFIYVTH---DQEealALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-228 |
3.64e-37 |
|
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: 132.04 E-value: 3.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGK-KQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENT--KEIRNM---V 77
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFvAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgKKLRKLrrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 78 GYLPQDFSMYPNMTVYK--------AMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLI 149
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLEnvlhgrlgYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 150 HNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKVIYNGSTEALAKLAEEKV 227
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRHI 241
|
.
gi 497584106 228 Y 228
Cdd:TIGR02315 242 Y 242
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
7-227 |
5.27e-37 |
|
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: 131.63 E-value: 5.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENT---KEIRNMVGYLPQ 82
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGeIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpmhERARLGIGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 DFSMYPNMTVYKamDYLAVL---SDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDE 159
Cdd:TIGR04406 84 EASIFRKLTVEE--NIMAVLeirKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 160 PTAGLDPEERIRFRNLLCEIANDRIVILST-HIVGDIEATCENVAILNSGKVIYNGSTEALakLAEEKV 227
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERGIGVLITdHNVRETLDICDRAYIISDGKVLAEGTPAEI--VANEKV 228
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-265 |
5.38e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 133.67 E-value: 5.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF-------G--------------KKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHM 62
Cdd:COG4586 2 IEVENLSKTYrvyekepGlkgalkglfrreyrEVEAVDDISFTIEPGeIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 63 CG-VPIENTKEIRNMVGylpqdFSM------YPNMTVYKAMDYLAVLSDIP---LRKRRKIIAKLLskvNLTNYQNVKVK 132
Cdd:COG4586 82 LGyVPFKRRKEFARRIG-----VVFgqrsqlWWDLPAIDSFRLLKAIYRIPdaeYKKRLDELVELL---DLGELLDTPVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 133 SLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKV 210
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 211 IYNGSTEAL-AKLAEEKVYSIEVDKK-DIENIKSRFIVIGmlTHGGKAILRIISDDK 265
Cdd:COG4586 234 IYDGSLEELkERFGPYKTIVLELAEPvPPLELPRGGEVIE--REGNRVRLEVDPRES 288
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-219 |
6.09e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 134.12 E-value: 6.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCG------VPienTKEiRN 75
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGeLVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlftnLP---PRE-RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 76 mVGYLPQDFSMYPNMTVYkamDYLAV-LSDIPLRK--RRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNP 152
Cdd:COG1118 77 -VGFVFQHYALFPHMTVA---ENIAFgLRVRPPSKaeIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497584106 153 RVLIVDEPTAGLD----PEERIRFRNLLCEIanDRIVILSTHivgDIE---ATCENVAILNSGKVIYNGSTEAL 219
Cdd:COG1118 153 EVLLLDEPFGALDakvrKELRRWLRRLHDEL--GGTTVFVTH---DQEealELADRVVVMNQGRIEQVGTPDEV 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-225 |
8.35e-37 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 131.08 E-value: 8.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKK----QALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN--TKEIRNMV 77
Cdd:COG1124 2 LEVRNLSVSYGQGgrrvPVLKDVSLEVAPGeSFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrrRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 78 GYLPQDF--SMYPNMTVYKAMDYLAVLSDIPLRKRRkiIAKLLSKVNLT-NYQNVKVKSLSGGMNRRLGIAQSLIHNPRV 154
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREER--IAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497584106 155 LIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKVIYNGSTEALAKLAEE 225
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-190 |
1.18e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 130.17 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF-GKKQALDNINLEIDSGMFGLL-GRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE-----IRNMV 77
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 78 GYLPQDFSMYPNMTVYkamDYLAvlsdIPLR---KRRKIIAK----LLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIH 150
Cdd:COG2884 82 GVVFQDFRLLPDRTVY---ENVA----LPLRvtgKSRKEIRRrvreVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 497584106 151 NPRVLIVDEPTAGLDPEERIRFRNLLCEIaNDR--IVILSTH 190
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEI-NRRgtTVLIATH 195
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-214 |
2.41e-36 |
|
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: 129.76 E-value: 2.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSK---------------------RFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHM 62
Cdd:cd03267 1 IEVSNLSKsyrvyskepgligslkslfkrKYREVEALKGISFTIEKGeIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 63 CG-VPIENTKEIRNMVGY-LPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNR 140
Cdd:cd03267 81 AGlVPWKRRKKFLRRIGVvFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 141 RLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKVIYNG 214
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-219 |
3.79e-36 |
|
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: 128.84 E-value: 3.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSGM-FGLLGRNGAGKTTFMRILATLL-----SKTEGSIHMCGVPI----ENTKEIR 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEiTALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydldVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 75 NMVGYLPQDFSMYPnMTVYKAMDYLAVLSDIPLRKRRK-IIAKLLSKVNLTNY--QNVKVKSLSGGMNRRLGIAQSLIHN 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDeRVEEALRKAALWDEvkDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497584106 152 PRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-219 |
8.86e-35 |
|
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: 125.91 E-value: 8.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGYLP 81
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGeLVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 QDFSMYPNMTVYkamDYLAVLSDIPLRKRR----KIIAK---LLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRV 154
Cdd:cd03296 81 QHYALFRHMTVF---DNVAFGLRVKPRSERppeaEIRAKvheLLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497584106 155 LIVDEPTAGLDPEERIRFRNLLCEIaNDRIVILSTHIVGDIEATCE---NVAILNSGKVIYNGSTEAL 219
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRL-HDELHVTTVFVTHDQEEALEvadRVVVMNKGRIEQVGTPDEV 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-219 |
1.79e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.88 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIeNTKEI--RNmVGYLP 81
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFlVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPkdRN-IAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 QDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPT 161
Cdd:COG3839 82 QSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497584106 162 AGLDPEERIRFRNllcEIAndRI-------VILSTHivgD-IEA-T-CENVAILNSGKVIYNGSTEAL 219
Cdd:COG3839 162 SNLDAKLRVEMRA---EIK--RLhrrlgttTIYVTH---DqVEAmTlADRIAVMNDGRIQQVGTPEEL 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-218 |
6.38e-34 |
|
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: 124.00 E-value: 6.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK--EIRNM- 76
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGeIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPphRIARLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 VGYLPQDFSMYPNMTVY----------KAMDYLAVLSDIP--LRKRRKIIAK---LLSKVNLTNYQNVKVKSLSGGMNRR 141
Cdd:COG0411 81 IARTFQNPRLFPELTVLenvlvaaharLGRGLLAALLRLPraRREEREARERaeeLLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 142 LGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRI--VILSTHIVGDIEATCENVAILNSGKVIYNGSTEA 218
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGitILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-210 |
6.79e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 122.62 E-value: 6.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK--EIRNMVGYLP 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECvAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 QDFSMYPNmTVYKAMDYLAVLSDIPLRkrRKIIAKLLSKVNLTN-YQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497584106 161 TAGLDPEERIRFRNLLCEIAN--DRIVILSTHIVGDIEATCENVAILNSGKV 210
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-227 |
7.27e-34 |
|
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: 123.21 E-value: 7.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQaLDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGYLPQD 83
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGdYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSMYPNMTVYKAMDY-LAVLSDIPLRKRRKI--IAKLLskvNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:cd03299 80 YALFPHMTVYKNIAYgLKKRKVDKKEIERKVleIAEML---GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 161 TAGLDPEERIRFRNLLCEI--ANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGS-TEALAKLAEEKV 227
Cdd:cd03299 157 FSALDVRTKEKLREELKKIrkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKpEEVFKKPKNEFV 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-217 |
7.70e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 125.58 E-value: 7.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKK----QALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNM- 76
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGeIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 --VGYLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRV 154
Cdd:COG1135 82 rkIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497584106 155 LIVDEPTAGLDPE--ERIrfRNLLCEIaNDRI---VILSTH---IVGDIeatCENVAILNSGKVIYNGSTE 217
Cdd:COG1135 162 LLCDEATSALDPEttRSI--LDLLKDI-NRELgltIVLITHemdVVRRI---CDRVAVLENGRIVEQGPVL 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-224 |
1.15e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 128.22 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCG--VPIENTKE-IRNM 76
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGeIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDaIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 VGYLPQDFSMYPNMTVYK----AMDYLAVLSdIPLRKRRKIIAKLLSKVNLtnyqNV----KVKSLSGGMNRRLGIAQSL 148
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAEnivlGLEPTKGGR-LDRKAARARIRELSERYGL----DVdpdaKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 149 IHNPRVLIVDEPTAGLDPEERIRF----RNLlceIANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL--AKL 222
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELfeilRRL---AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETseEEL 233
|
..
gi 497584106 223 AE 224
Cdd:COG3845 234 AE 235
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-162 |
1.34e-33 |
|
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: 120.06 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 20 LDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI--ENTKEIRNMVGYLPQDFSMYPNMTVYKAM 96
Cdd:pfam00005 1 LKNVSLTLNPGeILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 97 DYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKV----KSLSGGMNRRLGIAQSLIHNPRVLIVDEPTA 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-219 |
2.55e-33 |
|
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: 121.92 E-value: 2.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFG----KKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE-----IR 74
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGeIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrkAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 75 NMVGYLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRV 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497584106 155 LIVDEPTAGLDPEERIRFRNLLCEIaNDRI---VILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDI-NRELgltIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-219 |
8.06e-33 |
|
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: 125.79 E-value: 8.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRF--GKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKT---EGSIHMCGVPIENTKE-- 72
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETvALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 73 IRNMVGYLPQDFSMYPNM-TVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHN 151
Cdd:COG1123 81 RGRRIGMVFQDPMTQLNPvTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 152 PRVLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-214 |
9.52e-33 |
|
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: 119.19 E-value: 9.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 15 GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLS--KTEGSIHMCGVPIEnTKEIRNMVGYLPQDFSMYPNMT 91
Cdd:cd03213 20 SGKQLLKNVSGKAKPGeLTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLD-KRSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 92 VYKAMDYLAVLsdiplrkrrkiiakllskvnltnyqnvkvKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIR 171
Cdd:cd03213 99 VRETLMFAAKL-----------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497584106 172 FRNLLCEIAND-RIVILSTHIV-GDIEATCENVAILNSGKVIYNG 214
Cdd:cd03213 150 VMSLLRRLADTgRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-214 |
9.71e-33 |
|
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: 120.07 E-value: 9.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 16 KKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLL---SKTEGSIHMCGVPIeNTKEIRNMVGYLPQDFSMYPNMT 91
Cdd:cd03234 19 YARILNDVSLHVESGqVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPR-KPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 92 VYKAMDYLAVLSdIPLRKRRKIIAK-----LLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDP 166
Cdd:cd03234 98 VRETLTYTAILR-LPRKSSDAIRKKrvedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497584106 167 EERIRFRNLLCEIA-NDRIVILSTHIVG-DIEATCENVAILNSGKVIYNG 214
Cdd:cd03234 177 FTALNLVSTLSQLArRNRIVILTIHQPRsDLFRLFDRILLLSSGEIVYSG 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-236 |
1.20e-32 |
|
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: 120.57 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEG-SIHMCGVPI--ENTKEIRNMVGY- 79
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHwAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRggEDVWELRKRIGLv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 ---LPQDFsmYPNMTVYKAmdylaVLS---------DIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQS 147
Cdd:COG1119 84 spaLQLRF--PRDETVLDV-----VLSgffdsiglyREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 148 LIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRI--VILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL---AKL 222
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAptLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVltsENL 236
|
250
....*....|....
gi 497584106 223 AEEKVYSIEVDKKD 236
Cdd:COG1119 237 SEAFGLPVEVERRD 250
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-167 |
2.12e-32 |
|
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: 118.79 E-value: 2.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK----EIRNMVGY 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGeVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKkninELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSMYPNMTVYKAMdylaVLSDIPLRKRRKIIA-----KLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRV 154
Cdd:cd03262 81 VFQQFNLFPHLTVLENI----TLAPIKVKGMSKAEAeeralELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170
....*....|...
gi 497584106 155 LIVDEPTAGLDPE 167
Cdd:cd03262 157 MLFDEPTSALDPE 169
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-190 |
3.36e-32 |
|
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: 116.71 E-value: 3.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFG--KKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGY 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKvAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRdlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSMYpNMTVYKamdylavlsdiplrkrrkiiakllskvNLtnyqnvkvksLSGGMNRRLGIAQSLIHNPRVLIVDE 159
Cdd:cd03228 81 VPQDPFLF-SGTIRE---------------------------NI----------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190
....*....|....*....|....*....|.
gi 497584106 160 PTAGLDPEERIRFRNLLCEIANDRIVILSTH 190
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAH 153
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-165 |
3.64e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 124.02 E-value: 3.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSGM-FGLLGRNGAGKTTFMRILATLLSKTEGSIHMcgvpienTKEIRnmVGYLPQDFS 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDrIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-------PKGLR--IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 86 MYPNMTVYKA-MDYLAVLSDIpLRKRRKI--------------------------------IAKLLSKVNLT-NYQNVKV 131
Cdd:COG0488 72 LDDDLTVLDTvLDGDAELRAL-EAELEELeaklaepdedlerlaelqeefealggweaearAEEILSGLGFPeEDLDRPV 150
|
170 180 190
....*....|....*....|....*....|....
gi 497584106 132 KSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLD 165
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-219 |
4.33e-32 |
|
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: 118.94 E-value: 4.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGK-KQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI--ENTKEIRNMVGYL 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFlVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIreQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNL--TNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497584106 159 EPTAGLDPEERIR----FRNLLCEIAndRIVILSTHivgDI-EATC--ENVAILNSGKVIYNGSTEAL 219
Cdd:cd03295 161 EPFGALDPITRDQlqeeFKRLQQELG--KTIVFVTH---DIdEAFRlaDRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-213 |
6.40e-32 |
|
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: 118.11 E-value: 6.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGYLPQD 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFfTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497584106 164 LDPEERirfRNLLCEIAN--DRI---VILSTHIVGDIEATCENVAILNSGKV--------IYN 213
Cdd:cd03300 161 LDLKLR---KDMQLELKRlqKELgitFVFVTHDQEEALTMSDRIAVMNKGKIqqigtpeeIYE 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-228 |
2.44e-31 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 123.02 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFG--KKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGY 79
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERvAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqiDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSMYP-----NMT----------VYKAMDYLAVLSDI---PLRkrrkiiakllskvnltnYQNV---KVKSLSGGM 138
Cdd:COG2274 554 VLQDVFLFSgtireNITlgdpdatdeeIIEAARLAGLHDFIealPMG-----------------YDTVvgeGGSNLSGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 139 NRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTH---IVGDieatCENVAILNSGKVIYNGS 215
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHrlsTIRL----ADRIIVLDKGRIVEDGT 692
|
250
....*....|...
gi 497584106 216 TEALakLAEEKVY 228
Cdd:COG2274 693 HEEL--LARKGLY 703
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-210 |
3.30e-31 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 115.58 E-value: 3.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKK-QALDNINLEIDSGMFG-LLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE-----IRNMV 77
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVfLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 78 GYLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIV 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497584106 158 DEPTAGLDPEERIRFRNLLCEIaNDR--IVILSTHIVGDIEATCENVAILNSGKV 210
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKI-NKAgtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-167 |
6.19e-31 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 115.48 E-value: 6.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK----EIRNMVGY 79
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGeVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKkdinKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSMYPNMTVykaMDYLAvLSDIPLRKRRKIIAK-----LLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRV 154
Cdd:COG1126 82 VFQQFNLFPHLTV---LENVT-LAPIKVKKMSKAEAEerameLLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170
....*....|...
gi 497584106 155 LIVDEPTAGLDPE 167
Cdd:COG1126 158 MLFDEPTSALDPE 170
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-211 |
7.04e-31 |
|
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: 113.29 E-value: 7.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIentkEIRNmvgylpqd 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGeVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV----SFAS-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 fsmypnmtvykamdylavlsdiPLRKRRKIIAkllskvnlTNYQnvkvksLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:cd03216 69 ----------------------PRDARRAGIA--------MVYQ------LSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497584106 164 LDPEERIRFRNLLCEIANDRI-VILSTHIVGDIEATCENVAILNSGKVI 211
Cdd:cd03216 113 LTPAEVERLFKVIRRLRAQGVaVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
9-214 |
7.79e-31 |
|
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: 114.70 E-value: 7.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 9 NLSKRFGKKQA---LdNINLEIDSGMFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNM------VGY 79
Cdd:cd03297 1 MLCVDIEKRLPdftL-KIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLppqqrkIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSMYPNMTVYKAMDY-LAVLSDIPLRKRrkiIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVD 158
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFgLKRKRNREDRIS---VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497584106 159 EPTAGLDPEERIRFRNLLCEIAND--RIVILSTHIVGDIEATCENVAILNSGKVIYNG 214
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-220 |
1.21e-30 |
|
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: 114.45 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENT---KEIRNMVGYLPQ 82
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGeIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpphERARAGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 DFSMYPNMTVykaMDYLAV-LSDIPLRKRRKIIAKLLSKV-NLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:cd03224 83 GRRIFPELTV---EENLLLgAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497584106 161 TAGLDP--EERIrFRnLLCEIANDRI-VILSTHIVGDIEATCENVAILNSGKVIYNGSTEALA 220
Cdd:cd03224 160 SEGLAPkiVEEI-FE-AIRELRDEGVtILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-196 |
2.17e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 116.72 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGYLP 81
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGqMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 QDFSMYPNMTVYkamDYLAV-LSDIPLRKR------RKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRV 154
Cdd:PRK10851 81 QHYALFRHMTVF---DNIAFgLTVLPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497584106 155 LIVDEPTAGLDPEERIRFRNLL---------------------CEIAnDRIVILSThivGDIE 196
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLrqlheelkftsvfvthdqeeaMEVA-DRVVVMSQ---GNIE 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-224 |
6.68e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.99 E-value: 6.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGK-----KQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE----NTKE 72
Cdd:PRK13637 1 MSIKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFvGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 73 IRNMVGYLPQdfsmYPNM-----TVYKAMDYLAV---LSDIPLRKRRKiiaKLLSKVNLtNYQNVKVKS---LSGGMNRR 141
Cdd:PRK13637 81 IRKKVGLVFQ----YPEYqlfeeTIEKDIAFGPInlgLSEEEIENRVK---RAMNIVGL-DYEDYKDKSpfeLSGGQKRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 142 LGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEI--ANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhkEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
....*
gi 497584106 220 AKLAE 224
Cdd:PRK13637 233 FKEVE 237
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-211 |
1.00e-29 |
|
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: 111.58 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQ-ALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENtKEIRNMVGYLPQD- 83
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGeIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRKSIGYVMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 -FSMYPNmTVYKAMDylavLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTA 162
Cdd:cd03226 81 dYQLFTD-SVREELL----LGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497584106 163 GLDPEERIRFRNLLCEIAN-DRIVILSTHivgDIE---ATCENVAILNSGKVI 211
Cdd:cd03226 156 GLDYKNMERVGELIRELAAqGKAVIVITH---DYEflaKVCDRVLLLANGAIV 205
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-227 |
1.47e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 112.29 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 9 NLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSI-----HMCGVPIEntKEIRNMVGYLPQ 82
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGeIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddeDISLLPLH--ARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 DFSMYPNMTVY-KAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPT 161
Cdd:PRK10895 86 EASIFRRLSVYdNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 162 AGLDPEERIRFRNLLCEIANDRI-VILSTHIVGDIEATCENVAILNSGKVIYNGSTEALakLAEEKV 227
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSGLgVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI--LQDEHV 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-220 |
4.23e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 110.87 E-value: 4.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCG--------VPIENTKEI 73
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGeTLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 74 RNMVGYLPQDFSMYPNMTVykaMDYLA-----VLsDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSL 148
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTV---MENLIeapckVL-GLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497584106 149 IHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIV-ILSTHIVGDIEATCENVAILNSGKVIYNGSTEALA 220
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITqVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFT 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-196 |
5.20e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.11 E-value: 5.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMkIAVSNLSKRFGK----KQALDNINLEIDSGMFG-LLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRN 75
Cdd:COG4525 1 MSM-LTVRHVSVRYPGggqpQPALQDVSLTIESGEFVvALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 76 MVGylpQDFSMYPNMTVykaMDYLAV---LSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNP 152
Cdd:COG4525 80 VVF---QKDALLPWLNV---LDNVAFglrLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497584106 153 RVLIVDEPTAGLDPEERIRFRNLLCEIAND--RIVILSTHivgDIE 196
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVWQRtgKGVFLITH---SVE 196
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-210 |
8.51e-29 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 109.27 E-value: 8.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGYLPQD 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFvVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSMYPNMTVYKAMDYLAVLSDIP---LRKRRKIIAKLLSkvnLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPkdeIDERVREVAELLQ---IEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497584106 161 TAGLDPEERIRFRNLLCEI--ANDRIVILSTHIVGDIEATCENVAILNSGKV 210
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLqqRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
10-225 |
1.04e-28 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 115.14 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 10 LSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSK---TEGSIHMCGVPIeNTKEIRNMVGYLPQDFS 85
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGeLLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI-DAKEMRAISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 86 MYPNMTVYKAMDYLAVL---SDIPLRKRRKIIAKLLSKVNLTNYQNVK------VKSLSGGMNRRLGIAQSLIHNPRVLI 156
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497584106 157 VDEPTAGLDPEERIRFRNLLCEIAND-RIVILSTH-IVGDIEATCENVAILNSGKVIYNGSTEALAKLAEE 225
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHqPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSD 260
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-219 |
1.58e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 110.10 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLS--KTEGS-IHMCGVPIE-------N 69
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGeMVALLGPSGSGKSTLLRHLSGLITgdKSAGShIELLGRTVQregrlarD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 70 TKEIRNMVGYLPQDFSMYPNMTVYKAMdYLAVLSDIPL---------RKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNR 140
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENV-LIGALGSTPFwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 141 RLGIAQSLIHNPRVLIVDEPTAGLDPEE-RIRFRNLLCEIANDRI-VILSTHIVGDIEATCENVAILNSGKVIYNGSTEA 218
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESaRIVMDTLRDINQNDGItVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
.
