|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
45-268 |
2.36e-125 |
|
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: 355.66 E-value: 2.36e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQSI 124
Cdd:cd03263 1 LQIRNLTKTYKK---GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFL 204
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641957197 205 DEPTTGMDPKARRFLWNLILDIlKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLK 268
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-270 |
1.29e-119 |
|
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: 376.66 E-value: 1.29e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 17 SSQPIEDDDEDVASERRRVLRGEADNDMLKIDNLTKVYKSRKMGrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLT 96
Cdd:TIGR01257 1910 AKEPIFDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSP---AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLT 1986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 97 GDESTTGGEAFIGGSSILKELLRVQQSIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADM 176
Cdd:TIGR01257 1987 GDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADR 2066
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 177 PAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNG 256
Cdd:TIGR01257 2067 LAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
250
....*....|....
gi 641957197 257 RFKCLGSIQHLKNR 270
Cdd:TIGR01257 2147 AFQCLGTIQHLKSK 2160
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
45-270 |
5.28e-89 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 263.85 E-value: 5.28e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQSI 124
Cdd:COG1131 1 IEVRGLTKRY-----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFL 204
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 205 DEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKNR 270
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
57-270 |
8.93e-70 |
|
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: 217.26 E-value: 8.93e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 57 RKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQSIGYCPQFDALFED 136
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 137 LTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKAR 216
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 641957197 217 RFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKNR 270
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRR 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
47-268 |
2.35e-69 |
|
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: 213.39 E-value: 2.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 47 IDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQSIGY 126
Cdd:cd03265 3 VENLVKKY-----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 127 CPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDE 206
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 207 PTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLK 268
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
45-258 |
3.77e-68 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 208.79 E-value: 3.77e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQSI 124
Cdd:cd03230 1 IEVRNLSKRYGKKT-----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLElytrlrgipwkdeervvswaleklelskyadmpagtYSGGNKRKLSTAIALIGYPSLVFL 204
Cdd:cd03230 76 GYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 641957197 205 DEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRF 258
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
44-270 |
1.59e-63 |
|
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: 199.31 E-value: 1.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQS 123
Cdd:COG4555 1 MIEVENLSKKYGKVP-----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVF 203
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641957197 204 LDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKNR 270
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
45-257 |
1.00e-52 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 173.84 E-value: 1.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQSI 124
Cdd:PRK13537 8 IDFRNVEKRY-----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFL 204
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 641957197 205 DEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
45-257 |
1.37e-51 |
|
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: 167.78 E-value: 1.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQsI 124
Cdd:cd03268 1 LKTNDLTKTYGKKR-----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVvswaLEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFL 204
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 641957197 205 DEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
44-270 |
9.17e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 168.36 E-value: 9.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKEllrVQQS 123
Cdd:COG4152 1 MLELKGLTKRFGDKT-----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQFDALFEDLTAREHLELYTRLRGIPWKD-EERVVSWaLEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLV 202
Cdd:COG4152 73 IGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEaKRRADEW-LERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641957197 203 FLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKNR 270
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
44-257 |
1.82e-50 |
|
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: 165.23 E-value: 1.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQS 123
Cdd:cd03266 1 MITADALTKRFRDVK-KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVF 203
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 641957197 204 LDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
45-259 |
2.02e-50 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 164.67 E-value: 2.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmgrilAVDRLCLGVRPGeCFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQSI 124
Cdd:cd03264 1 LQLENLTKRYGKKR-----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFL 204
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 205 DEPTTGMDPKAR-RFLwNLILDiLKTGRSVVLTSHSMEECEALCTRLGIMVNGRFK 259
