|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-214 |
1.58e-118 |
|
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: 339.17 E-value: 1.58e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQMIGYLPQ 82
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 163 GLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-228 |
1.36e-94 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 279.26 E-value: 1.36e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQMIGYLP 81
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGeIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVaRDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPT 161
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1436942050 162 AGLDPEERVRIRNLLSDLA-ENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSDDHIY 228
Cdd:COG1131 160 SGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVF 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-233 |
3.90e-70 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 217.42 E-value: 3.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQMIGYLP 81
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGeITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPT 161
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 162 AGLDPEERVRIRNLLSDLA-ENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQ-SDDHIYEINLS 233
Cdd:COG4555 161 NGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEiGEENLEDAFVA 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-210 |
2.26e-69 |
|
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: 212.64 E-value: 2.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQMIGYLP 81
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGeIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVLYYlgflskinqtdfdkyvdlilrkvnlidyknkkvkslSGGMKKRLGIAQAILHDPKVIIVDEPT 161
Cdd:cd03230 80 EEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1436942050 162 AGLDPEERVRIRNLLSDLA-ENKIVIISTHIVSDIESTCNRIAILDKGSL 210
Cdd:cd03230 124 SGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-214 |
4.97e-64 |
|
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: 200.81 E-value: 4.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSY-DGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQMIGYL 80
Cdd:cd03263 1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGeIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEP 160
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 161 TAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-230 |
1.43e-62 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 199.56 E-value: 1.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIknSQKIRQMIGYLPQ 82
Cdd:COG4152 2 LELKGLTKRFGDKT-AVDDVSFTVPKGeIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL--DPEDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:COG4152 79 ERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1436942050 163 GLDPEERVRIRNLLSDLAEN-KIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSDDHIYEI 230
Cdd:COG4152 159 GLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRL 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-214 |
1.74e-58 |
|
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: 186.27 E-value: 1.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQMIGYLPQ 82
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGeIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFDFYPNMKVSEVLYYLGFLSKINqtdfDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 163 GLDPEERVRIRNLLSDLAENKI-VIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGItVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
4-267 |
1.53e-57 |
|
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: 186.90 E-value: 1.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQMIGYLP 81
Cdd:TIGR03522 3 IRVSSLTKLY-GTQNALDEVSFEAQKGrIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVlQNPKEVQRNIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPT 161
Cdd:TIGR03522 82 EHNPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 162 AGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSDDHIYEINLS-PSELESF 240
Cdd:TIGR03522 162 TGLDPNQLVEIRNVIKNIGKDKTIILSTHIMQEVEAICDRVIIINKGKIVADKKLDELSAANKKQVIEVEFEeQIDLQLF 241
|
250 260
....*....|....*....|....*..
gi 1436942050 241 RENDLFITKTQEIENKLKVRFISETKV 267
Cdd:TIGR03522 242 ETLEEISSVKNTGGNTWKLTFETPNDT 268
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-224 |
1.59e-56 |
|
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: 182.15 E-value: 1.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--KNSQKIRQMIGYL 80
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFvAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItkKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQDFD---FYP-----------NMKVSEvlyylgflSKInqtdfDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQ 146
Cdd:COG1122 81 FQNPDdqlFAPtveedvafgpeNLGLPR--------EEI-----RERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1436942050 147 AILHDPKVIIVDEPTAGLDPEERVRIRNLLSDL-AENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSD 224
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-214 |
1.31e-53 |
|
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: 174.01 E-value: 1.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIknSQKIRQMIGYLPQDF 84
Cdd:cd03269 3 VENVTKRF-GRVTALDDISFSVEKGeIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL--DIAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 85 DFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGL 164
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 165 DPEERVRIRNLLSDLAEN-KIVIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:cd03269 160 DPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-212 |
1.21e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 172.58 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGieiKNSQKIRQMIGYLPQ 82
Cdd:COG1121 7 IELENLTVSYGGRP-VLEDVSLTIPPGeFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG---KPPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFDFYPN--MKVSEV-----LYYLGFLSKINQTDFDKyVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVI 155
Cdd:COG1121 83 RAEVDWDfpITVRDVvlmgrYGRRGLFRRPSRADREA-VDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1436942050 156 IVDEPTAGLDPEERVRIRNLLSDL-AENKIVIISTHIVSDIESTCNRIAILDKGSLVY 212
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-214 |
3.91e-52 |
|
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: 170.24 E-value: 3.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKD---ALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQMIG 78
Cdd:cd03266 2 ITADALTKRFRDVKKtvqAVDGVSFTVKPGeVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVD 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 159 EPTAGLDPEERVRIRNLLSDL-AENKIVIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-208 |
7.91e-51 |
|
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: 166.87 E-value: 7.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 5 VIKGLSKSY-DGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQ--KIRQMIGYL 80
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFvLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlkELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQDFD---FYPNmkV-SEVLYYLGFLsKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVII 156
Cdd:cd03225 81 FQNPDdqfFGPT--VeEEVAFGLENL-GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 157 VDEPTAGLDPEERVRIRNLLSDL-AENKIVIISTHIVSDIESTCNRIAILDKG 208
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-214 |
1.30e-50 |
|
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: 166.39 E-value: 1.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQMIGYLP 81
Cdd:cd03265 1 IEVENLVKKYGDFE-AVRGVSFRVRRGeIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPT 161
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 162 AGLDPEERVRIRNLLSDL--AENKIVIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-215 |
7.13e-50 |
|
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: 165.60 E-value: 7.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN--SQKIRQMIGYL 80
Cdd:COG1120 2 LEAENLSVGYGGRP-VLDDVSLSLPPGEVtALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQDFDFYPNMKVSE-VLY----YLGFLSKINQTDFDKyVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVI 155
Cdd:COG1120 81 PQEPPAPFGLTVRElVALgrypHLGLFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 156 IVDEPTAGLDPEERVRIRNLLSDLA--ENKIVIISTHivsDIE---STCNRIAILDKGSLVYKGD 215
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLAreRGRTVVMVLH---DLNlaaRYADRLVLLKDGRIVAQGP 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-225 |
9.08e-50 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 164.77 E-value: 9.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 2 NKIVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNS-----QKIRQ 75
Cdd:COG1127 4 PMIEVRNLTKSFGDRV-VLDGVSLDVPRGeILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLsekelYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 76 MIGYLPQD---FDfypNMKVSE-VLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHD 151
Cdd:COG1127 83 RIGMLFQGgalFD---SLTVFEnVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 152 PKVIIVDEPTAGLDPEERVRIRNLLSDL-AENKI-VIISTHIVSDIESTCNRIAILDKGSLVYKGDiPSLIQQSDD 225
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELrDELGLtSVVVTHDLDSAFAIADRVAVLADGKIIAEGT-PEELLASDD 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-214 |
2.87e-48 |
|
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: 160.39 E-value: 2.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKdALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGieiKNSQKIRQMIGYLPQ-- 82
Cdd:cd03235 2 VEDLTVSYGGHP-VLEDVSFEVKPGEFlAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG---KPLEKERKRIGYVPQrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFDFYPNMKVSEV-----LYYLGFLSKINQTDFDKyVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIV 157
Cdd:cd03235 78 SIDRDFPISVRDVvlmglYGHKGLFRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 158 DEPTAGLDPEERVRIRNLLSDL-AENKIVIISTHivsDIEST---CNRIAILDKGsLVYKG 214
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELrREGMTILVVTH---DLGLVleyFDRVLLLNRT-VVASG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-210 |
6.20e-48 |
|
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: 159.58 E-value: 6.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSY---DGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN------SQKI 73
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFvAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 74 RQMIGYLPQDFDFYPNMKVSE-VLYYLgFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDP 152
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALEnVELPL-LLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 153 KVIIVDEPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHIVsDIESTCNRIAILDKGSL 210
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-228 |
2.44e-47 |
|
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: 158.89 E-value: 2.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-----KNSQKIRQMI 77
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGeFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQDFDFYPNMKVSE-VLyyLGFLSKINQ--------TDFDKYVDL-ILRKVNLIDYKNKKVKSLSGGMKKRLGIAQA 147
Cdd:cd03256 81 GMIFQQFNLIERLSVLEnVL--SGRLGRRSTwrslfglfPKEEKQRALaALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 148 ILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLA--ENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSDD 225
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINreEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLD 238
|
...
gi 1436942050 226 HIY 228
Cdd:cd03256 239 EIY 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-230 |
6.16e-47 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 157.91 E-value: 6.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-----KNSQKIRQMI 77
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFvALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalrgRALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQDFDFYPNMKVSE-V----LYYLGF----LSKINQTDFDKYVDLiLRKVNLIDYKNKKVKSLSGGMKKRLGIAQAI 148
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTnVlagrLGRTSTwrslLGLFPPEDRERALEA-LERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 149 LHDPKVIIVDEPTAGLDPEERVRIRNLLSDLA-ENKI-VIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLiqqSDDH 226
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGItVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL---TDAV 238
|
....
gi 1436942050 227 IYEI 230
Cdd:COG3638 239 LREI 242
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-225 |
1.31e-46 |
|
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: 156.51 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-----KNSQKIRQMI 77
Cdd:cd03261 1 IELRGLTKSFGGRT-VLKGVDLDVRRGeILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglseAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQD---FDfypNMKVSE-VLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPK 153
Cdd:cd03261 80 GMLFQSgalFD---SLTVFEnVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 154 VIIVDEPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSlIQQSDD 225
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE-LRASDD 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-211 |
6.83e-46 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 154.21 E-value: 6.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQMIGYLPQ 82
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGeFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFDFYPNMKVSE-VLYYLGfLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPT 161
Cdd:cd03259 80 DYALFPHLTVAEnIAFGLK-LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 162 AGLDPEERVRIRNLLSDLAEN--KIVIISTHIVSDIESTCNRIAILDKGSLV 211
Cdd:cd03259 159 SALDAKLREELREELKELQRElgITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-211 |
1.10e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.05 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIV-IKGLSKSY---DGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI---KNSQ- 71
Cdd:COG1136 1 MSPLLeLRNLTKSYgtgEGEVTALRGVSLSIEAGEFvAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslSEREl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 72 -KIR-QMIGYLPQDFDFYPNMKVSE----VLYYLGFLSKINQTDFDKyvdlILRKVNLIDYKNKKVKSLSGGMKKRLGIA 145
Cdd:COG1136 81 aRLRrRHIGFVFQFFNLLPELTALEnvalPLLLAGVSRKERRERARE----LLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 146 QAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHivsD--IESTCNRIAILDKGSLV 211
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTH---DpeLAARADRVIRLRDGRIV 223
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-237 |
1.19e-45 |
|
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: 156.40 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 11 KSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQMIGYLPQDFDFYP 88
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGeVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvREPRKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 89 NMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEE 168
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 169 RVRIRNLLSDLAENKI-VIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQ-SDDHIYEINLSPSEL 237
Cdd:TIGR01188 160 RRAIWDYIRALKEEGVtILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRlGKDTLESRPRDIQSL 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-228 |
4.33e-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: 156.99 E-value: 4.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKD----ALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-----KNSQKI 73
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvrAVDDVSLTLRRGeTLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklsrRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 74 RQMIGYLPQD----FDfyPNMKVSEVLYY-LGFLSKINQTDFDKYVDLILRKVNLI-DYKNKKVKSLSGGMKKRLGIAQA 147
Cdd:COG1123 341 RRRVQMVFQDpyssLN--PRMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 148 ILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK---IVIIsTHIVSDIESTCNRIAILDKGSLVYKGDiPSLIQQSD 224
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELgltYLFI-SHDLAVVRYIADRVAVMYDGRIVEDGP-TEEVFANP 496
|
....
gi 1436942050 225 DHIY 228
Cdd:COG1123 497 QHPY 500
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-211 |
7.28e-44 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 149.05 E-value: 7.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDALNSLDLVIPNGMFGIL-GRNGSGKSTLMNIIATILQPSKGTVTINGIE---IKNSQ--KIRQMI 77
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREipYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQDFDFYPNMKVSE----VLYYLGFlskiNQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPK 153
Cdd:COG2884 82 GVVFQDFRLLPDRTVYEnvalPLRVTGK----SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1436942050 154 VIIVDEPTAGLDPEERVRIRNLLSDLAENKI-VIISTHIVSDIESTCNRIAILDKGSLV 211
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTtVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-206 |
8.18e-44 |
|
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: 148.40 E-value: 8.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQMIGYLP 81
Cdd:COG4133 3 LEAENLSCRRGERL-LFSGLSFTLAAGeALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEvlyYLGFLSKINQTDFDK-YVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEP 160
Cdd:COG4133 82 HADGLKPELTVRE---NLRFWAALYGLRADReAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1436942050 161 TAGLDPEERVRIRNLLSDLAEN-KIVIISTHIVSDIEStCNRIAILD 206
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARgGAVLLTTHQPLELAA-ARVLDLGD 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-208 |
6.99e-43 |
|
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: 144.31 E-value: 6.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--KNSQKIRQMIGYLPQ 82
Cdd:cd00267 2 IENLSFRYGGRT-ALDNVSLTLKAGeIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIakLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 dfdfypnmkvsevlyylgflskinqtdfdkyvdlilrkvnlidyknkkvksLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1436942050 163 GLDPEERVRIRNLLSDLA-ENKIVIISTHIVSDIESTCNRIAILDKG 208
Cdd:cd00267 110 GLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-208 |
1.15e-42 |
|
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: 144.64 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI----KNSQKIRQMIG 78
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGeIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdleDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDFDFYPNMKVSEVLYYLgflskinqtdfdkyvdlilrkvnlidyknkkvksLSGGMKKRLGIAQAILHDPKVIIVD 158
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 159 EPTAGLDPEERVRIRNLLSDLAEN--KIVIISTHIVSDIESTCNRIAILDKG 208
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-214 |
1.93e-42 |
|
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: 144.12 E-value: 1.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN--SQKIRQMIGYLPQ 82
Cdd:cd03214 2 VENLSVGY-GGRTVLDDLSLSIEAGeIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlsPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 dfdfypnmkvsevlyylgflskinqtdfdkyvdlILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 163 GLDPEERVRIRNLLSDLA--ENKIVIISTHivsDIEST---CNRIAILDKGSLVYKG 214
Cdd:cd03214 127 HLDIAHQIELLELLRRLAreRGKTVVMVLH---DLNLAaryADRVILLKDGRIVAQG 180
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-228 |
4.34e-41 |
|
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: 142.82 E-value: 4.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDALNSLDLVI-PNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-----KNSQKIRQMI 77
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNInPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrgKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQDFDFYPNMKVSE-VLY-YLGFLSKINQ-----TDFDKYVDL-ILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAIL 149
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLEnVLHgRLGYKPTWRSllgrfSEEDKERALsALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 150 HDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK--IVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSDDHI 227
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRHI 241
|
.
gi 1436942050 228 Y 228
Cdd:TIGR02315 242 Y 242
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-214 |
9.31e-41 |
|
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: 141.25 E-value: 9.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 11 KSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSK---GTVTINGIEIKnSQKIRQMIGYLPQDFDF 86
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGqVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRK-PDQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 87 YPNMKVSEVLYY-LGFLSKINQTDFDK---YVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:cd03234 93 LPGLTVRETLTYtAILRLPRKSSDAIRkkrVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 163 GLDPEERVRIRNLLSDLA-ENKIVIISTHI-VSDIESTCNRIAILDKGSLVYKG 214
Cdd:cd03234 173 GLDSFTALNLVSTLSQLArRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-208 |
1.09e-40 |
|
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: 139.06 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGK-KDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGY 79
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKvAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRdlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDFYpNMKVSEvlyylgflskinqtdfdkyvdlilrkvNLidyknkkvksLSGGMKKRLGIAQAILHDPKVIIVDE 159
Cdd:cd03228 81 VPQDPFLF-SGTIRE---------------------------NI----------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1436942050 160 PTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIEStCNRIAILDKG 208
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-214 |
1.92e-40 |
|
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: 140.33 E-value: 1.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKD---ALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKI----RQM 76
Cdd:cd03257 4 VKNLSVSFPTGGGsvkALDDVSFSIKKGeTLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlKLSRRLrkirRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 77 IGYLPQD----FDfyPNMKV----SEVLYYLGFLSKinQTDFDKYVDLILRKVNL-IDYKNKKVKSLSGGMKKRLGIAQA 147
Cdd:cd03257 84 IQMVFQDpmssLN--PRMTIgeqiAEPLRIHGKLSK--KEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 148 ILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK---IVIIsTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELgltLLFI-THDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-240 |
2.54e-40 |
|
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: 141.43 E-value: 2.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGK----KDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK-----I 73
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFvAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkklkdL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 74 RQMIGYLPQ-------------DFDFYP-NMKVSEvlyylgflskinqTDFDKYVDLILRKVNL-IDYKNKKVKSLSGGM 138
Cdd:TIGR04521 81 RKKVGLVFQfpehqlfeetvykDIAFGPkNLGLSE-------------EEAEERVKEALELVGLdEEYLERSPFELSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 139 KKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDL--AENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGdI 216
Cdd:TIGR04521 148 MRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG-T 226
|
250 260
....*....|....*....|....
gi 1436942050 217 PSLIQQSDDHIYEINLSPSELESF 240
Cdd:TIGR04521 227 PREVFSDVDELEKIGLDVPEITEL 250
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-222 |
4.25e-40 |
|
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: 148.44 E-value: 4.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDG-KKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGY 79
Cdd:COG2274 474 IELENVSFRYPGdSPPVLDNISLTIKPGERvAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqiDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDFYP-----NMKVSEvlyylgflskiNQTDFDKYVDlILRKVNLIDYKNK-------KV----KSLSGGMKKRLG 143
Cdd:COG2274 554 VLQDVFLFSgtireNITLGD-----------PDATDEEIIE-AARLAGLHDFIEAlpmgydtVVgeggSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1436942050 144 IAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIEStCNRIAILDKGSLVYKGDIPSLIQQ 222
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-260 |
4.37e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 140.61 E-value: 4.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSY---DGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKnsqKIRQM 76
Cdd:COG1116 5 APALELRGVSKRFptgGGGVTALDDVSLTVAAGEFvALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT---GPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 77 IGYLPQDFDFYPNMKVSE-VLYYLGfLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVI 155
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDnVALGLE-LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 156 IVDEPTAGLDPEERVRIRNLLSDL--AENKIVIISTHivsDIE---STCNRIAILDKGslvykgdiPSLIQqsddHIYEI 230
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTH---DVDeavFLADRVVVLSAR--------PGRIV----EEIDV 225
|
250 260 270
....*....|....*....|....*....|
gi 1436942050 231 NLSPSELESFRENDLFITKTQEIENKLKVR 260
Cdd:COG1116 226 DLPRPRDRELRTSPEFAALRAEILDLLREE 255
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-216 |
5.18e-40 |
|
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: 139.64 E-value: 5.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKD---ALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-----KNSQKIR 74
Cdd:cd03258 2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGeIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsgKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 75 QMIGYLPQDFDFYPNMKVSE-VLYYLGfLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPK 153
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFEnVALPLE-IAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1436942050 154 VIIVDEPTAGLDPEERVRIRNLLSDLaeNK-----IVIIsTHIVSDIESTCNRIAILDKGSLVYKGDI 216
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDI--NRelgltIVLI-THEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-216 |
5.14e-39 |
|
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: 136.76 E-value: 5.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--KNSQKIRQMIGYL 80
Cdd:TIGR03740 1 LETKNLSKRF-GKQTAVNNISLTVPKNsVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWtrKDLHKIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 P--QDFDFYPNMKVSEVLYYLGFlSKINQtdfdkyvdlILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVD 158
Cdd:TIGR03740 80 PlyENLTARENLKVHTTLLGLPD-SRIDE---------VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1436942050 159 EPTAGLDPEERVRIRNLLSDLAENKI-VIISTHIVSDIESTCNRIAILDKGSLVYKGDI 216
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQGItVILSSHILSEVQQLADHIGIISEGVLGYQGKI 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-162 |
1.00e-38 |
|
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: 133.54 E-value: 1.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--KNSQKIRQMIGYLPQDFDFYPNMKVSEVL 96
Cdd:pfam00005 1 LKNVSLTLNPGeILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 97 YYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKV----KSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-223 |
1.40e-38 |
|
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: 142.98 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDG-KKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGY 79
Cdd:COG4987 334 LELEDVSFRYPGaGRPVLDGLSLTLPPGeRVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdlDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDFYpNMKVSEVLYylgfLSKINQTDfdkyVDLI--LRKVNLIDYknkkVKS---------------LSGGMKKRL 142
Cdd:COG4987 414 VPQRPHLF-DTTLRENLR----LARPDATD----EELWaaLERVGLGDW----LAAlpdgldtwlgeggrrLSGGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 143 GIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIEStCNRIAILDKGSLVYKGDIPSLIQQ 222
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQ 559
|
.
gi 1436942050 223 S 223
Cdd:COG4987 560 N 560
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-215 |
1.96e-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: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--KNSQKIRQM-IGYLP 81
Cdd:cd03219 3 VRGLTKRFGGLV-ALDDVSFSVRPGeIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItgLPPHEIARLgIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVL----------YYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHD 151
Cdd:cd03219 82 QIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 152 PKVIIVDEPTAGLDPEERVRIRNLLSDLAENKI-VIISTHIVSDIESTCNRIAILDKGSLVYKGD 215
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-227 |
4.17e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 137.65 E-value: 4.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKI-RQMIGYLP 81
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGeCFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLaRARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPT 161
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 162 AGLDPEERVRI-RNLLSDLAENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIqqsDDHI 227
Cdd:PRK13536 201 TGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI---DEHI 264
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-211 |
8.39e-38 |
|
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: 132.77 E-value: 8.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRqMIGYLPQDF 84
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGeIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRK-SIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 85 D--FYPNMKVSEVLYYLGFLSKINQTdfdkyVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:cd03226 81 DyqLFTDSVREELLLGLKELDAGNEQ-----AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 163 GLDPEERVRIRNLLSDLA-ENKIVIISTHivsDIE---STCNRIAILDKGSLV 211
Cdd:cd03226 156 GLDYKNMERVGELIRELAaQGKAVIVITH---DYEflaKVCDRVLLLANGAIV 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-211 |
1.13e-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: 133.78 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGK---KDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK--IRQMI 77
Cdd:COG1124 2 LEVRNLSVSYGQGgrrVPVLKDVSLEVAPGeSFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkaFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQD----FDfyPNMKV----SEVLYYLGFlskinqTDFDKYVDLILRKVNL-IDYKNKKVKSLSGGMKKRLGIAQAI 148
Cdd:COG1124 82 QMVFQDpyasLH--PRHTVdrilAEPLRIHGL------PDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 149 LHDPKVIIVDEPTAGLDPEERVRIRNLLSDL-AENKI-VIISTHIVSDIESTCNRIAILDKGSLV 211
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLtYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-205 |
1.38e-37 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 132.60 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGK---KDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIknsQKIRQMIGY 79
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFvALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV---TGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDFYPNMKVSE-VLyyLGF-LSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIV 157
Cdd:cd03293 78 VFQQDALLPWLTVLDnVA--LGLeLQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 158 DEPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHivsDIE---STCNRIAIL 205
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIWRetGKTVLLVTH---DIDeavFLADRVVVL 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-222 |
2.26e-37 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 139.51 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN--SQKIRQMIGYL 80
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGeRVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDldPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQDfdfyPnmkvsevlyYLgF---------LSKINQTDFDkyVDLILRKVNLIDYknkkVKS---------------LSG 136
Cdd:COG4988 417 PQN----P---------YL-FagtirenlrLGRPDASDEE--LEAALEAAGLDEF----VAAlpdgldtplgeggrgLSG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 137 GMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIEStCNRIAILDKGSLVYKGDI 216
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTH 555
|
....*.
gi 1436942050 217 PSLIQQ 222
Cdd:COG4988 556 EELLAK 561
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-232 |
4.69e-37 |
|
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: 132.94 E-value: 4.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSY-DGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQ---KIRQMIG 78
Cdd:TIGR04520 1 IEVENVSFSYpESEKPALKNVSLSIEKGEFvAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnlwEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDFDfypNMKVSEV--------LYYLGflskINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILH 150
Cdd:TIGR04520 81 MVFQNPD---NQFVGATveddvafgLENLG----VPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 151 DPKVIIVDEPTAGLDPEERVRIRNLLSDL-AENKIVIIS-THivsDIEST--CNRIAILDKGSLVYKGDiPSLIQQSDDH 226
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISiTH---DMEEAvlADRVIVMNKGKIVAEGT-PREIFSQVEL 229
|
....*.