gi 497584106 219 L 219
Cdd:PRK09984 240 F 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-243 |
2.55e-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: 114.73 E-value: 2.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGK--KQALDNINLEI-DSGMFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE-NTKEIRNMVGYL 80
Cdd:TIGR01257 929 VCVKNLVKIFEPsgRPAVDRLNITFyENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtNLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 161 TAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEALAKLAEEKVYSIEVDKkdIENI 240
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRK--MKNI 1166
|
...
gi 497584106 241 KSR 243
Cdd:TIGR01257 1167 QSQ 1169
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-219 |
3.86e-28 |
|
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: 110.14 E-value: 3.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRF----GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSK---TEGSIHMCGVPI-----ENTKEI 73
Cdd:COG0444 4 VRNLKVYFptrrGVVKAVDGVSFDVRRGeTLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklseKELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 74 R-NMVGYLPQDF--SMYPNMTVYKAM-DYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVkVKS----LSGGMNRRLGIA 145
Cdd:COG0444 84 RgREIQMIFQDPmtSLNPVMTVGDQIaEPLRIHGGLSKAEARERAIELLERVGLPDPERR-LDRypheLSGGMRQRVMIA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 146 QSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRI--VILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:COG0444 163 RALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGlaILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-215 |
7.01e-28 |
|
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: 108.29 E-value: 7.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF--GKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI---ENTKEIRNMVG 78
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFvAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 79 YLPQD---------------FSMyPNMTVykamdylavlsdiPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLG 143
Cdd:TIGR04520 81 MVFQNpdnqfvgatveddvaFGL-ENLGV-------------PREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 144 IAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHivgDIE--ATCENVAILNSGKVIYNGS 215
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITH---DMEeaVLADRVIVMNKGKIVAEGT 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-221 |
7.48e-28 |
|
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: 112.55 E-value: 7.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF--GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGY 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGeRVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdlDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQD---FsmypNMTVykaMDYLAV----LSDIPLRKrrkiiakLLSKVNLTNYqnvkVKS---------------LSGG 137
Cdd:COG4987 414 VPQRphlF----DTTL---RENLRLarpdATDEELWA-------ALERVGLGDW----LAAlpdgldtwlgeggrrLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 138 MNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEAtCENVAILNSGKVIYNGSTE 217
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHE 554
|
....
gi 497584106 218 ALAK 221
Cdd:COG4987 555 ELLA 558
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-219 |
1.53e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 109.04 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 9 NLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTkEIRN----MVGylpQD 83
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGtMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHR-SIQQrdicMVF---QS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 164 LDPEERIRFRNLLCEIaNDRIVILS---THIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK11432 167 LDANLRRSMREKIREL-QQQFNITSlyvTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-227 |
1.61e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.88 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNM- 76
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGeVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrSPRDAQAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 VGYLPQDFSMYPNMTVY------------KAMDYlavlsdiplRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGI 144
Cdd:COG1129 81 IAIIHQELNLVPNLSVAeniflgreprrgGLIDW---------RAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 145 AQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRI-VILSTHIVGDIEATCENVAILNSGKVIyngSTEALAKLA 223
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVaIIYISHRLDEVFEIADRVTVLRDGRLV---GTGPVAELT 228
|
....
gi 497584106 224 EEKV 227
Cdd:COG1129 229 EDEL 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-196 |
2.02e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 106.71 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGylpQDFS 85
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGeLLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVF---QNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 86 MYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLD 165
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190
....*....|....*....|....*....|...
gi 497584106 166 PEERIRFRNLLCEIAND--RIVILSTHivgDIE 196
Cdd:PRK11248 161 AFTREQMQTLLLKLWQEtgKQVLLITH---DIE 190
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-218 |
2.23e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 106.25 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE-----NTKEIRNM 76
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGeTLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsktpSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 ---VGYLPQDFSMYPNMTVykaMDYL-------AVLSDIPLRKRRKiiaKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQ 146
Cdd:PRK11124 81 rrnVGMVFQQYNLWPHLTV---QQNLieapcrvLGLSKDQALARAE---KLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497584106 147 SLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRI--VILsTHIVGDIEATCENVAILNSGKVIYNGSTEA 218
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGItqVIV-THEVEVARKTASRVVYMENGHIVEQGDASC 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3-219 |
2.81e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 109.16 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENT--KEIRNMVGY 79
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLvGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsaRAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSMYPNMTVYKAMDylavLSDIPLRKR--------RKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHN 151
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVE----MGRTPHRSRfdtwtetdRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497584106 152 PRVLIVDEPTAGLDPEERIRFRNLLCEIAND-RIVILSTHivgDIEAT---CENVAILNSGKVIYNGSTEAL 219
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIH---DLDLAaryCDELVLLADGRVRAAGPPADV 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-219 |
1.28e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 104.40 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGV----PIENTKEIRNMVGY 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGeVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvndPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSMYPNMTvykAMDYLAVLsdiPLRKR-------RKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNP 152
Cdd:PRK09493 82 VFQQFYLFPHLT---ALENVMFG---PLRVRgaskeeaEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497584106 153 RVLIVDEPTAGLDPEERIRFRNLLCEIANDRI-VILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMtMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-217 |
2.71e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.07 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGYLPQDFS 85
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGeIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 86 MYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLD 165
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497584106 166 PEERIRFRNLLCEIAnDRI---VILSTHIVGDIEATCENVAILNSGKVIYNGSTE 217
Cdd:PRK11607 182 KKLRDRMQLEVVDIL-ERVgvtCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-216 |
3.07e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 104.78 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGKK-----QALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGV----------- 65
Cdd:PRK13651 1 MQIKVKNIVKIFNKKlptelKALDNVSVEINQGEFiAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKdeknkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 66 ---------------PIENTKEIRNMVGYLPQdFSMYP--NMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNL-TNYQ 127
Cdd:PRK13651 81 ekvleklviqktrfkKIKKIKEIRRRVGVVFQ-FAEYQlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 128 NVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEI-ANDRIVILSTHIVGDIEATCENVAILN 206
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
250
....*....|
gi 497584106 207 SGKVIYNGST 216
Cdd:PRK13651 240 DGKIIKDGDT 249
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-217 |
4.01e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.07 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 4 KIAVSNLSKRFGKKQALDNINLEI-DSGMFGLLGRNGAGKTTFMRILATLL-----SKTEGSIHMCGVPI--ENTKEIRN 75
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIpDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfkMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 76 MVGYLPQDFSMYPNMTVYKAMDYLAVLSDIpLRKRRKIIAKL---LSKVNL----TNYQNVKVKSLSGGMNRRLGIAQSL 148
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLNRL-VKSKKELQERVrwaLEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 149 IHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTE 217
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTR 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-219 |
4.39e-26 |
|
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: 103.49 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 10 LSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNM----VGYLPQ 82
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGeIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamSRKELRELrrkkISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 DFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTA 162
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497584106 163 GLDPEERIRFRNLLCEIAND--RIVILSTHivgD-IEAT--CENVAILNSGKVIYNGSTEAL 219
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAElqKTIVFITH---DlDEALrlGDRIAIMKDGRLVQVGTPEEI 248
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-192 |
5.04e-26 |
|
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: 101.35 E-value: 5.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 15 GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK----EIRNMVGYLPQDfsmyPN 89
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGeVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRkgllERRQRVGLVFQD----PD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 90 MTVYKAmdylAVLSDIPLRKR---------RKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:TIGR01166 79 DQLFAA----DVDQDVAFGPLnlglseaevERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 497584106 161 TAGLDPEERIRFRNLLCEI-ANDRIVILSTHIV 192
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLrAEGMTVVISTHDV 187
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-208 |
8.72e-26 |
|
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: 101.77 E-value: 8.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 20 LDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRnMVGYlpQDFSMYPNMTVYKAMdY 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFiSLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR-MVVF--QNYSLLPWLTVRENI-A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 99 LAV---LSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNL 175
Cdd:TIGR01184 77 LAVdrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 497584106 176 LCEIANDR--IVILSTHIVGDIEATCENVAILNSG 208
Cdd:TIGR01184 157 LMQIWEEHrvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-219 |
8.99e-26 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 106.75 E-value: 8.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEiRNMVG----Y 79
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGcMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARH-RRAVCpriaY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDF--SMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIV 157
Cdd:NF033858 81 MPQGLgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 158 DEPTAGLDPEERIRFRNLLCEIANDR---IVILSThivGDIE--ATCENVAILNSGKVIYNGSTEAL 219
Cdd:NF033858 161 DEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVAT---AYMEeaERFDWLVAMDAGRVLATGTPAEL 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-219 |
1.45e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 101.75 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMkIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK-------- 71
Cdd:PRK11264 1 MSA-IEVKNLVKKFHGQTVLHGIDLEVKPGeVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 72 --EIRNMVGYLPQDFSMYPNMTVYK-AMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSL 148
Cdd:PRK11264 80 irQLRQHVGFVFQNFNLFPHRTVLEnIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497584106 149 IHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAND-RIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-191 |
1.57e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 100.33 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVgYL- 80
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGeALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH-YLg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDFsMYPNMTVykaMDYLAVLSDIpLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:PRK13539 80 HRNA-MKPALTV---AENLEFWAAF-LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 497584106 161 TAGLDPEERIRFRNLLCE-IANDRIVILSTHI 191
Cdd:PRK13539 155 TAALDAAAVALFAELIRAhLAQGGIVIAATHI 186
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-232 |
1.80e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 101.35 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 6 AVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE--IRNM-VGYLP 81
Cdd:COG4674 12 YVEDLTVSFDGFKALNDLSLYVDPGeLRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEheIARLgIGRKF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 QDFSMYPNMTVYKAMDyLAVLSDIP----LRKRRK-----IIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNP 152
Cdd:COG4674 92 QKPTVFEELTVFENLE-LALKGDRGvfasLFARLTaeerdRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 153 RVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEALAklAEEKVysIEV 232
Cdd:COG4674 171 KLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQ--ADPRV--IEV 246
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-220 |
2.39e-25 |
|
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: 100.83 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMkIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK--EI-RNM 76
Cdd:COG0410 1 MPM-LEVENLHAGYGGIHVLHGVSLEVEEGeIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPphRIaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 VGYLPQDFSMYPNMTVykaMDYLAVLSdiPLRKRRKIIAKLLSKV-----NLTNYQNVKVKSLSGG---MnrrLGIAQSL 148
Cdd:COG0410 80 IGYVPEGRRIFPSLTV---EENLLLGA--YARRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGeqqM---LAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 149 IHNPRVLIVDEPTAGLDP------EERIRfrnllcEIANDRIVIL----STHIVGDIeatCENVAILNSGKVIYNGSTEA 218
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPliveeiFEIIR------RLNREGVTILlveqNARFALEI---ADRAYVLERGRIVLEGTAAE 222
|
..
gi 497584106 219 LA 220
Cdd:COG0410 223 LL 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-232 |
2.68e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.00 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK--EIRNMVGY 79
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGeVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSM-YPnMTVYK--AMDyLAVLSDIPLRKRRkIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLI------H 150
Cdd:PRK13548 81 LPQHSSLsFP-FTVEEvvAMG-RAPHGLSRAEDDA-LVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 151 NPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR----IVILstHivgDIEAT---CENVAILNSGKVIYNGS-TEALAKL 222
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglavIVVL--H---DLNLAaryADRIVLLHQGRLVADGTpAEVLTPE 232
|
250
....*....|
gi 497584106 223 AEEKVYSIEV 232
Cdd:PRK13548 233 TLRRVYGADV 242
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-214 |
7.09e-25 |
|
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: 99.14 E-value: 7.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF----------------------GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIH 61
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGeRIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 62 MCG--VPIentkeIRNMVGylpqdfsMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMN 139
Cdd:cd03220 81 VRGrvSSL-----LGLGGG-------FNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 140 RRLGIAQSLIHNPRVLIVDEPTAGLDPEERIR-FRNLLCEIANDRIVILSTHIVGDIEATCENVAILNSGKVIYNG 214
Cdd:cd03220 149 ARLAFAIATALEPDILLIDEVLAVGDAAFQEKcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-197 |
2.00e-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: 97.43 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEI--RNM--VGY 79
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGeALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphENIlyLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPqdfSMYPNMTVYKAMDYLAVLsdipLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDE 159
Cdd:TIGR01189 81 LP---GLKPELSALENLHFWAAI----HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 497584106 160 PTAGLDPEERIRFRNLLCE-IANDRIVILSTHI-VGDIEA 197
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAhLARGGIVLLTTHQdLGLVEA 193
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-167 |
3.24e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSGM-FGLLGRNGAGKTTFMRILATLLSKTEGSIHMcGvpiENTKeirnmVGYLPQD 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDrIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-G---ETVK-----IGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 F-SMYPNMTVYkamDYLAVLSDiplRKRRKIIAKLLSKVNLT-NYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPT 161
Cdd:COG0488 387 QeELDPDKTVL---DELRDGAP---GGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
....*.
gi 497584106 162 AGLDPE 167
Cdd:COG0488 461 NHLDIE 466
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-165 |
4.15e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.02 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGYLPQD 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFlTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
..
gi 497584106 164 LD 165
Cdd:PRK09452 175 LD 176
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-219 |
4.80e-24 |
|
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: 101.37 E-value: 4.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF-GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN--TKEIRNMVGYL 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGeRVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDldPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDfsmyP---------NMTVYKAmdylavlsDIPlrkrRKIIAKLLSKVNLTNYqnvkVKS---------------LSG 136
Cdd:COG4988 417 PQN----PylfagtireNLRLGRP--------DAS----DEELEAALEAAGLDEF----VAAlpdgldtplgeggrgLSG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 137 GMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEAtCENVAILNSGKVIYNGST 216
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTH 555
|
...
gi 497584106 217 EAL 219
Cdd:COG4988 556 EEL 558
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-245 |
9.93e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.37 E-value: 9.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFG--KKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI--ENTKEIRNMVGY 79
Cdd:PRK13632 8 IKVENVSFSYPnsENNALKNVSFEINEGEYvAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIskENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQD-FSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVD 158
Cdd:PRK13632 88 IFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 159 EPTAGLDPEERIRFRNLLCEIANDR--IVILSTHivgDI-EAT-CENVAILNSGKVIYNGSTEalaklaeekvySIEVDK 234
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRkkTLISITH---DMdEAIlADKVIVFSEGKLIAQGKPK-----------EILNNK 233
|
250
....*....|...
gi 497584106 235 KDIENIK--SRFI 245
Cdd:PRK13632 234 EILEKAKidSPFI 246
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-217 |
1.32e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.33 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF----GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEI---R 74
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGeIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 75 NMVGYLPQDFSMYPNMTVYkamDYLAV---LSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHN 151
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVF---DNVALpleLAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 152 PRVLIVDEPTAGLDPEERIRFRNLLCEIaNDRI---VILSTHIVGDIEATCENVAILNSGKVIYNGSTE 217
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDI-NRELgltIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVS 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-219 |
1.60e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.21 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 16 KKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI------ENTKEIRNMVGYLPQdfsmYP 88
Cdd:PRK13641 19 EKKGLDNISFELEEGSFvALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgnKNLKKLRKKVSLVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 89 NMTVYKAmdylAVLSDI---PL------RKRRKIIAKLLSKVNLTnyQNVKVKS---LSGGMNRRLGIAQSLIHNPRVLI 156
Cdd:PRK13641 95 EAQLFEN----TVLKDVefgPKnfgfseDEAKEKALKWLKKVGLS--EDLISKSpfeLSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497584106 157 VDEPTAGLDPEERIRFRNLLCEI-ANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK13641 169 LDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-219 |
1.69e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.58 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 2 EMKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGvpiENTKEIRNMVGYL 80
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGdVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG---QTINLVRDKDGQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 P------------------QDFSMYPNMTVYK-AMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKS-LSGGMNR 140
Cdd:PRK10619 80 KvadknqlrllrtrltmvfQHFNLWSHMTVLEnVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 141 RLGIAQSLIHNPRVLIVDEPTAGLDPE---ERIRFRNLLCEIANDRIVIlsTHIVGDIEATCENVAILNSGKVIYNGSTE 217
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVV--THEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
..
gi 497584106 218 AL 219
Cdd:PRK10619 238 QL 239
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-217 |
3.19e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.15 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRF----------------------GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTE 57
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGeSVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 58 GSIHMCG---VPIEntkeirnmVGylpqdFSMYPNMTVYKAMDYLAVLsdipLRKRRKIIAKLLSKV----NLTNYQNVK 130
Cdd:COG1134 81 GRVEVNGrvsALLE--------LG-----AGFHPELTGRENIYLNGRL----LGLSRKEIDEKFDEIvefaELGDFIDQP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 131 VKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAND-RIVILSTHIVGDIEATCENVAILNSGK 209
Cdd:COG1134 144 VKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
....*...