Cdd:cd03264 155 DEPTAGLDPEERiRFR-NLLSE-LGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
44-238 |
8.54e-49 |
|
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: 160.34 E-value: 8.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQS 123
Cdd:COG4133 2 MLEAENLSCRR-----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQFDALFEDLTAREHLELYTRLRGIPWkDEERVVSwALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVF 203
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRA-DREAIDE-ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 641957197 204 LDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSH 238
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
45-257 |
1.30e-48 |
|
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: 160.14 E-value: 1.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKEllrVQQSI 124
Cdd:cd03269 1 LEVENVTKRF-----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFL 204
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 641957197 205 DEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
47-269 |
2.72e-48 |
|
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: 171.73 E-value: 2.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 47 IDNLTKVYKSrkMGRIlAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQSIGY 126
Cdd:TIGR01257 931 VKNLVKIFEP--SGRP-AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 127 CPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDE 206
Cdd:TIGR01257 1008 CPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 207 PTTGMDPKARRFLWNLILDiLKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKN 269
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLK-YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
44-257 |
4.10e-48 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 162.69 E-value: 4.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDnLTKVYKSrkMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQS 123
Cdd:PRK13536 39 TVAID-LAGVSKS--YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVF 203
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 641957197 204 LDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
45-257 |
3.01e-42 |
|
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: 144.50 E-value: 3.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI--LKELLRVQQ 122
Cdd:cd03219 1 LEVRGLTKRF-----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItgLPPHEIARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 SIGYCPQFDALFEDLTAREHLEL-------YTRLRGIPWKDEERVVSWA---LEKLELSKYADMPAGTYSGGNKRKLSTA 192
Cdd:cd03219 76 GIGRTFQIPRLFPELTVLENVMVaaqartgSGLLLARARREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 193 IALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
45-257 |
6.12e-41 |
|
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: 141.14 E-value: 6.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELL--RVQQ 122
Cdd:cd03218 1 LRAENLSKRYGKRK-----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhkRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 SIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLV 202
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 203 FLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
45-257 |
2.18e-40 |
|
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: 138.81 E-value: 2.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRvQQSI 124
Cdd:cd03259 1 LELKGLSKTY-----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFL 204
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 641957197 205 DEPTTGMDPKARRFLWNLILDILK-TGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQReLGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
46-257 |
2.13e-38 |
|
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: 133.75 E-value: 2.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 46 KIDNLTKVYKSRKmgrILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLR-VQQSI 124
Cdd:cd03225 1 ELKNLSFSYPDGA---RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKeLRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQF--DALFEDlTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLV 202
Cdd:cd03225 78 GLVFQNpdDQFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 203 FLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
45-257 |
4.89e-38 |
|
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: 133.23 E-value: 4.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYksrkMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLR-VQQS 123
Cdd:COG1122 1 IELENLSFSY----PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLReLRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQF--DALFEDlTAREHLELYTRLRGIPwKDE-ERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPS 200
Cdd:COG1122 77 VGLVFQNpdDQLFAP-TVEEDVAFGPENLGLP-REEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 641957197 201 LVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
44-257 |
6.02e-38 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 133.23 E-value: 6.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELL--RVQ 121
Cdd:COG1137 3 TLEAENLVKSYGKRT-----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhkRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSL 201
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 202 VFLDEPTTGMDPKArrflwnlILDI------LKT-GRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:COG1137 158 ILLDEPFAGVDPIA-------VADIqkiirhLKErGIGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
44-257 |
3.61e-37 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 131.70 E-value: 3.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI--LKELLRVQ 121
Cdd:COG0411 4 LLEVRGLTKRF-----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItgLPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYCPQFDALFEDLTAREHLEL--YTRLRGIPWKDEERVVSWA-------------LEKLELSKYADMPAGTYSGGNK 186
Cdd:COG0411 79 LGIARTFQNPRLFPELTVLENVLVaaHARLGRGLLAALLRLPRARreereareraeelLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641957197 187 RKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILK-TGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
40-266 |