gi 1436942050 227 IYEINL 232
Cdd:TIGR04520 230 LKEIGL 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-214 |
1.20e-36 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 130.88 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDALNSLDLVIPNGMFGIL-GRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGYL 80
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLiGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNL--IDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 159 EPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHivsDIEST---CNRIAILDKGSLVYKG 214
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQelGKTIVFVTH---DIDEAfrlADRIAIMKNGEIVQVG 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-270 |
1.44e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 132.90 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSY------DG--------------KKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTI 62
Cdd:COG4586 2 IEVENLSKTYrvyekePGlkgalkglfrreyrEVEAVDDISFTIEPGeIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 63 NGI-----EIKNSQKI-------RQMIGYLPqdfdfypnmkVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKK 130
Cdd:COG4586 82 LGYvpfkrRKEFARRIgvvfgqrSQLWWDLP----------AIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 131 VKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDL-AENKI-VIISTHIVSDIESTCNRIAILDKG 208
Cdd:COG4586 152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTtILLTSHDMDDIEALCDRVIVIDHG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 209 SLVYKGDIPSLIQQ-SDDHIYEINLSpselESFRENDL--FITKTQEIENKLKVRFISETKVANA 270
Cdd:COG4586 232 RIIYDGSLEELKERfGPYKTIVLELA----EPVPPLELprGGEVIEREGNRVRLEVDPRESLAEV 292
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-216 |
2.95e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 132.51 E-value: 2.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKD---ALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-----KNSQKIR 74
Cdd:COG1135 2 IELENLSKTFPTKGGpvtALDDVSLTIEKGeIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalseRELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 75 QMIGYLPQDFDFYPNMKVSE-VLYYLgFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPK 153
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAEnVALPL-EIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1436942050 154 VIIVDEPTAGLDPEERVRIRNLLSDLaeNK-----IVIIsTHIVSDIESTCNRIAILDKGSLVYKGDI 216
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDI--NRelgltIVLI-THEMDVVRRICDRVAVLENGRIVEQGPV 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-210 |
4.05e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.78 E-value: 4.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDaLNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNS--QKIRQMIGYL 80
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECvAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMppPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQDFDFYPNMkVSEVLYYlGFLSKINQTDFDKYVDLiLRKVNL-IDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDE 159
Cdd:COG4619 80 PQEPALWGGT-VRDNLPF-PFQLRERKFDRERALEL-LERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 160 PTAGLDPEERVRIRNLLSDLA--ENKIVIISTHIVSDIESTCNRIAILDKGSL 210
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLaeEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-211 |
4.45e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 132.50 E-value: 4.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYdGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQMIGY 79
Cdd:COG3839 1 MASLELENVSKSY-GGVEALKDIDLDIEDGEFlVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDFYPNMKVSE-VLYYLGfLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVD 158
Cdd:COG3839 80 VFQSYALYPHMTVYEnIAFPLK-LRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1436942050 159 EPTAGLDPEERVRIRNLLSDL-AENKI-VIISTHivsD-IE--STCNRIAILDKGSLV 211
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLhRRLGTtTIYVTH---DqVEamTLADRIAVMNDGRIQ 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-208 |
4.69e-36 |
|
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: 128.42 E-value: 4.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI----KNSQKIRQMIG 78
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGeVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDFDFYPNMKVSE-VLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIV 157
Cdd:cd03262 80 MVFQQFNLFPHLTVLEnITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 158 DEPTAGLDPEERVRIRNLLSDLAENKI-VIISTHIVSDIESTCNRIAILDKG 208
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMtMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
13-192 |
6.29e-36 |
|
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: 127.54 E-value: 6.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 13 YDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK----IRQMIGYLPQDFD-- 85
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGeVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKglleRRQRVGLVFQDPDdq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 86 -FYPNM--KVSEVLYYLGflskINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:TIGR01166 81 lFAADVdqDVAFGPLNLG----LSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|.
gi 1436942050 163 GLDPEERVRIRNLLSDL-AENKIVIISTHIV 192
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLrAEGMTVVISTHDV 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-221 |
1.31e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 129.93 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDL-VIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQMIGYLP 81
Cdd:PRK13537 8 IDFRNVEKRY-GDKLVVDGLSFhVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPT 161
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 162 AGLDPEER----VRIRNLlsdLAENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQ 221
Cdd:PRK13537 167 TGLDPQARhlmwERLRSL---LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-214 |
1.49e-35 |
|
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: 126.51 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 10 SKSYDGKKDALNSLDLVI-PNGMFGILGRNGSGKSTLMNIIA--TILQPSKGTVTINGIEIKnSQKIRQMIGYLPQDFDF 86
Cdd:cd03213 15 SSPSKSGKQLLKNVSGKAkPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD-KRSFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 87 YPNMKVSEVLYYlgflskinqtdfdkyvdlilrkvnlidykNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDP 166
Cdd:cd03213 94 HPTLTVRETLMF-----------------------------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1436942050 167 EERVRIRNLLSDLA-ENKIVIISTHIVS-DIESTCNRIAILDKGSLVYKG 214
Cdd:cd03213 145 SSALQVMSLLRRLAdTGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-220 |
1.99e-35 |
|
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: 127.84 E-value: 1.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKsyDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQMIGYLPQ 82
Cdd:cd03299 1 LKVENLSK--DWKEFKLKNVSLEVERGdYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 163 GLDPEERVRIRNLLSDL-AENKIVIIS-THIVSDIESTCNRIAILDKGSLVYKGDIPSLI 220
Cdd:cd03299 159 ALDVRTKEKLREELKKIrKEFGVTVLHvTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-210 |
1.88e-34 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 124.44 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDALNSLDLVIPNGMFGIL-GRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK-----IRQMI 77
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLvGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIV 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 158 DEPTAGLDPEERVRIRNLLSDL-AENKIVIISTHIVSDIESTCNRIAILDKGSL 210
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-211 |
1.98e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 127.91 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN--SQKiRQmI 77
Cdd:COG3842 3 MPALELENVSKRYGDVT-ALDDVSLSIEPGeFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlpPEK-RN-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQDFDFYPNMKVSE-VLYYLGFLsKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVII 156
Cdd:COG3842 80 GMVFQDYALFPHLTVAEnVAFGLRMR-GVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 157 VDEPTAGLDPEERVRIRNLLSDL-AENKI-VIISTH------IVSDiestcnRIAILDKGSLV 211
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLqRELGItFIYVTHdqeealALAD------RIAVMNDGRIE 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-214 |
6.44e-34 |
|
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: 123.60 E-value: 6.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTING-IEIKNSQKIRQMIGY-LPQ 82
Cdd:cd03267 23 LKSLFKRKYREVEALKGISFTIEKGeIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKRRKKFLRRIGVvFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:cd03267 103 KTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 163 GLDPEERVRIRNLLSDL-AENKI-VIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:cd03267 183 GLDVVAQENIRNFLKEYnRERGTtVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-222 |
1.52e-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: 128.48 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIV-IKGLSKSY-DGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPS---KGTVTINGIEIKN-SQKI 73
Cdd:COG1123 1 MTPLLeVRDLSVRYpGGDVPAVDGVSLTIAPGETvALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLElSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 74 R-QMIGYLPQDFDFYPNM-----KVSEVLyylgFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQA 147
Cdd:COG1123 81 RgRRIGMVFQDPMTQLNPvtvgdQIAEAL----ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 148 ILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQ 222
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-214 |
2.39e-33 |
|
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: 121.93 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSYDG-KKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIG 78
Cdd:cd03245 2 RIEFRNVSFSYPNqEIPALDNVSLTIRAGeKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDfdfypnmkvsEVLYYlGFLsKINQTDFDKYVD--LILRKVNLI---DYKNKKVK-----------SLSGGMKKRL 142
Cdd:cd03245 82 YVPQD----------VTLFY-GTL-RDNITLGAPLADdeRILRAAELAgvtDFVNKHPNgldlqigergrGLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 143 GIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSdIESTCNRIAILDKGSLVYKG 214
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-229 |
1.35e-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: 120.03 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQMIGYLPQ 82
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFfTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 163 GLDPEERVRIRNLLSDLAEN--KIVIISTHIVSDIESTCNRIAILDKGSlvykgdipslIQQ--SDDHIYE 229
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKElgITFVFVTHDQEEALTMSDRIAVMNKGK----------IQQigTPEEIYE 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-220 |
1.46e-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: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKG-TVTINGIEIK--NSQKIRQMIGY 79
Cdd:COG1119 4 LELRNVTVRRGGKT-ILDDISWTVKPGEHwAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGgeDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDF--DFYPNMKVSEVL---YY--LGFLSKINQTDFDKyVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDP 152
Cdd:COG1119 83 VSPALqlRFPRDETVLDVVlsgFFdsIGLYREPTDEQRER-ARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 153 KVIIVDEPTAGLDPEERVRIRNLLSDLAENK---IVIIsTHIVSDIESTCNRIAILDKGSLVYKGDIPSLI 220
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGaptLVLV-THHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-214 |
3.99e-32 |
|
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: 118.55 E-value: 3.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 23 LDLVIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKI------RQMIGYLPQDFDFYPNMKVSE-V 95
Cdd:cd03297 17 IDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlppqQRKIGLVFQQYALFPHLNVREnL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 96 LYYLGFLSKINQTDFdkyVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNL 175
Cdd:cd03297 97 AFGLKRKRNREDRIS---VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1436942050 176 LSDLAEN-KI-VIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:cd03297 174 LKQIKKNlNIpVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-232 |
1.23e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 118.64 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 7 KGLSKSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK----IRQMIGYLP 81
Cdd:PRK13639 5 RDLKYSYPDGTEALKGINFKAEKGeMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKslleVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFD---FYPnmKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVD 158
Cdd:PRK13639 85 QNPDdqlFAP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 159 EPTAGLDPEERVRIRNLLSDLAENKI-VIISTHIVSDIESTCNRIAILDKGSLVyKGDIPSLIQQSDDHIYEINL 232
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGItIIISTHDVDLVPVYADKVYVMSDGKII-KEGTPKEVFSDIETIRKANL 236
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-223 |
1.50e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 123.35 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGYL 80
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGeTVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRdlTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQDFDFYpNMKVSE-VLYylgflSKINQTDFDkyVDLILRKVNLIDYknkkVKS---------------LSGGMKKRLGI 144
Cdd:COG1132 420 PQDTFLF-SGTIREnIRY-----GRPDATDEE--VEEAAKAAQAHEF----IEAlpdgydtvvgergvnLSGGQRQRIAI 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 145 AQAILHDPKVIIVDEPTAGLDPE-ERvRIRNLLSDLAENKIVIISTHIVSDIEStCNRIAILDKGSLVYKGDIPSLIQQS 223
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTEtEA-LIQEALERLMKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELLARG 565
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-216 |
2.13e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 117.10 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNK-IVIKGLSKSY---------------------DGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSK 57
Cdd:COG1134 1 MSSmIEVENVSKSYrlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGeSVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 58 GTVTINGieiknsqKIRQMI----GylpqdfdFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKS 133
Cdd:COG1134 81 GRVEVNG-------RVSALLelgaG-------FHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 134 LSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAEN-KIVIISTHIVSDIESTCNRIAILDKGSLVY 212
Cdd:COG1134 147 YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
....
gi 1436942050 213 KGDI 216
Cdd:COG1134 227 DGDP 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-219 |
2.90e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 117.16 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNS--------- 70
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQT-VLHGIDLEVKPGeVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 71 -QKIRQMIGYLPQDFDFYPNMKVSE-VLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAI 148
Cdd:PRK11264 80 iRQLRQHVGFVFQNFNLFPHRTVLEnIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 149 LHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK-IVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSL 219
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-215 |
5.27e-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: 116.25 E-value: 5.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI----KNSQKIRQMIG 78
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGeVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDFDFYPNMKVSE--------VLyylgflsKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILH 150
Cdd:COG1126 81 MVFQQFNLFPHLTVLEnvtlapikVK-------KMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 151 DPKVIIVDEPTAGLDPeERVR-IRNLLSDLAENKI-VIISTH------IVSDiestcnRIAILDKGSLVYKGD 215
Cdd:COG1126 154 EPKVMLFDEPTSALDP-ELVGeVLDVMRDLAKEGMtMVVVTHemgfarEVAD------RVVFMDGGRIVEEGP 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-224 |
8.47e-31 |
|
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: 115.33 E-value: 8.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN---SQKIRQMIGY 79
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmHKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDFYPNMKVSE----VLYYLGFLSKINQtdfdKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVI 155
Cdd:cd03218 80 LPQEASIFRKLTVEEnilaVLEIRGLSKKERE----EKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 156 IVDEPTAGLDPEERVRIRNLLSDLAENKI-VIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSD 224
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIgVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-214 |
1.86e-30 |
|
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: 114.17 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSY---------------------DGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVT 61
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgeVGEFWALKDVSFEVPRGeRIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 62 INGieiknsqKIRQMIGyLPQDFDfyPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKR 141
Cdd:cd03220 81 VRG-------RVSSLLG-LGGGFN--PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 142 LGIAQAILHDPKVIIVDEPTAGLDPEER----VRIRNLLSDlaeNKIVIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQekcqRRLRELLKQ---GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-215 |
1.97e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.78 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYdGKKDALNSLDLVIPNGM-FGILGRNGSGKSTLMNIIATILQPSKGTVTIngieiknSQKIRqmIGYLPQDF 84
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDrIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-------PKGLR--IGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 85 DFYPNMKVSEVLY------------YLGFLSKINQTDFD--KYVDL------------------ILRKVNL-IDYKNKKV 131
Cdd:COG0488 71 PLDDDLTVLDTVLdgdaelraleaeLEELEAKLAEPDEDleRLAELqeefealggweaearaeeILSGLGFpEEDLDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 132 KSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLaENKIVIIStHivsD---IESTCNRIAILDKG 208
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNY-PGTVLVVS-H---DryfLDRVATRILELDRG 225
|
....*...
gi 1436942050 209 SL-VYKGD 215
Cdd:COG0488 226 KLtLYPGN 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
2.41e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 115.29 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYDGKKDALNSLDLVIP-NGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--KNSQKIRQMI 77
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEALNNINFIAPrNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItkENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQDFD---FYPNmkVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKV 154
Cdd:PRK13652 81 GLVFQNPDdqiFSPT--VEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 155 IIVDEPTAGLDPEERVRIRNLLSDLAEN--KIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSD 224
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-222 |
3.50e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 119.54 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKD-ALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGY 79
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpVLKGLSLQIKAGEKvALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdySEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDFYP-----NMKvsevlyylgfLSKINQTDfDKYVDlILRKV---NLIDyKNKKVKS--------LSGGMKKRLG 143
Cdd:PRK11160 419 VSQRVHLFSatlrdNLL----------LAAPNASD-EALIE-VLQQVgleKLLE-DDKGLNAwlgeggrqLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 144 IAQAILHDPKVIIVDEPTAGLDPE-ERvRIRNLLSDLAENKIVIISTHIVSDIESTcNRIAILDKGSLVYKGDIPSLIQQ 222
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAEtER-QILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQ 563
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-214 |
4.78e-30 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 120.12 E-value: 4.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYD-GKKDALNSLDLVI-PNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK-NSQKIRQMIGYL 80
Cdd:TIGR01257 929 VCVKNLVKIFEpSGRPAVDRLNITFyENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIEtNLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEP 160
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 161 TAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-219 |
7.69e-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: 112.53 E-value: 7.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNS---QKIRQMIGYLP 81
Cdd:cd03224 3 VENLNAGY-GKSQILFGVSLTVPEGeIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpphERARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVL---YYLGFLSKInQTDFDKYVDL--ILRkvnliDYKNKKVKSLSGGMKKRLGIAQAILHDPKVII 156
Cdd:cd03224 82 EGRRIFPELTVEENLllgAYARRRAKR-KARLERVYELfpRLK-----ERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 157 VDEPTAGLDPEERVRIRNLLSDLAENKI-VIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSL 219
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDEGVtILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-214 |
9.37e-30 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 118.61 E-value: 9.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 28 PNGMFGILGRNGSGKSTLMNIIATILQPS---KGTVTINGIEIkNSQKIRQMIGYLPQDFDFYPNMKVSEVLYYLGFLSK 104
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRM 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 105 INQTDFDK---YVDLILRKVNLIDYKNKK------VKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNL 175
Cdd:TIGR00955 129 PRRVTKKEkreRVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1436942050 176 LSDLAEN-KIVIISTH-IVSDIESTCNRIAILDKGSLVYKG 214
Cdd:TIGR00955 209 LKGLAQKgKTIICTIHqPSSELFELFDKIILMAEGRVAYLG 249
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
1.07e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 113.68 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIV-IKGLSKSY-DGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--KNSQKIRQ 75
Cdd:PRK13647 1 MDNIIeVEDLHFRYkDGTK-ALKGLSLSIPEGsKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnaENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 76 MIGYLPQDFD-------------FYP-NMKVSevlyylgflskinQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKR 141
Cdd:PRK13647 80 KVGLVFQDPDdqvfsstvwddvaFGPvNMGLD-------------KDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 142 LGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDL-AENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDiPSLI 220
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD-KSLL 225
|
....*....
gi 1436942050 221 qqSDDHIYE 229
Cdd:PRK13647 226 --TDEDIVE 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-214 |
1.26e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.90 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKD---ALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-----KNSQKIR 74
Cdd:PRK11153 2 IELKNISKVFPQGGRtihALNNVSLHIPAGeIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalseKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 75 QMIGYLPQDFDFYPNMKVSE-VLYYLGfLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPK 153
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDnVALPLE-LAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 154 VIIVDEPTAGLDPEERVRIRNLLSDLaeNK-----IVIIsTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDI--NRelgltIVLI-THEMDVVKRICDRVAVIDAGRLVEQG 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-208 |
2.43e-29 |
|
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: 110.00 E-value: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDA-LNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGY 79
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGeSLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDfdfypnmkvseVLYYLGFLSkinqtdfdkyvDLIlrkvnlidyknkkvksLSGGMKKRLGIAQAILHDPKVIIVDE 159
Cdd:cd03246 81 LPQD-----------DELFSGSIA-----------ENI----------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1436942050 160 PTAGLDPEERVRIRNLLSDL-AENKIVIISTHIVSDIEStCNRIAILDKG 208
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLAS-ADRILVLEDG 171
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-222 |
2.60e-29 |
|
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: 113.61 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKD---ALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQP---SKGTVTINGIEI-----KNSQKI 73
Cdd:COG0444 4 VRNLKVYFPTRRGvvkAVDGVSFDVRRGeTLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklseKELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 74 R----QMIgylPQD----FDfyPNMKV----SEVLYYLGFLSKinqTDFDKYVDLILRKVNlIDYKNKKVKS----LSGG 137
Cdd:COG0444 84 RgreiQMI---FQDpmtsLN--PVMTVgdqiAEPLRIHGGLSK---AEARERAIELLERVG-LPDPERRLDRypheLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 138 MKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK---IVIIsTH---IVSDIestCNRIAILDKGSLV 211
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglaILFI-THdlgVVAEI---ADRVAVMYAGRIV 230
|
250
....*....|.
gi 1436942050 212 YKGDIPSLIQQ 222
Cdd:COG0444 231 EEGPVEELFEN 241
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-211 |
4.75e-29 |
|
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: 108.67 E-value: 4.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNS---QKIRQMIGY 79
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGeVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsprDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQdfdfypnmkvsevlyylgflskinqtdfdkyvdlilrkvnlidyknkkvksLSGGMKKRLGIAQAILHDPKVIIVDE 159
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 160 PTAGLDPEERVRIRNLLSDLAENKI-VIISTHIVSDIESTCNRIAILDKGSLV 211
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQGVaVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-211 |
5.51e-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: 110.04 E-value: 5.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQMIGYLPQ 82
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFvVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 163 GLDPEERVRIRNLLSDLAEN--KIVIISTHIVSDIESTCNRIAILDKGSLV 211
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRlgTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-196 |
6.02e-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: 6.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYDGKKD---ALNSLDLVIPNGMFG-ILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRqm 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVvALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 77 iGYLPQDFDFYPNMKVSEVLYyLGF-LSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVI 155
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVA-FGLrLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1436942050 156 IVDEPTAGLDPEERVRIRNLLSDL--AENKIVIISTHivsDIE 196
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH---SVE 196
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
9.01e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.48 E-value: 9.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 2 NKIVIKGLSKSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK----IRQM 76
Cdd:PRK13636 4 YILKVEELNYNYSDGTHALKGININIKKGeVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmkLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 77 IGYLPQDFDfypNMKVSEVLYY---LGFLS-KINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDP 152
Cdd:PRK13636 84 VGMVFQDPD---NQLFSASVYQdvsFGAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 153 KVIIVDEPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDI 216
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-224 |
1.75e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.52 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGK----KDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK----NSQKIR 74
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFvGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 75 QMIGYLPQdfdfYPNMKVSEVLYY--LGFLSK---INQTDFDKYVDLILRKVNLiDYKNKKVKS---LSGGMKKRLGIAQ 146
Cdd:PRK13637 83 KKVGLVFQ----YPEYQLFEETIEkdIAFGPInlgLSEEEIENRVKRAMNIVGL-DYEDYKDKSpfeLSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 147 AILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSD 224
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-214 |
2.19e-28 |
|
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: 108.35 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 23 LDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQMIGYLPQDFDFYPNMKVSEVLYyLGF 101
Cdd:cd03298 17 FDLTFAQGeITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVG-LGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 102 LSKINQTDFD-KYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDL- 179
Cdd:cd03298 96 SPGLKLTAEDrQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLh 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1436942050 180 AENKI-VIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:cd03298 176 AETKMtVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-214 |
5.02e-28 |
|
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: 106.63 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGK-KDALNSLDLVIPNGM-FGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK-IRQMIGYL 80
Cdd:cd03247 1 LSINNVSFSYPEQeQQVLKNLSLELKQGEkIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKaLSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQDfdfyPNMKVSEVLYYLGflskinqtdfdkyvdlilrkvnlidyknkkvKSLSGGMKKRLGIAQAILHDPKVIIVDEP 160
Cdd:cd03247 81 NQR----PYLFDTTLRNNLG-------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 161 TAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTcNRIAILDKGSLVYKG 214
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-208 |
5.98e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 110.62 E-value: 5.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQM-IGYLP 81
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGeLVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERrVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSE-VLYYLGFLsKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEP 160
Cdd:COG1118 82 QHYALFPHMTVAEnIAFGLRVR-PPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 161 TAGLDPEERVRIRNLLSDL-AENKI-VIISTHivsDIE---STCNRIAILDKG 208
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLhDELGGtTVFVTH---DQEealELADRVVVMNQG 210
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-215 |
7.40e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 107.81 E-value: 7.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN---SQKIRQM 76
Cdd:COG1137 1 MMTLEAENLVKSY-GKRTVVKDVSLEVNQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmHKRARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 77 IGYLPQDFDFYPNMKVSEVLyyLGFL--SKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKV 154
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNI--LAVLelRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 155 IIVDEPTAGLDP---EErvrIRNLLSDLAENKI-VIISTHIVSDIESTCNRIAILDKGSLVYKGD 215
Cdd:COG1137 158 ILLDEPFAGVDPiavAD---IQKIIRHLKERGIgVLITDHNVRETLGICDRAYIISEGKVLAEGT 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-222 |
8.59e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.18 E-value: 8.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGY 79
Cdd:PRK11231 2 TLRTENLTVGY-GTKRILNDLSLSLPTGkITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmlSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDFYPNMKVSE-VLY----YLGFLSKINQTDfDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKV 154
Cdd:PRK11231 81 LPQHHLTPEGITVRElVAYgrspWLSLWGRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 155 IIVDEPTAGLDPEERVRIRNLLSDL-AENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGD-----IPSLIQQ 222
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTpeevmTPGLLRT 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-222 |
9.57e-28 |
|
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: 107.31 E-value: 9.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSYDGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKI--RQMIGY 79
Cdd:cd03254 2 EIEFENVNFSYDEKKPVLKDINFSIKPGETvAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKslRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDfDFYPNMKVSEVLYYLGFLSKinqtdfDKYVDLILRKVNLIDYKNK-----------KVKSLSGGMKKRLGIAQAI 148
Cdd:cd03254 82 VLQD-TFLFSGTIMENIRLGRPNAT------DEEVIEAAKEAGAHDFIMKlpngydtvlgeNGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 149 LHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTcNRIAILDKGSLVYKGDIPSLIQQ 222
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNA-DKILVLDDGKIIEEGTHDELLAK 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-221 |
3.75e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 105.87 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTING--------IEIKNSQKIR 74
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGeTLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 75 QMIGYLPQDFDFYPNMKVSEVLY-----YLGFLSKINQTDFDKyvdlILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAIL 149
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIeapckVLGLSKEQAREKAMK----LLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 150 HDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIV-IISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQ 221
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITqVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQ 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-211 |
7.76e-27 |
|
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: 104.57 E-value: 7.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNGM-FGILGRNGSGKSTLMNIIATIL-----QPSKGTVTINGIEIKNSQK----I 73
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEiTALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVdvleL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 74 RQMIGYLPQdfdfYPN---MKVSE-VLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVK--SLSGGMKKRLGIAQA 147
Cdd:cd03260 80 RRRVGMVFQ----KPNpfpGSIYDnVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 148 ILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTCNRIAILDKGSLV 211
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-211 |
8.37e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 8.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTING--IEIKNSQKIRQM-IGYLP 81
Cdd:COG1129 7 MRGISKSFGGVK-ALDGVSLELRPGeVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQAAgIAIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVLyYLGFLSK----INQTDFDKYVDLILRKVNL-IDyKNKKVKSLSGGMKKRLGIAQAILHDPKVII 156
Cdd:COG1129 86 QELNLVPNLSVAENI-FLGREPRrgglIDWRAMRRRARELLARLGLdID-PDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 157 VDEPTAGLDPEERVRIRNLLSDLAENK--IVIIStHIVSDIESTCNRIAILDKGSLV 211
Cdd:COG1129 164 LDEPTASLTEREVERLFRIIRRLKAQGvaIIYIS-HRLDEVFEIADRVTVLRDGRLV 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-211 |
8.45e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 109.35 E-value: 8.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTING--IEIKNSQK-IRQMIGY 79
Cdd:COG3845 6 LELRGITKRFGGVV-ANDDVSLTVRPGeIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDaIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDFYPNMKVSE-VLyyLG----FLSKINQTDFDKYVDLILRKVNL-IDyKNKKVKSLSGGMKKRLGIAQAILHDPK 153
Cdd:COG3845 85 VHQHFMLVPNLTVAEnIV--LGleptKGGRLDRKAARARIRELSERYGLdVD-PDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 154 VIIVDEPTAGLDPEErvrIRNLLSDL----AENKIVIISTHIVSDIESTCNRIAILDKGSLV 211
Cdd:COG3845 162 ILILDEPTAVLTPQE---ADELFEILrrlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-259 |
9.49e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.61 E-value: 9.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQMIGYLPQDF 84
Cdd:PRK11607 22 IRNLTKSFDGQH-AVDDVSLTIYKGeIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 85 DFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGL 164
Cdd:PRK11607 101 ALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 165 DPEERVRIRNLLSDLAENKIV--IISTHIVSDIESTCNRIAILDKGSLVYKGDiPSLIQQ------SDDHIYEINLSPSE 236
Cdd:PRK11607 181 DKKLRDRMQLEVVDILERVGVtcVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE-PEEIYEhpttrySAEFIGSVNVFEGV 259
|
250 260
....*....|....*....|...