gi 497584106 210 VIYNGSTE 217
Cdd:COG1134 224 LVMDGDPE 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-217 |
3.48e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.49 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQALDNINLEIDSGM-FGLLGRNGAGKTTFMRILATLL-----SKTEGSIHMCGVPIENTK--- 71
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKvTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDIYDPDvdv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 72 -EIRNMVGYLPQdfsmYPN---MTVYKAMDYLAVLSDIplRKRRK---IIAKLLSKVNLtnYQNVKVK------SLSGGM 138
Cdd:COG1117 88 vELRRRVGMVFQ----KPNpfpKSIYDNVAYGLRLHGI--KSKSEldeIVEESLRKAAL--WDEVKDRlkksalGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 139 NRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHI------VGDieatceNVAILNSGKVIY 212
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNmqqaarVSD------YTAFFYLGELVE 233
|
....*
gi 497584106 213 NGSTE 217
Cdd:COG1117 234 FGPTE 238
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-214 |
3.53e-23 |
|
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: 94.58 E-value: 3.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 19 ALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGYLPQD---F--SMYPNM 90
Cdd:cd03245 19 ALDNVSLTIRAGeKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPADLRRNIGYVPQDvtlFygTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 91 TvykamdylavLSDIPLRKRRKIIAKLLSKVN-LTNYQ----NVKV----KSLSGGMNRRLGIAQSLIHNPRVLIVDEPT 161
Cdd:cd03245 99 T----------LGAPLADDERILRAAELAGVTdFVNKHpnglDLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 162 AGLD--PEERI--RFRNLLCeianDRIVILSTHIVGdIEATCENVAILNSGKVIYNG 214
Cdd:cd03245 169 SAMDmnSEERLkeRLRQLLG----DKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-210 |
3.68e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 95.51 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE-IRNMVgylpQ 82
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFvAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREdTRLMF----Q 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 DFSMYPNMTVykaMDYLAvlsdIPLR-KRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPT 161
Cdd:PRK11247 89 DARLLPWKKV---IDNVG----LGLKgQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497584106 162 AGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKV 210
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-210 |
4.13e-23 |
|
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: 93.05 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQA--LDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGY 79
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGeSLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDfsmypnmtvykamdylavlsdiplrkrrkiiAKLLSKvnlTNYQNVkvksLSGGMNRRLGIAQSLIHNPRVLIVDE 159
Cdd:cd03246 81 LPQD-------------------------------DELFSG---SIAENI----LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497584106 160 PTAGLDPE-ERIRFRNLLCEIANDRIVILSTHIVGDIEAtCENVAILNSGKV 210
Cdd:cd03246 123 PNSHLDVEgERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
18-221 |
4.97e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.68 E-value: 4.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 18 QALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK----EIRNMVGYLPQD-----FSMy 87
Cdd:PRK13636 20 HALKGININIKKGeVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglmKLRESVGMVFQDpdnqlFSA- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 88 pnmTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPE 167
Cdd:PRK13636 99 ---SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 168 ERIRFRNLLCEIAN--DRIVILSTHIVGDIEATCENVAILNSGKVIYNGS-TEALAK 221
Cdd:PRK13636 176 GVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNpKEVFAE 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-217 |
4.98e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.91 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQALDNINLEI-DSGMFGLLGRNGAGKTTFMRILATLL-----SKTEGSIHMCGVPIENTK--- 71
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIpQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPDvdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 72 -EIRNMVGYLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRR--KIIAKLLSKVNL----TNYQNVKVKSLSGGMNRRLGI 144
Cdd:PRK14267 81 iEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497584106 145 AQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTE 217
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-219 |
6.58e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.03 E-value: 6.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFG---------------KKQALD---------NINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSK 55
Cdd:PRK10070 1 MAIKLEIKNLYKIFGehpqrafkyieqglsKEQILEktglslgvkDASLAIEEGeIFVIMGLSGSGKSTMVRLLNRLIEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 56 TEGSIHMCGVPIENTKEI------RNMVGYLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNV 129
Cdd:PRK10070 81 TRGQVLIDGVDIAKISDAelrevrRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 130 KVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEI--ANDRIVILSTHIVGDIEATCENVAILNS 207
Cdd:PRK10070 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
250
....*....|..
gi 497584106 208 GKVIYNGSTEAL 219
Cdd:PRK10070 241 GEVVQVGTPDEI 252
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-215 |
8.60e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.19 E-value: 8.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 18 QALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENT------KEIRNMVGYLPQdfsmYPNM 90
Cdd:PRK13643 20 RALFDIDLEVKKGSYtALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkeiKPVRKKVGVVFQ----FPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 91 TVYKAmdylAVLSDIPL---------RKRRKIIAKLLSKVNLTN-YQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:PRK13643 96 QLFEE----TVLKDVAFgpqnfgipkEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 161 TAGLDPEERIRFRNLLCEI-ANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGS 215
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-217 |
1.77e-22 |
|
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: 96.80 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF-----GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGS---------IHMCGVPIEN 69
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGeIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnvrvgdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 70 TKEIRNMVGYLPQDFSMYPNMTVykaMDYL--AVLSDIP--LRKRRKIIAklLSKVNLTNYQNVKV-----KSLSGGMNR 140
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPHRTV---LDNLteAIGLELPdeLARMKAVIT--LKMVGFDEEKAEEIldkypDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 141 RLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNllcEIANDRIVILSTHIVGD-----IEATCENVAILNSGKVIYNGS 215
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTH---SILKAREEMEQTFIIVShdmdfVLDVCDRAALMRDGKIVKIGD 511
|
..
gi 497584106 216 TE 217
Cdd:TIGR03269 512 PE 513
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-208 |
2.82e-22 |
|
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: 97.01 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 19 ALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-ENTKEIRNMVGYLPQdFSMYPNMTVYKAM 96
Cdd:TIGR01257 1954 AVDRLCVGVRPGeCFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQNMGYCPQ-FDAIDDLLTGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 97 DYL-AVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNL 175
Cdd:TIGR01257 2033 LYLyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170 180 190
....*....|....*....|....*....|....
gi 497584106 176 LCEIAND-RIVILSTHIVGDIEATCENVAILNSG 208
Cdd:TIGR01257 2113 IVSIIREgRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-219 |
3.31e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.75 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN--TKEIRNM-VGYL 80
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQeIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlpGHQIARMgVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDFSMYPNMTVYKAM----------DYLAVLSDIPL--RKRRKII---AKLLSKVNLTNYQNVKVKSLSGGMNRRLGIA 145
Cdd:PRK11300 86 FQHVRLFREMTVIENLlvaqhqqlktGLFSGLLKTPAfrRAESEALdraATWLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 146 QSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-214 |
3.46e-22 |
|
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: 90.84 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFG--KKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN-TKEIRNMVGYL 80
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGeKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDlEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDFSMYpnmtvykamdylavlsdiplrkrrkiiakllskvNLTNYQNVKvKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:cd03247 81 NQRPYLF----------------------------------DTTLRNNLG-RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497584106 161 TAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEATcENVAILNSGKVIYNG 214
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-211 |
5.16e-22 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 91.73 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF----GKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE-----IR 74
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESvAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdararLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 75 N-MVGYLPQDFSMYPNMTvykAMDYLAVlsdiPL-----RKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSL 148
Cdd:COG4181 89 ArHVGFVFQSFQLLPTLT---ALENVML----PLelagrRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497584106 149 IHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEAtCENVAILNSGKVI 211
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAAR-CDRVLRLRAGRLV 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-166 |
6.04e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.07 E-value: 6.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGK-----KQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIR--NM 76
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFvTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKraKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 VGYLPQDFSM--YPNMTVYK--AMDY---------LAVLsdiplRKRRKIIAKLLSKVN--LTNYQNVKVKSLSGGMNRR 141
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEEnlALAYrrgkrrglrRGLT-----KKRRELFRELLATLGlgLENRLDTKVGLLSGGQRQA 156
|
170 180
....*....|....*....|....*
gi 497584106 142 LGIAQSLIHNPRVLIVDEPTAGLDP 166
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDP 181
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-215 |
7.72e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.06 E-value: 7.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 18 QALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK----EIRNMVGYL---PQDFSMYPn 89
Cdd:PRK13639 16 EALKGINFKAEKGeMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKksllEVRKTVGIVfqnPDDQLFAP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 90 mTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEER 169
Cdd:PRK13639 95 -TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497584106 170 IRFRNLLCEIANDRI-VILSTHIVGDIEATCENVAILNSGKVIYNGS 215
Cdd:PRK13639 174 SQIMKLLYDLNKEGItIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
2.55e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.95 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGK-KQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI--ENTKEIRNM 76
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGsKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnaENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 VGYLPQD-----FSMypnmTVYKAMDYLAV---LSDIPLRKRrkiIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSL 148
Cdd:PRK13647 81 VGLVFQDpddqvFSS----TVWDDVAFGPVnmgLDKDEVERR---VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 149 IHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAND-RIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEALA--KLAEE 225
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTdeDIVEQ 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
34-214 |
4.24e-21 |
|
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: 88.70 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 34 LLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGYLPQDFSMYPNMTVYKAMDyLAVLSDIPLR-KRRK 112
Cdd:cd03298 29 IVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVG-LGLSPGLKLTaEDRQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 113 IIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTH 190
Cdd:cd03298 108 AIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTH 187
|
170 180
....*....|....*....|....
gi 497584106 191 IVGDIEATCENVAILNSGKVIYNG 214
Cdd:cd03298 188 QPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-215 |
4.29e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.07 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEID-SGMFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE----IRNMVGY 79
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSlSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllaLRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDfsmyPNMTVYkamdYLAVLSDIPLRKRRKIIAK---------LLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIH 150
Cdd:PRK13638 82 VFQD----PEQQIF----YTDIDSDIAFSLRNLGVPEaeitrrvdeALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 151 NPRVLIVDEPTAGLDPEERIRFRNLLCEI-ANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGS 215
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-190 |
4.60e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 92.73 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF-GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGYL 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGeRVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdaDADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDFSMYPNmtvykamdylAVLSDIPLRKR---RKIIAKLLSKVNLTNY-------QNVKVKS----LSGGMNRRLGIAQ 146
Cdd:TIGR02857 402 PQHPFLFAG----------TIAENIRLARPdasDAEIREALERAGLDEFvaalpqgLDTPIGEggagLSGGQAQRLALAR 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 497584106 147 SLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTH 190
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
3-219 |
6.46e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.84 E-value: 6.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGK-----KQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN-TKE--- 72
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYyAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 73 --IRNMVGYLPQdfsmYPNM-----TVYKAMDYLAVLSDIPLRKRRKIIAKLLskVNLTNYQNVKVKS---LSGGMNRRL 142
Cdd:PRK13646 81 rpVRKRIGMVFQ----FPESqlfedTVEREIIFGPKNFKMNLDEVKNYAHRLL--MDLGFSRDVMSQSpfqMSGGQMRKI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 143 GIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAND--RIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
9-220 |
8.44e-21 |
|
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: 90.56 E-value: 8.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 9 NLSKRFGKKQaLDnINLEIDS-GMFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-ENTKEI-----RNMVGYLP 81
Cdd:TIGR02142 4 RFSKRLGDFS-LD-ADFTLPGqGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGIflppeKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 QDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKiiAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPT 161
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRARPSERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497584106 162 AGLDPEERIR----FRNLLCEIandRI-VILSTHIVGDIEATCENVAILNSGKVIYNGSTEALA 220
Cdd:TIGR02142 160 AALDDPRKYEilpyLERLHAEF---GIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-235 |
1.20e-20 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 88.31 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFG--KKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGY 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGeVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAlaDPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSMYpNMTVykaMDYLAVLSDIPLRKRRKIIAKL------LSKVNLTNYQNVKVK--SLSGGMNRRLGIAQSLIHN 151
Cdd:cd03252 81 VLQENVLF-NRSI---RDNIALADPGMSMERVIEAAKLagahdfISELPEGYDTIVGEQgaGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 152 PRVLIVDEPTAGLDPE-ERIRFRNLLcEIANDRIVILSTHIVGDIEaTCENVAILNSGKVIYNGSTEALakLAEEKVYSI 230
Cdd:cd03252 157 PRILIFDEATSALDYEsEHAIMRNMH-DICAGRTVIIIAHRLSTVK-NADRIIVMEKGRIVEQGSHDEL--LAENGLYAY 232
|
....*
gi 497584106 231 EVDKK 235
Cdd:cd03252 233 LYQLQ 237
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-197 |
2.02e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.77 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLS---KTEGSI-----HMCGVPIENtkeiRNmV 77
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGeILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVllngrRLTALPAEQ----RR-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 78 GYLPQDFSMYPNMTVYKAMDYlAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIV 157
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 497584106 158 DEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEA 197
Cdd:COG4136 158 DEPFSKLDAALRAQFREFVFEQIRQRgiPALLVTHDEEDAPA 199
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-215 |
3.00e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.88 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 19 ALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENT------KEIRNMVGYLPQdfsmYPNMT 91
Cdd:PRK13649 22 ALFDVNLTIEDGSYtAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkdiKQIRKKVGLVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 92 VYKAmdylAVLSDIPL---------RKRRKIIAKLLSKVNLTnyQNVKVKS---LSGGMNRRLGIAQSLIHNPRVLIVDE 159
Cdd:PRK13649 98 LFEE----TVLKDVAFgpqnfgvsqEEAEALAREKLALVGIS--ESLFEKNpfeLSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 160 PTAGLDPEERIRFRNLLCEIANDRIVI-LSTHIVGDIEATCENVAILNSGKVIYNGS 215
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSGMTIvLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-225 |
4.70e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.77 E-value: 4.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGKK-----QALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE---- 72
Cdd:PRK13634 1 MDITFQKVEHRYQYKtpferRALYDVNVSIPSGSYvAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 73 --IRNMVGYLPQdfsmYPNMTVYKAmdylAVLSDI---------PLRKRRKIIAKLLSKVNLTnyQNVKVKS---LSGGM 138
Cdd:PRK13634 81 kpLRKKVGIVFQ----FPEHQLFEE----TVEKDIcfgpmnfgvSEEDAKQKAREMIELVGLP--EELLARSpfeLSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 139 NRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKVIYNGST 216
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTP 230
|
....*....
gi 497584106 217 EALAKLAEE 225
Cdd:PRK13634 231 REIFADPDE 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-219 |
4.79e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 86.35 E-value: 4.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKkQALdNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGYLPQD 83
Cdd:COG3840 2 LRLDDLTYRYGD-FPL-RFDLTIAAGERvAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSMYPNMTVYKAMdYLAVLSDIPL-RKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTA 162
Cdd:COG3840 80 NNLFPHLTVAQNI-GLGLRPGLKLtAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 163 GLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
15-217 |
1.01e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.40 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 15 GKKQALDNINLEID-SGMFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI--ENTKEIRNMVGYL---PQDFSMYP 88
Cdd:PRK13652 15 GSKEALNNINFIAPrNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItkENIREVRKFVGLVfqnPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 89 NMTVYKAMDYLAVLSDIPLRKRRkiIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPE- 167
Cdd:PRK13652 95 TVEQDIAFGPINLGLDEETVAHR--VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQg 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497584106 168 --ERIRFRNLLCEIANdRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTE 217
Cdd:PRK13652 173 vkELIDFLNDLPETYG-MTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-209 |
1.32e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 82.88 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIhmcgvpienTKEIRNMVGYLPQd 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGdRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------TWGSTVKIGYFEQ- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 fsmypnmtvykamdylavlsdiplrkrrkiiakllskvnltnyqnvkvksLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:cd03221 71 --------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497584106 164 LDPEERIRFRNLLceIANDRIVILSTHivgD---IEATCENVAILNSGK 209
Cdd:cd03221 101 LDLESIEALEEAL--KEYPGTVILVSH---DryfLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-215 |
1.38e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.39 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 16 KKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLL---SKTEGSIHMCGVPI--ENTKEIRNMVGYLPQD-FSMYP 88
Cdd:PRK13640 19 KKPALNDISFSIPRGSWtALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLtaKTVWDIREKVGIVFQNpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 89 NMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEE 168
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497584106 169 RIRFRNLLCEIANDR--IVILSTHivgDIE--ATCENVAILNSGKVIYNGS 215
Cdd:PRK13640 179 KEQILKLIRKLKKKNnlTVISITH---DIDeaNMADQVLVLDDGKLLAQGS 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-267 |
1.86e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.70 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 19 ALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEiRNMVGYLPQ----DFSmYP----- 88
Cdd:PRK15056 22 ALRDASFTVPGGsIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ-KNLVAYVPQseevDWS-FPvlved 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 89 --NMTVYKAMDYLAvlsdIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDP 166
Cdd:PRK15056 100 vvMMGRYGHMGWLR----RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 167 EERIRFRNLLCEIAND-RIVILSTHIVGDIEATCEnVAILNSGKVIYNGSTEALAKLAE-EKVYSievdkkdieniksrf 244
Cdd:PRK15056 176 KTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFTAENlELAFS--------------- 239
|
250 260
....*....|....*....|....*...
gi 497584106 245 iviGMLTH----GGKAilRIISDD-KPF 267
Cdd:PRK15056 240 ---GVLRHvalnGSEE--SIITDDeRPF 262
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-232 |
2.42e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.68 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKiavsNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLL--SKTEGSIHMCGVPIE--NTKEI-R 74
Cdd:PRK13549 6 LEMK----NITKTFGGVKALDNVSLKVRAGeIVSLCGENGAGKSTLMKVLSGVYphGTYEGEIIFEGEELQasNIRDTeR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 75 NMVGYLPQDFSMYPNMTV------------YKAMDYLAVLSDIplrkrrkiiAKLLSKVNLTNYQNVKVKSLSGGMNRRL 142
Cdd:PRK13549 82 AGIAIIHQELALVKELSVleniflgneitpGGIMDYDAMYLRA---------QKLLAQLKLDINPATPVGNLGLGQQQLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 143 GIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIV-ILSTHIVGDIEATCENVAILNSGKVIyngSTEALAK 221
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIAcIYISHKLNEVKAISDTICVIRDGRHI---GTRPAAG 229
|
250
....*....|.
gi 497584106 222 LAEEKVYSIEV 232
Cdd:PRK13549 230 MTEDDIITMMV 240
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-214 |
2.46e-19 |
|
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: 83.45 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 15 GKKQALDNINLEIDSGMFG-LLGRNGAGKTTFMRILA--TLLSKTEGSIHMCGVPIenTKEIRNMVGYLPQDFSMYPNMT 91
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTaLMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPL--DKNFQRSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 92 VYKAMDYLAVLSDIPLRKRrkiiakllskvnltnyqnvkvkslsggmnRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIR 171
Cdd:cd03232 96 VREALRFSALLRGLSVEQR-----------------------------KRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497584106 172 FRNLLCEIAND-RIVILSTH-IVGDIEATCENVAIL-NSGKVIYNG 214
Cdd:cd03232 147 IVRFLKKLADSgQAILCTIHqPSASIFEKFDRLLLLkRGGKTVYFG 192
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-230 |
2.57e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 9 NLSKRFGKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN--TKEIRNMVGYLPQDFS 85
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFtAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaSKEVARRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 86 MYPNMTVYKAMDYlAVLSDIPLRKR-RK----IIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:PRK10253 92 TPGDITVQELVAR-GRYPHQPLFTRwRKedeeAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497584106 161 TAGLDPEERIRFRNLLCEIANDRIVILSThIVGDIEATCE---NVAILNSGKVIYNGS-TEALAKLAEEKVYSI 230
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAA-VLHDLNQACRyasHLIALREGKIVAQGApKEIVTAELIERIYGL 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-247 |
2.66e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.55 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATL--LSKTEGSI--HM----------------- 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGeVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyHValcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 63 ----CGVPIEN------------TKEIRNMVGYLPQ-DFSMYPNMTVYKamDYLAVLSDI--PLRKRRKIIAKLLSKVNL 123
Cdd:TIGR03269 81 pcpvCGGTLEPeevdfwnlsdklRRRIRKRIAIMLQrTFALYGDDTVLD--NVLEALEEIgyEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 124 TNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCE--IANDRIVILSTHIVGDIEATCEN 201
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 497584106 202 VAILNSGKVIYNG-STEALAKLAE-----EKVYSIEVdKKDI---ENIKSRFIVI 247
Cdd:TIGR03269 239 AIWLENGEIKEEGtPDEVVAVFMEgvsevEKECEVEV-GEPIikvRNVSKRYISV 292
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-232 |
3.16e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.68 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 3 MKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGY 79
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGkITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmlSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSMYPNMTV-----YKAMDYLAV---LSDiplrKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHN 151
Cdd:PRK11231 81 LPQHHLTPEGITVrelvaYGRSPWLSLwgrLSA----EDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 152 PRVLIVDEPTAGLDPEERIRFRNLLCEI-ANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGS-----TEALAKlaee 225
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTpeevmTPGLLR---- 232
|
....*..