gi 1436942050 237 LESfRENDLFITKTQEIENKLKV 259
Cdd:PRK11607 260 LKE-RQEDGLVIDSPGLVHPLKV 281
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-214 |
1.06e-26 |
|
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: 104.62 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQ--KIRQMIGYL 80
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGkKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTldSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQD---FDfypnmkvSEVLYYLGFlSKINQTDFDKYV--------DLILrkvNLIDYKNKKVKS----LSGGMKKRLGIA 145
Cdd:cd03253 81 PQDtvlFN-------DTIGYNIRY-GRPDATDEEVIEaakaaqihDKIM---RFPDGYDTIVGErglkLSGGEKQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1436942050 146 QAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIeSTCNRIAILDKGSLVYKG 214
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERG 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-223 |
1.21e-26 |
|
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: 104.54 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKD--ALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIG 78
Cdd:cd03249 1 IEFKNVSFRYPSRPDvpILKGLSLTIPPGKTvALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDFDFYpNMKVSEVLYYlgflSKINQTDFDkyVDLILRKVNLIDYKNK-----------KVKSLSGGMKKRLGIAQA 147
Cdd:cd03249 81 LVSQEPVLF-DGTIAENIRY----GKPDATDEE--VEEAAKKANIHDFIMSlpdgydtlvgeRGSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 148 ILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIeSTCNRIAILDKGSLVYKGDIPSLIQQS 223
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-208 |
1.76e-26 |
|
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: 104.34 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQMIGYLPQ 82
Cdd:cd03296 3 IEVRNVSKRF-GDFVALDDVSLDIPSGeLVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFDFYPNMKVSE-VLYYLGF---LSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVD 158
Cdd:cd03296 82 HYALFRHMTVFDnVAFGLRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 159 EPTAGLDPEERVRIRNLLSDLaENKIVIISTHIVSDIEST---CNRIAILDKG 208
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRL-HDELHVTTVFVTHDQEEAlevADRVVVMNKG 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-243 |
2.11e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.68 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK---IRQMIGY 79
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYiGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlqgIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDF-YPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVD 158
Cdd:PRK13644 82 VFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 159 EPTAGLDPEERVRIRNLLSDLAEN-KIVIISTHIVSDIESTcNRIAILDKGSLVYKGDIPSLIqqSDDHIYEINLSPSEL 237
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDA-DRIIVMDRGKIVLEGEPENVL--SDVSLQTLGLTPPSL 238
|
....*.
gi 1436942050 238 ESFREN 243
Cdd:PRK13644 239 IELAEN 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-216 |
2.51e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.23 E-value: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNGM-FGILGRNGSGKSTLMNIIATILQPSKGTVTInGIEIKnsqkirqmIGYLPQ 82
Cdd:COG0488 316 LELEGLSKSYGDKT-LLDDLSLRIDRGDrIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--------IGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFD--------------FYPNMKVSEVLYYLG-FLskinqtdFDKyvdlilrkvnliDYKNKKVKSLSGGMKKRLGIAQA 147
Cdd:COG0488 386 HQEeldpdktvldelrdGAPGGTEQEVRGYLGrFL-------FSG------------DDAFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 148 ILHDPKVIIVDEPTAGLDPEervrIRNLLSDLAEN---KIVIIStHivsD---IESTCNRIAILDKGSLV-YKGDI 216
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIE----TLEALEEALDDfpgTVLLVS-H---DryfLDRVATRILEFEDGGVReYPGGY 514
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-222 |
2.94e-26 |
|
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: 103.46 E-value: 2.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKD-ALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNS--QKIRQMIGY 79
Cdd:cd03251 1 VEFKNVTFRYPGDGPpVLRDISLDIPAGeTVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYtlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQD-FDFypNMKVSEVLYYlgflSKINQTDFDkyVDLILRKVNLIDYKNKK------------VKsLSGGMKKRLGIAQ 146
Cdd:cd03251 81 VSQDvFLF--NDTVAENIAY----GRPGATREE--VEEAARAANAHEFIMELpegydtvigergVK-LSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 147 AILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTcNRIAILDKGSLVYKGDIPSLIQQ 222
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLAQ 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-214 |
3.33e-26 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 104.19 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDALNSLDLVIPNGMFGIL-GRNGSGKSTLMNIIATILQPSKGTVTINGIEIKnsQKIRQ-MIGYLP 81
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALvGVNGSGKSTLFKALMGFVRLASGKISILGQPTR--QALQKnLVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 Q--DFDFYPNMKVSEVLY-----YLGFLSKINQTDfDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKV 154
Cdd:PRK15056 85 QseEVDWSFPVLVEDVVMmgrygHMGWLRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 155 IIVDEPTAGLDPEERVRIRNLLSDL-AENKIVIISTHIVSDIESTCNrIAILDKGSLVYKG 214
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASG 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-221 |
3.85e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 3.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTING--------IEIKNSQKIR 74
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGeTLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 75 QMIGYLPQDFDFYPNMKVSEVLY-----YLGFLSKINQTDFDKyvdlILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAIL 149
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIeapcrVLGLSKDQALARAEK----LLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 150 HDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIV-IISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQ 221
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITqVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-221 |
4.47e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.25 E-value: 4.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK----IRQMIG 78
Cdd:PRK09493 2 IEFKNVSKHF-GPTQVLHNIDLNIDQGeVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVderlIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDFDFYPNMKVSE-VLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIV 157
Cdd:PRK09493 81 MVFQQFYLFPHLTALEnVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 158 DEPTAGLDPEERVRIRNLLSDLAENKI-VIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQ 221
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMtMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-232 |
4.64e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.68 E-value: 4.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 2 NKIVIKGLSKSYDGKKD-ALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTING--IEIKNSQKIRQMI 77
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASfTLKDVSFNIPKGQWtSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQDFDfypNMKV-SEVLYYLGFLSKINQTDFDKY---VDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPK 153
Cdd:PRK13648 86 GIVFQNPD---NQFVgSIVKYDVAFGLENHAVPYDEMhrrVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 154 VIIVDEPTAGLDPEERVRIRNLLSDLAENK-IVIIS-THIVSD-IEStcNRIAILDKGSlVYKGDIPSLIQQSDDHIYEI 230
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHnITIISiTHDLSEaMEA--DHVIVMNKGT-VYKEGTPTEIFDHAEELTRI 239
|
..
gi 1436942050 231 NL 232
Cdd:PRK13648 240 GL 241
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-232 |
5.34e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 103.53 E-value: 5.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDG-KKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--KNSQKIRQMIGY 79
Cdd:PRK13632 8 IKVENVSFSYPNsENNALKNVSFEINEGEYvAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIskENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDfypNMKV-SEVLYYLGFLSKINQTDFDKYVDLIL---RKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVI 155
Cdd:PRK13632 88 IFQNPD---NQFIgATVEDDIAFGLENKKVPPKKMKDIIDdlaKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 156 IVDEPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHivsDIEST--CNRIAILDKGSLVYKGDiPSLIQQSDDHIYEIN 231
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITH---DMDEAilADKVIVFSEGKLIAQGK-PKEILNNKEILEKAK 240
|
.
gi 1436942050 232 L 232
Cdd:PRK13632 241 I 241
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-190 |
5.48e-26 |
|
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: 107.06 E-value: 5.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGYL 80
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGeRVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSslDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQD---FDfypnMKVSEVLyylgFLSKINQTDFDKYVdlILRKVNLIDY-------KNKKV----KSLSGGMKKRLGIAQ 146
Cdd:TIGR02868 415 AQDahlFD----TTVRENL----RLARPDATDEELWA--ALERVGLADWlralpdgLDTVLgeggARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1436942050 147 AILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTH 190
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-214 |
5.53e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.63 E-value: 5.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 17 KDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGI---EIKNSQKIRQMIGYLPQDFDfypNMKV 92
Cdd:PRK13633 23 KLALDDVNLEVKKGEFlVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdtsDEENLWDIRNKAGMVFQNPD---NQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 93 SEVLYY--------LGflskINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGL 164
Cdd:PRK13633 100 ATIVEEdvafgpenLG----IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 165 DPEERVRIRNLLSDLAENK--IVIISTHIVSDIeSTCNRIAILDKGSLVYKG 214
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYgiTIILITHYMEEA-VEADRIIVMDSGKVVMEG 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-190 |
6.27e-26 |
|
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: 106.99 E-value: 6.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGYL 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGeRVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdaDADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQDFDFYPNMKVSEVLyylgfLSKINQTDFDkyVDLILRKVNLIDY-------KNKKVKS----LSGGMKKRLGIAQAIL 149
Cdd:TIGR02857 402 PQHPFLFAGTIAENIR-----LARPDASDAE--IREALERAGLDEFvaalpqgLDTPIGEggagLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1436942050 150 HDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTH 190
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-228 |
2.03e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 102.01 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKG----------TVTINGIEIKNSQK 72
Cdd:PRK09984 5 IRVEKLAKTFNQHQ-ALHAVDLNIHHGeMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 73 IRQMIGYLPQDFDFYPNMKVSE-VLyyLGFL--SKINQTDFDKYVDL-------ILRKVNLIDYKNKKVKSLSGGMKKRL 142
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLEnVL--IGALgsTPFWRTCFSWFTREqkqralqALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 143 GIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK--IVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLI 220
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFD 241
|
....*...
gi 1436942050 221 QQSDDHIY 228
Cdd:PRK09984 242 NERFDHLY 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-241 |
2.79e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.12 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN---SQKIRQM 76
Cdd:PRK10895 1 MATLTAKNLAKAYKGRR-VVEDVSLTVNSGeIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlplHARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 77 IGYLPQDFDFYPNMKV-SEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVI 155
Cdd:PRK10895 80 IGYLPQEASIFRRLSVyDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 156 IVDEPTAGLDPEERVRIRNLLSDLAENKI-VIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQqsDDHIYEINLSp 234
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLgVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ--DEHVKRVYLG- 236
|
....*..
gi 1436942050 235 selESFR 241
Cdd:PRK10895 237 ---EDFR 240
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-225 |
3.55e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.60 E-value: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDgkkDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGieiknsqkirQMIGYLP- 81
Cdd:COG3840 2 LRLDDLTYRYG---DFPLRFDLTIAAGERvAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG----------QDLTALPp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 ---------QDFDFYPNMKVSEVLYyLGFLSKINQTDFDK-YVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHD 151
Cdd:COG3840 69 aerpvsmlfQENNLFPHLTVAQNIG-LGLRPGLKLTAEQRaQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 152 PKVIIVDEPTAGLDPEERVRIRNLLSDLAENK--IVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSDD 225
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-232 |
7.76e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.86 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 2 NKIVIKGLSKSYDGKKD-ALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--KNSQKIRQMI 77
Cdd:PRK13635 4 EIIRVEHISFRYPDAATyALKDVSFSVYEGEWvAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQDFD--FYPNMKVSEVLYYL---GflskINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDP 152
Cdd:PRK13635 84 GMVFQNPDnqFVGATVQDDVAFGLeniG----VPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 153 KVIIVDEPTAGLDPEERVRIRNLLSDLAENK-IVIIS-THivsDIE--STCNRIAILDKGSLVYKGdIPSLIQQSDDHIY 228
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKgITVLSiTH---DLDeaAQADRVIVMNKGEILEEG-TPEEIFKSGHMLQ 235
|
....
gi 1436942050 229 EINL 232
Cdd:PRK13635 236 EIGL 239
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-190 |
1.53e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.69 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 12 SYDGKkDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGieiknsqkiRQMIGYLPQ---DFDFY 87
Cdd:NF040873 1 GYGGR-PVLHGVDLTIPAGsLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQrseVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 88 PnMKVSEVLY-----YLGFLSKINQTDfDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:NF040873 71 P-LTVRDLVAmgrwaRRGLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180
....*....|....*....|....*....
gi 1436942050 163 GLDPEERVRIRNLLSDL-AENKIVIISTH 190
Cdd:NF040873 149 GLDAESRERIIALLAEEhARGATVVVVTH 177
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-215 |
2.41e-24 |
|
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: 98.13 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN--SQKIRQM-IGYLP 81
Cdd:COG0410 6 VENLHAGY-GGIHVLHGVSLEVEEGeIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpPHRIARLgIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVL----YYLGFLSKINQtDFDKYVDL--ILRkvnliDYKNKKVKSLSGGMKKRLGIAQAILHDPKVI 155
Cdd:COG0410 85 EGRRIFPSLTVEENLllgaYARRDRAEVRA-DLERVYELfpRLK-----ERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 156 IVDEPTAGLDP---EErvrIRNLLSDLAENKIVII----STHIVSDIestCNRIAILDKGSLVYKGD 215
Cdd:COG0410 159 LLDEPSLGLAPlivEE---IFEIIRRLNREGVTILlveqNARFALEI---ADRAYVLERGRIVLEGT 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-219 |
2.42e-24 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 103.17 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 9 LSKSYDGKKD-ALNSLDL-VIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQMIGYLPQdFD 85
Cdd:TIGR01257 1943 LTKVYSGTSSpAVDRLCVgVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQNMGYCPQ-FD 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 86 FYPNMKVS-EVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGL 164
Cdd:TIGR01257 2022 AIDDLLTGrEHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 165 DPEERVRIRN-LLSDLAENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSL 219
Cdd:TIGR01257 2102 DPQARRMLWNtIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-224 |
2.81e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.42 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 19 ALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK------IRQMIGYLPQdfdfYPNMK 91
Cdd:PRK13643 21 ALFDIDLEVKKGSYtALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeikpVRKKVGVVFQ----FPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 92 VSE--VLYYLGFLSK---INQTDFDKYVDLILRKVNLI-DYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLD 165
Cdd:PRK13643 97 LFEetVLKDVAFGPQnfgIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 166 PEERVRIRNLLSDLAEN-KIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSD 224
Cdd:PRK13643 177 PKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVD 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-261 |
2.82e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 99.32 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGK----KDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTI------NGIEIKNSQK 72
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYvAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 73 IRQMIGYLPQ-------------DFDFYP-NMKVSEvlyylgflskinqTDFDKYVDLILRKVNLI-DYKNKKVKSLSGG 137
Cdd:PRK13634 83 LRKKVGIVFQfpehqlfeetvekDICFGPmNFGVSE-------------EDAKQKAREMIELVGLPeELLARSPFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 138 MKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK--IVIISTHIVSDIESTCNRIAILDKGSLVYKGD 215
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1436942050 216 iPSLIQQSDDHIYEINLSPSELESFRendlfitktQEIENKLKVRF 261
Cdd:PRK13634 230 -PREIFADPDELEAIGLDLPETVKFK---------RALEEKFGISF 265
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-216 |
4.49e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.78 E-value: 4.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVI-PNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQM--IGY 79
Cdd:PRK09700 6 ISMAGIGKSFGPVH-ALKSVNLTVyPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnKLDHKLAAQlgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDFYPNMKVSEVLYYLGFLSK----INQTDFDKY---VDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDP 152
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKkvcgVNIIDWREMrvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 153 KVIIVDEPTAGLDPEERVRIRNLLSDL-AENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDI 216
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLrKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMV 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-211 |
4.57e-24 |
|
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: 97.18 E-value: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSY-DGKKDALNSLDLVIPNGM-FGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIG 78
Cdd:cd03244 2 DIEFKNVSLRYrPNLPPVLKNISFSIKPGEkVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkiGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDfdfyPNMKVSEVLYYLGFLSKINqtdfDKYVDLILRKVNLIDYKNKKVKSL-----------SGGMKKRLGIAQA 147
Cdd:cd03244 82 IIPQD----PVLFSGTIRSNLDPFGEYS----DEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 148 ILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIeSTCNRIAILDKGSLV 211
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTI-IDSDRILVLDKGRVV 216
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-210 |
4.79e-24 |
|
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: 101.66 E-value: 4.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 15 GKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGYLPQDFDFYPNmK 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEAlAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwDRETFGKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 92 VSEvlyylgflskiNQTDFDKYVD---------------LILRKVNLID-YKNKKVKSLSGGMKKRLGIAQAILHDPKVI 155
Cdd:TIGR01842 408 VAE-----------NIARFGENADpekiieaaklagvheLILRLPDGYDtVIGPGGATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 156 IVDEPTAGLDPEERVRIRNLLSDL-AENKIVIISTHIVSDIESTcNRIAILDKGSL 210
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCV-DKILVLQDGRI 531
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-211 |
1.28e-23 |
|
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: 97.33 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSYDGKKD----ALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-----KNSQK 72
Cdd:cd03294 19 KLLAKGKSKEEILKKTgqtvGVNDVSLDVREGeIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsrKELRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 73 IR-QMIGYLPQDFDFYPNMKVSE-VLYYLGfLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILH 150
Cdd:cd03294 99 LRrKKISMVFQSFALLPHRTVLEnVAFGLE-VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 151 DPKVIIVDEPTAGLDPEERVRIRNLLSDLAEN--KIVIISTHIVSDIESTCNRIAILDKGSLV 211
Cdd:cd03294 178 DPDILLMDEAFSALDPLIRREMQDELLRLQAElqKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-214 |
1.65e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.52 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYdGKKDALNSLDLVIP-NGMFGILGRNGSGKSTLMNIIATI--LQPS---KGTVTINGIEIKNSQKIR 74
Cdd:PRK14247 1 MNKIEIRDLKVSF-GQVEVLDGVNLEIPdNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 75 -----QMIGYLPQDFdfyPNMKVSEVLYyLGF-LSKI--NQTDFDKYVDLILRKVNLID-YKNK---KVKSLSGGMKKRL 142
Cdd:PRK14247 80 lrrrvQMVFQIPNPI---PNLSIFENVA-LGLkLNRLvkSKKELQERVRWALEKAQLWDeVKDRldaPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 143 GIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-232 |
2.29e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 96.74 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 19 ALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK------IRQMIGYLPQdfdfYPNMK 91
Cdd:PRK13649 22 ALFDVNLTIEDGSYtAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdikqIRKKVGLVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 92 VSE--VLYYLGFLSKINQTDFDKYVDLILRKVNLI----DYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLD 165
Cdd:PRK13649 98 LFEetVLKDVAFGPQNFGVSQEEAEALAREKLALVgiseSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1436942050 166 PEERVRIRNLLSDLAENKIVII-STHIVSDIESTCNRIAILDKGSLVYKGDiPSLIQQSDDHIYEINL 232
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANYADFVYVLEKGKLVLSGK-PKDIFQDVDFLEEKQL 244
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-258 |
2.76e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.82 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 16 KKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI------KNSQKIRQMIGYLPQ--DFDF 86
Cdd:PRK13641 19 EKKGLDNISFELEEGSFvALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgnKNLKKLRKKVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 87 YPNMKVSEVLY---YLGFLSKINQTDFDKYvdliLRKVNLI-DYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:PRK13641 99 FENTVLKDVEFgpkNFGFSEDEAKEKALKW----LKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 163 GLDPEERVRIRNLLSDL-AENKIVIISTHIVSDIESTCNRIAILDKGSLVyKGDIPSLIQQSDDHIYEINLS-------P 234
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI-KHASPKEIFSDKEWLKKHYLDepatsrfA 253
|
250 260
....*....|....*....|....*....
gi 1436942050 235 SELES----FRENDLFITK-TQEIENKLK 258
Cdd:PRK13641 254 SKLEKggfkFSEMPLTIDElVDGIKNNLK 282
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-208 |
3.68e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 99.43 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK-NSQKIRQMIGYLP 81
Cdd:NF033858 267 IEARGLTMRF-GDFTAVDHVSFRIRRGeIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDaGDIATRRRVGYMS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPT 161
Cdd:NF033858 346 QAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1436942050 162 AGLDPEERVRIRNLLSDLA-ENKIVI-ISTHIVSDIEStCNRIAILDKG 208
Cdd:NF033858 426 SGVDPVARDMFWRLLIELSrEDGVTIfISTHFMNEAER-CDRISLMHAG 473
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-229 |
4.34e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 97.71 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQMIGYLPQ 82
Cdd:PRK09452 15 VELRGISKSFDGKE-VISNLDLTINNGEFlTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFDFYPNMKVSE-VLYYLGfLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPT 161
Cdd:PRK09452 94 SYALFPHMTVFEnVAFGLR-MQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 162 AGLDPEERVRIRNLLSDLAE--NKIVIISTHivsDIE---STCNRIAILDKGslvykgdipsLIQQ--SDDHIYE 229
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRklGITFVFVTH---DQEealTMSDRIVVMRDG----------RIEQdgTPREIYE 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
9-211 |
4.36e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 94.56 E-value: 4.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 9 LSKSYDGKKDALNSLDLVI-PNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI---KNSQK--IRQMIGYLPQ 82
Cdd:PRK10908 7 VSKAYLGGRQALQGVTFHMrPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVpfLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:PRK10908 87 DHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 163 GLDPEERVRIRNLLSDLaeNKI---VIISTHIVSDIESTCNRIAILDKGSLV 211
Cdd:PRK10908 167 NLDDALSEGILRLFEEF--NRVgvtVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-222 |
5.73e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.49 E-value: 5.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 12 SYDGKKDALNSLDL-VIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGYLPQDFDFYp 88
Cdd:PRK13657 343 SYDNSRQGVEDVSFeAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvTRASLRRNIAVVFQDAGLF- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 89 NMKVSEVLYylgfLSKINQTDFDKY--------VDLILRKVNLIDYK-NKKVKSLSGGMKKRLGIAQAILHDPKVIIVDE 159
Cdd:PRK13657 422 NRSIEDNIR----VGRPDATDEEMRaaaeraqaHDFIERKPDGYDTVvGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 160 PTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTcNRIAILDKGSLVYKGDIPSLIQQ 222
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNA-DRILVFDNGRVVESGSFDELVAR 559
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-230 |
6.67e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 95.24 E-value: 6.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTING--IEIKNSQKIRQMIGYLPQDFDFYPNMKVSEVL 96
Cdd:PRK10575 27 LHPLSLTFPAGkVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpLESWSSKAFARKVAYLPQQLPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 97 Y-----YLGFLSKINQTDFDKyVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVR 171
Cdd:PRK10575 107 AigrypWHGALGRFGAADREK-VEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 172 IRNLLSDLAENK--IVIISTHIVSDIESTCNRIAILDKGSLVYKGDiPSLIQQSD--DHIYEI 230
Cdd:PRK10575 186 VLALVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGT-PAELMRGEtlEQIYGI 247
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-224 |
7.68e-23 |
|
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: 96.72 E-value: 7.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 23 LDLVIP-NGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNS-QKI-----RQMIGYLPQDFDFYPNMKVSEV 95
Cdd:TIGR02142 16 ADFTLPgQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrKGIflppeKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 96 LYYlGF---LSKINQTDFDKYVDLIlrkvNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRI 172
Cdd:TIGR02142 96 LRY-GMkraRPSERRISFERVIELL----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 173 RNLLSDL-AENKI-VIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSD 224
Cdd:TIGR02142 171 LPYLERLhAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-215 |
8.32e-23 |
|
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: 98.28 E-value: 8.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 15 GKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGYLPQDFDFYP--- 88
Cdd:COG4618 343 SKRPILRGVSFSLEPGeVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwDREELGRHIGYLPQDVELFDgti 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 89 --NmkvsevlyylgfLSKINQTDFDKYV---------DLILRkvnLID-YkNKKV----KSLSGGMKKRLGIAQAILHDP 152
Cdd:COG4618 423 aeN------------IARFGDADPEKVVaaaklagvhEMILR---LPDgY-DTRIgeggARLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 153 KVIIVDEPTAGLDPEERVRIRNLLSDL-AENKIVIISTHIVSdIESTCNRIAILDKGSLVYKGD 215
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGP 549
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-220 |
8.77e-23 |
|
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: 94.09 E-value: 8.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDG-KKDALNSLDLVI-PNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTING--IEIKNSQKIRQMIGY 79
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIkPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDfdfypnmkvsEVLYYLGFLSKINQTDFDKYVDLILRKVNLID-----------YKN---KKVKSLSGGMKKRLGIA 145
Cdd:cd03252 81 VLQE----------NVLFNRSIRDNIALADPGMSMERVIEAAKLAGahdfiselpegYDTivgEQGAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 146 QAILHDPKVIIVDEPTAGLDPE-ERVRIRNlLSDLAENKIVIISTHIVSDIEsTCNRIAILDKGSLVYKGDIPSLI 220
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYEsEHAIMRN-MHDICAGRTVIIIAHRLSTVK-NADRIIVMEKGRIVEQGSHDELL 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-215 |
1.00e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.69 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 28 PNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK----IRQMIGYLPQDFD---FYPNMKvSEVLYYLG 100
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllaLRQQVATVFQDPEqqiFYTDID-SDIAFSLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 101 FLSkINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDL- 179
Cdd:PRK13638 105 NLG-VPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIv 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1436942050 180 AENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGD 215
Cdd:PRK13638 184 AQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-222 |
1.29e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.85 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 16 KKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK------IRQMIGYLPQ------ 82
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYyAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirpVRKRIGMVFQfpesql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 -------DFDFYP---NMKVSEVLYYLgflskinqtdFDKYVDLILRKvnliDYKNKKVKSLSGGMKKRLGIAQAILHDP 152
Cdd:PRK13646 99 fedtverEIIFGPknfKMNLDEVKNYA----------HRLLMDLGFSR----DVMSQSPFQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 153 KVIIVDEPTAGLDPEERVRIRNLLSDLA--ENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQ 222
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-210 |
1.35e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN--SQKIRQMIGYL 80
Cdd:PRK09536 4 IDVSDLSVEF-GDTTVLDGVDLSVREGSLvGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlsARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQD----FDFypnmKVSEVLY-----YLGFLSKINQTDfDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHD 151
Cdd:PRK09536 83 PQDtslsFEF----DVRQVVEmgrtpHRSRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 152 PKVIIVDEPTAGLDPEERVRIRNLLSDLAEN-KIVIISTHIVSDIESTCNRIAILDKGSL 210
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-263 |
1.70e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.48 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 2 NKIVIKGLSKSY-DGKKDALNSLDLVIPNGMFGIL-GRNGSGKSTLMNIIATILQP---SKGTVTINGIEI--KNSQKIR 74
Cdd:PRK13640 4 NIVEFKHVSFTYpDSKKPALNDISFSIPRGSWTALiGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLtaKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 75 QMIGYLPQDFD--FYPNMKVSEVLYYLGFlSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDP 152
Cdd:PRK13640 84 EKVGIVFQNPDnqFVGATVGDDVAFGLEN-RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 153 KVIIVDEPTAGLDPEERVRIRNLLSDLA-ENKIVIISthIVSDIE--STCNRIAILDKGSLvykgdipsLIQQSDDHIYe 229
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVIS--ITHDIDeaNMADQVLVLDDGKL--------LAQGSPVEIF- 231
|
250 260 270
....*....|....*....|....*....|....
gi 1436942050 230 inlspSELESFRENDLFITKTQEIENKLKVRFIS 263
Cdd:PRK13640 232 -----SKVEMLKEIGLDIPFVYKLKNKLKEKGIS 260
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-216 |
3.52e-22 |
|
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: 92.53 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRqMIGYlpQDFDFYPNMKVSEVLYY 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFiSLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR-MVVF--QNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 99 L--GFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLL 176
Cdd:TIGR01184 78 AvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1436942050 177 SDLAENK--IVIISTHIVSDIESTCNRIAILDKGSLVYKGDI 216
Cdd:TIGR01184 158 MQIWEEHrvTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-231 |
1.17e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 91.30 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNGmfGI---LGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN--SQKIRQMIG 78
Cdd:COG4604 2 IEIKNVSKRYGGKV-VLDDVSLTIPKG--GItalIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtpSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDFDFYPNMKVSEVL------YYLGFLSKINQtdfdKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDP 152
Cdd:COG4604 79 ILRQENHINSRLTVRELVafgrfpYSKGRLTAEDR----EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 153 KVIIVDEPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHivsDIE---STCNRIAILDKGSLVYKGDiPSLIQQSD--D 225
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLADelGKTVVIVLH---DINfasCYADHIVAMKDGRVVAQGT-PEEIITPEvlS 230
|
....*.
gi 1436942050 226 HIYEIN 231
Cdd:COG4604 231 DIYDTD 236
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-208 |
1.25e-21 |
|
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: 88.66 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTIngieiknSQKIRqmIGYLPQ 82
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGdRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-------GSTVK--IGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 dfdfypnmkvsevlyylgflskinqtdfdkyvdlilrkvnlidyknkkvksLSGGMKKRLGIAQAILHDPKVIIVDEPTA 162
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1436942050 163 GLDPEERVRIRNLLSDLaeNKIVIISTHIVSDIESTCNRIAILDKG 208
Cdd:cd03221 100 HLDLESIEALEEALKEY--PGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-211 |
1.79e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.99 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGYL 80
Cdd:PRK13548 3 LEARNLSVRL-GGRTLLDDVSLTLRPGeVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQ----DFDFypnmKVSEV----LYYLGflskINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAIL--- 149
Cdd:PRK13548 82 PQhsslSFPF----TVEEVvamgRAPHG----LSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 150 ---HDPKVIIVDEPTAGLDPEERVRIRNLLSDLA--ENKIVIISTHivsDIEST---CNRIAILDKGSLV 211
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAheRGLAVIVVLH---DLNLAaryADRIVLLHQGRLV 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-211 |
2.01e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 90.87 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSYdGKKDALNSLDLVIP-NGMFGILGRNGSGKSTL------MNIiatiLQPS---KGTVTINGIEIKNSQ- 71
Cdd:COG1117 11 KIEVRNLNVYY-GDKQALKDINLDIPeNKVTALIGPSGCGKSTLlrclnrMND----LIPGarvEGEILLDGEDIYDPDv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 72 ---KIRQMIGYLPQdfdfYPN---MKVSE-VLY---YLGFLSKinqTDFDKYVDLILRKVNLIDyknkKVK--------S 133
Cdd:COG1117 86 dvvELRRRVGMVFQ----KPNpfpKSIYDnVAYglrLHGIKSK---SELDEIVEESLRKAALWD----EVKdrlkksalG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 134 LSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHI------VSDiestcnRIAILDK 207
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNmqqaarVSD------YTAFFYL 228
|
....
gi 1436942050 208 GSLV 211
Cdd:COG1117 229 GELV 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-222 |
2.57e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.48 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 2 NKIVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQMIGYL 80
Cdd:PRK11432 5 NFVVLKNITKRF-GSNTVIDNLNLTIKQGtMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQDFDFYPNMKVSE-VLYYLGFLsKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDE 159
Cdd:PRK11432 84 FQSYALFPHMSLGEnVGYGLKML-GVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 160 PTAGLDPEERVRIRNLLSDLaENKIVIIS---THIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQ 222
Cdd:PRK11432 163 PLSNLDANLRRSMREKIREL-QQQFNITSlyvTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
34-191 |
3.16e-21 |
|
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: 88.95 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 34 ILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIR-QMIGYLPQdfdfYPNMK-VSEVLYYLGFLSKINQTDfD 111
Cdd:TIGR01189 31 VTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPhENILYLGH----LPGLKpELSALENLHFWAAIHGGA-Q 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 112 KYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSD-LAENKIVIISTH 190
Cdd:TIGR01189 106 RTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
.
gi 1436942050 191 I 191
Cdd:TIGR01189 186 Q 186
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-222 |
5.41e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 92.56 E-value: 5.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSY----DGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTIN-GIE--------IKN 69
Cdd:TIGR03269 280 IKVRNVSKRYisvdRGVVKAVDNVSLEVKEGeIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvdmtkpgPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 70 SQKIRQMIGYLPQDFDFYPN---------------------MKVSEVLYYLGFLSKINQTDFDKYVDlilrkvnlidykn 128
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPHrtvldnlteaiglelpdelarMKAVITLKMVGFDEEKAEEILDKYPD------------- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 129 kkvkSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHIVSDIESTCNRIAILD 206
Cdd:TIGR03269 427 ----ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMR 502
|
250
....*....|....*.
gi 1436942050 207 KGSLVYKGDIPSLIQQ 222
Cdd:TIGR03269 503 DGKIVKIGDPEEIVEE 518
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
34-202 |
6.37e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.39 E-value: 6.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 34 ILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQMIgYL-PQDFdFYPNMKVSEVlyyLGFLSKINQTDfDK 112
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH-YLgHRNA-MKPALTVAEN---LEFWAAFLGGE-EL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 113 YVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSD-LAENKIVIISTHI 191
Cdd:PRK13539 107 DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIAATHI 186
|
170
....*....|.
gi 1436942050 192 vsDIESTCNRI 202
Cdd:PRK13539 187 --PLGLPGARE 195
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-216 |
1.25e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.97 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK-IRQMIgylp 81
Cdd:PRK11247 13 LLLNAVSKRY-GERTVLNQLDLHIPAGQFvAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREdTRLMF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVLyYLGFlskinQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPT 161
Cdd:PRK11247 88 QDARLLPWKKVIDNV-GLGL-----KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 162 AGLDPEERVRIRNLLSDLAENK--IVIISTHIVSDiestcnRIAILDKGSLVYKGDI 216
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSE------AVAMADRVLLIEEGKI 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-214 |
2.22e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.09 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSYDGKKDALN----SLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN------SQ 71
Cdd:PRK10070 23 KYIEQGLSKEQILEKTGLSlgvkDASLAIEEGeIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 72 KIRQMIGYLPQDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHD 151
Cdd:PRK10070 103 VRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAIN 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 152 PKVIIVDEPTAGLDPEERVRIRNLLSDL--AENKIVIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:PRK10070 183 PDILLMDEAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-257 |
2.30e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 88.61 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIV-IKGLSKSYDGKKDA--LNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTING--IEIKNSQKIR 74
Cdd:PRK13642 1 MNKILeVENLVFKYEKESDVnqLNGVSFSITKGEWvSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 75 QMIGYLPQDFDF-YPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPK 153
Cdd:PRK13642 81 RKIGMVFQNPDNqFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 154 VIIVDEPTAGLDPEERVRIRNLLSDLAEN-KIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSDDHI---YE 229
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVeigLD 240
|
250 260
....*....|....*....|....*...
gi 1436942050 230 INLSPSELESFRENDLFITKTQEIENKL 257
Cdd:PRK13642 241 VPFSSNLMKDLRKNGFDLPEKYLSEDEL 268
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-215 |
3.81e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 87.33 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 2 NKIVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI------------- 67
Cdd:PRK10619 4 NKLNVIDLHKRY-GEHEVLKGVSLQANAGdVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 68 --KNSQKIRQMIGYLPQDFDFYPNMKVSE-----VLYYLGFLSKINQTDFDKYVDlilrKVNLIDYKNKKVKS-LSGGMK 139
Cdd:PRK10619 83 dkNQLRLLRTRLTMVFQHFNLWSHMTVLEnvmeaPIQVLGLSKQEARERAVKYLA----KVGIDERAQGKYPVhLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1436942050 140 KRLGIAQAILHDPKVIIVDEPTAGLDPE---ERVRIRNLLSDlaENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGD 215
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAE--EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-214 |
5.26e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 87.35 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 15 GKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN--SQKIRQMIGYLPQDFDFYPNMK 91
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFtAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaSKEVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 92 VSEVLY-----YLGFLSKINQTDFDKyVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDP 166
Cdd:PRK10253 98 VQELVArgrypHQPLFTRWRKEDEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 167 EERVRIRNLLSDLAENKIVIISThIVSDIESTC---NRIAILDKGSLVYKG 214
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAA-VLHDLNQACryaSHLIALREGKIVAQG 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-214 |
5.89e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 89.94 E-value: 5.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 28 PNGMFGILGRNGSGKSTLMNIIATILQPS--KGTVTINGIEIknSQKIRQMIGYLPQDFDFYPNMKVSEVLYYLGF---- 101
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKP--TKQILKRTGFVTQDDILYPHLTVRETLVFCSLlrlp 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 102 --LSKINQTDFDKYV--DLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLS 177
Cdd:PLN03211 171 ksLTKQEKILVAESVisELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLG 250
|
170 180 190
....*....|....*....|....*....|....*....
gi 1436942050 178 DLAEN-KIVIISTHIVSD-IESTCNRIAILDKGSLVYKG 214
Cdd:PLN03211 251 SLAQKgKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFG 289
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-196 |
6.99e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 85.61 E-value: 6.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 22 SLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQP---SKGTVTINGIEIKNSQKIRQMIGYLPQDFDFYPNMKVSEVLY 97
Cdd:COG4136 19 PLSLTVAPGeILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHLSVGENLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 98 YlGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLS 177
Cdd:COG4136 99 F-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVF 177
|
170 180
....*....|....*....|.
gi 1436942050 178 DLAE--NKIVIISTHIVSDIE 196
Cdd:COG4136 178 EQIRqrGIPALLVTHDEEDAP 198
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-210 |
8.14e-20 |
|
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: 84.79 E-value: 8.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKsydgkKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK---NSQKIRQMIGYLP 81
Cdd:cd03215 7 VRGLSV-----KGAVRDVSFEVRAGeIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrsPRDAIRAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QD------FdfyPNMKVSEvlyylgflskiNqtdfdkyvdLILRKVnlidyknkkvksLSGGMKKRLGIAQAILHDPKVI 155
Cdd:cd03215 82 EDrkreglV---LDLSVAE-----------N---------IALSSL------------LSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 156 IVDEPTAGLDPEERVRIRNLLSDLAENK--IVIISTHIvSDIESTCNRIAILDKGSL 210
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGkaVLLISSEL-DELLGLCDRILVMYEGRI 182
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-196 |
1.12e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.29 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRqmiGYLPQDF 84
Cdd:PRK11248 4 ISHLYADYGGKP-ALEDINLTLESGeLLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---GVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 85 DFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGL 164
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190
....*....|....*....|....*....|....
gi 1436942050 165 DPEERVRIRNLLSDLAEN--KIVIISTHivsDIE 196
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQEtgKQVLLITH---DIE 190
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-214 |
1.38e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 86.05 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 13 YDGKKDALNSLDLVIP-NGMFGILGRNGSGKSTLMNIIATILQPS-----KGTVTINGIEIKNSQ----KIRQMIGYLPQ 82
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPqNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDvdpiEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFDFYPNMKVSEVLYYLGFLSKI--NQTDFDKYVDLILRKVNLIDYKNKKVK----SLSGGMKKRLGIAQAILHDPKVII 156
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1436942050 157 VDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-254 |
1.42e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 86.68 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSYDGKK----DALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTIN-----------GIE 66
Cdd:PRK13651 2 QIKVKNIVKIFNKKLptelKALDNVSVEINQGEFiAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktkEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 67 ---------------IKNSQKIRQMIGYLPQdFDFYPNMKVS-EVLYYLGFLS-KINQTDFDKYVDLILRKVNL-IDYKN 128
Cdd:PRK13651 82 kvleklviqktrfkkIKKIKEIRRRVGVVFQ-FAEYQLFEQTiEKDIIFGPVSmGVSKEEAKKRAAKYIELVGLdESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 129 KKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAEN-KIVIISTHIVSDIESTCNRIAILDK 207
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 208 GSLVYKGDIPSlIQQSDDHIYEINLSPSELESF----RENDLFITKTQEIE 254
Cdd:PRK13651 241 GKIIKDGDTYD-ILSDNKFLIENNMEPPKLLNFvnklEKKGIDVPKVTSIE 290
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-215 |
1.70e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.83 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKD----ALNSLDLVIP-NGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGI--------------- 65
Cdd:PRK13631 24 VKNLYCVFDEKQEnelvALNNISYTFEkNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdkknnhelitnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 66 ---EIKNSQKIRQMIGYLPQdFDFYPNMK--VSEVLYYLGFLSKINQTDFDKYVDLILRKVNL-IDYKNKKVKSLSGGMK 139
Cdd:PRK13631 104 yskKIKNFKELRRRVSMVFQ-FPEYQLFKdtIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQK 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 140 KRLGIAQAILHDPKVIIVDEPTAGLDPE-ERVRIRNLLSDLAENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGD 215
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKgEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-212 |
1.86e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYD----GKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQ--KIRQM 76
Cdd:COG1101 2 LELKNLSKTFNpgtvNEKRALDGLNLTIEEGDFvTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPeyKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 77 IGYLPQDfdfyP------NMKVSE--VLYYL-----GFLSKINQTDFDKYVDLiLRKVN--LIDYKNKKVKSLSGGMKKR 141
Cdd:COG1101 82 IGRVFQD----PmmgtapSMTIEEnlALAYRrgkrrGLRRGLTKKRRELFREL-LATLGlgLENRLDTKVGLLSGGQRQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 142 LGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDL-AENKI-VIISTHIVSDIESTCNRIAILDKGSLVY 212
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLtTLMVTHNMEQALDYGNRLIMMHEGRIIL 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-216 |
2.35e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 86.85 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 23 LDLVIP-NGMFGILGRNGSGKSTLMNIIATILQPSKGTVTING-IEIKNSQKI-----RQMIGYLPQDFDFYPNMKVSEV 95
Cdd:PRK11144 17 VNLTLPaQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGIclppeKRRIGYVFQDARLFPHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 96 LYYlGfLSKINQTDFDKYVDLI-----LRKVNLidyknkkvkSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLD-Peer 169
Cdd:PRK11144 97 LRY-G-MAKSMVAQFDKIVALLgieplLDRYPG---------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlP--- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 170 vRIRNL---LSDLAEN-KIVII-STHIVSDIESTCNRIAILDKGSLVYKGDI 216
Cdd:PRK11144 163 -RKRELlpyLERLAREiNIPILyVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-211 |
2.44e-19 |
|
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: 84.79 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSY---DGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIknSQ-------K 72
Cdd:COG4181 9 IELRGLTKTVgtgAGELTILKGISLEVEAGESvAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL--FAldedaraR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 73 IR-QMIGYLPQDFDFYPNMKVSE-VLYYLGFLSKINqtDFDKYVDLiLRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILH 150
Cdd:COG4181 87 LRaRHVGFVFQSFQLLPTLTALEnVMLPLELAGRRD--ARARARAL-LERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 151 DPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK---IVIIsTHIVSDIEStCNRIAILDKGSLV 211
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERgttLVLV-THDPALAAR-CDRVLRLRAGRLV 225
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-166 |
2.63e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 88.26 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIA--TILQpsKGTVTINGIEIKNSQKIRQM---I 77
Cdd:NF033858 2 ARLEGVSHRY-GKTVALDDVSLDIPAGcMVGLIGPDGVGKSSLLSLIAgaRKIQ--QGRVEVLGGDMADARHRRAVcprI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQDF--DFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVI 155
Cdd:NF033858 79 AYMPQGLgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLL 158
|
170
....*....|.
gi 1436942050 156 IVDEPTAGLDP 166
Cdd:NF033858 159 ILDEPTTGVDP 169
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-211 |
4.36e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.89 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 8 GLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK-NSQK--IRQMIGYLPQD 83
Cdd:PRK11288 9 GIGKTFPGVK-ALDDISFDCRAGqVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTaaLAAGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 84 FDFYPNMKVSEVLyYLGFLSK----INQTDFDKYVDLILRKVNL-IDyKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVD 158
Cdd:PRK11288 88 LHLVPEMTVAENL-YLGQLPHkggiVNRRLLNYEAREQLEHLGVdID-PDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 159 EPTAGLDPEERVRIRNLLSDL-AENKIVIISTHIVSDIESTCNRIAILDKGSLV 211
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELrAEGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-222 |
4.69e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.00 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGK-KDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN------------ 69
Cdd:PRK11176 342 IEFRNVTFTYPGKeVPALRNINFKIPAGkTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytlaslrnqval 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 70 -SQK-------IRQMIGYLPQD-FDFYPNMKVSEVLYYLGFLSKInqtdfDKYVDLILRKvNLIdyknkkvkSLSGGMKK 140
Cdd:PRK11176 422 vSQNvhlfndtIANNIAYARTEqYSREQIEEAARMAYAMDFINKM-----DNGLDTVIGE-NGV--------LLSGGQRQ 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 141 RLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTcNRIAILDKGSLVYKGDIPSLI 220
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKA-DEILVVEDGEIVERGTHAELL 566
|
..