gi 497584106 226 KVYSIEV 232
Cdd:PRK11231 233 TVFDVEA 239
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-191 |
4.73e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 82.93 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEI--RNMVgYLP 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGeALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiaRGLL-YLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 QDFSMYPNMTVYKAMDYLAVLSDiplrkrRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPT 161
Cdd:cd03231 80 HAPGIKTTLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|.
gi 497584106 162 AGLDPEERIRFRNLLC-EIANDRIVILSTHI 191
Cdd:cd03231 154 TALDKAGVARFAEAMAgHCARGGMVVLTTHQ 184
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-165 |
4.86e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.01 E-value: 4.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIhmcgvpiENTKEIRnmVGY 79
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGkILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------KRNGKLR--IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSMYPNM--TVYKAMDylavlsdipLRK--RRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVL 155
Cdd:PRK09544 72 VPQKLYLDTTLplTVNRFLR---------LRPgtKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170
....*....|
gi 497584106 156 IVDEPTAGLD 165
Cdd:PRK09544 143 VLDEPTQGVD 152
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-219 |
5.05e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.76 E-value: 5.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDS-GMFGLLGRNGAGKTTFMRILATLLSKTEG-----SIHMCGVPIENTK---EIRN 75
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPArAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRdvlEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 76 MVGYLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKS----LSGGMNRRLGIAQSLIHN 151
Cdd:PRK14271 102 RVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497584106 152 PRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-215 |
5.16e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 84.75 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 17 KQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVP---IENTKEIRNMVGYLPQDfsmyPNMTV 92
Cdd:PRK13633 23 KLALDDVNLEVKKGEFlVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdEENLWDIRNKAGMVFQN----PDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 93 YKAMdylaVLSD---------IPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:PRK13633 99 VATI----VEEDvafgpenlgIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497584106 164 LDPEERIRFRNLLCEIaNDR---IVILSTHIVgDIEATCENVAILNSGKVIYNGS 215
Cdd:PRK13633 175 LDPSGRREVVNTIKEL-NKKygiTIILITHYM-EEAVEADRIIVMDSGKVVMEGT 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-190 |
6.04e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.28 E-value: 6.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 13 RFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIH-MCGVPientkeirnmVGYLPQDFSMYPNM 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGsLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRrAGGAR----------VAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 91 --TVYKAMDyLAVLSDIPLRKR-----RKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:NF040873 71 plTVRDLVA-MGRWARRGLWRRltrddRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180
....*....|....*....|....*...
gi 497584106 164 LDPEERIRFRNLLCEIAND-RIVILSTH 190
Cdd:NF040873 150 LDAESRERIIALLAEEHARgATVVVVTH 177
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-230 |
1.24e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.30 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 6 AVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGYLPQ 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGkVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 DFSMYPNMTVYKamdyLAVLSDIPL--------RKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRV 154
Cdd:PRK10575 93 QLPAAEGMTVRE----LVAIGRYPWhgalgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 155 LIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKVIYNGSTEALAKLAE-EKVYSI 230
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETlEQIYGI 247
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-219 |
1.56e-18 |
|
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: 82.27 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 15 GKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGYLPQDFSMYPNmT 91
Cdd:cd03254 14 EKKPVLKDINFSIKPGETvAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRdiSRKSLRSMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 92 VykaMDYLAVLSDIPLRKRRKIIAKLL--------SKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:cd03254 93 I---MENIRLGRPNATDEEVIEAAKEAgahdfimkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 164 LDPEERIRFRNLLCEIANDRIVILSTHIVGDIEaTCENVAILNSGKVIYNGSTEAL 219
Cdd:cd03254 170 IDTETEKLIQEALEKLMKGRTSIIIAHRLSTIK-NADKILVLDDGKIIEEGTHDEL 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-210 |
1.80e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 84.31 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSGMFGL-LGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGYLPQD 83
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVfVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSMYPNMTVYKAMDY---LAVLSDIPLRKRRKIIAKLLskvNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:PRK11000 84 YALYPHLSVAENMSFglkLAGAKKEEINQRVNQVAEVL---QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 161 TAGLDPEERIRFRnllCEIAN-----DRIVILSTHivGDIEAT--CENVAILNSGKV 210
Cdd:PRK11000 161 LSNLDAALRVQMR---IEISRlhkrlGRTMIYVTH--DQVEAMtlADKIVVLDAGRV 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-214 |
1.86e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVP---IENTKEIRNM 76
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGeIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 VGYLPQDFSMYPNMTVYKAMdYLAVLS-----DIPL---RKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSL 148
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENL-YIGRHLtkkvcGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 149 IHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAND-RIVILSTHIVGDIEATCENVAILNSGKVIYNG 214
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-225 |
2.33e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.49 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 19 ALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI--ENTKEIRNMVGYLPQDfsmyP-NMTVYK 94
Cdd:PRK13648 24 TLKDVSFNIPKGQWtSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItdDNFEKLRKHIGIVFQN----PdNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 95 AMDYLAVLS----DIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERI 170
Cdd:PRK13648 100 IVKYDVAFGlenhAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497584106 171 RFRNLLCEI-ANDRIVILSthIVGDIEATCEN--VAILNSGKVIYNGSTEALAKLAEE 225
Cdd:PRK13648 180 NLLDLVRKVkSEHNITIIS--ITHDLSEAMEAdhVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-219 |
3.56e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.02 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEI-DSGMFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEI--------RNMV 77
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIpNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIfqidaiklRKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 78 GYLPQDFSMYPNMTVYKAMDYLAVLSDIP-LRKRRKIIAKLLSKVNL----TNYQNVKVKSLSGGMNRRLGIAQSLIHNP 152
Cdd:PRK14246 93 GMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 153 RVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-217 |
4.42e-18 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 81.42 E-value: 4.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIH-----------MCGVPIENTKE 72
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGeVLGIVGESGSGKSTLLGCLAGRLAPDHGTATyimrsgaelelYQLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 73 IRNMVGYLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIA---KLLSKVNL-TNYQNVKVKSLSGGMNRRLGIAQSL 148
Cdd:TIGR02323 84 MRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRAtaqDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497584106 149 IHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKVIYNGSTE 217
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLglAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTD 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-229 |
6.29e-18 |
|
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: 80.74 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 17 KQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK--EIRNMVGYLPQDFSMYpNMTVY 93
Cdd:cd03253 14 RPVLKDVSFTIPAGkKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTldSLRRAIGVVPQDTVLF-NDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 94 KAMDYLAV-LSDIPLRKRRKiIAKLLSKV-NLTNYQNVKVKS----LSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPE 167
Cdd:cd03253 93 YNIRYGRPdATDEEVIEAAK-AAQIHDKImRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTH 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497584106 168 -ERIRFRNLLcEIANDRIVILSTHIVGDIeATCENVAILNSGKVIYNGSTEALakLAEEKVYS 229
Cdd:cd03253 172 tEREIQAALR-DVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEEL--LAKGGLYA 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-228 |
7.41e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 83.29 E-value: 7.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 15 GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGYLPQDFSMY---- 87
Cdd:COG1132 351 GDRPVLKDISLTIPPGeTVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRdlTLESLRRQIGVVPQDTFLFsgti 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 88 --------PNMT---VYKAMDyLAVLSDiplrkrrkIIAKLLSKvnltnYQNVkV----KSLSGGMNRRLGIAQSLIHNP 152
Cdd:COG1132 431 renirygrPDATdeeVEEAAK-AAQAHE--------FIEALPDG-----YDTV-VgergVNLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 153 RVLIVDEPTAGLDPE-ERIRFRNLLcEIANDRIVI-----LSThivgdIEAtCENVAILNSGKVIYNGSTEALakLAEEK 226
Cdd:COG1132 496 PILILDEATSALDTEtEALIQEALE-RLMKGRTTIviahrLST-----IRN-ADRILVLDDGRIVEQGTHEEL--LARGG 566
|
..
gi 497584106 227 VY 228
Cdd:COG1132 567 LY 568
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-219 |
1.04e-17 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 80.11 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 19 ALDNINLEIDSG-MFGLLGRNGAGKTT----FMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGYLPQD--FSMYPNMT 91
Cdd:TIGR02770 1 LVQDLNLSLKRGeVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 92 VYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVK---SLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEE 168
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLKKypfQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497584106 169 RIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:TIGR02770 161 QARVLKLLRELRQLFgtGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEI 213
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-190 |
1.28e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.08 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 21 DNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEI--RNM--VGYLPqdfSMYPNMTVYKA 95
Cdd:PRK13538 18 SGLSFTLNAGeLVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhQDLlyLGHQP---GIKTELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 96 MDYLAVLSDIPlrkRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNL 175
Cdd:PRK13538 95 LRFYQRLHGPG---DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAL 171
|
170
....*....|....*.
gi 497584106 176 LCE-IANDRIVILSTH 190
Cdd:PRK13538 172 LAQhAEQGGMVILTTH 187
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-190 |
1.66e-17 |
|
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: 82.02 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 15 GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK--EIRNMVGYLPQDfsmypnmt 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGeRVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqdEVRRRVSVCAQD-------- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 92 vykamdylAVLSDIPLRKRRKI---------IAKLLSKVNLTNY-------QNVKV----KSLSGGMNRRLGIAQSLIHN 151
Cdd:TIGR02868 418 --------AHLFDTTVRENLRLarpdatdeeLWAALERVGLADWlralpdgLDTVLgeggARLSGGERQRLALARALLAD 489
|
170 180 190
....*....|....*....|....*....|....*....
gi 497584106 152 PRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTH 190
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-225 |
1.90e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.06 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRF--GKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI--ENTKEIRN 75
Cdd:PRK13635 2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWvAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 76 MVGYLPQDfsmyPN-----MTVykAMDYLAVLSD--IPlrkRRKIIAKL---LSKVNLTNYQNVKVKSLSGGMNRRLGIA 145
Cdd:PRK13635 82 QVGMVFQN----PDnqfvgATV--QDDVAFGLENigVP---REEMVERVdqaLRQVGMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 146 QSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEI-ANDRIVILS-THivgDIE--ATCENVAILNSGKVIYNGSTEALAK 221
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSiTH---DLDeaAQADRVIVMNKGEILEEGTPEEIFK 229
|
....
gi 497584106 222 LAEE 225
Cdd:PRK13635 230 SGHM 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-176 |
1.91e-17 |
|
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: 79.02 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRF------GKK-QALDNINLEIDSGMF-GLLGRNGAGKTTFMR-ILATLLSkTEGSIHMC--GVPIEN 69
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECvALTGPSGAGKSTLLKcIYGNYLP-DSGSILVRhdGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 70 TK----EI----RNMVGYLPQDFSMYPNMTvykAMDYLAVlsdiPLRKR-------RKIIAKLLSKVNL-----TNYQNv 129
Cdd:COG4778 80 AQasprEIlalrRRTIGYVSQFLRVIPRVS---ALDVVAE----PLLERgvdreeaRARARELLARLNLperlwDLPPA- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497584106 130 kvkSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLL 176
Cdd:COG4778 152 ---TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELI 195
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-215 |
3.22e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.28 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQ-----ALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGV------------- 65
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNkIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdkknnhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 66 -----PIENTKEIRNMVGYLPQ--DFSMYPNmTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNL-TNYQNVKVKSLSGG 137
Cdd:PRK13631 102 npyskKIKNFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 138 MNRRLGIAQSLIHNPRVLIVDEPTAGLDPE-ERIRFRNLLCEIANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGS 215
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKgEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-219 |
3.36e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.65 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 19 ALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVP---IENTKEIRNMVGYLPQD-FSMYPNMTVY 93
Cdd:PRK13644 17 ALENINLVIKKGEYiGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDtgdFSKLQGIRKLVGIVFQNpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 94 KAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIR-F 172
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAvL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497584106 173 RNLLCEIANDRIVILSTHIVGDIEATcENVAILNSGKVIYNGSTEAL 219
Cdd:PRK13644 177 ERIKKLHEKGKTIVYITHNLEELHDA-DRIIVMDRGKIVLEGEPENV 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-210 |
4.94e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.99 E-value: 4.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF-GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE-----IRNMV 77
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGeMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNrevpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 78 GYLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIV 157
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 158 DEPTAGLDPEERIRFRNLLCEIanDRI---VILSTHIVGDIEATCENVAILNSGKV 210
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEF--NRVgvtVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-167 |
5.84e-17 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 78.30 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 4 KIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE---------- 72
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGdVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgelvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 73 -----IRNMVGYLPQDFSMYPNMTVykamdyLAVLSDIPL----RKRRKIIAK---LLSKVNLTNYQNVKVKSLSGGMNR 140
Cdd:COG4598 88 rqlqrIRTRLGMVFQSFNLWSHMTV------LENVIEAPVhvlgRPKAEAIERaeaLLAKVGLADKRDAYPAHLSGGQQQ 161
|
170 180
....*....|....*....|....*..
gi 497584106 141 RLGIAQSLIHNPRVLIVDEPTAGLDPE 167
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPE 188
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-235 |
6.31e-17 |
|
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: 80.64 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKiavsNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLL--SKTEGSIHMCGVPIEnTKEIRNM- 76
Cdd:TIGR02633 2 LEMK----GIVKTFGGVKALDGIDLEVRPGeCVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLK-ASNIRDTe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 ---VGYLPQDFSMYPNMTVYK------AMDYLAVLSDIPLRKRRkiIAKLLSKVNLTNYQNVK-VKSLSGGMNRRLGIAQ 146
Cdd:TIGR02633 77 ragIVIIHQELTLVPELSVAEniflgnEITLPGGRMAYNAMYLR--AKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 147 SLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIV-ILSTHIVGDIEATCENVAILNSGKVIyngSTEALAKLAEE 225
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVAcVYISHKLNEVKAVCDTICVIRDGQHV---ATKDMSTMSED 231
|
250
....*....|
gi 497584106 226 KVYSIEVDKK 235
Cdd:TIGR02633 232 DIITMMVGRE 241
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-228 |
6.80e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.25 E-value: 6.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF--GKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE--IRNMVGY 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKvALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEaaLRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQdfsmypnmTVYkamdylaVLSDiPLRKRRKIIA------KL---LSKVNLTNY-QNVKV---------KSLSGGMNR 140
Cdd:PRK11160 419 VSQ--------RVH-------LFSA-TLRDNLLLAApnasdeALievLQQVGLEKLlEDDKGlnawlgeggRQLSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 141 RLGIAQSLIHNPRVLIVDEPTAGLDPE-ERIRFRNLLcEIANDRIVILSTHIVGDIEATcENVAILNSGKVIYNGSTEAL 219
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAEtERQILELLA-EHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
....*....
gi 497584106 220 akLAEEKVY 228
Cdd:PRK11160 561 --LAQQGRY 567
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-165 |
7.61e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.06 E-value: 7.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRfgkkQALDNINLEIDSG----MFGLLGrngAGKTTFMRILATLLSKTEGSIHMCG--VPIENTKE-IRNMVGY 79
Cdd:COG1129 259 VEGLSVG----GVVRDVSFSVRAGeilgIAGLVG---AGRTELARALFGADPADSGEIRLDGkpVRIRSPRDaIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQD---------FSMYPNMTvykamdyLAVLSD------IPLRKRRKIIAKLLSKVNL-TNYQNVKVKSLSGGMNRRLG 143
Cdd:COG1129 332 VPEDrkgeglvldLSIRENIT-------LASLDRlsrgglLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVV 404
|
170 180
....*....|....*....|..
gi 497584106 144 IAQSLIHNPRVLIVDEPTAGLD 165
Cdd:COG1129 405 LAKWLATDPKVLILDEPTRGID 426
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-214 |
1.07e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.92 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILAtllskteGSIH---MCGVPIEN----TKEIRNMVG 78
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEIlAVLGPSGSGKSTLLNALA-------GRIQgnnFTGTILANnrkpTKQILKRTG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 79 YLPQDFSMYPNMTVYKAMDYLAVL-------SDIPLRKRRKIIAKL-LSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIH 150
Cdd:PLN03211 144 FVTQDDILYPHLTVRETLVFCSLLrlpksltKQEKILVAESVISELgLTKCENTIIGNSFIRGISGGERKRVSIAHEMLI 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 151 NPRVLIVDEPTAGLDPEERIRFRNLLCEIAND-RIVILSTHIVGD-IEATCENVAILNSGKVIYNG 214
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQKgKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFG 289
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
7-165 |
1.26e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 78.62 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKK-----------QALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-----EN 69
Cdd:COG4608 10 VRDLKKHFPVRgglfgrtvgvvKAVDGVSFDIRRGeTLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglsgRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 70 TKEIRNMVGYLPQD--FSMYPNMTVYKAMDY-LAVLSDIPLRKRRKIIAKLLSKVNL-TNYQNVKVKSLSGGMNRRLGIA 145
Cdd:COG4608 90 LRPLRRRMQMVFQDpyASLNPRMTVGDIIAEpLRIHGLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIA 169
|
170 180
....*....|....*....|
gi 497584106 146 QSLIHNPRVLIVDEPTAGLD 165
Cdd:COG4608 170 RALALNPKLIVCDEPVSALD 189
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
17-219 |
1.62e-16 |
|
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: 78.60 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 17 KQALDNINLEID-----SGMFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNM------VGYLPQDFS 85
Cdd:COG4148 8 RLRRGGFTLDVDftlpgRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLpphrrrIGYVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 86 MYPNMTVYKAMDYlaVLSDIPlRKRRKI----------IAKLLSKvnltnyqnvKVKSLSGGMNRRLGIAQSLIHNPRVL 155
Cdd:COG4148 88 LFPHLSVRGNLLY--GRKRAP-RAERRIsfdevvellgIGHLLDR---------RPATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 156 IVDEPTAGLDPE---------ERIRfrnllceianDRI---VILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:COG4148 156 LMDEPLAALDLArkaeilpylERLR----------DELdipILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
36-167 |
3.04e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.66 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 36 GRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNM--VGYLPqdfSMYPNMTVYKAMDYLAVLSDiplRKRRKI 113
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMayLGHLP---GLKADLSTLENLHFLCGLHG---RRAKQM 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 497584106 114 IAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPE 167
Cdd:PRK13543 118 PGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-221 |
3.08e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.55 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN-TKEIRNMVG-YL- 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGeVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAKAHQLGiYLv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLtnyqNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDL----DSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497584106 161 TAGLDPEERIRF----RNLLCEIANdrIVILStHIVGDIEATCENVAILNSGKVIYNGSTEALAK 221
Cdd:PRK15439 168 TASLTPAETERLfsriRELLAQGVG--IVFIS-HKLPEIRQLADRISVMRDGTIALSGKTADLST 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-214 |
6.75e-16 |
|
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: 74.22 E-value: 6.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 4 KIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLS---KTEGSIHMCGVPIENTKEI-RNMVG 78
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGeMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFAEKyPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 79 YLPQDFSMYPNMTVYKAMDYLAvlsdiplrkrrkiiakllskvNLTNYQNVKVksLSGGMNRRLGIAQSLIHNPRVLIVD 158
Cdd:cd03233 87 YVSEEDVHFPTLTVRETLDFAL---------------------RCKGNEFVRG--ISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497584106 159 EPTAGLDPEERIRFRNLLCEIANdriVILSTHIVG------DIEATCENVAILNSGKVIYNG 214
Cdd:cd03233 144 NSTRGLDSSTALEILKCIRTMAD---VLKTTTFVSlyqasdEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-228 |
7.63e-16 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 74.88 E-value: 7.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 18 QALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGYLPQDFSMYpNMTVYK 94
Cdd:cd03249 17 PILKGLSLTIPPGKTvALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlNLRWLRSQIGLVSQEPVLF-DGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 95 AMDY---LAVLSDIPLRKRRKIIAKLLSKvnLTN-YQNV---KVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPE 167
Cdd:cd03249 96 NIRYgkpDATDEEVEEAAKKANIHDFIMS--LPDgYDTLvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497584106 168 ERIRFRNLLCEIANDRIVILSTHIVGDIEAtCENVAILNSGKVIYNGSTEALakLAEEKVY 228
Cdd:cd03249 174 SEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL--MAQKGVY 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-166 |
8.29e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.92 E-value: 8.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI---ENTKEIRNM 76
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGeIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 VGYLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRR-KIIAKLLSKVNLTNYQnvKVKSLSGGMNRRLGIAQSLIHNPRVL 155
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERiKWVYELFPRLHERRIQ--RAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170
....*....|.