gi 1436942050 221 QQ 222
Cdd:PRK11176 567 AQ 568
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-206 |
5.47e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 86.79 E-value: 5.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 19 ALNSLDLVIPNGMFGILGRNGSGKSTLMNIIATILQPS-----------------KGTVTINGI------EIKNSQKIrQ 75
Cdd:PRK13409 89 KLYGLPIPKEGKVTGILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfRGTELQNYFkklyngEIKVVHKP-Q 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 76 MIGYLPQDFDfypnMKVSEVlyylgfLSKINQTD-FDKYVDlilrKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKV 154
Cdd:PRK13409 168 YVDLIPKVFK----GKVREL------LKKVDERGkLDEVVE----RLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 155 IIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHivsDiestcnrIAILD 206
Cdd:PRK13409 234 YFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEH---D-------LAVLD 275
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-210 |
6.38e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.52 E-value: 6.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN-SQKIRQmIGYLP 81
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLNDISLDIPSGqMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlHARDRK-VGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSE-VLYYLGFL---SKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIV 157
Cdd:PRK10851 81 QHYALFRHMTVFDnIAFGLTVLprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 158 DEPTAGLDPEERVRIRNLLSDLAEN-KIV-IISTHIVSDIESTCNRIAILDKGSL 210
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEElKFTsVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-214 |
6.79e-19 |
|
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: 84.11 E-value: 6.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKDALN-SLDLViPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTING-----------IEIKNSQKI 73
Cdd:TIGR02323 6 VSGLSKSYGGGKGCRDvSFDLY-PGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaelelyqlSEAERRRLM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 74 RQMIGYLPQDFDFYPNMKVS------EVLYYLG--FLSKINQTDFDkyvdlILRKVNL-IDYKNKKVKSLSGGMKKRLGI 144
Cdd:TIGR02323 85 RTEWGFVHQNPRDGLRMRVSaganigERLMAIGarHYGNIRATAQD-----WLEEVEIdPTRIDDLPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 145 AQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK--IVIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLglAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-190 |
7.66e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.06 E-value: 7.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 13 YDGKKDALNSLDLVIP-NGMFGILGRNGSGKSTLMNIIATI--LQPS---KGTVTINGIEIKNSQ----KIRQMIGYLPQ 82
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPkNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYAPDvdpvEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DfdfyPNMKVSEVLYYLGFLSKIN--QTDFDKYVDLILRKVNLIDYKNKKVK----SLSGGMKKRLGIAQAILHDPKVII 156
Cdd:PRK14243 99 K----PNPFPKSIYDNIAYGARINgyKGDMDELVERSLRQAALWDEVKDKLKqsglSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....
gi 1436942050 157 VDEPTAGLDPEERVRIRNLLSDLAENKIVIISTH 190
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-208 |
8.08e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.40 E-value: 8.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYDGKKD--ALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTING--IEIKNSQKIRQ 75
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEkyTLNDVSFHVKQGeWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdlLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 76 MIGYLPQDFD--FYPNMKVSEVLYylGFLSK-INQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDP 152
Cdd:PRK13650 82 KIGMVFQNPDnqFVGATVEDDVAF--GLENKgIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1436942050 153 KVIIVDEPTAGLDPEERVR-IRNLLSDLAENKIVIIS-THIVSDIeSTCNRIAILDKG 208
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLElIKTIKGIRDDYQMTVISiTHDLDEV-ALSDRVLVMKNG 216
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-190 |
1.10e-18 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 83.31 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSYdGKKDALNSLDL------VIpngmfGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--------- 67
Cdd:COG4598 8 ALEVRDLHKSF-GDLEVLKGVSLtarkgdVI-----SIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 68 ------KNSQKIRQMIGYLPQDFDFYPNMKVSE--------VLyylgflsKINQTDFDKYVDLILRKVNLIDYKNKKVKS 133
Cdd:COG4598 82 lvpadrRQLQRIRTRLGMVFQSFNLWSHMTVLEnvieapvhVL-------GRPKAEAIERAEALLAKVGLADKRDAYPAH 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 134 LSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPE---ERVR-IRnllsDLA-ENKIVIISTH 190
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPElvgEVLKvMR----DLAeEGRTMLVVTH 212
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-208 |
1.36e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 84.70 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYDG---KKDalnsLDLVIPNGMFGI-LGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQM 76
Cdd:PRK11000 1 MASVTLRNVTKAYGDvviSKD----INLDIHEGEFVVfVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 77 IGYLPQDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVII 156
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 157 VDEPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHIVSDIESTCNRIAILDKG 208
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
34-214 |
1.41e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 83.30 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 34 ILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK------NSQKIRqMIGYLPQDfDFYPNMKVSEVL-YYLGFLSKIN 106
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysyRSQRIR-MIFQDPST-SLNPRQRISQILdFPLRLNTDLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 107 QTDFDKYVDLILRKVNLI-DYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIV 185
Cdd:PRK15112 122 PEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGI 201
|
170 180 190
....*....|....*....|....*....|.
gi 1436942050 186 --IISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:PRK15112 202 syIYVTQHLGMMKHISDQVLVMHQGEVVERG 232
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-222 |
3.52e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.51 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLS-KSYDGKKdALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILqPSKGTVTINGIEIK--NSQKIRQMIGY 79
Cdd:PRK11174 350 IEAEDLEiLSPDGKT-LAGPLNFTLPAGQRiALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRelDPESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDFYPNMKVSEVLyylgfLSKINQTDFDkyVDLILRKVNLIDYKNKKVK-----------SLSGGMKKRLGIAQAI 148
Cdd:PRK11174 428 VGQNPQLPHGTLRDNVL-----LGNPDASDEQ--LQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 149 LHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIEStCNRIAILDKGSLVYKGDIPSLIQQ 222
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQA 573
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
26-211 |
7.18e-18 |
|
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: 80.15 E-value: 7.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 26 VIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNS--QKIRQMIGYLPQDfdfyPNMkvsevlyYLGFLs 103
Cdd:cd03369 31 VKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIplEDLRSSLTIIPQD----PTL-------FSGTI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 104 KINQTDFDKYVDLILrkvnlidYKNKKVKS----LSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDL 179
Cdd:cd03369 99 RSNLDPFDEYSDEEI-------YGALRVSEgglnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREE 171
|
170 180 190
....*....|....*....|....*....|..
gi 1436942050 180 AENKIVIISTHIVSDIeSTCNRIAILDKGSLV 211
Cdd:cd03369 172 FTNSTILTIAHRLRTI-IDYDKILVMDAGEVK 202
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-229 |
7.23e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.88 E-value: 7.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKdALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATI--LQPSKGTVTINGIEIKN---SQKIRQMIGY 79
Cdd:COG0396 3 IKNLHVSVEGKE-ILKGVNLTIKPGEVhAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILElspDERARAGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 L---PQDFdfyPNMKVSEvlyylgFL---------SKINQTDFDKYVDLILRKVNL-IDYKNKKV-KSLSGGMKKRLGIA 145
Cdd:COG0396 82 AfqyPVEI---PGVSVSN------FLrtalnarrgEELSAREFLKLLKEKMKELGLdEDFLDRYVnEGFSGGEKKRNEIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 146 QAILHDPKVIIVDEPTAGLDPeERVRI-RNLLSDLA-ENKIVIISTH-------IVSDiestcnRIAILDKGSLVYKGDi 216
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLDI-DALRIvAEGVNKLRsPDRGILIITHyqrildyIKPD------FVHVLVDGRIVKSGG- 224
|
250
....*....|...
gi 1436942050 217 PSLIQQSDDHIYE 229
Cdd:COG0396 225 KELALELEEEGYD 237
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-214 |
7.70e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.25 E-value: 7.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 13 YDGKKDALNSLDLVIPN-GMFGILGRNGSGKSTLMNIIATILQPSKGTVTING--------IEIKNSQKIRQMIGYLPQD 83
Cdd:PRK14246 19 YINDKAILKDITIKIPNnSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlyfgkdIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 84 FDFYPNMKVSE-VLYYLGFLSKINQTDFDKYVDLILRKVNL----IDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVD 158
Cdd:PRK14246 99 PNPFPHLSIYDnIAYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 159 EPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-227 |
9.14e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.18 E-value: 9.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQ--KIRQMIGYL 80
Cdd:PRK15439 12 LCARSISKQYSGVE-VLKGIDFTLHAGeVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpaKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 -PQDFDFYPNMKVSE-VLYYLgflsKINQTDFDKYVDLiLRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVD 158
Cdd:PRK15439 91 vPQEPLLFPNLSVKEnILFGL----PKRQASMQKMKQL-LAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 159 EPTAGLDPEERVR----IRNLLSDlaENKIVIIStHIVSDIESTCNRIAILDKGSLVYKGDIPSLiqqSDDHI 227
Cdd:PRK15439 166 EPTASLTPAETERlfsrIRELLAQ--GVGIVFIS-HKLPEIRQLADRISVMRDGTIALSGKTADL---STDDI 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-227 |
1.24e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 80.59 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYdGKKDALNSLDL-VIPNGMFGILGRNGSGKSTLMNIIATI--LQPS---KGTVTINGIEI----KNSQKIRQ 75
Cdd:PRK14239 8 VSDLSVYY-NKKKALNSVSLdFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIysprTDTVDLRK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 76 MIGYLPQDFDFYPnMKVSE-VLYYLGFLSKINQTDFDKYVDLILRKVNLIDyknkKVK--------SLSGGMKKRLGIAQ 146
Cdd:PRK14239 87 EIGMVFQQPNPFP-MSIYEnVVYGLRLKGIKDKQVLDEAVEKSLKGASIWD----EVKdrlhdsalGLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 147 AILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLI-----Q 221
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFmnpkhK 241
|
....*.
gi 1436942050 222 QSDDHI 227
Cdd:PRK14239 242 ETEDYI 247
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
32-211 |
1.62e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.37 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 32 FGILGRNGSGKSTLMNIIATILQPSKGTVTING--IEIKN-SQKIRQMIGYLPQD------FdfyPNMKVSE-------- 94
Cdd:COG1129 281 LGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSpRDAIRAGIAYVPEDrkgeglV---LDLSIREnitlasld 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 95 VLYYLGFLSKINQTDF-DKYVDLiLR-KVNLIDyknKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRI 172
Cdd:COG1129 358 RLSRGGLLDRRRERALaEEYIKR-LRiKTPSPE---QPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEI 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1436942050 173 RNLLSDLAENK--IVIISthivSDIE---STCNRIAILDKGSLV 211
Cdd:COG1129 434 YRLIRELAAEGkaVIVIS----SELPellGLSDRILVMREGRIV 473
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
34-223 |
2.08e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 79.24 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 34 ILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQMIGYLPQDFDFYPNMKVSEVLyYLGfLS---KINQTDF 110
Cdd:PRK10771 30 ILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNI-GLG-LNpglKLNAAQR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 111 DKYVDlILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK---IVII 187
Cdd:PRK10771 108 EKLHA-IARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqltLLMV 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 1436942050 188 StHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQS 223
Cdd:PRK10771 187 S-HSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
34-215 |
3.21e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.11 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 34 ILGRNGSGKSTLMNIIATILqPSKGTVTINGIEIK--NSQKIRQMIGYLPQDFDFYPNMKVSEVLyYLGFLSKINQTDFD 111
Cdd:COG4138 27 LIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSdwSAAELARHRAYLSQQQSPPFAMPVFQYL-ALHQPAGASSEAVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 112 KYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILH-------DPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKI 184
Cdd:COG4138 105 QLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGI 184
|
170 180 190
....*....|....*....|....*....|....*
gi 1436942050 185 -VIISTHivsDIESTC---NRIAILDKGSLVYKGD 215
Cdd:COG4138 185 tVVMSSH---DLNHTLrhaDRVWLLKQGKLVASGE 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-206 |
3.45e-17 |
|
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: 81.75 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 33 GILGRNGSGKSTLMNIIATILQPS-----------------KGTV-------TINGiEIKNSQKIrQMIGYLPQDFDfyp 88
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfRGTElqdyfkkLANG-EIKVAHKP-QYVDLIPKVFK--- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 89 nMKVSEVLyylgflskiNQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEE 168
Cdd:COG1245 178 -GTVRELL---------EKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180 190
....*....|....*....|....*....|....*....
gi 1436942050 169 RVRIRNLLSDLAE-NKIVIISTHivsDiestcnrIAILD 206
Cdd:COG1245 248 RLNVARLIRELAEeGKYVLVVEH---D-------LAILD 276
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-209 |
3.46e-17 |
|
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: 78.28 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKD----ALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTINGieiknsqkirqMIG 78
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELvAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQdFDFYPNMKVSE-VLyylgFLSKINQTDFDKYVDLI-LRKvnliDYKN-----------KKVkSLSGGMKKRLGIA 145
Cdd:cd03250 70 YVSQ-EPWIQNGTIREnIL----FGKPFDEERYEKVIKACaLEP----DLEIlpdgdlteigeKGI-NLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 146 QAILHDPKVIIVDEPTAGLDPEERVRI--RNLLSDLAENKIVIISTHIVSDIEStCNRIAILDKGS 209
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-186 |
4.36e-17 |
|
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: 81.37 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 33 GILGRNGSGKSTLMNIIATILQPSKGTVTIngiEIKNSQKIRqmigYLPQDFDfypnMKVSEvlyylgFLSKINQTDFD- 111
Cdd:COG1245 370 GIVGPNGIGKTTFAKILAGVLKPDEGEVDE---DLKISYKPQ----YISPDYD----GTVEE------FLRSANTDDFGs 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 112 -KYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK----IVI 186
Cdd:COG1245 433 sYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgktaMVV 512
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
28-210 |
5.22e-17 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 78.28 E-value: 5.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 28 PNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN--------------------SQKIRQMIGYLPQDFDFY 87
Cdd:cd03248 39 PGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkylhskvslvgqepvlfARSLQDNIAYGLQSCSFE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 88 PNMKVSEVLYYLGFLSKInQTDFDKYVDlilrkvnlidyknKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPE 167
Cdd:cd03248 119 CVKEAAQKAHAHSFISEL-ASGYDTEVG-------------EKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1436942050 168 ERVRIRNLLSDLAENKIVIISTHIVSDIESTcNRIAILDKGSL 210
Cdd:cd03248 185 SEQQVQQALYDWPERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-208 |
7.62e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 7.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKdALNSLDL-VIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-----KNSQKirQMIGY 79
Cdd:PRK10762 7 LKGIDKAFPGVK-ALSGAALnVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpKSSQE--AGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDFYPNMKVSEVLYyLG--FLSKINQTDFDKY---VDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKV 154
Cdd:PRK10762 84 IHQELNLIPQLTIAENIF-LGreFVNRFGRIDWKKMyaeADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 155 IIVDEPTAGLDPEERVRIRNLLSDLAENK--IVIIStHIVSDIESTCNRIAILDKG 208
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGrgIVYIS-HRLKEIFEICDDVTVFRDG 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-167 |
7.64e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 80.32 E-value: 7.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 2 NKIVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVtingieiKNSQKIRqmIGYL 80
Cdd:PRK15064 318 NALEVENLTKGFDNGP-LFKNLNLLLEAGeRLAIIGENGVGKTTLLRTLVGELEPDSGTV-------KWSENAN--IGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQD--FDFYPNMKVSEvlyylgFLSKINQTDFDkyvDLILRKV--NLI---DYKNKKVKSLSGGMKKRLGIAQAILHDPK 153
Cdd:PRK15064 388 AQDhaYDFENDLTLFD------WMSQWRQEGDD---EQAVRGTlgRLLfsqDDIKKSVKVLSGGEKGRMLFGKLMMQKPN 458
|
170
....*....|....
gi 1436942050 154 VIIVDEPTAGLDPE 167
Cdd:PRK15064 459 VLVMDEPTNHMDME 472
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
11-232 |
7.99e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.38 E-value: 7.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 11 KSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKS----TLMNIIAT---IlqpsKGTVTINGIEIKNSQ-----KIR-QM 76
Cdd:PRK09473 23 STPDGDVTAVNDLNFSLRAGeTLGIVGESGSGKSqtafALMGLLAAngrI----GGSATFNGREILNLPekelnKLRaEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 77 IGYLPQD--FDFYPNMKVSEVLYYLGFLSK--INQTDFDKYVDLiLRKVNLIDYKnKKVK----SLSGGMKKRLGIAQAI 148
Cdd:PRK09473 99 ISMIFQDpmTSLNPYMRVGEQLMEVLMLHKgmSKAEAFEESVRM-LDAVKMPEAR-KRMKmyphEFSGGMRQRVMIAMAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 149 LHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSdDH 226
Cdd:PRK09473 177 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP-SH 255
|
....*.
gi 1436942050 227 IYEINL 232
Cdd:PRK09473 256 PYSIGL 261
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-215 |
8.00e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 79.39 E-value: 8.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKD----------ALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--KNS 70
Cdd:COG4608 8 LEVRDLKKHFPVRGGlfgrtvgvvkAVDGVSFDIRRGeTLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItgLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 71 QKIR------QMIgylpqdF-DFY----PNMKV----SEVLYYLGFLSKinqTDFDKYVDLILRKVNL-IDYKNKKVKSL 134
Cdd:COG4608 88 RELRplrrrmQMV------FqDPYaslnPRMTVgdiiAEPLRIHGLASK---AERRERVAELLELVGLrPEHADRYPHEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 135 SGGMKKRLGIAQAILHDPKVIIVDEPTAGLDpeerVRIR----NLLSDLAENK---IVIIStHIVSDIESTCNRIAILDK 207
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALD----VSIQaqvlNLLEDLQDELgltYLFIS-HDLSVVRHISDRVAVMYL 233
|
....*...
gi 1436942050 208 GSLVYKGD 215
Cdd:COG4608 234 GKIVEIAP 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-183 |
9.18e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 80.24 E-value: 9.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 33 GILGRNGSGKSTLMNIIATILQPSKGTVTIngiEIKnsqkirqmIGYLPQ----DFDfypnMKVSEvlyylgFLSKINqT 108
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELK--------ISYKPQyikpDYD----GTVED------LLRSIT-D 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 109 DFDK--YVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK 183
Cdd:PRK13409 427 DLGSsyYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER 503
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-211 |
9.54e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.19 E-value: 9.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSY--------DGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI---K 68
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkHQHQTVLNNVSLSLKSGeTVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 69 NSQK--IRQMIGYLPQDF--DFYPNMKVSEVLYY-LGFLSKINQTDFDKYVDLILRKVNLID-YKNKKVKSLSGGMKKRL 142
Cdd:PRK10419 81 RAQRkaFRRDIQMVFQDSisAVNPRKTVREIIREpLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 143 GIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAEN---KIVIIsTHIVSDIESTCNRIAILDKGSLV 211
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfgtACLFI-THDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-190 |
9.60e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.54 E-value: 9.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSY---DGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN------SQKIRQ 75
Cdd:PRK10535 7 LKDIRRSYpsgEEQVEVLKGISLDIYAGeMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadalAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 76 MIGYLPQDFDFYP------NMKVSEVlyYLGFLSKINQtdfDKYVDLILRkVNLIDYKNKKVKSLSGGMKKRLGIAQAIL 149
Cdd:PRK10535 87 HFGFIFQRYHLLShltaaqNVEVPAV--YAGLERKQRL---LRAQELLQR-LGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1436942050 150 HDPKVIIVDEPTAGLDPEERVRIRNLLSDLAEN-KIVIISTH 190
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTH 202
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-224 |
1.27e-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: 78.99 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 24 DLVIP-NGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGiEI--KNSQKI------RQmIGYLPQD---FdfyPNMK 91
Cdd:COG4148 19 DFTLPgRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVlqDSARGIflpphrRR-IGYVFQEarlF---PHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 92 VSEVLYY-LGFLSKIN-QTDFDKYVDL-----ILrkvnlidykNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGL 164
Cdd:COG4148 94 VRGNLLYgRKRAPRAErRISFDEVVELlgighLL---------DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 165 DPEERVRIRNLLSDLAEN-KI-VIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSD 224
Cdd:COG4148 165 DLARKAEILPYLERLRDElDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-228 |
1.91e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 76.03 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNGM-FGILGRNGSGKSTLMNIIA--TILQPSKGTVTINGIEIKN---SQKIRQMI 77
Cdd:cd03217 1 LEIKDLHVSVGGKE-ILKGVNLTIKKGEvHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDlppEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQDFDFYPNMKVSEVLyylgflskinqtdfdkyvdlilRKVNlidyknkkvKSLSGGMKKRLGIAQAILHDPKVIIV 157
Cdd:cd03217 80 FLAFQYPPEIPGVKNADFL----------------------RYVN---------EGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 158 DEPTAGLDPEERVRIRNLLSDLA-ENKIVIISTH---IVSDIEStcNRIAILDKGSLVYKGDiPSLIQQSDDHIY 228
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqrLLDYIKP--DRVHVLYDGRIVKSGD-KELALEIEKKGY 200
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-227 |
2.65e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 19 ALNSLDL-VIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN--SQKI-RQMIGYLPQDFDFYPNMKVSE 94
Cdd:PRK11300 20 AVNNVNLeVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlpGHQIaRMGVVRTFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 95 VLYYL-------GFLSKINQT-DFDK-------YVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDE 159
Cdd:PRK11300 100 NLLVAqhqqlktGLFSGLLKTpAFRRaesealdRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 160 PTAGLDPEERVRIRNLLSDLAE--NKIVIISTHIVSDIESTCNRIAILDKGSLVYKGdIPSLIQQSDDHI 227
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG-TPEEIRNNPDVI 248
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-219 |
5.40e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 77.08 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 2 NKIVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTlMNIIATILQPSKGTVTIN-GIEIKNSQKIRQMIG- 78
Cdd:NF000106 12 NAVEVRGLVKHF-GEVKAVDGVDLDVREGtVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRf*TWCANRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVD 158
Cdd:NF000106 90 HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 159 EPTAGLDPEERV----RIRNLLSDLAenkIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSL 219
Cdd:NF000106 170 EPTTGLDPRTRNevwdEVRSMVRDGA---TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-245 |
8.57e-16 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 77.24 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 19 ALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTvtingIEIKNSQKIRQMIGYLPQDFDFYPNMKVSevly 97
Cdd:PRK13545 39 ALNNISFEVPEGeIVGIIGLNGSGKSTLSNLIAGVTMPNKGT-----VDIKGSAALIAISSGLNGQLTGIENIELK---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 98 ylGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLS 177
Cdd:PRK13545 110 --GLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMN 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 178 DLAEN-KIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSDDHIYEIN-LSPSELESFRENDL 245
Cdd:PRK13545 188 EFKEQgKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNqMSVEERKDFREEQI 257
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-190 |
9.35e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.35 E-value: 9.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 5 VIKGLSKSYDGKKDALN-SLDLViPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIE------IKNSQKIRQMI 77
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDvSFDLY-PGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 -----GYLPQDfdfyP----NMKVS------EVLYYLG--FLSKINQTDFDkyvdlILRKVNL----IDyknKKVKSLSG 136
Cdd:PRK11701 87 lrtewGFVHQH----PrdglRMQVSaggnigERLMAVGarHYGDIRATAGD-----WLERVEIdaarID---DLPTTFSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1436942050 137 GMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVR----IRNLLSDLaeNKIVIISTH 190
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARlldlLRGLVREL--GLAVVIVTH 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-173 |
1.12e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 76.42 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYDGKKDALNSLDLVIPNGMF-GILGRNGSGKSTLMNIIATILQPSKGTVTI-----NGIEIKNsqkiR 74
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFiVLVGPSGCGKSTLLRMVAGLERITSGEIWIggrvvNELEPAD----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 75 QmIGYLPQDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKV 154
Cdd:PRK11650 77 D-IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170
....*....|....*....
gi 1436942050 155 IIVDEPTAGLDPEERVRIR 173
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMR 174
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-225 |
1.13e-15 |
|
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: 76.90 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKDALNSLDL-VIPNGMFGILGRNGSGKSTLMNIIATILQPSKGtvtingiEIKNSQKIRqmIGYLPQDF 84
Cdd:TIGR03719 7 MNRVSKVVPPKKEILKDISLsFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------EARPQPGIK--VGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 85 DFYPN--------MKVSEVLYYLGFLSKIN------QTDFDKYVDLILRKVNLIDYKN---------------------K 129
Cdd:TIGR03719 78 QLDPTktvrenveEGVAEIKDALDRFNEISakyaepDADFDKLAAEQAELQEIIDAADawdldsqleiamdalrcppwdA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 130 KVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENkiVIISTHIVSDIESTCNRIAILDKGS 209
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGT--VVAVTHDRYFLDNVAGWILELDRGR 235
|
250
....*....|....*..
gi 1436942050 210 LV-YKGDIPSLIQQSDD 225
Cdd:TIGR03719 236 GIpWEGNYSSWLEQKQK 252
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
34-191 |
1.33e-15 |
|
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: 73.68 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 34 ILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQMIGYLPQDfdfyPNMK-VSEVLYYLGFLSKINQTDfd 111
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdFQRDSIARGLLYLGHA----PGIKtTLSVLENLRFWHADHSDE-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 112 kYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLL-SDLAENKIVIISTH 190
Cdd:cd03231 105 -QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMaGHCARGGMVVLTTH 183
|
.
gi 1436942050 191 I 191
Cdd:cd03231 184 Q 184
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-216 |
1.50e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.53 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK---IRQMIGYLP 81
Cdd:PRK11614 8 FDKVSAHY-GKIQALHEVSLHINQGeIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakiMREAVAIVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVLYYLGFLSKINQ--TDFDKYVDLILRkvnLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDE 159
Cdd:PRK11614 87 EGRRVFSRMTVEENLAMGGFFAERDQfqERIKWVYELFPR---LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1436942050 160 PTAGLDPEERVRIRNLLSDLAENKIVIISthivsdIESTCNR-IAILDKGSLVYKGDI 216
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQGMTIFL------VEQNANQaLKLADRGYVLENGHV 215
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-237 |
1.83e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKK----DALNSLDLVIP-NGMFGILGRNGSGKSTLMNIIATILQPSKGTVTI-------NGIEIKNSQ 71
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefKALNNTSLTFKkNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipaNLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 72 KIRQMIGYLPQ--DFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLiLRKVNLI-DYKNKKVKSLSGGMKKRLGIAQAI 148
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPEL-LKLVQLPeDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 149 LHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAEN--KIVIISTHIVSDIESTCNRIAILDKGSLVYKGDiPSLIQQSDDH 226
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS-PFEIFSNQEL 244
|
250
....*....|.
gi 1436942050 227 IYEINLSPSEL 237
Cdd:PRK13645 245 LTKIEIDPPKL 255
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-211 |
3.20e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 5 VIKGLSKSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--KNSQKIRQM-IGYL 80
Cdd:COG3845 259 EVENLSVRDDRGVPALKDVSLEVRAGeILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItgLSPRERRRLgVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQD---FDFYPNMKVSE--VL--YYLGFLSKINQTDFDKYVDLILRKVNliDYK------NKKVKSLSGGMKKRLGIAQA 147
Cdd:COG3845 339 PEDrlgRGLVPDMSVAEnlILgrYRRPPFSRGGFLDRKAIRAFAEELIE--EFDvrtpgpDTPARSLSGGNQQKVILARE 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1436942050 148 ILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK--IVIISThivsDIE---STCNRIAILDKGSLV 211
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGaaVLLISE----DLDeilALSDRIAVMYEGRIV 481
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-221 |
3.90e-15 |
|
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: 73.17 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 23 LDLVIPNG-MFGILGRNGSGKST----LMNIIATILQPSKGTVTINGIEIkNSQKIRQM-IGYLPQD----FDFYPNMK- 91
Cdd:TIGR02770 5 LNLSLKRGeVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPL-LPLSIRGRhIATIMQNprtaFNPLFTMGn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 92 -VSEVLYYLGFLSKINQtdfdkyvDLI---LRKVNLIDYKnKKVKS----LSGGMKKRLGIAQAILHDPKVIIVDEPTAG 163
Cdd:TIGR02770 84 hAIETLRSLGKLSKQAR-------ALIleaLEAVGLPDPE-EVLKKypfqLSGGMLQRVMIALALLLEPPFLIADEPTTD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 164 LDPEERVRIRNLLSDLAENK---IVIIsTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQ 221
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQLFgtgILLI-THDLGVVARIADEVAVMDDGRIVERGTVKEIFY 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-193 |
6.51e-15 |
|
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: 74.59 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYdGKKDALNSLDLVIP-NGMFGILGRNGSGKSTLMNIIATILQPSKGTVTInGIEIKnsqkirqmIGYLPQ 82
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPpGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK--------LAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFD-FYPNMKVSEVLyylgflskinqTDFDKYVDLILRKVNLIDY----------KNKKVKSLSGGMKKRLGIAQAILHD 151
Cdd:TIGR03719 393 SRDaLDPNKTVWEEI-----------SGGLDIIKLGKREIPSRAYvgrfnfkgsdQQKKVGQLSGGERNRVHLAKTLKSG 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 152 PKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVI---------ISTHIVS 193
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVIshdrwfldrIATHILA 512
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
36-167 |
8.66e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.80 E-value: 8.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 36 GRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQM--IGYLP---QDFDFYPNmkvsevlyyLGFLSKINQTDF 110
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMayLGHLPglkADLSTLEN---------LHFLCGLHGRRA 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 111 DKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPE 167
Cdd:PRK13543 115 KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
27-197 |
1.11e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 71.06 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 27 IPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKirQMIGYLPQDFDFYPNMKVSEvlyYLGFLSKIn 106
Cdd:PRK13541 24 LPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK--PYCTYIGHNLGLKLEMTVFE---NLKFWSEI- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 107 qTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAEN-KIV 185
Cdd:PRK13541 98 -YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSgGIV 176
|
170
....*....|..
gi 1436942050 186 IISTHIVSDIES 197
Cdd:PRK13541 177 LLSSHLESSIKS 188
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-216 |
1.13e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 74.37 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLD-LVIPNGMFGILGRNGSGKSTLMNIIA---TILQPSKGTVTINGIEIKNS-QKIrqmIGYLPQDFDFYPNMKVSE 94
Cdd:TIGR00956 779 LNNVDgWVKPGTLTALMGASGAGKTTLLNVLAervTTGVITGGDRLVNGRPLDSSfQRS---IGYVQQQDLHLPTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 95 VLYYLGFL---SKINQTDFDKYVDLILRKVNLIDYKNKKV----KSLSGGMKKRLGIAQAILHDPKVII-VDEPTAGLDP 166
Cdd:TIGR00956 856 SLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS 935
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 167 EERVRIRNLLSDLAENKIVIIST-HIVS-DIESTCNRIAILDKGS-LVYKGDI 216
Cdd:TIGR00956 936 QTAWSICKLMRKLADHGQAILCTiHQPSaILFEEFDRLLLLQKGGqTVYFGDL 988
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
34-224 |
1.37e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.99 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 34 ILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGYLPQDFDFYPNMKVSEVLYYLGFLSKINQTDFD 111
Cdd:TIGR00958 512 LVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqyDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAA 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 112 KYV---DLILRKVNLIDYK-NKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDpeerVRIRNLLSDL--AENKIV 185
Cdd:TIGR00958 592 KAAnahDFIMEFPNGYDTEvGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESrsRASRTV 667
|
170 180 190
....*....|....*....|....*....|....*....
gi 1436942050 186 IISTHIVSDIEStCNRIAILDKGSLVYKGDIPSLIQQSD 224
Cdd:TIGR00958 668 LLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-179 |
3.23e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYdGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTvtingieIKNSQKIRqmIGY 79
Cdd:PRK09544 2 TSLVSLENVSVSF-GQRRVLSDVSLELKPGkILTLLGPNGAGKSTLVRVVLGLVAPDEGV-------IKRNGKLR--IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQDFDFYPNMKVSeVLYYLGFLSKINQTDfdkyVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDE 159
Cdd:PRK09544 72 VPQKLYLDTTLPLT-VNRFLRLRPGTKKED----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180
....*....|....*....|
gi 1436942050 160 PTAGLDPEERVRIRNLLSDL 179
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQL 166
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-188 |
3.37e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.84 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVI-PNGMFGILGRNGSGKSTLMNIIATiLQPSKGTVTING-IEI---------KNSQK 72
Cdd:PRK14258 8 IKVNNLSFYYDTQK-ILEGVSMEIyQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGrVEFfnqniyerrVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 73 IRQMIGYLPQDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLID-YKNKKVKS---LSGGMKKRLGIAQAI 148
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDeIKHKIHKSaldLSGGQQQRLCIARAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1436942050 149 LHDPKVIIVDEPTAGLDPEERVRIRNLLSDL---AENKIVIIS 188
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrSELTMVIVS 208
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-208 |
3.62e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.55 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKdALNSLDL-VIPNGMFGILGRNGSGKSTLMNIIATILQPS--KGTVTINGIEIKnSQKIRQM----IG 78
Cdd:TIGR02633 4 MKGIVKTFGGVK-ALDGIDLeVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLK-ASNIRDTeragIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDFDFYPNMKVSEVLYyLG--FLSKINQTDFDKYV---DLILRKVNL-IDYKNKKVKSLSGGMKKRLGIAQAILHDP 152
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIF-LGneITLPGGRMAYNAMYlraKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 153 KVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIIS-THIVSDIESTCNRIAILDKG 208
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYiSHKLNEVKAVCDTICVIRDG 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-222 |
5.21e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 72.16 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN-SQK-IRQMIGY 79
Cdd:COG5265 357 EVRFENVSFGYDPERPILKGVSFEVPAGkTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQAsLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQD---FD---FY------PNMKVSEVLYylgfLSKINQTDfdkyvDLILRkvnLIDYKNKKV-----KsLSGGMKKRL 142
Cdd:COG5265 437 VPQDtvlFNdtiAYniaygrPDASEEEVEA----AARAAQIH-----DFIES---LPDGYDTRVgerglK-LSGGEKQRV 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 143 GIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIEStCNRIAILDKGSLVYKGDIPSLIQQ 222
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAELLAQ 582
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-263 |
5.22e-14 |
|
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: 72.14 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATI--LQPSKGTVTIN----------GIEIKNS 70
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGeVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyvERPSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 71 QKIRQMIGYL-PQDFDFYpnmKVSEVLYYlGFLSKIN---QTDF-----DKYVDLILRKVNLIDYKNKK----------- 130
Cdd:TIGR03269 80 EPCPVCGGTLePEEVDFW---NLSDKLRR-RIRKRIAimlQRTFalygdDTVLDNVLEALEEIGYEGKEavgravdliem 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 131 ----------VKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK--IVIISTHIVSDIEST 198
Cdd:TIGR03269 156 vqlshrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 199 CNRIAILDKGSLVYKGDipsliqqSDDHIYEINLSPSELESFRENDLF--ITKTQEienkLKVRFIS 263
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGT-------PDEVVAVFMEGVSEVEKECEVEVGepIIKVRN----VSKRYIS 291
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-214 |
5.53e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 69.19 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 26 VIPNGMFGILGRNGSGKSTLMNIIA--TILQPSKGTVTINGIEIKNSqkIRQMIGYLPQDFDFYPNMKVSEVLYYLGFLS 103
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLDKN--FQRSTGYVEQQDVHSPNLTVREALRFSALLR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 104 KINQTDfdkyvdlilrkvnlidyknkkvkslsggmKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK 183
Cdd:cd03232 108 GLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSG 158
|
170 180 190
....*....|....*....|....*....|....
gi 1436942050 184 IVIIST-HIVS-DIESTCNRIAILDK-GSLVYKG 214
Cdd:cd03232 159 QAILCTiHQPSaSIFEKFDRLLLLKRgGKTVYFG 192
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-208 |
6.24e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 7 KGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILqPS---KGTVTINGIEIKnSQKIRQM----IG 78
Cdd:PRK13549 9 KNITKTFGGVK-ALDNVSLKVRAGeIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQ-ASNIRDTeragIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYV---DLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVI 155
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYlraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 156 IVDEPTAGLDPEERVRIRNLLSDLAENKI--VIIStHIVSDIESTCNRIAILDKG 208
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLKAHGIacIYIS-HKLNEVKAISDTICVIRDG 219
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-211 |
1.13e-13 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 70.52 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSY-DGKKDALNSLD----------------------LVIPNG-MFGILGRNGSGKSTLMNIIATILQPS 56
Cdd:COG4175 1 MPKIEVRNLYKIFgKRPERALKLLDqgkskdeilektgqtvgvndasFDVEEGeIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 57 KGTVTINGIEI--KNSQKIRQM----IGYLPQDFDFYPNMKVSE-VLYYLGfLSKINQTDFDKYVDLILRKVNLIDYKNK 129
Cdd:COG4175 81 AGEVLIDGEDItkLSKKELRELrrkkMSMVFQHFALLPHRTVLEnVAFGLE-IQGVPKAERRERAREALELVGLAGWEDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 130 KVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAE--NK-IVIIsTHivsDIESTC---NRIA 203
Cdd:COG4175 160 YPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAklKKtIVFI-TH---DLDEALrlgDRIA 235
|
....*...
gi 1436942050 204 ILDKGSLV 211
Cdd:COG4175 236 IMKDGRIV 243
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-179 |
1.86e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.30 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 9 LSKSY-DGK--KDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTV-----TINGIEIKNSQKIR-QMIG 78
Cdd:PRK11629 11 LCKRYqEGSvqTDVLHNVSFSIGEGeMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqPMSKLSSAAKAELRnQKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDFDFYPNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVD 158
Cdd:PRK11629 91 FIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180
....*....|....*....|.
gi 1436942050 159 EPTAGLDPEERVRIRNLLSDL 179
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGEL 191
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
31-210 |
2.52e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.81 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 31 MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK---IRQMIGYLPQ---------DFDFYPNMKVSEVLY- 97
Cdd:PRK09700 291 ILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldaVKKGMAYITEsrrdngffpNFSIAQNMAISRSLKd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 98 --YLGFLSKINQTDFDKYVDLILRKVNL-IDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRN 174
Cdd:PRK09700 371 ggYKGAMGLFHEVDEQRTAENQRELLALkCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYK 450
|
170 180 190
....*....|....*....|....*....|....*..
gi 1436942050 175 LLSDLAEN-KIVIISTHIVSDIESTCNRIAILDKGSL 210
Cdd:PRK09700 451 VMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-224 |
2.55e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.64 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSyDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQK-----IR 74
Cdd:PRK11831 5 ANLVDMRGVSFT-RGNRCIFDNISLTVPRGkITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRsrlytVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 75 QMIGYLPQDFDFYPNMKVSE-VLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPK 153
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDnVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 154 VIIVDEPTAGLDPEERVRIRNLLSDL--AENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSD 224
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-192 |
3.07e-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: 70.32 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSY-DGKKDALNSLDLVIPNGM-FGILGRNGSGKSTLMNIIATILQpSKGTVTINGIEIkNS---QKIRQMI 77
Cdd:TIGR01271 1217 QMDVQGLTAKYtEAGRAVLQDLSFSVEGGQrVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSW-NSvtlQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQD-FDF-------------YPNMKVSEVLYYLGFLSKINQtdFDKYVDLILRKVNLIdyknkkvksLSGGMKKRLG 143
Cdd:TIGR01271 1295 GVIPQKvFIFsgtfrknldpyeqWSDEEIWKVAEEVGLKSVIEQ--FPDKLDFVLVDGGYV---------LSNGHKQLMC 1363
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1436942050 144 IAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIV 192
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-215 |
3.11e-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: 69.71 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 7 KGLSKSYDGKKDALNSLDLVIPNG-MFGILGRNGSGKSTL-MNIIAtiLQPSKGTVTINGIEI--KNSQKIR------QM 76
Cdd:COG4172 289 RGLFRRTVGHVKAVDGVSLTLRRGeTLGLVGESGSGKSTLgLALLR--LIPSEGEIRFDGQDLdgLSRRALRplrrrmQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 77 IgylpqdF-DFY----PNMKVSEV----LYYLGflSKINQTDFDKYVDLILRKVNL-IDYKNKKVKSLSGGMKKRLGIAQ 146
Cdd:COG4172 367 V------FqDPFgslsPRMTVGQIiaegLRVHG--PGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 147 AILHDPKVIIVDEPTAGLDPEERVRIRNLLSDL-AENKI--VIIStHIVSDIESTCNRIAILDKGSLVYKGD 215
Cdd:COG4172 439 ALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLayLFIS-HDLAVVRALAHRVMVMKDGKVVEQGP 509
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-214 |
3.61e-13 |
|
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: 66.90 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYDGKKDALNSLDLVI-PNGMFGILGRNGSGKSTLMNIIATILQPS---KGTVTINGIEIK-NSQKIRQ 75
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVkPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKeFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 76 MIGYLPQDFDFYPNMKVSEVLYylgFLSKINQTDFdkyvdlilrkvnlidyknkkVKSLSGGMKKRLGIAQAILHDPKVI 155
Cdd:cd03233 84 EIIYVSEEDVHFPTLTVRETLD---FALRCKGNEF--------------------VRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 156 IVDEPTAGLDPEERVRIRNLLSDLA--ENKIVIISTHIVSD-IESTCNRIAILDKGSLVYKG 214
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMAdvLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-219 |
4.62e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.81 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 17 KDALNSLDLVIP-NGMFGILGRNGSGKSTLMNIIATILQPSKG-----TVTINGIEIKNSQKI---RQMIGYLPQDFDFY 87
Cdd:PRK14271 34 KTVLDQVSMGFPaRAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVlefRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 88 PNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKS----LSGGMKKRLGIAQAILHDPKVIIVDEPTAG 163
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 164 LDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSL 219
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-215 |
4.73e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYDgkkDA--LNSLDLVI-PNGMFGILGRNGSGKSTLMNIIA------------------TILQ--PSK 57
Cdd:PRK11147 1 MSLISIHGAWLSFS---DAplLDNAELHIeDNERVCLVGRNGAGKSTLMKILNgevllddgriiyeqdlivARLQqdPPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 58 ---GTV---TINGIE-----IKNSQKIRQMIGYLPQDFDFYPNMKVSEVLYYLG---FLSKINQTdfdkyvdliLRKVNL 123
Cdd:PRK11147 78 nveGTVydfVAEGIEeqaeyLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNlwqLENRINEV---------LAQLGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 124 idYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLaENKIVIIStHIVSDIESTCNRIA 203
Cdd:PRK11147 149 --DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF-QGSIIFIS-HDRSFIRNMATRIV 224
|
250
....*....|...
gi 1436942050 204 ILDKGSLV-YKGD 215
Cdd:PRK11147 225 DLDRGKLVsYPGN 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
33-179 |
5.72e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.19 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 33 GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQK----IRQMIGYLPQD--FDFYPNMKVSEVL------YYl 99
Cdd:PRK15079 51 GVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlGMKDDewraVRSDIQMIFQDplASLNPRMTIGEIIaeplrtYH- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 100 gflSKINQTDFDKYVDLILRKV----NLIdykNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNL 175
Cdd:PRK15079 130 ---PKLSRQEVKDRVKAMMLKVgllpNLI---NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNL 203
|
....
gi 1436942050 176 LSDL 179
Cdd:PRK15079 204 LQQL 207
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-236 |
6.01e-13 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 67.57 E-value: 6.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSY-DGKKDALNSLDLVIPNGM-FGILGRNGSGKSTLMNIIATILQpSKGTVTINGIEIKNS--QKIRQMIG 78
Cdd:cd03289 2 QMTVKDLTAKYtEGGNAVLENISFSISPGQrVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVplQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQ-----------DFDFYPNMKVSEVLYY---LGFLSKINQtdFDKYVDLILRKVNLIdyknkkvksLSGGMKKRLGI 144
Cdd:cd03289 81 VIPQkvfifsgtfrkNLDPYGKWSDEEIWKVaeeVGLKSVIEQ--FPGQLDFVLVDGGCV---------LSHGHKQLMCL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 145 AQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIEStCNRIAILDKGSLVYKGDIPSLIqqSD 224
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLL--NE 226
|
250
....*....|..
gi 1436942050 225 DHIYEINLSPSE 236
Cdd:cd03289 227 KSHFKQAISPSD 238
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
12-183 |
8.05e-13 |
|
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: 66.66 E-value: 8.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 12 SYDGKKDALNSLDLVIPNGMF------GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIknsqkirqmiGYLPQDFD 85
Cdd:cd03237 2 TYPTMKKTLGEFTLEVEGGSIseseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV----------SYKPQYIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 86 FYPNMKVSEVLYylgflSKINQTDFDKYVDL-ILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGL 164
Cdd:cd03237 72 ADYEGTVRDLLS-----SITKDFYTHPYFKTeIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170
....*....|....*....
gi 1436942050 165 DPEERVRIRNLLSDLAENK 183
Cdd:cd03237 147 DVEQRLMASKVIRRFAENN 165
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-211 |
1.35e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 14 DGKKDALNSLDLVIPNGMFG-ILGRNGSGKSTLMNIIATIL--QPSKGTVTIngieiknsqkirqmigylpQDFDFYPNM 90
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVlIVGASGSGKSTLLRLLAGALkgTPVAGCVDV-------------------PDNQFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 91 KVSEVLYYLGflskinqtDFDKYVDlILRKVNLID---YKnKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPE 167
Cdd:COG2401 101 SLIDAIGRKG--------DFKDAVE-LLNAVGLSDavlWL-RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1436942050 168 ERVRIRNLLSDLA-ENKI--VIISTH--IVSDIEStcNRIAILDKGSLV 211
Cdd:COG2401 171 TAKRVARNLQKLArRAGItlVVATHHydVIDDLQP--DLLIFVGYGGVP 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
34-214 |
1.36e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 34 ILGRNGSGKSTLMNIIATILqPSKGTVTING--IEIKNSQKIRQMIGYLPQDFDFYPNMKVSEVL-YYLGflSKINQTDF 110
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLL-PGSGSIQFAGqpLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLtLHQP--DKTRTEAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 111 DKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILH-------DPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK 183
Cdd:PRK03695 104 ASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQG 183
|
170 180 190
....*....|....*....|....*....|....*
gi 1436942050 184 I-VIISTHivsDIEST---CNRIAILDKGSLVYKG 214
Cdd:PRK03695 184 IaVVMSSH---DLNHTlrhADRVWLLKQGKLLASG 215
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-167 |
1.68e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIV--IKGLSKSYDGKKDALNSLDL-VIPNGMFGILGRNGSGKSTLMNIIATILQPSKGtvtingiEIKNSQKIRqmI 77
Cdd:PRK11819 2 MAQYIytMNRVSKVVPPKKQILKDISLsFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------EARPAPGIK--V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 GYLPQDFDFYPN--------MKVSEVLYYLGFLSKINQ------TDFDKYVDLILRKVNLIDYKN--------------- 128
Cdd:PRK11819 73 GYLPQEPQLDPEktvrenveEGVAEVKAALDRFNEIYAayaepdADFDALAAEQGELQEIIDAADawdldsqleiamdal 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1436942050 129 ------KKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPE 167
Cdd:PRK11819 153 rcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-190 |
2.62e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 23 LDLVI-PNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGieiknsQKIRQmigylpQDFDFYPNmkvsevLYYLG- 100
Cdd:PRK13538 20 LSFTLnAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG------EPIRR------QRDEYHQD------LLYLGh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 101 ---------------FLSKINQ-TDFDKYVDlILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGL 164
Cdd:PRK13538 82 qpgikteltalenlrFYQRLHGpGDDEALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*..