gi 497584106 156 IVDEPTAGLDP 166
Cdd:PRK11614 160 LLDEPSLGLAP 170
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-240 |
1.93e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.10 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 9 NLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKE-IRNMVGYLPQDF 84
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGqVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAaLAAGVAIIYQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 85 SMYPNMTVykaMDYLaVLSDIPLR----KRRKIIA---KLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIV 157
Cdd:PRK11288 89 HLVPEMTV---AENL-YLGQLPHKggivNRRLLNYearEQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 158 DEPTAGLD-PEERIRFRnLLCEI-ANDRIVILSTHIVGDIEATCENVAILNSGKVIynGSTEALAKLAEEKVYSIEVDkK 235
Cdd:PRK11288 165 DEPTSSLSaREIEQLFR-VIRELrAEGRVILYVSHRMEEIFALCDAITVFKDGRYV--ATFDDMAQVDRDQLVQAMVG-R 240
|
....*
gi 497584106 236 DIENI 240
Cdd:PRK11288 241 EIGDI 245
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-166 |
1.98e-15 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 75.53 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 4 KIAVSNLSKRFGKKQ------------------------ALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEG 58
Cdd:COG4175 3 KIEVRNLYKIFGKRPeralklldqgkskdeilektgqtvGVNDASFDVEEGeIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 59 SIHMCGVPIE--NTKEIRN-------MVGylpQDFSMYPNMTVykaMDYLAV---LSDIPLRKRRKIIAKLLSKVNLTNY 126
Cdd:COG4175 83 EVLIDGEDITklSKKELRElrrkkmsMVF---QHFALLPHRTV---LENVAFgleIQGVPKAERRERAREALELVGLAGW 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 497584106 127 QNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDP 166
Cdd:COG4175 157 EDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDP 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-229 |
2.05e-15 |
|
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: 73.80 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQ--ALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK--EIRNMVGY 79
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGeTVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlaSLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQDFSMYpNMTVYKAMDYLAvlsdipLRKRRKIIAKLLSKVNLTN--------YQNV----KVKsLSGGMNRRLGIAQS 147
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGR------PGATREEVEEAARAANAHEfimelpegYDTVigerGVK-LSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 148 LIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEATCENVaILNSGKVIYNGSTEALakLAEEKV 227
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIV-VLEDGKIVERGTHEEL--LAQGGV 229
|
..
gi 497584106 228 YS 229
Cdd:cd03251 230 YA 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-215 |
2.66e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.27 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKK-----QALDNINLEI-DSGMFGLLGRNGAGKTTFMRILATLLSKTEGS--IHMCGVP-----IENTK 71
Cdd:PRK13645 7 IILDNVSYTYAKKtpfefKALNNTSLTFkKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtiVGDYAIPanlkkIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 72 EIRNMVGYLPQ--DFSMYPNmTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNL-TNYQNVKVKSLSGGMNRRLGIAQSL 148
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 149 IHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAND--RIVILSTHIVGDIEATCENVAILNSGKVIYNGS 215
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-190 |
4.91e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.50 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQA----LDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-----ENTKEIR 74
Cdd:PRK10584 7 VEVHHLKKSVGQGEHelsiLTGVELVVKRGeTIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdeEARAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 75 -NMVGYLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPR 153
Cdd:PRK10584 87 aKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 497584106 154 VLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTH 190
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTH 205
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-219 |
4.93e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.39 E-value: 4.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMrILATLLSKTEGS-----IHMCGvpieNTKEIRNMVG 78
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGtVLGVLGP*GAA**RGA-LPAHV*GPDAGRrpwrf*TWCA----NRRALRRTIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 79 -YLPQDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIV 157
Cdd:NF000106 89 *HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497584106 158 DEPTAGLDPEERIRFRNLLCEIAND-RIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-165 |
6.49e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 72.16 E-value: 6.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 8 SNLSKRF--GKKQA--LDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE-----NTKEIRNM- 76
Cdd:PRK11629 9 DNLCKRYqeGSVQTdvLHNVSFSIGEGeMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaAKAELRNQk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 VGYLPQDFSMYPNMTvykAMDYLAVLSDIPLRKRRKIIAK---LLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPR 153
Cdd:PRK11629 89 LGFIYQFHHLLPDFT---ALENVAMPLLIGKKKPAEINSRaleMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170
....*....|..
gi 497584106 154 VLIVDEPTAGLD 165
Cdd:PRK11629 166 LVLADEPTGNLD 177
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-222 |
7.89e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 74.31 E-value: 7.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 15 GKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGYLPQDFSMYPNmT 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEAlAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwDRETFGKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 92 VYKAmdyLAVLSDIPlrKRRKII-AKLLSKV-----NLTN-YQNV---KVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPT 161
Cdd:TIGR01842 408 VAEN---IARFGENA--DPEKIIeAAKLAGVhelilRLPDgYDTVigpGGATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497584106 162 AGLDPEERIRFRNLLCEI-ANDRIVILSTHIVGDIEATcENVAILNSGKV-IYNGSTEALAKL 222
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCV-DKILVLQDGRIaRFGERDEVLAKL 544
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-243 |
7.99e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.76 E-value: 7.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEI-DSGMFGLLGRNGAGKTTFMRILATLLS-----KTEGSIHMCGVPIE----NTKEIR 74
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIyQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYerrvNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 75 NMVGYLPQDFSMYPnMTVYKAMDY-LAVLSDIPLRKRRKIIAKLLSKVNLtnYQNVKVK------SLSGGMNRRLGIAQS 147
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYgVKIVGWRPKLEIDDIVESALKDADL--WDEIKHKihksalDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 148 LIHNPRVLIVDEPTAGLDPEERIRFRNLL--CEIANDRIVILSTHivgdieaTCENVAILNSGKVIYNGSTEALAKLAE- 224
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSH-------NLHQVSRLSDFTAFFKGNENRIGQLVEf 237
|
250 260
....*....|....*....|..
gi 497584106 225 ---EKVYSIEVDKKDIENIKSR 243
Cdd:PRK14258 238 gltKKIFNSPHDSRTREYVLSR 259
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-219 |
9.03e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 72.12 E-value: 9.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQALDNINLEI-DSGMFGLLGRNGAGKTTFMRILATLLS-----KTEGSI----HMCGVPIENT 70
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFyPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIvyngHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 71 KEIRNMVGYLPQDFSMYPnMTVYKAMDYLAVLSDIplrKRRKIIAKLLSK--VNLTNYQNVKVK------SLSGGMNRRL 142
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGI---KDKQVLDEAVEKslKGASIWDEVKDRlhdsalGLSGGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 143 GIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-171 |
9.60e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.07 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 2 EMKIAVSNLSKRFGkkqaldNINLEIDSG------MFGLLGRNGAGKTTFMRILATLLSKTEGSIhmcgvpienTKEIRn 75
Cdd:PRK13409 338 ETLVEYPDLTKKLG------DFSLEVEGGeiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---------DPELK- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 76 mVGYLPQDFSMYPNMTVYkamdylAVLSDIPLRKRRKII-AKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRV 154
Cdd:PRK13409 402 -ISYKPQYIKPDYDGTVE------DLLRSITDDLGSSYYkSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADL 474
|
170
....*....|....*..
gi 497584106 155 LIVDEPTAGLDPEERIR 171
Cdd:PRK13409 475 YLLDEPSAHLDVEQRLA 491
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-211 |
9.97e-15 |
|
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: 71.29 E-value: 9.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 4 KIAVSNLSKRFGKK--QALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK--EIRNMVG 78
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGeKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 79 YLPQDFSMYPNmTVYKAMDYLAVLSDIPLrkrrkiiakllskvnltnYQNVKVKS----LSGGMNRRLGIAQSLIHNPRV 154
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNLDPFDEYSDEEI------------------YGALRVSEgglnLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 155 LIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIeATCENVAILNSGKVI 211
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTI-IDYDKILVMDAGEVK 202
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-227 |
1.21e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.43 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQALDNIN---LEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCG--VPIENTKEIR 74
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNgvsFSITKGEWvSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 75 NMVGYLPQD-FSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPR 153
Cdd:PRK13642 81 RKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497584106 154 VLIVDEPTAGLDPEERIRFRNLLCEIAND-RIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEALAKLAEEKV 227
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMV 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-219 |
1.73e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 73.18 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 10 LSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSkTEGSIHMCGVPIE--NTKEIRnmvgylP----- 81
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGeTLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDglSRRALR------Plrrrm 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 ----QD-F-SMYPNMTVykamdylavlSDI---PLR---------KRRKIIAKLLSKVNLT-NYQNVKVKSLSGGMNRRL 142
Cdd:COG4172 365 qvvfQDpFgSLSPRMTV----------GQIiaeGLRvhgpglsaaERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 143 GIAQSLIHNPRVLIVDEPTAGLDpeeR-IRFR--NLLCEIANDR----IVIlsTHIVGDIEATCENVAILNSGKVIYNGS 215
Cdd:COG4172 435 AIARALILEPKLLVLDEPTSALD---VsVQAQilDLLRDLQREHglayLFI--SHDLAVVRALAHRVMVMKDGKVVEQGP 509
|
....
gi 497584106 216 TEAL 219
Cdd:COG4172 510 TEQV 513
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-171 |
1.74e-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: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 16 KKQALDNINLEIDSGMF------GLLGRNGAGKTTFMRILATLLSKTEGSIhmcgvPIENTKeirnmVGYLPQDFSMYPN 89
Cdd:cd03237 6 MKKTLGEFTLEVEGGSIseseviGILGPNGIGKTTFIKMLAGVLKPDEGDI-----EIELDT-----VSYKPQYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 90 MTVYkamdylAVLSDIPLRKR-----RKIIAKLLSKVNLTNYQnvkVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGL 164
Cdd:cd03237 76 GTVR------DLLSSITKDFYthpyfKTEIAKPLQIEQILDRE---VPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
....*..
gi 497584106 165 DPEERIR 171
Cdd:cd03237 147 DVEQRLM 153
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-223 |
1.84e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.22 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 20 LDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEI----RNMVGYLPQDFSMYPNMTV 92
Cdd:PRK10535 24 LKGISLDIYAGeMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtlDADALaqlrREHFGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 93 YKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDP---EER 169
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDShsgEEV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497584106 170 IRFRNLLCEiaNDRIVILSTHiVGDIEATCENVAILNSGKVIYNGSTEALAKLA 223
Cdd:PRK10535 184 MAILHQLRD--RGHTVIIVTH-DPQVAAQAERVIEIRDGEIVRNPPAQEKVNVA 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-211 |
1.99e-14 |
|
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: 70.60 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 4 KIAVSNLSKRF--GKKQALDNINLEIDSGM-FGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVG 78
Cdd:cd03244 2 DIEFKNVSLRYrpNLPPVLKNISFSIKPGEkVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkiGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 79 YLPQD---FSmypnMTVYKAMDYLAVLSDiplrkrrKIIAKLLSKVNLTNYqnvkVKSLSGGMNRR-------------- 141
Cdd:cd03244 82 IIPQDpvlFS----GTIRSNLDPFGEYSD-------EELWQALERVGLKEF----VESLPGGLDTVveeggenlsvgqrq 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497584106 142 -LGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIeATCENVAILNSGKVI 211
Cdd:cd03244 147 lLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTI-IDSDRILVLDKGRVV 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-211 |
2.45e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.26 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRF---------GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI-----EN 69
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGeTVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnrAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 70 TKEIRNMVGYLPQDF--SMYPNMTV----YKAMDYLAVLSDiplRKRRKIIAKLLSKVNLTNYQNVKV-KSLSGGMNRRL 142
Cdd:PRK10419 84 RKAFRRDIQMVFQDSisAVNPRKTVreiiREPLRHLLSLDK---AERLARASEMLRAVDLDDSVLDKRpPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497584106 143 GIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAN--DRIVILSTHIVGDIEATCENVAILNSGKVI 211
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-210 |
3.23e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 70.92 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQ---ALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCG--VPIENTKEIR 74
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGeWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdlLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 75 NMVGYLPQD-FSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPR 153
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 154 VLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIeATCENVAILNSGKV 210
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-173 |
4.36e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 71.41 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 4 KIAVSNLSKRF-GKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIeNTKEIRN----MV 77
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFiVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELEPADrdiaMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 78 GylpQDFSMYPNMTVYKAMDY---LAVLSDIPLRKRRKIIAKLLskvNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRV 154
Cdd:PRK11650 82 F---QNYALYPHMSVRENMAYglkIRGMPKAEIEERVAEAARIL---ELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170
....*....|....*....
gi 497584106 155 LIVDEPTAGLDPEERIRFR 173
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMR 174
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-232 |
5.26e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.68 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 8 SNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKE-IRNMVGYLPQD 83
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHsIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfkSSKEaLENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSMYPNMTVykaMDYL----------AVLSDIPLRKRRKIIAKLLSKVNltnyQNVKVKSLSGGMNRRLGIAQSLIHNPR 153
Cdd:PRK10982 82 LNLVLQRSV---MDNMwlgryptkgmFVDQDKMYRDTKAIFDELDIDID----PRAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 154 VLIVDEPTAGLDPEErirfRNLLCEIAN---DR---IVILStHIVGDIEATCENVAILNSGKVIyngSTEALAKLAEEKV 227
Cdd:PRK10982 155 IVIMDEPTSSLTEKE----VNHLFTIIRklkERgcgIVYIS-HKMEEIFQLCDEITILRDGQWI---ATQPLAGLTMDKI 226
|
....*
gi 497584106 228 YSIEV 232
Cdd:PRK10982 227 IAMMV 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-210 |
6.64e-14 |
|
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: 68.23 E-value: 6.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 6 AVSNLSKrfgkKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE---NTKEIRNMVGYLP 81
Cdd:cd03215 6 EVRGLSV----KGAVRDVSFEVRAGeIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrsPRDAIRAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 QDfsmypnmtvykamdylavlsdiplRKRRKIIAkllskvNLTNYQNVKVKS-LSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:cd03215 82 ED------------------------RKREGLVL------DLSVAENIALSSlLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497584106 161 TAGLDPEERIRFRNLLCEIANDR--IVILSThivgDIE---ATCENVAILNSGKV 210
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAGkaVLLISS----ELDellGLCDRILVMYEGRI 182
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-176 |
7.56e-14 |
|
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: 67.95 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 20 LDNINLEIDSGMFGLL-GRNGAGKTTFMRILATLLSKTEGSIHMCGvpientkeiRNMVGYLPQDfsmyPnmtvykamdY 98
Cdd:cd03223 17 LKDLSFEIKPGDRLLItGPSGTGKSSLFRALAGLWPWGSGRIGMPE---------GEDLLFLPQR----P---------Y 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497584106 99 LAVLSdipLRKrrkIIAKLLSKVnltnyqnvkvksLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLL 176
Cdd:cd03223 75 LPLGT---LRE---QLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-167 |
1.36e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 70.69 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCgvpiENTKeirnmVGYLPQDFS 85
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGeRLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS----ENAN-----IGYYAQDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 86 -MYPN-MTVYKAM--------DYLAVlsdiplrkrRKIIAKLLSKVNLTNYqnvKVKSLSGGMNRRLGIAQSLIHNPRVL 155
Cdd:PRK15064 393 yDFENdLTLFDWMsqwrqegdDEQAV---------RGTLGRLLFSQDDIKK---SVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170
....*....|..
gi 497584106 156 IVDEPTAGLDPE 167
Cdd:PRK15064 461 VMDEPTNHMDME 472
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-207 |
1.42e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.59 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 13 RFGKKQALDNINLEIDSGMFGLL-GRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGYLPQDFSMYPN 89
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEIYRQQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 90 mTVYkamDYLAVLSDIplRKRR---KIIAKLLSKVNLTNYQNVK-VKSLSGGMNRRLgiaqSLIHN----PRVLIVDEPT 161
Cdd:PRK10247 96 -TVY---DNLIFPWQI--RNQQpdpAIFLDDLERFALPDTILTKnIAELSGGEKQRI----SLIRNlqfmPKVLLLDEIT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497584106 162 AGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIeATCENVAILNS 207
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEI-NHADKVITLQP 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-171 |
1.45e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.58 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 8 SNLSKRFGkkqaldNINLEIDSGMF------GLLGRNGAGKTTFMRILATLLSKTEGSIHMcgvpientkEIRnmVGYLP 81
Cdd:COG1245 345 PDLTKSYG------GFSLEVEGGEIregevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDE---------DLK--ISYKP 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 QDFSMYPNMTVykaMDYL--AVLSDIPLRKRRKIIAKLLskvNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDE 159
Cdd:COG1245 408 QYISPDYDGTV---EEFLrsANTDDFGSSYYKTEIIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170
....*....|..
gi 497584106 160 PTAGLDPEERIR 171
Cdd:COG1245 482 PSAHLDVEQRLA 493
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-229 |
1.45e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.43 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 17 KQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK--EIRNMVGYLPQDFSMYpNMTVY 93
Cdd:PRK11176 356 VPALRNINFKIPAGkTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlaSLRNQVALVSQNVHLF-NDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 94 KAMDYLAvlSDIPLRKRRKIIAKLLSKVNLTNyqnvKVK------------SLSGGMNRRLGIAQSLIHNPRVLIVDEPT 161
Cdd:PRK11176 435 NNIAYAR--TEQYSREQIEEAARMAYAMDFIN----KMDngldtvigengvLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497584106 162 AGLDPEERIRFRNLLCEIANDRIVILSTHIVGDIEATCENVAILNsGKVIYNGSTEALakLAEEKVYS 229
Cdd:PRK11176 509 SALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVED-GEIVERGTHAEL--LAQNGVYA 573
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-192 |
1.56e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 70.71 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRF--GKKQALDNINLEIDSGM-FGLLGRNGAGKTTFMRILATLLSkTEGSIHMCGVPIENT--KEIRNMVGYLP 81
Cdd:TIGR01271 1220 VQGLTAKYteAGRAVLQDLSFSVEGGQrVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVtlQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 QDFSMYPNmTVYKAMDYLAVLSDIPLRK------RRKIIAKLLSKVNLTNYQNVKVksLSGGMNRRLGIAQSLIHNPRVL 155
Cdd:TIGR01271 1299 QKVFIFSG-TFRKNLDPYEQWSDEEIWKvaeevgLKSVIEQFPDKLDFVLVDGGYV--LSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190
....*....|....*....|....*....|....*..
gi 497584106 156 IVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHIV 192
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-229 |
2.18e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.14 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 16 KKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGYLPQDFSMYpNMTV 92
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGeVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqyDHHYLHRQVALVGQEPVLF-SGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 93 YKAMDYlaVLSDIPLRKRRKIiAKL------LSKVNLTNYQNVKVKS--LSGGMNRRLGIAQSLIHNPRVLIVDEPTAGL 164
Cdd:TIGR00958 572 RENIAY--GLTDTPDEEIMAA-AKAanahdfIMEFPNGYDTEVGEKGsqLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497584106 165 DPEERIRFRNLLCeiANDRIVILSTHIVGDIEaTCENVAILNSGKVIYNGSTEALakLAEEKVYS 229
Cdd:TIGR00958 649 DAECEQLLQESRS--RASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQL--MEDQGCYK 708
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-226 |
2.20e-13 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 68.73 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 4 KIAVSNLSKRF--GKKQALDNINLEIDSGM-FGLLGRNGAGKTTFMRILATLLSkTEGSIHMCGVPIENT--KEIRNMVG 78
Cdd:cd03289 2 QMTVKDLTAKYteGGNAVLENISFSISPGQrVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVplQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 79 YLPQDFSMYPNmTVYKAMDYLAVLSDIPLRK------RRKIIAKLLSKVNLTNYQNVKVksLSGGMNRRLGIAQSLIHNP 152
Cdd:cd03289 81 VIPQKVFIFSG-TFRKNLDPYGKWSDEEIWKvaeevgLKSVIEQFPGQLDFVLVDGGCV--LSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 153 RVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTHivgDIEAT--CENVAILNSGKViynGSTEALAKLAEEK 226
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEH---RIEAMleCQRFLVIEENKV---RQYDSIQKLLNEK 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-210 |
2.93e-13 |
|
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: 67.50 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 18 QALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK-----EIRNMVGYLPQDFSMypnmT 91
Cdd:cd03248 28 LVLQDVSFTLHPGeVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEhkylhSKVSLVGQEPVLFAR----S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 92 VYKAMDYlaVLSDIPLRKRRKIIAK-----LLSKVNLTNYQNVKVKS--LSGGMNRRLGIAQSLIHNPRVLIVDEPTAGL 164
Cdd:cd03248 104 LQDNIAY--GLQSCSFECVKEAAQKahahsFISELASGYDTEVGEKGsqLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497584106 165 DPEERIRFRNLLCEIANDRIVILSTHIVGDIEATcENVAILNSGKV 210
Cdd:cd03248 182 DAESEQQVQQALYDWPERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
34-214 |
3.05e-13 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 69.87 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 34 LLGRNGAGKTTFMRILATllSKT----EGSIHMCGVPiENTKEIRNMVGYLPQDFSMYPNMTVYKAMDYLAVL---SDIP 106
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFP-KKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLrlpKEVS 987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 107 LRKRRKIIAKLLSKVNLTNYQNV-----KVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPE-ERIRFRNLLCEIA 180
Cdd:PLN03140 988 KEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARaAAIVMRTVRNTVD 1067
|
170 180 190
....*....|....*....|....*....|....*.
gi 497584106 181 NDRIVILSTHIVG-DI-EATCENVAILNSGKVIYNG 214
Cdd:PLN03140 1068 TGRTVVCTIHQPSiDIfEAFDELLLMKRGGQVIYSG 1103
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-219 |
3.95e-13 |
|
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: 69.33 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMK--IAVSNLSKRFGK----KQALDNINLEIDSG-MFGLLGRNGAGKT----TFMRILATLLSKTEGSIHMCGVPIEN 69
Cdd:COG4172 1 MMSMplLSVEDLSVAFGQgggtVEAVKGVSFDIAAGeTLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 70 TKE-----IR-NMVGYLPQD--FSMYPNMTVYKAM-DYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNvKVKS----LSG 136
Cdd:COG4172 81 LSErelrrIRgNRIAMIFQEpmTSLNPLHTIGKQIaEVLRLHRGLSGAAARARALELLERVGIPDPER-RLDAyphqLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 137 GMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTH---IVGDIeatCENVAILNSGKVI 211
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHdlgVVRRF---ADRVAVMRQGEIV 236
|
....*...
gi 497584106 212 YNGSTEAL 219
Cdd:COG4172 237 EQGPTAEL 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-219 |
4.82e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 19 ALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN-----TKEIRNMVGYLPQD--FSMYPNM 90
Cdd:PRK10261 339 AVEKVSFDLWPGeTLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgkLQALRRDIQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 91 TV-YKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKV-KSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEE 168
Cdd:PRK10261 419 TVgDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYpHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497584106 169 RIRFRNLLCEIANDRIV--ILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
17-217 |
4.96e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 68.36 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 17 KQALDNINLEID-----SGMFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCG---VPIEN----TKEIRNmVGYLPQDF 84
Cdd:PRK11144 7 KQQLGDLCLTVNltlpaQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgiclPPEKRR-IGYVFQDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 85 SMYPNMTV-----Y---KAM----DYLAVLSDI-PLRKRRKIiakllskvnltnyqnvkvkSLSGGMNRRLGIAQSLIHN 151
Cdd:PRK11144 86 RLFPHYKVrgnlrYgmaKSMvaqfDKIVALLGIePLLDRYPG-------------------SLSGGEKQRVAIGRALLTA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497584106 152 PRVLIVDEPTAGLD-PeeriRFRNL---LCEIAND-RIVIL-STHIVGDIEATCENVAILNSGKVIYNGSTE 217
Cdd:PRK11144 147 PELLLMDEPLASLDlP----RKRELlpyLERLAREiNIPILyVSHSLDEILRLADRVVVLEQGKVKAFGPLE 214
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-220 |
5.51e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.51 E-value: 5.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKK---------QALDNINLEIDSGM-FGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE-- 68
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQtLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 69 ----NTKEIRnMVGYLPQDfSMYPNMTVYKAMDY-LAVLSDIPLRKRRKIIAKLLSKVNL-TNYQNVKVKSLSGGMNRRL 142
Cdd:PRK15112 81 dysyRSQRIR-MIFQDPST-SLNPRQRISQILDFpLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 143 GIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIV--ILSTHIVGDIEATCENVAILNSGKVIYNGST-EAL 219
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTaDVL 238
|
.
gi 497584106 220 A 220
Cdd:PRK15112 239 A 239
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-167 |
7.83e-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: 68.42 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 9 NLSKRF-GKKQALDNINLEIDSGM-FGLLGRNGAGKTTFMRILATLLSKTEGSIhmcgVPIENTKeirnmVGYLPQDFSM 86
Cdd:TIGR03719 9 RVSKVVpPKKEILKDISLSFFPGAkIGVLGLNGAGKSTLLRIMAGVDKDFNGEA----RPQPGIK-----VGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 87 YPNMTVY--------KAMDYLAVLSDI------PLRKRRKII---AKLLSKVNLTNYQNV------------------KV 131
Cdd:TIGR03719 80 DPTKTVRenveegvaEIKDALDRFNEIsakyaePDADFDKLAaeqAELQEIIDAADAWDLdsqleiamdalrcppwdaDV 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 497584106 132 KSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPE 167
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE 195
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-191 |
8.05e-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: 68.42 E-value: 8.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEI-DSGMFGLLGRNGAGKTTFMRILATLLSKTEGSIHMcGvpiENTKeirnmVGYLPQ- 82
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLpPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-G---ETVK-----LAYVDQs 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 -DfSMYPNMTVYKAM----DYLAVLS-DIPLRkrrkiiaKLLSKVNLT-NYQNVKVKSLSGGMNRRLGIAQSLIHNPRVL 155
Cdd:TIGR03719 394 rD-ALDPNKTVWEEIsgglDIIKLGKrEIPSR-------AYVGRFNFKgSDQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497584106 156 IVDEPTAGLDPEERIRFRNLLCEIANDRIVI---------LSTHI 191
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLNFAGCAVVIshdrwfldrIATHI 510
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-179 |
8.17e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.42 E-value: 8.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 18 QALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSI-----HMCGVPIENTKEIRNMVGYLPQD--FSMYPN 89
Cdd:PRK15079 35 KAVDGVTLRLYEGeTLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkDLLGMKDDEWRAVRSDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 90 MTVykamdylavlSDI---PLR------KRRKIIAK---LLSKVNL-TNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLI 156
Cdd:PRK15079 115 MTI----------GEIiaePLRtyhpklSRQEVKDRvkaMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLII 184
|
170 180
....*....|....*....|...
gi 497584106 157 VDEPTAGLDPEERIRFRNLLCEI 179
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQL 207
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-219 |
8.99e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.14 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 24 NLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKEIRNMVGYLPQDFSMYPNMTVYKAmdyLAVL 102
Cdd:PRK10771 19 DLTVERGeRVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQN---IGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 103 SDIPLR---KRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEI 179
Cdd:PRK10771 96 LNPGLKlnaAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 497584106 180 ANDRIVIL--STHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK10771 176 CQERQLTLlmVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-190 |
1.19e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 65.57 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQ-----ALDNINLEIDSGMF-GLLGRNGAGKTTFmrILATL--LSKTEGSIHMCGvpientkeirnM 76
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELvAIVGPVGSGKSSL--LSALLgeLEKLSGSVSVPG-----------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 VGYLPQdFSMYPNMTV---------YKAMDYLAVLSDIPLRKRRKIiaklLSKVNLTNyqnVKVK--SLSGGMNRRLGIA 145
Cdd:cd03250 68 IAYVSQ-EPWIQNGTIrenilfgkpFDEERYEKVIKACALEPDLEI----LPDGDLTE---IGEKgiNLSGGQKQRISLA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497584106 146 QSLIHNPRVLIVDEPTAGLDP--EERIrFRNLLC-EIANDRIVILSTH 190
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAhvGRHI-FENCILgLLLNNKTRILVTH 186
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-219 |
1.48e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.33 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK-----EIRNMVG 78
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGkITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlyTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 79 YLPQDFSMYPNMTVYKAMDYlavlsdiPLRKRRKIIAKL--------LSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIH 150
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAY-------PLREHTQLPAPLlhstvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497584106 151 NPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIV--ILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVtcVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-215 |
1.59e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.83 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 16 KKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILAtllSKTEGS-------IHMCGVPIEN-TKEIRNMVGYLPQDFSM 86
Cdd:TIGR00956 73 TFDILKPMDGLIKPGeLTVVLGRPGSGCSTLLKTIA---SNTDGFhigvegvITYDGITPEEiKKHYRGDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 87 YPNMTVYKAMDYLAVLSDIPLRKR---RKIIAKLLSKVNLTNY-----QNVKV-----KSLSGGMNRRLGIAQSLIHNPR 153
Cdd:TIGR00956 150 FPHLTVGETLDFAARCKTPQNRPDgvsREEYAKHIADVYMATYglshtRNTKVgndfvRGVSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 154 VLIVDEPTAGLDPEERIRFRNLLCEIANdrivIL-STHIVG------DIEATCENVAILNSGKVIYNGS 215
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRALKTSAN----ILdTTPLVAiyqcsqDAYELFDKVIVLYEGYQIYFGP 294
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-211 |
1.65e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 1 MEMKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCG--VPIENTKEIRNM- 76
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGrVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkeVTFNGPKSSQEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 VGYLPQDFSMYPNMTV----YKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNP 152
Cdd:PRK10762 81 IGIIHQELNLIPQLTIaeniFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497584106 153 RVLIVDEPTAGL-DPEERIRFRnLLCEIANDR--IVILStHIVGDIEATCENVAILNSGKVI 211
Cdd:PRK10762 161 KVIIMDEPTDALtDTETESLFR-VIRELKSQGrgIVYIS-HRLKEIFEICDDVTVFRDGQFI 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-216 |
7.08e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.18 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 6 AVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHM---CGVPIE----NTKEIRNMV 77
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGeVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDlyalSEAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 78 ----GYLPQDfsmypnmtvykAMDYLavlsdiplrkRRKI-----IAKLLSKVNLTNYQNVKVKSL-------------- 134
Cdd:PRK11701 88 rtewGFVHQH-----------PRDGL----------RMQVsaggnIGERLMAVGARHYGDIRATAGdwlerveidaarid 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 135 ------SGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDR--IVILSTHIVGDIEATCENVAILN 206
Cdd:PRK11701 147 dlpttfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLLAHRLLVMK 226
|
250
....*....|
gi 497584106 207 SGKVIYNGST 216
Cdd:PRK11701 227 QGRVVESGLT 236
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-165 |
1.10e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 2 EMKIAVSNLSKrfgkkQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE---IRNMV 77
Cdd:PRK10762 255 EVRLKVDNLSG-----PGVNDVSFTLRKGeILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqdgLANGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 78 GYLPQD---------FSMYPNMTVyKAMDYLAVLSdIPLRKRRKIIA-----KLLskvnltnyqNVKVKS-------LSG 136
Cdd:PRK10762 330 VYISEDrkrdglvlgMSVKENMSL-TALRYFSRAG-GSLKHADEQQAvsdfiRLF---------NIKTPSmeqaiglLSG 398
|
170 180
....*....|....*....|....*....
gi 497584106 137 GMNRRLGIAQSLIHNPRVLIVDEPTAGLD 165
Cdd:PRK10762 399 GNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
34-238 |
1.25e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 34 LLGRNGAGKTTFMRILATLLSkTEGSIHMCGVPIE--NTKEIRNMVGYLPQDFSMYPNMTVYKamdYLAV-LSD-IPLRK 109
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEawSAAELARHRAYLSQQQTPPFAMPVFQ---YLTLhQPDkTRTEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 110 RRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSL--IH---NP--RVLIVDEPTAGLDPEERIRFRNLLCEIAND 182
Cdd:PRK03695 103 VASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWpdiNPagQLLLLDEPMNSLDVAQQAALDRLLSELCQQ 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497584106 183 RI-VILSTHivgDIEATCEN---VAILNSGKVIYNGSTEALakLAEE---KVYSIEVDKKDIE 238
Cdd:PRK03695 183 GIaVVMSSH---DLNHTLRHadrVWLLKQGKLLASGRRDEV--LTPEnlaQVFGVNFRRLDVE 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-165 |
1.61e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.28 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLS-KRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN--TKEIRNM-VGYLP 81
Cdd:COG3845 260 VENLSvRDDRGVPALKDVSLEVRAGeILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlsPRERRRLgVAYIP 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 QD---FSMYPNMTVYKAMdylaVLSDI---PLRKR------------RKIIAKLlsKVNLTNyQNVKVKSLSGGMNRRLG 143
Cdd:COG3845 340 EDrlgRGLVPDMSVAENL----ILGRYrrpPFSRGgfldrkairafaEELIEEF--DVRTPG-PDTPARSLSGGNQQKVI 412
|
170 180
....*....|....*....|..
gi 497584106 144 IAQSLIHNPRVLIVDEPTAGLD 165
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLD 434
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-211 |
1.71e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 2 EMKiavsNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLL--SKTEGSIHMCGVPIE----NTKEIR 74
Cdd:NF040905 3 EMR----GITKTFPGVKALDDVNLSVREGeIHALCGENGAGKSTLMKVLSGVYphGSYEGEILFDGEVCRfkdiRDSEAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 75 NMVgYLPQDFSMYPnmtvykamdYLAVLSDIPL---RKRRKII---------AKLLSKVNLTNYQNVKVKSLSGGMNRRL 142
Cdd:NF040905 79 GIV-IIHQELALIP---------YLSIAENIFLgneRAKRGVIdwnetnrraRELLAKVGLDESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 143 GIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIV-ILSTHIVGDIEATCENVAILNSGKVI 211
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITsIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
7-221 |
2.21e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.22 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKK----QALDNINLEIDSG-MFGLLGRNGAGKT----TFM-------RILATLLSKTEGSIHMCgvpieNT 70
Cdd:PRK11022 6 VDKLSVHFGDEsapfRAVDRISYSVKQGeVVGIVGESGSGKSvsslAIMglidypgRVMAEKLEFNGQDLQRI-----SE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 71 KEIRNMVG----YLPQD--FSMYPNMTV-YKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTNYQ---NVKVKSLSGGMNR 140
Cdd:PRK11022 81 KERRNLVGaevaMIFQDpmTSLNPCYTVgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 141 RLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAN--DRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEA 218
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
...
gi 497584106 219 LAK 221
Cdd:PRK11022 241 IFR 243
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-223 |
2.52e-11 |
|
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: 63.61 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 4 KIAVSNLSKRF--GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVG 78
Cdd:COG4618 330 RLSVENLTVVPpgSKRPILRGVSFSLEPGeVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwDREELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 79 YLPQDFSMYP-----NmtvykamdyLAVLSDIPlrkRRKII--AKL-------LSkvnLTN-YQNVkV----KSLSGGMN 139
Cdd:COG4618 410 YLPQDVELFDgtiaeN---------IARFGDAD---PEKVVaaAKLagvhemiLR---LPDgYDTR-IgeggARLSGGQR 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 140 RRLGIAQSLIHNPRVLIVDEPTAGLDPE-ErirfRNLLCEIANDR----IVILSTHIVGdIEATCENVAILNSGKVIYNG 214
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEgE----AALAAAIRALKargaTVVVITHRPS-LLAAVDKLLVLRDGRVQAFG 548
|
250
....*....|
gi 497584106 215 ST-EALAKLA 223
Cdd:COG4618 549 PRdEVLARLA 558
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-190 |
4.18e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.29 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 20 LDNINLEIDSGMfGLL--GRNGAGKTTFMRILATLLSKTEGSIHMcgvPientkEIRNMVgYLPQdfSMY-PNMTVYKAM 96
Cdd:COG4178 379 LEDLSLSLKPGE-RLLitGPSGSGKSTLLRAIAGLWPYGSGRIAR---P-----AGARVL-FLPQ--RPYlPLGTLREAL 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 97 DYLAVLSDIPlrkrRKIIAKLLSKVNL----------TNYQNVkvksLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDP 166
Cdd:COG4178 447 LYPATAEAFS----DAELREALEAVGLghlaerldeeADWDQV----LSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180
....*....|....*....|....