gi 1436942050 165 DPEERVRIRNLLSDLAENK-IVIISTH 190
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGgMVILTTH 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-210 |
2.70e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 22 SLDlVIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN---SQKIRQMIGYLPQD-------FDFYPNMK 91
Cdd:PRK15439 283 SLE-VRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlstAQRLARGLVYLPEDrqssglyLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 92 VSEVLYY-LGFLSKINQTD--FDKYVDLILRKVNLIDyknKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEE 168
Cdd:PRK15439 362 VCALTHNrRGFWIKPARENavLERYRRALNIKFNHAE---QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1436942050 169 RVRIRNLLSDLAENKIVIIstHIVSD---IESTCNRIAILDKGSL 210
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVL--FISSDleeIEQMADRVLVMHQGEI 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
5-216 |
2.82e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.06 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 5 VIKGLSKSYDGKK-DALNSLDLVI-PNGMFGILGRNGSGKSTLMNIIATILQPSK----GTVTINGI---EIKNsqKIRQ 75
Cdd:TIGR00956 61 GFRKLKKFRDTKTfDILKPMDGLIkPGELTVVLGRPGSGCSTLLKTIASNTDGFHigveGVITYDGItpeEIKK--HYRG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 76 MIGYLPQDFDFYPNMKVSEVLYYLGFL----SKINQTDFDKYV----DLILRKVNLIDYKNKKV-----KSLSGGMKKRL 142
Cdd:TIGR00956 139 DVVYNAETDVHFPHLTVGETLDFAARCktpqNRPDGVSREEYAkhiaDVYMATYGLSHTRNTKVgndfvRGVSGGERKRV 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1436942050 143 GIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHIVS-DIESTCNRIAILDKGSLVYKGDI 216
Cdd:TIGR00956 219 SIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANilDTTPLVAIYQCSqDAYELFDKVIVLYEGYQIYFGPA 295
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
33-217 |
3.36e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.49 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 33 GILGRNGSGKSTLMNIIATILQ-PSKGTVTING--IEIKNSQK-IRQMIGYLPQD---FDFYPNMKVSE--VLYYLGFLS 103
Cdd:PRK13549 292 GIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRNPQQaIAQGIAMVPEDrkrDGIVPVMGVGKniTLAALDRFT 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 104 KINQTDFDKYVDLILRKVNLIDYKNK----KVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDL 179
Cdd:PRK13549 372 GGSRIDDAAELKTILESIQRLKVKTAspelAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQL 451
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1436942050 180 AENKIVIIsthIVS----DIESTCNRIAILDKGSLvyKGDIP 217
Cdd:PRK13549 452 VQQGVAII---VISselpEVLGLSDRVLVMHEGKL--KGDLI 488
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-210 |
8.19e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.64 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLDLVI-PNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN-----SQKIR-QMIGYLPQDFDFYPNMKV 92
Cdd:PRK10584 26 LTGVELVVkRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeaRAKLRaKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 93 SEVLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRI 172
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1436942050 173 RNLLSDLAEN--KIVIISTHiVSDIESTCNRIAILDKGSL 210
Cdd:PRK10584 186 ADLLFSLNREhgTTLILVTH-DLQLAARCDRRLRLVNGQL 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-195 |
1.04e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIKGLSKSYDGKKDA--LNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTIN---GIEIKNSQKIR 74
Cdd:PTZ00265 380 IKKIQFKNVRFHYDTRKDVeiYKDLNFTLTEGkTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshNLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 75 QMIGYLPQDFDFYPNMKVSEVLYYLGFLSKI-------NQTDFDKYVDLILRKV-------------------NLIDYK- 127
Cdd:PTZ00265 460 SKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLealsnyyNEDGNDSQENKNKRNScrakcagdlndmsnttdsnELIEMRk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 128 -------------NKKV---------------------KSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIR 173
Cdd:PTZ00265 540 nyqtikdsevvdvSKKVlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260
....*....|....*....|....
gi 1436942050 174 NLLSDLA--ENKIVIISTHIVSDI 195
Cdd:PTZ00265 620 KTINNLKgnENRITIIIAHRLSTI 643
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-214 |
1.08e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.26 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 22 SLDLvIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN-----SQKIRQMIGYLPQD--FDFYPNMKVS- 93
Cdd:PRK10261 344 SFDL-WPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgkLQALRRDIQFIFQDpyASLDPRQTVGd 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 94 ---EVLYYLGFLskiNQTDFDKYVDLILRKVNLI-DYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEER 169
Cdd:PRK10261 423 simEPLRVHGLL---PGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1436942050 170 VRIRNLLSDLAEN---KIVIIStHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:PRK10261 500 GQIINLLLDLQRDfgiAYLFIS-HDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-215 |
1.47e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 63.83 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIVIK--GLSKSYDGKK---------DALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK 68
Cdd:PRK11308 1 SQQPLLQaiDLKKHYPVKRglfkperlvKALDGVSFTLERGkTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 69 NSQK-----IRQMIGYLPQD--FDFYPNMKVSEVLyylGFLSKINqTDFDKY-----VDLILRKVNL-IDYKNKKVKSLS 135
Cdd:PRK11308 81 KADPeaqklLRQKIQIVFQNpyGSLNPRKKVGQIL---EEPLLIN-TSLSAAerrekALAMMAKVGLrPEHYDRYPHMFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 136 GGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAEN---KIVIIStHIVSDIESTCNRIAILDKGSLVY 212
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElglSYVFIS-HDLSVVEHIADEVMVMYLGRCVE 235
|
...
gi 1436942050 213 KGD 215
Cdd:PRK11308 236 KGT 238
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-188 |
1.81e-11 |
|
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: 61.40 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLDLVIPNGM-FGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEiknsqkirQMIgYLPQDfdfyPnmkvsevlyY 98
Cdd:cd03223 17 LKDLSFEIKPGDrLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE--------DLL-FLPQR----P---------Y 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 99 LGFLSkinqtdfdkyvdliLRKVnlIDYKNKKVksLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSD 178
Cdd:cd03223 75 LPLGT--------------LREQ--LIYPWDDV--LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE 136
|
170
....*....|
gi 1436942050 179 LaenKIVIIS 188
Cdd:cd03223 137 L---GITVIS 143
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
28-165 |
1.88e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.87 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 28 PNGMFGILGRNGSGKSTLMNIIATILQPS--KGTVTINGIEiKNSQKIRQMIGYLPQDFDFYPNMKVSEVLYYLGFL--- 102
Cdd:PLN03140 905 PGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP-KKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLrlp 983
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1436942050 103 SKINQTDFDKYVDLILRKVNLIDYKNK-----KVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLD 165
Cdd:PLN03140 984 KEVSKEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-239 |
1.95e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.35 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSYDGKKDALNSLDLVIPN-GMFGILGRNGSGKSTLMNIIATILQPSKGTVTING--IEIKNSQKIRQMIGY 79
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSrGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrpLSSLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 80 LPQD-----FDFYPNM----KVSEvlyylgflSKINQtdfdkyvdlILRKVNLIDYknkkVKSLSGGMKKRLG------- 143
Cdd:PRK10790 420 VQQDpvvlaDTFLANVtlgrDISE--------EQVWQ---------ALETVQLAEL----ARSLPDGLYTPLGeqgnnls 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 144 --------IAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTcNRIAILDKGSLVYKGD 215
Cdd:PRK10790 479 vgqkqllaLARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEA-DTILVLHRGQAVEQGT 557
|
250 260
....*....|....*....|....*.
gi 1436942050 216 IPSLIQQSDDH--IYEINLSPSELES 239
Cdd:PRK10790 558 HQQLLAAQGRYwqMYQLQLAGEELAA 583
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-215 |
2.13e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 7 KGLSKSYDGKKDALNSLDLVI-PNGMFGILGRNGSGKST----LMNIIAtilqpSKGTVTINGIEIKNSQKiRQMIGYLP 81
Cdd:PRK15134 289 KGILKRTVDHNVVVKNISFTLrPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNR-RQLLPVRH 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 ------QDfdfyPNMKVSEVLYYLGFLSK--------INQTDFDKYVDLILRKVNL-IDYKNKKVKSLSGGMKKRLGIAQ 146
Cdd:PRK15134 363 riqvvfQD----PNSSLNPRLNVLQIIEEglrvhqptLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 147 AILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK---IVIIStHIVSDIESTCNRIAILDKGSLVYKGD 215
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlaYLFIS-HDLHVVRALCHQVIVLRQGEVVEQGD 509
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-190 |
3.60e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 62.00 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 19 ALNSLDLVIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTIN-----------GIEIKN------SQKIRQMIGylP 81
Cdd:cd03236 16 KLHRLPVPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPpdwdeildefrGSELQNyftkllEGDVKVIVK--P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNM---KVSEVLyylgflSKINQTD-FDKYVD-LILRKVnlidyKNKKVKSLSGGMKKRLGIAQAILHDPKVII 156
Cdd:cd03236 94 QYVDLIPKAvkgKVGELL------KKKDERGkLDELVDqLELRHV-----LDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1436942050 157 VDEPTAGLDPEERVRIRNLLSDLAE-NKIVIISTH 190
Cdd:cd03236 163 FDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEH 197
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-190 |
3.87e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 63.28 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 2 NKIVIKGLSKSYDGKKD----ALNSLDLVIPNG--MFgILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--KNSQKI 73
Cdd:COG4615 326 QTLELRGVTYRYPGEDGdegfTLGPIDLTIRRGelVF-IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtaDNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 74 RQMigylpqdF-----DFYpnmkVSEVLYylGFLSKINQTDFDKYvdliLRKVNLidykNKKVK---------SLSGGMK 139
Cdd:COG4615 405 RQL-------FsavfsDFH----LFDRLL--GLDGEADPARAREL----LERLEL----DHKVSvedgrfsttDLSQGQR 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1436942050 140 KRLGIAQAILHDPKVIIVDEPTAGLDPEERvRI--RNLLSDL-AENKIVIISTH 190
Cdd:COG4615 464 KRLALLVALLEDRPILVFDEWAADQDPEFR-RVfyTELLPELkARGKTVIAISH 516
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-190 |
6.44e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.68 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSYDGKKDALNSLDLVIPNG--MFGIlGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--KNSQKIRQMIG 78
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGelLFLI-GGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtaEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQDFDFY-----PNMKVSEVLYYLGFLSKINQTDfdkyvdlilrKVNLIDYKNKKVKsLSGGMKKRLGIAQAILHDPK 153
Cdd:PRK10522 401 AVFTDFHLFdqllgPEGKPANPALVEKWLERLKMAH----------KLELEDGRISNLK-LSKGQKKRLALLLALAEERD 469
|
170 180 190
....*....|....*....|....*....|....*....
gi 1436942050 154 VIIVDEPTAGLDPE-ERVRIRNLLSDLAE-NKIVIISTH 190
Cdd:PRK10522 470 ILLLDEWAADQDPHfRREFYQVLLPLLQEmGKTIFAISH 508
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
31-216 |
7.54e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.53 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 31 MFGILGRNGSGKSTLMNIIATILqPSK--GTVTING--IEIKNSQK-IRQMIGYLPQD---FDFYPNMKVSE--VLYYLG 100
Cdd:TIGR02633 288 ILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGkpVDIRNPAQaIRAGIAMVPEDrkrHGIVPILGVGKniTLSVLK 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 101 FLSKINQTDFDKYVDLILRKVNLIDYKNKK----VKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLL 176
Cdd:TIGR02633 367 SFCFKMRIDAAAELQIIGSAIQRLKVKTASpflpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLI 446
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1436942050 177 SDLAEN--KIVIISTHIvSDIESTCNRIAILDKGSLvyKGDI 216
Cdd:TIGR02633 447 NQLAQEgvAIIVVSSEL-AEVLGLSDRVLVIGEGKL--KGDF 485
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-190 |
7.95e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.88 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLDLVIPNGMFG-ILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIK--NSQKIRQMIGYLPQDfdfyPNMKVSEVL 96
Cdd:PRK10247 23 LNNISFSLRAGEFKlITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEIYRQQVSYCAQT----PTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 97 YYLGFLSKI--NQTDFDKYVDLILRkVNLIDYK-NKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIR 173
Cdd:PRK10247 99 DNLIFPWQIrnQQPDPAIFLDDLER-FALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVN 177
|
170
....*....|....*....
gi 1436942050 174 NLLSDLAENK--IVIISTH 190
Cdd:PRK10247 178 EIIHRYVREQniAVLWVTH 196
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-211 |
9.41e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 26 VIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNS--QKIRQMIGYLPQDfdfyPNMKVSEVLYYLGFLS 103
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFglTDLRRVLSIIPQS----PVLFSGTVRFNIDPFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 104 KINQTDFDKYV------DLILRKVNLIDYK-NKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLL 176
Cdd:PLN03232 1335 EHNDADLWEALerahikDVIDRNPFGLDAEvSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTI 1414
|
170 180 190
....*....|....*....|....*....|....*
gi 1436942050 177 SDLAENKIVIISTHIVSDIeSTCNRIAILDKGSLV 211
Cdd:PLN03232 1415 REEFKSCTMLVIAHRLNTI-IDCDKILVLSSGQVL 1448
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
33-214 |
1.78e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.91 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 33 GILGRNGSGKS-TLMNIIATILQPskGTVTINGIEIKNS--QKI-----RQMIG----YLPQDfdfypNMKVSEVLYYLG 100
Cdd:PRK11022 37 GIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFNGQdlQRIsekerRNLVGaevaMIFQD-----PMTSLNPCYTVG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 101 F----LSKINQ-----TDFDKYVDLiLRKVNLIDYKNK---KVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEE 168
Cdd:PRK11022 110 FqimeAIKVHQggnkkTRRQRAIDL-LNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTI 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1436942050 169 RVRIRNLLSDLA--ENKIVIISTHIVSDIESTCNRIAILDKGSLVYKG 214
Cdd:PRK11022 189 QAQIIELLLELQqkENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-222 |
4.00e-10 |
|
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: 60.73 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNS--QKIRQMIGYLPQDfdfypnmkvsEVL 96
Cdd:TIGR00957 1302 LRHINVTIHGGeKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIglHDLRFKITIIPQD----------PVL 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 97 YYlGFLsKINQTDFDKYVD----LILRKVNLIDYKNKKV-----------KSLSGGMKKRLGIAQAILHDPKVIIVDEPT 161
Cdd:TIGR00957 1372 FS-GSL-RMNLDPFSQYSDeevwWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 162 AGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIESTcNRIAILDKGSLVYKGDIPSLIQQ 222
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-216 |
4.54e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.18 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 15 GKKDALNSLDL-VIPNGMFGILGRNGSGKSTLMNIIATILQPSKGtvtingiEIKNSQKIRqmIGYLPQdfdfypnmkvs 93
Cdd:PRK10636 323 GDRIILDSIKLnLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG-------EIGLAKGIK--LGYFAQ----------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 94 evlYYLGFLsKINQTDFDKYVDLILRKV--NLIDY------KNKKV----KSLSGGMKKRLGIAQAILHDPKVIIVDEPT 161
Cdd:PRK10636 383 ---HQLEFL-RADESPLQHLARLAPQELeqKLRDYlggfgfQGDKVteetRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 162 AGLDPEERVRIRNLLSDLaENKIVIIStHIVSDIESTCNRIAILDKGSL-VYKGDI 216
Cdd:PRK10636 459 NHLDLDMRQALTEALIDF-EGALVVVS-HDRHLLRSTTDDLYLVHDGKVePFDGDL 512
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-186 |
5.04e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.82 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLDLVIPNGMfGIL--GRNGSGKSTLMNIIATILQPSKGTVTINgieiknsQKIRQMigYLPQDfdfyPNMKVS---E 94
Cdd:COG4178 379 LEDLSLSLKPGE-RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARP-------AGARVL--FLPQR----PYLPLGtlrE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 95 VLYYLGFLSKINqtdfDKYVDLILRKVNLIDYKNK--------KVksLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDP 166
Cdd:COG4178 445 ALLYPATAEAFS----DAELREALEAVGLGHLAERldeeadwdQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180
....*....|....*....|
gi 1436942050 167 EERVRIRNLLSDLAENKIVI 186
Cdd:COG4178 519 ENEAALYQLLREELPGTTVI 538
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-209 |
7.10e-10 |
|
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: 57.83 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MN-KIVIKGLSKSY-----DGKK-DALNSLDLVIPNGMF-GILGRNGSGKSTLMNII-ATILqPSKGTVTIN----GIEI 67
Cdd:COG4778 1 MTtLLEVENLSKTFtlhlqGGKRlPVLDGVSFSVAAGECvALTGPSGAGKSTLLKCIyGNYL-PDSGSILVRhdggWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 68 KNSQKI------RQMIGYLPQDFDFYPNMK----VSEVLYYLGFLSKINQtdfDKYVDLiLRKVNLidykNKKVKSL--- 134
Cdd:COG4778 80 AQASPReilalrRRTIGYVSQFLRVIPRVSaldvVAEPLLERGVDREEAR---ARAREL-LARLNL----PERLWDLppa 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1436942050 135 --SGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIIS-THIVSDIESTCNRIAILDKGS 209
Cdd:COG4778 152 tfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGiFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-191 |
8.70e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 8.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGKKdALNSLDLVIP-NGMFGILGRNGSGKSTLMNIIATILQPSKGTVTInGIEIKnsqkirqmIGYLPQ 82
Cdd:PRK11819 325 IEAENLSKSFGDRL-LIDDLSFSLPpGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK--------LAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 83 DFD-FYPNMKVSEVLyylgflskinqTDFDKYVDLILRKVNLIDY----------KNKKVKSLSGGMKKRLGIAQAILHD 151
Cdd:PRK11819 395 SRDaLDPNKTVWEEI-----------SGGLDIIKVGNREIPSRAYvgrfnfkggdQQKKVGVLSGGERNRLHLAKTLKQG 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 152 PKVIIVDEPTAGLDPEErvrIRNL---LSDLAENKIVI---------ISTHI 191
Cdd:PRK11819 464 GNVLLLDEPTNDLDVET---LRALeeaLLEFPGCAVVIshdrwfldrIATHI 512
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-211 |
9.16e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 9.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKKdALNSLDL-VIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI--KNSQK-IRQMIGYLP 81
Cdd:PRK10982 1 MSNISKSFPGVK-ALDNVNLkVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEaLENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFYPNMKVSEVLYYLGFLSKINQTDFDK-YVDL--ILRKVNL-IDYKnKKVKSLSGGMKKRLGIAQAILHDPKVIIV 157
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRYPTKGMFVDQDKmYRDTkaIFDELDIdIDPR-AKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 158 DEPTAGLDPEERVRIRNLLSDLAEN--KIVIIStHIVSDIESTCNRIAILDKGSLV 211
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERgcGIVYIS-HKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-223 |
9.48e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 59.34 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 17 KDALNSLDLVI-PNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIknsqkirqmigylpqdfdfyPNMKVSEv 95
Cdd:PRK10789 328 HPALENVNFTLkPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL--------------------TKLQLDS- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 96 lyYLGFLSKINQTDFdKYVDLILRKVNL--IDYKNKKVKS----------------------------LSGGMKKRLGIA 145
Cdd:PRK10789 387 --WRSRLAVVSQTPF-LFSDTVANNIALgrPDATQQEIEHvarlasvhddilrlpqgydtevgergvmLSGGQKQRISIA 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1436942050 146 QAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTHIVSDIeSTCNRIAILDKGSLVYKGDIPSLIQQS 223
Cdd:PRK10789 464 RALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSAL-TEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
134-221 |
1.65e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.40 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 134 LSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKI--VIISTHIVSDIESTCNRIAILDKGSLV 211
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
90
....*....|
gi 1436942050 212 YKGDIPSLIQ 221
Cdd:PRK10418 221 EQGDVETLFN 230
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-243 |
3.54e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 56.36 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 19 ALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTING----IEIkNSQKIRQMIGYLPQDFDfypnmkvs 93
Cdd:PRK13546 39 ALDDISLKAYEGdVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGevsvIAI-SAGLSGQLTGIENIEFK-------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 94 evLYYLGFLSKinqtDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIR 173
Cdd:PRK13546 110 --MLCMGFKRK----EIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 174 NLLSDLAE-NKIVIISTHIVSDIESTCNRIAILDKGSLVYKGDIPSLIQQSDDHIYEI-NLSPSELESFREN 243
Cdd:PRK13546 184 DKIYEFKEqNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFkKKSKAEQKEFRNK 255
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-190 |
5.22e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.96 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLDLVIP-NGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEI-KNSQKIRQMIGYLPQDFDFYPNMKVSEVLY 97
Cdd:PRK13540 17 LQQISFHLPaGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 98 YlgflsKINQTDFDKYVDLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDpeERVrIRNLLS 177
Cdd:PRK13540 97 Y-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD--ELS-LLTIIT 168
|
170
....*....|....*..
gi 1436942050 178 DLAENK----IVIISTH 190
Cdd:PRK13540 169 KIQEHRakggAVLLTSH 185
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-195 |
1.13e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.15 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 28 PNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQMIGylpqdfdfypnmkvsevlyylgflskinq 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 108 tdfdkyvdlilrkvnliDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLA------- 180
Cdd:smart00382 52 -----------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkse 114
|
170
....*....|....*
gi 1436942050 181 ENKIVIISTHIVSDI 195
Cdd:smart00382 115 KNLTVILTTNDEKDL 129
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
134-215 |
1.29e-08 |
|
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: 55.46 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 134 LSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDL-AENK--IVIIsTH---IVSDIestCNRIAILDK 207
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGmaLLLI-THdlgVVRRF---ADRVAVMRQ 232
|
....*...
gi 1436942050 208 GSLVYKGD 215
Cdd:COG4172 233 GEIVEQGP 240
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-211 |
1.75e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 25 LVIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNS--QKIRQMIGYLPQdfdfypnmkvSEVLYYlGFL 102
Cdd:PLN03130 1261 EISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFglMDLRKVLGIIPQ----------APVLFS-GTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 103 sKINQTDFDKY--VDL--ILRKVNLIDYKNKKVKSL-----------SGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPE 167
Cdd:PLN03130 1330 -RFNLDPFNEHndADLweSLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVDVR 1408
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1436942050 168 ERVRIRNLLSDLAENKIVIISTHIVSDIeSTCNRIAILDKGSLV 211
Cdd:PLN03130 1409 TDALIQKTIREEFKSCTMLIIAHRLNTI-IDCDRILVLDAGRVV 1451
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
33-165 |
1.97e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 33 GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN---SQKIRQMIGYLPQD---------FDFYPNMKVSEVLYYLG 100
Cdd:PRK10762 282 GVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspQDGLANGIVYISEDrkrdglvlgMSVKENMSLTALRYFSR 361
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 101 FLSKINQTDFDKYVDLILRKVNL-IDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLD 165
Cdd:PRK10762 362 AGGSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-229 |
2.11e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 1 MNKIV--IKGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIA-----TILqpsKGTVTINGIEI--KNS 70
Cdd:CHL00131 3 KNKPIleIKNLHASVNENE-ILKGLNLSINKGeIHAIMGPNGSGKSTLSKVIAghpayKIL---EGDILFKGESIldLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 71 QKIRQMIGYLPqdFDfYP-------NMKVSEVLY-----YLGfLSKINQTDFDKYVDLILRKVNLID-YKNKKV-KSLSG 136
Cdd:CHL00131 79 EERAHLGIFLA--FQ-YPieipgvsNADFLRLAYnskrkFQG-LPELDPLEFLEIINEKLKLVGMDPsFLSRNVnEGFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 137 GMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLA--ENKIVIIsTH-------IVSDIestcnrIAILDK 207
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtsENSIILI-THyqrlldyIKPDY------VHVMQN 227
|
250 260
....*....|....*....|..
gi 1436942050 208 GSLVYKGDIpSLIQQSDDHIYE 229
Cdd:CHL00131 228 GKIIKTGDA-ELAKELEKKGYD 248
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-222 |
2.96e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLDLVI-PNGMFGILGRNGSGKSTLMNIIATILQPS--------KGTVTINGIEIK--NSQKIRQMIGYLPQD----F 84
Cdd:PRK13547 17 LRDLSLRIePGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAaiDAPRLARLRAVLPQAaqpaF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 85 DF----------YPNMKVSevlyylGFLSKINQtdfdkyvDLILRKVNLIDYK---NKKVKSLSGGMKKRLGIAQAI--L 149
Cdd:PRK13547 97 AFsareivllgrYPHARRA------GALTHRDG-------EIAWQALALAGATalvGRDVTTLSGGELARVQFARVLaqL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 150 H-------DPKVIIVDEPTAGLDPEERVRIRNLLSDLA-ENKIVIISthIVSDIE---STCNRIAILDKGSLVYKG---D 215
Cdd:PRK13547 164 WpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLGVLA--IVHDPNlaaRHADRIAMLADGAIVAHGapaD 241
|
....*....
gi 1436942050 216 I--PSLIQQ 222
Cdd:PRK13547 242 VltPAHIAR 250
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
32-214 |
7.97e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 32 FGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEiknsqkirqMIGYLPQDFDFYPNMKVSEV---------------- 95
Cdd:PRK15064 30 YGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNE---------RLGKLRQDQFAFEEFTVLDTvimghtelwevkqerd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 96 -LYYLGFLSkinQTDFDKYVDL------------------ILRKVNL-IDYKNKKVKSLSGGMKKRLGIAQAILHDPKVI 155
Cdd:PRK15064 101 rIYALPEMS---EEDGMKVADLevkfaemdgytaearageLLLGVGIpEEQHYGLMSEVAPGWKLRVLLAQALFSNPDIL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1436942050 156 IVDEPTAGLDPEErvrIRNLLSDLAENK--IVIIStHIVSDIESTCNRIAILDKGSL-VYKG 214
Cdd:PRK15064 178 LLDEPTNNLDINT---IRWLEDVLNERNstMIIIS-HDRHFLNSVCTHMADLDYGELrVYPG 235
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
128-223 |
1.40e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 128 NKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKI--VIISTHIvSDIESTCNRIAIL 205
Cdd:PRK10938 130 DRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGItlVLVLNRF-DEIPDFVQFAGVL 208
|
90
....*....|....*...