gi 497584106 167 EERIRFRNLLCEIANDRIVILSTH 190
Cdd:COG4178 519 ENEAALYQLLREELPGTTVISVGH 542
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-228 |
4.45e-11 |
|
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: 61.00 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSGM-FGLLGRNGAGKTTFMRILATLLSK--TEGSIHMCGvpientKEIRNMvgyLPQD 83
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEvHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKG------EDITDL---PPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSmypNMTVYKAMDYLAvlsDIPLRKrrkiIAKLLSKVNltnyqnvkvKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:cd03217 74 RA---RLGIFLAFQYPP---EIPGVK----NADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497584106 164 LDpeerIRFRNLLCEIAN-----DRIVILSTH---IVGDIEATceNVAILNSGKVIYNGSTEaLAKLAEEKVY 228
Cdd:cd03217 135 LD----IDALRLVAEVINklreeGKSVLIITHyqrLLDYIKPD--RVHVLYDGRIVKSGDKE-LALEIEKKGY 200
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-167 |
5.56e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 9 NLSKRFG-KKQALDNINLEIDSGM-FGLLGRNGAGKTTFMRILAtllsktegsihmcGVPIENTKEIRNM----VGYLPQ 82
Cdd:PRK11819 11 RVSKVVPpKKQILKDISLSFFPGAkIGVLGLNGAGKSTLLRIMA-------------GVDKEFEGEARPApgikVGYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 DFSMYPNMTVY--------KAMDYLAVLSDI------PLRKRRKII---AKLLSKVNLTNYQNV---------------- 129
Cdd:PRK11819 78 EPQLDPEKTVRenveegvaEVKAALDRFNEIyaayaePDADFDALAaeqGELQEIIDAADAWDLdsqleiamdalrcppw 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 497584106 130 --KVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPE 167
Cdd:PRK11819 158 daKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-167 |
6.11e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.74 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 9 NLSKRFGKKQALDNINLEIDSGMFGLL-GRNGAGKTTFMRILATLLSKTEGSIhmcgvpientkEIRNMVGYLPQDFSM- 86
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIvGASGSGKSTLLRLLAGALKGTPVAG-----------CVDVPDNQFGREASLi 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 87 ---YPNMTVYKAMDYLAV--LSDIPLRKRRkiiakllskvnltnyqnvkVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPT 161
Cdd:COG2401 104 daiGRKGDFKDAVELLNAvgLSDAVLWLRR-------------------FKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
....*.
gi 497584106 162 AGLDPE 167
Cdd:COG2401 165 SHLDRQ 170
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-190 |
6.40e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 33 GLLGRNGAGKTTFMRILATLL------SKTEGSI-----HMCGVPIEN------TKEIRnmVGYLPQDFSMYPNmtVYKA 95
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSGELipnlgdYEEEPSWdevlkRFRGTELQNyfkklyNGEIK--VVHKPQYVDLIPK--VFKG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 96 MdylavLSDIpLRK--RRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFR 173
Cdd:PRK13409 179 K-----VREL-LKKvdERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVA 252
|
170
....*....|....*..
gi 497584106 174 NLLCEIANDRIVILSTH 190
Cdd:PRK13409 253 RLIRELAEGKYVLVVEH 269
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-228 |
8.19e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.43 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 4 KIAVSNLSKRFGK-KQALDNINLEIDS-GMFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGY 79
Cdd:PRK10790 340 RIDIDNVSFAYRDdNLVLQNINLSVPSrGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSslSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 80 LPQD-----FSMYPNMTVYKAMDYLAVLsdiplrkrrkiiaKLLSKVNLTNYqnvkVKSLSGGMNRRLG----------- 143
Cdd:PRK10790 420 VQQDpvvlaDTFLANVTLGRDISEEQVW-------------QALETVQLAEL----ARSLPDGLYTPLGeqgnnlsvgqk 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 144 ----IAQSLIHNPRVLIVDEPTAGLDP--EERI-------RFRNLLCEIANDriviLSThIVgdiEAtcENVAILNSGKV 210
Cdd:PRK10790 483 qllaLARVLVQTPQILILDEATANIDSgtEQAIqqalaavREHTTLVVIAHR----LST-IV---EA--DTILVLHRGQA 552
|
250
....*....|....*...
gi 497584106 211 IYNGSTEALakLAEEKVY 228
Cdd:PRK10790 553 VEQGTHQQL--LAAQGRY 568
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-190 |
1.26e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.57 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 2 EMKIAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATL-----LSKTEGSIHMCGVPIENTK---- 71
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNqITAFIGPSGCGKSTILRCFNRLndlipGFRVEGKVTFHGKNLYAPDvdpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 72 EIRNMVGYL---PQDF--SMYPNMTV------YKA-MDYLAVLSdipLRKrrkiiAKLLSKVNLTNYQNVKvkSLSGGMN 139
Cdd:PRK14243 88 EVRRRIGMVfqkPNPFpkSIYDNIAYgaringYKGdMDELVERS---LRQ-----AALWDEVKDKLKQSGL--SLSGGQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497584106 140 RRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILSTH 190
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-220 |
1.59e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.52 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 15 GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIE--NTKEIRNMVGYLPQDFSMY---- 87
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGqTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvTRASLRRNIAVVFQDAGLFnrsi 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 88 --------PNMT---VYKAMDyLAVLSDIPLRKRRKiiakllskvnltnYQNV---KVKSLSGGMNRRLGIAQSLIHNPR 153
Cdd:PRK13657 426 ednirvgrPDATdeeMRAAAE-RAQAHDFIERKPDG-------------YDTVvgeRGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 154 VLIVDEPTAGLDPEERIRFRNLLCEIANDRivilSTHIVGDIEATCEN---VAILNSGKVIYNGSTEALA 220
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDELMKGR----TTFIIAHRLSTVRNadrILVFDNGRVVESGSFDELV 557
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-189 |
2.48e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.95 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 10 LSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMcgvpienTKEIRnmVGYLPQdfsmyp 88
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGsRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-------AKGIK--LGYFAQ------ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 89 nmtvyKAMDYLAVlSDIPLRKRRKIIAKLLSKvNLTNY------QNVKV----KSLSGGMNRRLGIAQSLIHNPRVLIVD 158
Cdd:PRK10636 383 -----HQLEFLRA-DESPLQHLARLAPQELEQ-KLRDYlggfgfQGDKVteetRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190
....*....|....*....|....*....|....*...
gi 497584106 159 EPTAGLDPEER-------IRFRNLLCEIANDRIVILST 189
Cdd:PRK10636 456 EPTNHLDLDMRqaltealIDFEGALVVVSHDRHLLRST 493
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-165 |
3.17e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 15 GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSK---TEGSIHMCGVPIENTKEIRnmVGYLPQDFSMYPNM 90
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGtLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQRS--IGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 91 TVYKAMDYLAVL---SDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMN----RRLGIAQSLIHNPRVLI-VDEPTA 162
Cdd:TIGR00956 852 TVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNveqrKRLTIGVELVAKPKLLLfLDEPTS 931
|
...
gi 497584106 163 GLD 165
Cdd:TIGR00956 932 GLD 934
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-229 |
4.29e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.54 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILA-----TLlskTEGSIHMCGvpientKEIRNM---- 76
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVhAIMGPNGSGKSTLAKVLMghpkyEV---TSGSILLDG------EDILELspde 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 77 -----VGYL---PQDFsmyPNMTVykaMDYL--AV----LSDIPLRKRRKIIAKLLSKVNLTN-----YQNVkvkSLSGG 137
Cdd:COG0396 74 raragIFLAfqyPVEI---PGVSV---SNFLrtALnarrGEELSAREFLKLLKEKMKELGLDEdfldrYVNE---GFSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 138 MNRRLGIAQSLIHNPRVLIVDEPTAGLDpeerIRFRNLLCEIAN-----DRIVILSTH---IVGDIEATceNVAILNSGK 209
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLD----IDALRIVAEGVNklrspDRGILIITHyqrILDYIKPD--FVHVLVDGR 218
|
250 260
....*....|....*....|
gi 497584106 210 VIYNGSTEaLAKLAEEKVYS 229
Cdd:COG0396 219 IVKSGGKE-LALELEEEGYD 237
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-165 |
4.39e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILAtllskteGSIHMCGVPIENTKEIRnmVGYLPQD 83
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNeRVCLVGRNGAGKSTLMKILN-------GEVLLDDGRIIYEQDLI--VARLQQD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSMYPNMTVYkamDYLA-------------------VLSDiPLRKRRKIIAKLLSKVNLTN-YQ---------------- 127
Cdd:PRK11147 75 PPRNVEGTVY---DFVAegieeqaeylkryhdishlVETD-PSEKNLNELAKLQEQLDHHNlWQlenrinevlaqlgldp 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 497584106 128 NVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLD 165
Cdd:PRK11147 151 DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-187 |
9.65e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 9.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 22 NINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK-EIRNMVG--YLPQD---------FSMYP 88
Cdd:PRK15439 281 NISLEVRAGeILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGlvYLPEDrqssglyldAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 89 NMT--VYKAMDYL-------AVLSdiplRKRRKIIAKLlskvnltNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDE 159
Cdd:PRK15439 361 NVCalTHNRRGFWikparenAVLE----RYRRALNIKF-------NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180
....*....|....*....|....*...
gi 497584106 160 PTAGLDPEERIRFRNLLCEIANDRIVIL 187
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQNVAVL 457
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-215 |
1.47e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.53 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 20 LDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLS--------KTEGSIHMCGVPIENTKEIR--NMVGYLPQD----- 83
Cdd:PRK13547 17 LRDLSLRIEPGrVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDAPRlaRLRAVLPQAaqpaf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 -FSmypnmtvykaMDYLAVLSDIPLRKR--------RKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSL------ 148
Cdd:PRK13547 97 aFS----------AREIVLLGRYPHARRagalthrdGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497584106 149 ---IHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAND-RIVILSthIVGDIEAT---CENVAILNSGKVIYNGS 215
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLA--IVHDPNLAarhADRIAMLADGAIVAHGA 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-219 |
1.58e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.18 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 10 LSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSkTEGSIHMCGVPIENTKE-----IRNMVGYLPQD 83
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGeTLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRrqllpVRHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 fsmyPNMTVYKAMDYLAVLSD--------IPLRKRRKIIAKLLSKVNLTNYQNVKVKS-LSGGMNRRLGIAQSLIHNPRV 154
Cdd:PRK15134 371 ----PNSSLNPRLNVLQIIEEglrvhqptLSAAQREQQVIAVMEEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 155 LIVDEPTAGLDPEERIRFRNLLCEIANDRIV--ILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-210 |
1.74e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.30 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 16 KKQALDNINLEIDSG-MFGLLGRNGAGKTTFMR-ILATLLSKTEGSIHMCGVPIEN---TKEIRNMVGYLPQD---FSMY 87
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGeILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIrnpAQAIRAGIAMVPEDrkrHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 88 PNMTVYK-----AMDYLAVLSDIPLRKRRKIIAKLLSKVNL-TNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPT 161
Cdd:TIGR02633 352 PILGVGKnitlsVLKSFCFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497584106 162 AGLDPEERIRFRNLLCEIANDRI-VILSTHIVGDIEATCENVAILNSGKV 210
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVaIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-219 |
2.39e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.63 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 21 DNINLEIDSG-MFGLLGRNGAGKTtfMRILATL------LSKTEGSIHMCGVPIENTKEIRNMVGYLPQD----FSMYPN 89
Cdd:PRK10418 20 HGVSLTLQRGrVLALVGGSGSGKS--LTCAAALgilpagVRQTAGRVLLDGKPVAPCALRGRKIATIMQNprsaFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 90 MTVYkAMDYLAVLSDIPlrkRRKIIAKLLSKVNLTNYQNVkVKS----LSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLD 165
Cdd:PRK10418 98 MHTH-ARETCLALGKPA---DDATLTAALEAVGLENAARV-LKLypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 166 PEERIRFRNLLCEIANDRI--VILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK10418 173 VVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
7-217 |
2.95e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.04 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRF----GKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSK---TEGSIHMCGVPIENTKE-----I 73
Cdd:PRK09473 15 VKDLRVTFstpdGDVTAVNDLNFSLRAGeTLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEkelnkL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 74 R-NMVGYLPQD--FSMYPNMTVYKAMdyLAVLSdipLRKR-RKIIA-----KLLSKVNLTNYQ---NVKVKSLSGGMNRR 141
Cdd:PRK09473 95 RaEQISMIFQDpmTSLNPYMRVGEQL--MEVLM---LHKGmSKAEAfeesvRMLDAVKMPEARkrmKMYPHEFSGGMRQR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497584106 142 LGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAND--RIVILSTHIVGDIEATCENVAILNSGKVIYNGSTE 217
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-221 |
3.04e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.55 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 17 KQALDNINLEIDSGMF-GLLGRNGAGKTTFMRILATLLsKTEGSIHMCGVPIE--NTKEIRNMVGYLPQDfSMYPNMTVy 93
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRiALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRelDPESWRKHLSWVGQN-PQLPHGTL- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 94 kaMDYLAvLSDIPLRKRRkiIAKLLSKVNLTNY--------------QNVkvkSLSGGMNRRLGIAQSLIHNPRVLIVDE 159
Cdd:PRK11174 440 --RDNVL-LGNPDASDEQ--LQQALENAWVSEFlpllpqgldtpigdQAA---GLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497584106 160 PTAGLD--PEERIrfRNLLCEIANDRIVILSTHIVGDIEAtCENVAILNSGKVIYNGSTEALAK 221
Cdd:PRK11174 512 PTASLDahSEQLV--MQALNAASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQ 572
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-207 |
3.59e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 55 KTEGSIHMCGVPI--ENTKEIRNMVGYLPQDfSMYPNMTVYKAMDY---LAVLSDIPLRKRRKIIAKLLSkvNLTNYQNV 129
Cdd:PTZ00265 1274 KNSGKILLDGVDIcdYNLKDLRNLFSIVSQE-PMLFNMSIYENIKFgkeDATREDVKRACKFAAIDEFIE--SLPNKYDT 1350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 130 KV----KSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAN--DRIVILSTHIVGDIEATcENVA 203
Cdd:PTZ00265 1351 NVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRS-DKIV 1429
|
....
gi 497584106 204 ILNS 207
Cdd:PTZ00265 1430 VFNN 1433
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-190 |
5.06e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.72 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 33 GLLGRNGAGKTTFMRILATLLS------KTEGSI-----HMCGVPIEN------TKEIRnmVGYLPQdfsmYpnmtVYKA 95
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKpnlgdyDEEPSWdevlkRFRGTELQDyfkklaNGEIK--VAHKPQ----Y----VDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 96 MDYL-AVLSDIpLRK--RRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRF 172
Cdd:COG1245 173 PKVFkGTVREL-LEKvdERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNV 251
|
170
....*....|....*....
gi 497584106 173 RNLLCEIAN-DRIVILSTH 190
Cdd:COG1245 252 ARLIRELAEeGKYVLVVEH 270
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-167 |
5.33e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEI-DSGMFGLLGRNGAGKTTFMRILATLLSKTEGSIHmcgvpIENTKEIrnmvGYLPQ- 82
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLpPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-----IGETVKL----AYVDQs 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 -DfSMYPNMTVYKAM----DYLAVLS-DIPLRkrrkiiaKLLSKVNLT-NYQNVKVKSLSGGMNRRLGIAQSLIHNPRVL 155
Cdd:PRK11819 396 rD-ALDPNKTVWEEIsgglDIIKVGNrEIPSR-------AYVGRFNFKgGDQQKKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
170
....*....|..
gi 497584106 156 IVDEPTAGLDPE 167
Cdd:PRK11819 468 LLDEPTNDLDVE 479
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-167 |
6.54e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHmCGVPIEntkeirnmVGYlpqdFS 85
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGdKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKLE--------VAY----FD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 86 MY-----PNMTVykaMDYLA--------------VLSDI------PLRKRrkiiakllskvnltnyqnVKVKSLSGGMNR 140
Cdd:PRK11147 389 QHraeldPEKTV---MDNLAegkqevmvngrprhVLGYLqdflfhPKRAM------------------TPVKALSGGERN 447
|
170 180
....*....|....*....|....*..
gi 497584106 141 RLGIAQSLIHNPRVLIVDEPTAGLDPE 167
Cdd:PRK11147 448 RLLLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-165 |
8.33e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 21 DNINLEIDSG-MFGLLGRNGAGKT-TFMRILATLLSKTEGSIHMCGVP--IENTKE-IRNMVGYLPQD---FSMYPNMTV 92
Cdd:PRK13549 279 DDVSFSLRRGeILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPvkIRNPQQaIAQGIAMVPEDrkrDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 93 YKAMDyLAVLSDIPLRKR----------RKIIAKLLSKvnlTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTA 162
Cdd:PRK13549 359 GKNIT-LAALDRFTGGSRiddaaelktiLESIQRLKVK---TASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
...
gi 497584106 163 GLD 165
Cdd:PRK13549 435 GID 437
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-176 |
1.34e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.97 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 18 QALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGV-----PIENTKEIRNMVGYLPQD--FSMYPN 89
Cdd:PRK11308 29 KALDGVSFTLERGkTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdllkaDPEAQKLLRQKIQIVFQNpyGSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 90 MTVYKAMDY-LAVLSDIPLRKRRKIIAKLLSKVNL-----TNYQNVkvksLSGGMNRRLGIAQSLIHNPRVLIVDEPTAG 163
Cdd:PRK11308 109 KKVGQILEEpLLINTSLSAAERREKALAMMAKVGLrpehyDRYPHM----FSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170
....*....|...
gi 497584106 164 LDPEERIRFRNLL 176
Cdd:PRK11308 185 LDVSVQAQVLNLM 197
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
7-229 |
1.76e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILA--TLLSKTEGSIHMCGVPI-ENTKEIRNMVG-YLP 81
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGeIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESIlDLEPEERAHLGiFLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 ------------QDFSMypnmTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLTN---YQNVKvKSLSGGMNRRLGIAQ 146
Cdd:CHL00131 90 fqypieipgvsnADFLR----LAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPsflSRNVN-EGFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 147 SLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAN-DRIVILSTH-------IVGDIeatcenVAILNSGKVIYNGSTEa 218
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMTsENSIILITHyqrlldyIKPDY------VHVMQNGKIIKTGDAE- 237
|
250
....*....|.
gi 497584106 219 LAKLAEEKVYS 229
Cdd:CHL00131 238 LAKELEKKGYD 248
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-165 |
3.51e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSGM-FGLLGRNGAGKTTFMRILATLLSKTEGSIHMCG---------------VP-- 66
Cdd:PRK10636 2 IVFSSLQIRRGVRVLLDNATATINPGQkVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpalpQPal 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 67 ---IENTKEIRNMVGYLPQDFSM---YPNMTVYKAMDYLAVLSdipLRKRrkiIAKLLSKVNLTNYQNVK-VKSLSGGMN 139
Cdd:PRK10636 82 eyvIDGDREYRQLEAQLHDANERndgHAIATIHGKLDAIDAWT---IRSR---AASLLHGLGFSNEQLERpVSDFSGGWR 155
|
170 180
....*....|....*....|....*.
gi 497584106 140 RRLGIAQSLIHNPRVLIVDEPTAGLD 165
Cdd:PRK10636 156 MRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-206 |
8.57e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.41 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 36 GRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKeiRNMVGYLPQDFSMYPNMTVYKAMDYLAVLSDiplrkRRKIIA 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHNLGLKLEMTVFENLKFWSEIYN-----SAETLY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 116 KLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAND-RIVILSTHivgd 194
Cdd:PRK13541 106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSgGIVLLSSH---- 181
|
170
....*....|..
gi 497584106 195 IEATCENVAILN 206
Cdd:PRK13541 182 LESSIKSAQILQ 193
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-159 |
1.01e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.97 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 19 ALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIhmcgvpientkEIRNMVGYLPQDFSMYPNMTVYKAMD 97
Cdd:PRK13545 39 ALNNISFEVPEGeIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----------DIKGSAALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497584106 98 YLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDE 159
Cdd:PRK13545 108 LKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-165 |
1.18e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMcgvpienTKEIRnmVGYLPQD 83
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGnRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL-------DPNER--LGKLRQD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 FSMYPNMTV-----------YKAM---------------DYLAVlSDIPLR---------KRRKiiAKLLSKVNL-TNYQ 127
Cdd:PRK15064 73 QFAFEEFTVldtvimghtelWEVKqerdriyalpemseeDGMKV-ADLEVKfaemdgytaEARA--GELLLGVGIpEEQH 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 497584106 128 NVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLD 165
Cdd:PRK15064 150 YGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-165 |
1.54e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK-EIRNMVGYLPQDF 84
Cdd:PRK13540 4 VIELDFDYHDQPLLQQISFHLPAGgLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLcTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 85 SMYPNMTVYKAMDYlavlsDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGL 164
Cdd:PRK13540 84 GINPYLTLRENCLY-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
.
gi 497584106 165 D 165
Cdd:PRK13540 159 D 159
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-227 |
1.61e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.09 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 7 VSNLSKRFGKKqaLDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTKE---IRNMVGYLPQ 82
Cdd:PRK09700 268 VRNVTSRDRKK--VRDISFSVCRGeILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldaVKKGMAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 83 ---------DFSMYPNMTVYKAMD---YLAVLSDIPLRKRRKIIAKLLSKVNLTNYQ-NVKVKSLSGGMNRRLGIAQSLI 149
Cdd:PRK09700 346 srrdngffpNFSIAQNMAISRSLKdggYKGAMGLFHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 150 HNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVILS-THIVGDIEATCENVAILNSGKViyNGSTEALAKLAEEKV 227
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMvSSELPEIITVCDRIAVFCEGRL--TQILTNRDDMSEEEI 502
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-219 |
3.17e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.24 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 5 IAVSNLSKRFGK----KQALDNINLEIDSG-MFGLLGRNGAGKT----TFMRILAT-LLSKTEGSIHMCGVPIENTKE-- 72
Cdd:PRK15134 6 LAIENLSVAFRQqqtvRTVVNDVSLQIEAGeTLALVGESGSGKSvtalSILRLLPSpPVVYPSGDIRFHGESLLHASEqt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 73 ---IR-NMVGYLPQD--FSMYPNMTVYKAMdyLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVK------SLSGGMNR 140
Cdd:PRK15134 86 lrgVRgNKIAMIFQEpmVSLNPLHTLEKQL--YEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdyphQLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 141 RLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAN--DRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEA 218
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAAT 243
|
.
gi 497584106 219 L 219
Cdd:PRK15134 244 L 244
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-167 |
4.55e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.10 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 20 LDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENT--KEIRNMVGYLPQD------------- 83
Cdd:TIGR00957 1302 LRHINVTIHGGeKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIglHDLRFKITIIPQDpvlfsgslrmnld 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 84 -FSMYPNMTVYKAMDyLAVLSDIplrkrrkiIAKLLSKVNLTNYQNVKvkSLSGGMNRRLGIAQSLIHNPRVLIVDEPTA 162
Cdd:TIGR00957 1382 pFSQYSDEEVWWALE-LAHLKTF--------VSALPDKLDHECAEGGE--NLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
....*
gi 497584106 163 GLDPE 167
Cdd:TIGR00957 1451 AVDLE 1455
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-169 |
1.05e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 13 RFGKKQALDNINLEIDSGM-FGLLGRNGAGKTTFMRILA-----------TLLSKTEGSihmcGvpiENTKEIRNMVGYL 80
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEhWQIVGPNGAGKSTLLSLITgdhpqgysndlTLFGRRRGS----G---ETIWDIKKHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 81 PQDFSM----------------YPNMTVYKAmdylavLSDiplrKRRKIIAKLLSKVNLTNYQ-NVKVKSLSGGMNRRLG 143
Cdd:PRK10938 342 SSSLHLdyrvstsvrnvilsgfFDSIGIYQA------VSD----RQQKLAQQWLDILGIDKRTaDAPFHSLSWGQQRLAL 411
|
170 180
....*....|....*....|....*.
gi 497584106 144 IAQSLIHNPRVLIVDEPTAGLDPEER 169
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLNR 437
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-220 |
1.47e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.33 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 17 KQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENTK--EIRN---MVGYLPQDFSmypnm 90
Cdd:PRK10789 328 HPALENVNFTLKPGqMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldSWRSrlaVVSQTPFLFS----- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 91 tvykamDYLAvlSDIPLRK----RRKI--IAKLLSK----VNLTNYQNVKVKS----LSGGMNRRLGIAQSLIHNPRVLI 156
Cdd:PRK10789 403 ------DTVA--NNIALGRpdatQQEIehVARLASVhddiLRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497584106 157 VDEPTAGLD--PEERIrFRNLLcEIANDRIVILSTHIVGDI-EATceNVAILNSGKVIYNGSTEALA 220
Cdd:PRK10789 475 LDDALSAVDgrTEHQI-LHNLR-QWGEGRTVIISAHRLSALtEAS--EILVMQHGHIAQRGNHDQLA 537
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
134-217 |
1.63e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 134 LSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRI--VILSTHIVGDIEATCENVAILNSGKVI 211
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....*.
gi 497584106 212 YNGSTE 217
Cdd:PRK10261 249 ETGSVE 254
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-190 |
4.02e-06 |
|
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: 46.98 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 28 DSGMFGLLGRNGAGKTTFMRILATLLSKTEGSI-----------HMCGVPIENT-KEIRN---MVGYLPQDFSMYPNMTV 92
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYfTKLLEgdvKVIVKPQYVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 93 YKAMDYLAVLSDiplrkrRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRF 172
Cdd:cd03236 105 GKVGELLKKKDE------RGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170
....*....|....*....
gi 497584106 173 RNLLCEIAND-RIVILSTH 190
Cdd:cd03236 179 ARLIRELAEDdNYVLVVEH 197
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-165 |
4.91e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 17 KQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSihmcgvpienTKEIRNMVGYLPQdFSMYPNMTV--- 92
Cdd:PLN03232 630 KPTLSDINLEIPVGsLVAIVGGTGEGKTSLISAMLGELSHAETS----------SVVIRGSVAYVPQ-VSWIFNATVren 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 93 ------------YKAMDYLAVLSDIPLRKRRKIIAKLLSKVNLtnyqnvkvkslSGGMNRRLGIAQSLIHNPRVLIVDEP 160
Cdd:PLN03232 699 ilfgsdfeseryWRAIDVTALQHDLDLLPGRDLTEIGERGVNI-----------SGGQKQRVSMARAVYSNSDIYIFDDP 767
|
....*
gi 497584106 161 TAGLD 165
Cdd:PLN03232 768 LSALD 772
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-165 |
6.68e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 32 FGLLGRNGAGKTTFMRILAtlLSKTEGSIHMCGV---------------------PIENTKEIRNMVGYLPQDFSM-YPN 89
Cdd:PLN03073 206 YGLVGRNGTGKTTFLRYMA--MHAIDGIPKNCQIlhveqevvgddttalqcvlntDIERTQLLEEEAQLVAQQRELeFET 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 90 MTVYKAMDYLAVLSDIPLRKRRKIIAKLLSKVNL-----------------TNYQNVKVKSLSGGMNRRLGIAQSLIHNP 152
Cdd:PLN03073 284 ETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAytaearaasilaglsftPEMQVKATKTFSGGWRMRIALARALFIEP 363
|
170
....*....|...
gi 497584106 153 RVLIVDEPTAGLD 165
Cdd:PLN03073 364 DLLLLDEPTNHLD 376
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2-210 |
1.19e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 2 EMKIAVSNLSKRfgKKQALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIEN----------- 69
Cdd:PRK10982 248 EVILEVRNLTSL--RQPSIRDVSFDLHKGeILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneainhgf 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 70 ---TKEIRN--MVGYLPQDF-SMYPNMTVYKamDYLAVLSDIPLRKRRK-IIAKLLSKvnlTNYQNVKVKSLSGGMNRRL 142
Cdd:PRK10982 326 alvTEERRStgIYAYLDIGFnSLISNIRNYK--NKVGLLDNSRMKSDTQwVIDSMRVK---TPGHRTQIGSLSGGNQQKV 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 143 GIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIAN-DRIVILSTHIVGDIEATCENVAILNSGKV 210
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKkDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-210 |
1.47e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 19 ALDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGvpientkeirnMVGYLPQDFSMYPNMTVYKAMD 97
Cdd:PRK13546 39 ALDDISLKAYEGdVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIAISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 98 YLAVLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLC 177
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIY 187
|
170 180 190
....*....|....*....|....*....|....
gi 497584106 178 EI-ANDRIVILSTHIVGDIEATCENVAILNSGKV 210
Cdd:PRK13546 188 EFkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-195 |
1.48e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 22 NINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVpiENTKEI-----RNMVGYLPQDFSMYPN------ 89
Cdd:PTZ00265 403 DLNFTLTEGkTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDInlkwwRSKIGVVSQDPLLFSNsiknni 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 90 -MTVYKAMDyLAVLSDI----------PLRKRRKIIAKLLSKVNL--------------TNYQNVK-------------- 130
Cdd:PTZ00265 481 kYSLYSLKD-LEALSNYynedgndsqeNKNKRNSCRAKCAGDLNDmsnttdsneliemrKNYQTIKdsevvdvskkvlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 131 -----------------VKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIA--NDRIVILSTHI 191
Cdd:PTZ00265 560 dfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHR 639
|
....
gi 497584106 192 VGDI 195
Cdd:PTZ00265 640 LSTI 643
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
10-170 |
1.91e-05 |
|
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: 44.10 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 10 LSKRFGKKQALDNINLEIDSGMFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVpientkeirnMVGYLPQdfsmypn 89
Cdd:cd03222 6 CVKRYGVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI----------TPVYKPQ------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 90 mtvykamdylavlsdiplrkrrKIiakllskvnltnyqnvkvkSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEER 169
Cdd:cd03222 69 ----------------------YI-------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQR 107
|
.
gi 497584106 170 I 170
Cdd:cd03222 108 L 108
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
19-176 |
2.54e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.35 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 19 ALDNINLEIDSG--MFgLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPI--ENTKEIRNMVGYLPQDFSMYPNMTVYK 94
Cdd:PRK10522 338 SVGPINLTIKRGelLF-LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtaEQPEDYRKLFSAVFTDFHLFDQLLGPE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 95 AMDYLAVLSDIPLRKrrkiiAKLLSKVNLTNYQNVKVKsLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPE-ERIRFR 173
Cdd:PRK10522 417 GKPANPALVEKWLER-----LKMAHKLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDPHfRREFYQ 490
|
...
gi 497584106 174 NLL 176
Cdd:PRK10522 491 VLL 493
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
101-190 |
3.21e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 44.69 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 101 VLSDIPLRKRRKIIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLI---HNPRVLIVDEPTAGLDPEERIRFRNLLC 177
Cdd:pfam13304 204 EGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLK 283
|
90
....*....|....
gi 497584106 178 EIANDRI-VILSTH 190
Cdd:pfam13304 284 ELSRNGAqLILTTH 297
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
114-219 |
3.60e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 114 IAKLLSKvnltnyqnvKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRI-VILSTHIV 192
Cdd:PRK10938 125 ITALLDR---------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGItLVLVLNRF 195
|
90 100
....*....|....*....|....*..
gi 497584106 193 GDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK10938 196 DEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-165 |
4.47e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 15 GKKQALDNINLEIDSGMF-GLLGRNGAGKTTFMR-ILATLLSKTEGSIhmcgvpientkEIRNMVGYLPQdFSMYPNMTV 92
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLvAIVGSTGEGKTSLISaMLGELPPRSDASV-----------VIRGTVAYVPQ-VSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 93 ---------------YKAMDYLAVLSDIplrkrrkiiaKLLSKVNLTNYQNVKVkSLSGGMNRRLGIAQSLIHNPRVLIV 157
Cdd:PLN03130 696 rdnilfgspfdperyERAIDVTALQHDL----------DLLPGGDLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIF 764
|
....*...
gi 497584106 158 DEPTAGLD 165
Cdd:PLN03130 765 DDPLSALD 772
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
20-190 |
5.00e-05 |
|
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: 44.22 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 20 LDNINLEIDSGMFGLLGRNGAGKTTFMRILATLLSKTEGS------IHMCGVPIENTKEI--------RNMVGYLP---- 81
Cdd:COG3593 14 IKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRkfdeedFYLGDDPDLPEIEIeltfgsllSRLLRLLLkeed 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 82 -------------------QDFSMYPNMTVYKAMDYLAVLSDIPLRKRRKIIAKLlsKVNLTNYQNVKVKSLSGGMNRRL 142
Cdd:COG3593 94 keeleealeelneelkealKALNELLSEYLKELLDGLDLELELSLDELEDLLKSL--SLRIEDGKELPLDRLGSGFQRLI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497584106 143 GIA-------QSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRI-VILSTH 190
Cdd:COG3593 172 LLAllsalaeLKRAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNqVIITTH 227
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
108-219 |
9.59e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 108 RKRRKIiaKLLSKVNLTNYQNVkVKS----LSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEI--AN 181
Cdd:PRK15093 132 RKRRAI--ELLHRVGIKDHKDA-MRSfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnqNN 208
|
90 100 110
....*....|....*....|....*....|....*...
gi 497584106 182 DRIVILSTHIVGDIEATCENVAILNSGKVIYNGSTEAL 219
Cdd:PRK15093 209 NTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-167 |
1.21e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.20 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 23 INLEIDSGMFGL-LGRNGAGKTTFMRILATLLSKTEGSIhmcgvpienTKEIRNMVGYLPQDfsmyPNMTVYKAMDYLAV 101
Cdd:TIGR00954 471 LSFEVPSGNNLLiCGPNGCGKSSLFRILGELWPVYGGRL---------TKPAKGKLFYVPQR----PYMTLGTLRDQIIY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 102 LSDIPLRKRR----KIIAKLLSKVNLTN----------YQNVKvKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPE 167
Cdd:TIGR00954 538 PDSSEDMKRRglsdKDLEQILDNVQLTHilereggwsaVQDWM-DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD 616
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-219 |
1.48e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 33 GLLGRNGAGKTTFMRILATLLSKTEGSIHM--CGVPIENTKEIRNMVGYLPQDFSMYPNmTVYKAMDYLAVLSDIPLRK- 109
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIddCDVAKFGLTDLRRVLSIIPQSPVLFSG-TVRFNIDPFSEHNDADLWEa 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 110 -RRKIIAKLLSKVNLTNYQNVKV--KSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLCEIANDRIVI 186
Cdd:PLN03232 1345 lERAHIKDVIDRNPFGLDAEVSEggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTML 1424
|
170 180 190
....*....|....*....|....*....|...
gi 497584106 187 LSTHIVGDIeATCENVAILNSGKVIYNGSTEAL 219
Cdd:PLN03232 1425 VIAHRLNTI-IDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-225 |
2.01e-04 |
|
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: 41.82 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 4 KIAVSNLSKRFGK--KQALDNINLEIDSGM-FGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPIENT--KEIRNMVG 78
Cdd:cd03288 19 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQkVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 79 YLPQDFSMYPNmTVYKAMDYLAVLSDiplrkrrkiiAKLLSKVNLTNYQNVkVKSLSGGMN--------------RRL-G 143
Cdd:cd03288 99 IILQDPILFSG-SIRFNLDPECKCTD----------DRLWEALEIAQLKNM-VKSLPGGLDavvteggenfsvgqRQLfC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 144 IAQSLIHNPRVLIVDEPTAGLD-PEERIRFRNLLCEIAnDRIVILSTHIVGDIeATCENVAILNSGKVIYNGSTEALakL 222
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDmATENILQKVVMTAFA-DRTVVTIAHRVSTI-LDADLVLVLSRGILVECDTPENL--L 242
|
...
gi 497584106 223 AEE 225
Cdd:cd03288 243 AQE 245
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
131-190 |
2.50e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 2.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497584106 131 VKSLSGGMNRRLGIAQSLIH---NPRVL-IVDEPTAGLDPEERIRFRNLLCEIA-NDRIVILSTH 190
Cdd:cd03227 75 RLQLSGGEKELSALALILALaslKPRPLyILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITH 139
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-195 |
2.72e-04 |
|
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: 40.43 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 33 GLLGRNGAGKTTFMRILATLLSKTEGSIHMCGVPientkeirnmvgylpqdfsmypnmtvykamdylavlsdiplrkrrk 112
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGE---------------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 113 IIAKLLSKVNLTNYQNVKVKSLSGGMNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERIRFRNLLC-------EIANDRIV 185
Cdd:smart00382 40 DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllllKSEKNLTV 119
|
170
....*....|
gi 497584106 186 ILSTHIVGDI 195
Cdd:smart00382 120 ILTTNDEKDL 129
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
22-128 |
6.77e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 22 NINLEIDSGMFGLLGRNGAGKTTFMRILATLLSKTEGSIhmcgvpieNTKEIRNMVGYLPQDFSMYPNMTVYKAMDYlav 101
Cdd:COG3950 18 EIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRL--------DDVKFRKLLIRNGEFGDSAKLILYYGTSRL--- 86
|
90 100
....*....|....*....|....*..
gi 497584106 102 LSDIPLRKRRKIIAKLLSKvnLTNYQN 128
Cdd:COG3950 87 LLDGPLKKLERLKEEYFSR--LDGYDS 111
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-191 |
7.77e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 4 KIAVSNLsKRFGKKQALDninleIDSGMFGLLGRNGAGKTTFMRILATLL-----SKTEGSIHMCGVPIENT-------- 70
Cdd:COG0419 4 RLRLENF-RSYRDTETID-----FDDGLNLIVGPNGAGKSTILEAIRYALygkarSRSKLRSDLINVGSEEAsvelefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 71 ----------------------KEIRNMVGYLPQDfsmypnMTVYKAMDYLAVLSDIP------LRKRRKIIAKLLSKvn 122
Cdd:COG0419 78 ggkryrierrqgefaefleakpSERKEALKRLLGL------EIYEELKERLKELEEALesaleeLAELQKLKQEILAQ-- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584106 123 LTNYQNvkVKSLSGGMNRRLGIAQSLihnprVLIVDepTAGLDPEERIRFRNLLceianDRIVILSTHI 191
Cdd:COG0419 150 LSGLDP--IETLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDAL-----EELAIITHVI 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-219 |
9.09e-04 |
|
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: 40.70 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 20 LDNINLEIDSG-MFGLLGRNGAGKTTFMRILATLLSKTEGSIHMCGvpientkeirnMVGYLPQD-------------FS 85
Cdd:TIGR00957 654 LNGITFSIPEGaLVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------SVAYVPQQawiqndslrenilFG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584106 86 MYPNMTVYKA-MDYLAVLSDI---PLRKRRKIIAKllsKVNLtnyqnvkvkslSGGMNRRLGIAQSLIHNPRVLIVDEPT 161
Cdd:TIGR00957 723 KALNEKYYQQvLEACALLPDLeilPSGDRTEIGEK---GVNL-----------SGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497584106 162 AGLDPE--ERIrFRNLLCE--IANDRIVILSTHIVGDIEATcENVAILNSGKVIYNGSTEAL 219
Cdd:TIGR00957 789 SAVDAHvgKHI-FEHVIGPegVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3-55 |
7.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 37.82 E-value: 7.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 497584106 3 MKIAVSNLsKRFGKkqaLDNINLEIDSGMFGLLGRNGAGKTTFMR-ILATLLSK 55
Cdd:COG4717 1 MKIKELEI-YGFGK---FRDRTIEFSPGLNVIYGPNEAGKSTLLAfIRAMLLER 50
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
131-190 |
7.76e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 36.82 E-value: 7.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497584106 131 VKSLSGG------MNRRLGIAQSLIHNPRVLIVDEPTAGLDPEERirfRNLLCEIANDR--------IVIlsTH 190
Cdd:cd03240 113 RGRCSGGekvlasLIIRLALAETFGSNCGILALDEPTTNLDEENI---EESLAEIIEERksqknfqlIVI--TH 181
|
|
| |