gi 1436942050 206 DKGSLVYKGDIPSLIQQS 223
Cdd:PRK10938 209 ADCTLAETGEREEILQQA 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
132-193 |
2.99e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 2.99e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 132 KSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDL---AENKIVIISTHIVS 193
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdkADKTIITIAHRIAS 1421
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
134-211 |
3.41e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.24 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 134 LSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAE--NKIVIISTHIVSDIESTCNRIAILDKGSLV 211
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
13-187 |
5.38e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 13 YDGKKDALNSLDLVIP-NGMFGILGRNGSGKSTLMNiiatilqpskgtvtingiEIKNSQKIRQMIGYLPQdfdFYPNMK 91
Cdd:cd03238 4 SGANVHNLQNLDVSIPlNVLVVVTGVSGSGKSTLVN------------------EGLYASGKARLISFLPK---FSRNKL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 92 VseVLYYLGFLSKINQTdfdkYVDLilrkvnlidykNKKVKSLSGGMKKRLGIAQAILHDPK--VIIVDEPTAGLDPEER 169
Cdd:cd03238 63 I--FIDQLQFLIDVGLG----YLTL-----------GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170
....*....|....*...
gi 1436942050 170 VRIRNLLSDLAENKIVII 187
Cdd:cd03238 126 NQLLEVIKGLIDLGNTVI 143
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
134-216 |
6.66e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 134 LSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKI--VIISTH---IVSDIestCNRIAILDKG 208
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHdmgVVAEI---ADRVLVMYQG 245
|
....*...
gi 1436942050 209 SLVYKGDI 216
Cdd:PRK10261 246 EAVETGSV 253
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-228 |
7.39e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.40 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 6 IKGLSKSYDGKkDALNSLDLVI-PNGMFGILGRNGSGKSTLMniiATILQPSKGTVTINGIEIKNsqkiRQMIGYLPQDF 84
Cdd:PRK09580 4 IKDLHVSVEDK-AILRGLNLEVrPGEVHAIMGPNGSGKSTLS---ATLAGREDYEVTGGTVEFKG----KDLLELSPEDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 85 --------------------DFYPNMKVSEVLYYLGfLSKINQTDFDKYV-----------DLILRKVNLidyknkkvkS 133
Cdd:PRK09580 76 agegifmafqypveipgvsnQFFLQTALNAVRSYRG-QEPLDRFDFQDLMeekiallkmpeDLLTRSVNV---------G 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 134 LSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLA-ENKIVIISTH---IVSDIEStcNRIAILDKGS 209
Cdd:PRK09580 146 FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHyqrILDYIKP--DYVHVLYQGR 223
|
250
....*....|....*....
gi 1436942050 210 LVYKGDIpSLIQQSDDHIY 228
Cdd:PRK09580 224 IVKSGDF-TLVKQLEEQGY 241
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-219 |
8.01e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.68 E-value: 8.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGtvtingiEIKNSQKIrqmiGYLPQDFDFYPNMKVSEVLYY 98
Cdd:TIGR01271 442 LKNISFKLEKGqLLAVAGSTGSGKSSLLMMIMGELEPSEG-------KIKHSGRI----SFSPQTSWIMPGTIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 99 LGF-----LSKINQTDFDKYVDLILRKVNLIDYKNKKvkSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLD-PEERVRI 172
Cdd:TIGR01271 511 LSYdeyryTSVIKACQLEEDIALFPEKDKTVLGEGGI--TLSGGQRARISLARAVYKDADLYLLDSPFTHLDvVTEKEIF 588
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1436942050 173 RNLLSDLAENKIVIISTHIVSDIESTcNRIAILDKGSLVYKGDIPSL 219
Cdd:TIGR01271 589 ESCLCKLMSNKTRILVTSKLEHLKKA-DKILLLHEGVCYFYGTFSEL 634
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-224 |
8.85e-07 |
|
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: 49.14 E-value: 8.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIVIKGLSKSYDGK-KDALNSLDLVI-PNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKN--SQKIRQMIG 78
Cdd:cd03288 19 EIKIHDLCVRYENNlKPVLKHVKAYIkPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlpLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 79 YLPQD---------FDFYPNMKVSEvlyylgflskinqtdfdkyvDLILRKVNLIDYKNkKVKSLSGGM----------- 138
Cdd:cd03288 99 IILQDpilfsgsirFNLDPECKCTD--------------------DRLWEALEIAQLKN-MVKSLPGGLdavvteggenf 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 139 ----KKRLGIAQAILHDPKVIIVDEPTAGLD-PEERVRIRNLLSDLAENKIVIIStHIVSDIeSTCNRIAILDKGSLVYK 213
Cdd:cd03288 158 svgqRQLFCLARAFVRKSSILIMDEATASIDmATENILQKVVMTAFADRTVVTIA-HRVSTI-LDADLVLVLSRGILVEC 235
|
250
....*....|.
gi 1436942050 214 GDIPSLIQQSD 224
Cdd:cd03288 236 DTPENLLAQED 246
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-217 |
9.24e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 30 GMFGILGrngSGKSTLMNIIATILQPSKGTVTING--IEIKN-SQKIRQMIGYLPQDFDF---------YPNMKVSEVLY 97
Cdd:PRK11288 283 GLFGLVG---AGRSELMKLLYGATRRTAGQVYLDGkpIDIRSpRDAIRAGIMLCPEDRKAegiipvhsvADNINISARRH 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 98 YLGFLSKINQTDFDKYVDLILRKVNlIDYKN--KKVKSLSGGMKKRlgiaqAIL-----HDPKVIIVDEPTAGLDPEERV 170
Cdd:PRK11288 360 HLRAGCLINNRWEAENADRFIRSLN-IKTPSreQLIMNLSGGNQQK-----AILgrwlsEDMKVILLDEPTRGIDVGAKH 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 171 RIRNLLSDLAENKIVIIsthIVS----DIESTCNRIAILDKGSLVykGDIP 217
Cdd:PRK11288 434 EIYNVIYELAAQGVAVL---FVSsdlpEVLGVADRIVVMREGRIA--GELA 479
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-173 |
9.56e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 2 NKIVIKGLSKSYDGKKdALNSLDL-VIPNGMFGILGRNGSGKSTLMNIIA-----------TILQPSKGT-VTIngieik 68
Cdd:PRK10938 259 PRIVLNNGVVSYNDRP-ILHNLSWqVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndlTLFGRRRGSgETI------ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 69 nsQKIRQMIGYLPQDF--DFYPNMKVSEVLYYlGFLSKIN--QTDFDKYVDLILRKVNLIDYKNKKVK----SLSGGMKK 140
Cdd:PRK10938 332 --WDIKKHIGYVSSSLhlDYRVSTSVRNVILS-GFFDSIGiyQAVSDRQQKLAQQWLDILGIDKRTADapfhSLSWGQQR 408
|
170 180 190
....*....|....*....|....*....|...
gi 1436942050 141 RLGIAQAILHDPKVIIVDEPTAGLDPEERVRIR 173
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQLVR 441
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-178 |
1.45e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 49.36 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLDLVIPNGM-FGILGRNGSGKSTLMNIIATILQPSKGTVTINGieiknsqkiRQMIGYLPQDfdfyPNMKV----SE 94
Cdd:TIGR00954 468 IESLSFEVPSGNnLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA---------KGKLFYVPQR----PYMTLgtlrDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 95 VLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNKKV---------KSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLD 165
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170
....*....|...
gi 1436942050 166 PEERVRIRNLLSD 178
Cdd:TIGR00954 615 VDVEGYMYRLCRE 627
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-167 |
1.97e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 3 KIV--IKGLSKSYDGKKDALNSLDLVIPNGMFGILGRNGSGKSTLMNIIATILQPSKG---------------------- 58
Cdd:PRK11147 317 KIVfeMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGrihcgtklevayfdqhraeldp 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 59 -------------TVTINGIEiknsqkiRQMIGYLpQDFDFYPnmkvsevlyylgflsKINQTdfdkyvdlilrkvnlid 125
Cdd:PRK11147 397 ektvmdnlaegkqEVMVNGRP-------RHVLGYL-QDFLFHP---------------KRAMT----------------- 436
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1436942050 126 yknkKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPE 167
Cdd:PRK11147 437 ----PVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-211 |
2.06e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 7 KGLSKSYDGKKdALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATIlQPS---KGTVTINGIE-----IKNSQKIRQMI 77
Cdd:NF040905 5 RGITKTFPGVK-ALDDVNLSVREGeIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVcrfkdIRDSEALGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 78 gyLPQDFDFYPNMKVSEVLyylgFLSK-------I--NQTdFDKYVDLiLRKVNLIDYKNKKVKSLSGGMKKRLGIAQAI 148
Cdd:NF040905 83 --IHQELALIPYLSIAENI----FLGNerakrgvIdwNET-NRRAREL-LAKVGLDESPDTLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1436942050 149 LHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKI--VIIStHIVSDIESTCNRIAILDKGSLV 211
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGItsIIIS-HKLNEIRRVADSITVLRDGRTI 218
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
33-212 |
4.71e-06 |
|
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: 46.03 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 33 GILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIknsqkirqmiGYLPQdfdfypnmkvsevlyylgflskinqtdfdk 112
Cdd:cd03222 29 GIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP----------VYKPQ------------------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 113 YVDLilrkvnlidyknkkvkslSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAEN--KIVIISTH 190
Cdd:cd03222 69 YIDL------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEH 130
|
170 180
....*....|....*....|..
gi 1436942050 191 IVSDIESTCNRIAILDKGSLVY 212
Cdd:cd03222 131 DLAVLDYLSDRIHVFEGEPGVY 152
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-165 |
5.04e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 4 IVIKGLSKSYDGK--KDALNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGTVTIngieiknsqkIRQMIGYL 80
Cdd:PLN03232 615 ISIKNGYFSWDSKtsKPTLSDINLEIPVGsLVAIVGGTGEGKTSLISAMLGELSHAETSSVV----------IRGSVAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 81 PQdFDFYPNMKVSE-VLYYLGFLSK-----INQTDFDKYVDLILRKvNLIDYKNKKVkSLSGGMKKRLGIAQAILHDPKV 154
Cdd:PLN03232 685 PQ-VSWIFNATVREnILFGSDFESErywraIDVTALQHDLDLLPGR-DLTEIGERGV-NISGGQKQRVSMARAVYSNSDI 761
|
170
....*....|.
gi 1436942050 155 IIVDEPTAGLD 165
Cdd:PLN03232 762 YIFDDPLSALD 772
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
31-208 |
1.27e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 31 MFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNSQKIRQM----------------IGYLPQDFdfypNMKVSE 94
Cdd:PRK10982 276 ILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAInhgfalvteerrstgiYAYLDIGF----NSLISN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 95 VLYYLGFLSKINQTDFDKYVDLILRKVNLIDYKNK-KVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIR 173
Cdd:PRK10982 352 IRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIY 431
|
170 180 190
....*....|....*....|....*....|....*.
gi 1436942050 174 NLLSDLA-ENKIVIISTHIVSDIESTCNRIAILDKG 208
Cdd:PRK10982 432 QLIAELAkKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
99-190 |
3.30e-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: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 99 LGFLSKINQTDFDKYVDLILRKVNLIDYKNKK---VKSLSGGMKKRLGIAQAILHDPK---VIIVDEPTAGLDPEERVRI 172
Cdd:pfam13304 199 LSDLGEGIEKSLLVDDRLRERGLILLENGGGGelpAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRL 278
|
90
....*....|....*....
gi 1436942050 173 RNLLSDLAENKI-VIISTH 190
Cdd:pfam13304 279 LELLKELSRNGAqLILTTH 297
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
28-57 |
3.99e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 40.66 E-value: 3.99e-05
10 20 30
....*....|....*....|....*....|
gi 1436942050 28 PNGMFGILGRNGSGKSTLMNIIATILQPSK 57
Cdd:pfam13555 21 PRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-225 |
4.12e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 44.46 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLDLVIPNG-MFGILGRNGSGKSTLMNIIATILQPSKGtvtingiEIKNSQKIrqmiGYLPQDFDFYPNMKVSEVLYY 98
Cdd:cd03291 53 LKNINLKIEKGeMLAITGSTGSGKTSLLMLILGELEPSEG-------KIKHSGRI----SFSSQFSWIMPGTIKENIIFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 99 LGF-----LSKIN----QTDFDKYVDlilrkvnlidyKNKKVK-----SLSGGMKKRLGIAQAILHDPKVIIVDEPTAGL 164
Cdd:cd03291 122 VSYdeyryKSVVKacqlEEDITKFPE-----------KDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1436942050 165 D--PEERVrIRNLLSDLAENKIVIISTHIVSDIESTcNRIAILDKGSLVYKGDIPSLIQQSDD 225
Cdd:cd03291 191 DvfTEKEI-FESCVCKLMANKTRILVTSKMEHLKKA-DKILILHEGSSYFYGTFSELQSLRPD 251
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-215 |
9.16e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 17 KDALNSLDLVIPNGMFG-ILGRNGSGKSTLMNIIATILQPSKGTVTIngieiknsqkiRQMIGYLPQDfDFYPNMKV-SE 94
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTvVLGATGSGKSTLLQSLLSQFEISEGRVWA-----------ERSIAYVPQQ-AWIMNATVrGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 95 VLyylgFLSKINQTDFDKYV-------DLILRKVNLIDYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPE 167
Cdd:PTZ00243 741 IL----FFDEEDAARLADAVrvsqleaDLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1436942050 168 --ERVRIRNLLSDLAeNKIVIISTHIVSdIESTCNRIAILDKGSLVYKGD 215
Cdd:PTZ00243 817 vgERVVEECFLGALA-GKTRVLATHQVH-VVPRADYVVALGDGRVEFSGS 864
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
131-190 |
9.85e-05 |
|
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: 41.96 E-value: 9.85e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 131 VKSLSGGMKKRLGIA-----QAILHDPkVIIVDEPTAGLDPEERVRIRNLLSDLAENK-IVIISTH 190
Cdd:cd03227 75 RLQLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKGaQVIVITH 139
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
34-203 |
1.20e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 42.65 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 34 ILGRNGSGKSTLMNIIATILQPS--------KGTVTINGIEIKNSQKIRQMIGYLPQDFDFYPNMKV----SEVLY--YL 99
Cdd:COG4938 25 LIGPNGSGKSTLIQALLLLLQSNfiylpaerSGPARLYPSLVRELSDLGSRGEYTADFLAELENLEIlddkSKELLeqVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 100 GFLSKINQTDFD-----KYVDLILRKVNliDYKNKKVKSLSGGMKKRLGIAQAILHDPK---VIIVDEPTAGLDPEERVR 171
Cdd:COG4938 105 EWLEKIFPGKVEvdassDLVRLVFRPSG--NGKRIPLSNVGSGVSELLPILLALLSAAKpgsLLIIEEPEAHLHPKAQSA 182
|
170 180 190
....*....|....*....|....*....|....*
gi 1436942050 172 IRNLLSDLAENKI-VIISTHivSD--IESTCNRIA 203
Cdd:COG4938 183 LAELLAELANSGVqVIIETH--SDyiLNGLRNLIK 215
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
134-211 |
1.45e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.87 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 134 LSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENK---IVIIStHIVSDIESTCNRIAILDKGSL 210
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNnttILLIS-HDLQMLSQWADKINVLYCGQT 237
|
.
gi 1436942050 211 V 211
Cdd:PRK15093 238 V 238
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
125-227 |
1.51e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 125 DYKNKKVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLsdLAENKIVIISTHIVSDIESTCNRIAI 204
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSHAREFLNTVVTDILH 413
|
90 100
....*....|....*....|....
gi 1436942050 205 LDKGSLV-YKGDIPSLIQQSDDHI 227
Cdd:PLN03073 414 LHGQKLVtYKGDYDTFERTREEQL 437
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-191 |
1.52e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 2 NKIVIKGLsKSYDGKkdalNSLDLviPNGMFGILGRNGSGKSTLMNIIATIL-----------------QPSKGTVTING 64
Cdd:COG0419 3 LRLRLENF-RSYRDT----ETIDF--DDGLNLIVGPNGAGKSTILEAIRYALygkarsrsklrsdlinvGSEEASVELEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 65 IEIKNSQKIRQMIGylpqDFDFYPNMKVSEVlyyLGFLSKINQTD-FDKYVDLI----------LRKVNLIDYKNKK--- 130
Cdd:COG0419 76 EHGGKRYRIERRQG----EFAEFLEAKPSER---KEALKRLLGLEiYEELKERLkeleealesaLEELAELQKLKQEila 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1436942050 131 -------VKSLSGGMKKRLGIAQAIlhdpkVIIVDepTAGLDPEERVRIRNLLSDLAenkivIISTHI 191
Cdd:COG0419 149 qlsgldpIETLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEELA-----IITHVI 204
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
133-190 |
1.81e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 42.61 E-value: 1.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1436942050 133 SLSGGMKKRLGIAqAILHDPK---VIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTH 190
Cdd:COG4637 258 ELSDGTLRFLALL-AALLSPRpppLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTH 317
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
22-207 |
2.85e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.52 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 22 SLDLVIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVT-----------------------------INGIEIKNSQK 72
Cdd:COG3950 18 EIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDdvkfrkllirngefgdsaklilyygtsrlLLDGPLKKLER 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 73 IRQMIGYLPQDFD--FYPNMKVSEVLYYLGF----LSKINQTDFDKYVDLI-------LRKVNLIDYKNKK--------- 130
Cdd:COG3950 98 LKEEYFSRLDGYDslLDEDSNLREFLEWLREyledLENKLSDELDEKLEAVrealnklLPDFKDIRIDRDPgrlvildkn 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 131 -----VKSLSGGMKKRLGIA--------------QAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKIVIISTH- 190
Cdd:COG3950 178 geelpLNQLSDGERSLLALVgdlarrlaelnpalENPLEGEGIVLIDEIDLHLHPKWQRRILPDLRKIFPNIQFIVTTHs 257
|
250
....*....|....*....
gi 1436942050 191 --IVSDIEStcNRIAILDK 207
Cdd:COG3950 258 plILSSLED--EEVIVLER 274
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-190 |
3.45e-04 |
|
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: 41.05 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 30 GMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGieiknsQKIRQMIGylpqdfdfypnmkVSEVLYY--LGFLSkinq 107
Cdd:cd03240 23 PLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGG------AHDPKLIR-------------EGEVRAQvkLAFEN---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 108 TDFDKYVdlILRKVNLIDY--------KNK----KVKSLSGGMKK------RLGIAQAILHDPKVIIVDEPTAGLDPEer 169
Cdd:cd03240 80 ANGKKYT--ITRSLAILENvifchqgeSNWplldMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEE-- 155
|
170 180
....*....|....*....|....*..
gi 1436942050 170 vRIRNLLSDLAE------NKIVIISTH 190
Cdd:cd03240 156 -NIEESLAEIIEerksqkNFQLIVITH 181
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-242 |
3.92e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 26 VIPNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTINGIEIKNS--QKIRQMIGYLPQD---FDFYPNMKVSEvlyylg 100
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYglRELRRQFSMIPQDpvlFDGTVRQNVDP------ 1406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 101 FLSKINQTdfdkyVDLILRKVNLidykNKKVKSLSGGMKKR---------------LGIAQAIL-HDPKVIIVDEPTAGL 164
Cdd:PTZ00243 1407 FLEASSAE-----VWAALELVGL----RERVASESEGIDSRvleggsnysvgqrqlMCMARALLkKGSGFILMDEATANI 1477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 165 DPEERVRIRNLLSDLAENKIVIISTHIVSDIeSTCNRIAILDKGSLVYKGDIPSLIQQSDDHIYEI--NLSPSELESFRE 242
Cdd:PTZ00243 1478 DPALDRQIQATVMSAFSAYTVITIAHRLHTV-AQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMveALGRSEAKRFLQ 1556
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
20-190 |
7.12e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 40.76 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 20 LNSLDLVIPNGMFGILGRNGSGKSTLMNIIATILQPSKG---------------------TVTIN---------GIEIKN 69
Cdd:COG3593 14 IKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSrkfdeedfylgddpdlpeieiELTFGsllsrllrlLLKEED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 70 SQKIRQMIGYLPQDFD-----FypNMKVSEVLYYLGFLSKINQTDFDKYVDLILRKVNLI--DYKNKKVKSLSGGMKKRL 142
Cdd:COG3593 94 KEELEEALEELNEELKealkaL--NELLSEYLKELLDGLDLELELSLDELEDLLKSLSLRieDGKELPLDRLGSGFQRLI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1436942050 143 GIA--QAILH-----DPKVIIVDEPTAGLDPEERVRIRNLLSDLAENKI-VIISTH 190
Cdd:COG3593 172 LLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNqVIITTH 227
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
2-190 |
1.11e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 39.37 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 2 NKIVIKGLsKSYDGKKDalnsldLVIPNGMFGILGRNGSGKStlmNIIATILQpskgtVTingieikNSQKIRQMIGYLP 81
Cdd:cd03278 2 KKLELKGF-KSFADKTT------IPFPPGLTAIVGPNGSGKS---NIIDAIRW-----VL-------GEQSAKSLRGEKM 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 82 QDFDFY-----PNMKVSEVLYYL----GFLSKINQTDFDKyvdlilrkvnLIDYKNKKVKS---LSGGMKKRLGIAQ--A 147
Cdd:cd03278 60 SDVIFAgsetrKPANFAEVTLTFdnsdGRYSIISQGDVSE----------IIEAPGKKVQRlslLSGGEKALTALALlfA 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1436942050 148 ILH---DPKVIIvDEPTAGLDPEERVRIRNLLSDLAENKIVIISTH 190
Cdd:cd03278 130 IFRvrpSPFCVL-DEVDAALDDANVERFARLLKEFSKETQFIVITH 174
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
29-191 |
2.18e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.79 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 29 NGMFGILGRNGSGKSTLMNIIATILQpskGTVTINGIEIKNSQKIRQMIGYLPQDFDFYPNMKVSEVLYYLGflskINQT 108
Cdd:cd03279 28 NGLFLICGPTGAGKSTILDAITYALY---GKTPRYGRQENLRSVFAPGEDTAEVSFTFQLGGKKYRVERSRG----LDYD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 109 DFDKYVdlILRKVNLIDYKNKKVKSLSGG------MKKRLGIAQAILHDPKV----IIVDEPTAGLDPEERVRIRNLLSD 178
Cdd:cd03279 101 QFTRIV--LLPQGEFDRFLARPVSTLSGGetflasLSLALALSEVLQNRGGArleaLFIDEGFGTLDPEALEAVATALEL 178
|
170
....*....|....
gi 1436942050 179 LA-ENKIVIISTHI 191
Cdd:cd03279 179 IRtENRMVGVISHV 192
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
130-217 |
2.50e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 130 KVKSLSGGMKKRLGIAQAILHDPKVIIVDEPTAGLDPEERVRIRNLLSDLA-ENK-IVIISTHIvSDIESTCNRIAILDK 207
Cdd:NF040905 401 KVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAaEGKgVIVISSEL-PELLGMCDRIYVMNE 479
|
90
....*....|
gi 1436942050 208 GSLVykGDIP 217
Cdd:NF040905 480 GRIT--GELP 487
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-165 |
5.85e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.23 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 28 PNGMFGILGRNGSGKSTLMNIIATILQPSKGTVTING------------------IE--IKNSQKIRQM----------- 76
Cdd:PRK10636 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpalpqpaLEyvIDGDREYRQLeaqlhdanern 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1436942050 77 ----IGYLPQDFD----FYPNMKVSEVLYYLGFlskiNQTDFDKyvdlilrkvnlidyknkKVKSLSGGMKKRLGIAQAI 148
Cdd:PRK10636 106 dghaIATIHGKLDaidaWTIRSRAASLLHGLGF----SNEQLER-----------------PVSDFSGGWRMRLNLAQAL 164
|
170
....*....|....*..
gi 1436942050 149 LHDPKVIIVDEPTAGLD 165
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLD 181
|
|
| |