7.87e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.59 E-value: 7.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 40 ADNDMLKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLR 119
Cdd:COG1121 2 MMMPAIELENLTVSY-----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 vqqsIGYCPQ---FDALFEdLTAREHLELYtRLRGIPW------KDEERVVSwALEKLELSKYADMPAGTYSGGNKRKLS 190
Cdd:COG1121 77 ----IGYVPQraeVDWDFP-ITVRDVVLMG-RYGRRGLfrrpsrADREAVDE-ALERVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 191 TAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLgIMVNGRFKCLGSIQH 266
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
46-257 |
1.62e-36 |
|
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: 127.36 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 46 KIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK-ELLRVQQSI 124
Cdd:cd00267 1 EIENLSFRYGGRT-----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFdalfedltarehlelytrlrgipwkdeervvswaleklelskyadmpagtySGGNKRKLSTAIALIGYPSLVFL 204
Cdd:cd00267 76 GYVPQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 641957197 205 DEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
45-269 |
3.00e-36 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 128.93 E-value: 3.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI--LKELLRVQQ 122
Cdd:TIGR04406 2 LVAENLIKSYKKRK-----VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIthLPMHERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 SIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWAL-EKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSL 201
Cdd:TIGR04406 77 GIGYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALlEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641957197 202 VFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKN 269
Cdd:TIGR04406 157 ILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
45-257 |
9.54e-35 |
|
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: 124.52 E-value: 9.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK------ELL 118
Cdd:cd03255 1 IELKNLSKTYGGGG-EKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekelAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 119 RVQQsIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGY 198
Cdd:cd03255 80 RRRH-IGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 199 PSLVFLDEPTTGMDPKARRFLWNLILDILK-TGRSVVLTSHSMEEcEALCTRLGIMVNGR 257
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
46-262 |
1.00e-34 |
|
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: 124.18 E-value: 1.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 46 KIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRvqqsIG 125
Cdd:cd03235 1 EVEDLTVSYGGHP-----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR----IG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 126 YCPQ---FDALFEdLTARE--HLELYTRLRGIPW--KDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGY 198
Cdd:cd03235 72 YVPQrrsIDRDFP-ISVRDvvLMGLYGHKGLFRRlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641957197 199 PSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLgIMVNGRFKCLG 262
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
45-258 |
1.32e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.77 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmgrILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK---ELLRvq 121
Cdd:COG4619 1 LELEGLSFRVGGKP---IL--SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmppPEWR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYCPQFDALFEDlTAREHLELYTRLRGIPWkDEERVVSWaLEKLELSK-YADMPAGTYSGGNKRKLSTAIALIGYPS 200
Cdd:COG4619 74 RQVAYVPQEPALWGG-TVRDNLPFPFQLRERKF-DRERALEL-LERLGLPPdILDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 641957197 201 LVFLDEPTTGMDPKARRFLWNLILDILK-TGRSVVLTSHSMEECEALCTRLGIMVNGRF 258
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAeEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
29-267 |
1.72e-34 |
|
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: 130.02 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 29 ASERRRVLRGEADNDMLKIDNLTKVYKSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFI 108
Cdd:COG1123 245 AARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 109 GGSSIL----KELLRVQQSIGYCPQ--FDALFEDLTAREHLELYTRLRGIPWKDE-ERVVSWALEKLELS-KYADMPAGT 180
Cdd:COG1123 325 DGKDLTklsrRSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAErRERVAELLERVGLPpDLADRYPHE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 181 YSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILK-TGRSVVLTSHSMEECEALCTRLGIMVNGRFK 259
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
....*...
gi 641957197 260 CLGSIQHL 267
Cdd:COG1123 485 EDGPTEEV 492
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
44-263 |
2.10e-33 |
|
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: 122.07 E-value: 2.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRkmgRILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI----LKELLR 119
Cdd:COG1120 1 MLEAENLSVGYGGR---PVL--DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslsRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VqqsIGYCPQFDALFEDLTAREHLEL----YTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIAL 195
Cdd:COG1120 76 R---IAYVPQEPPAPFGLTVRELVALgrypHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 196 IGYPSLVFLDEPTTGMDPKARRflwnLILDILK-----TGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGS 263
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQL----EVLELLRrlareRGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
44-270 |
2.51e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 123.66 E-value: 2.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYK----------------SRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAF 107
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkgalkglfRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 108 IGGSSILKELLRVQQSI----GycpQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAgtysg 183
Cdd:COG4586 81 VLGYVPFKRRKEFARRIgvvfG---QRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPV----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 184 gnkRKLS--------TAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCTRLGIMV 254
Cdd:COG4586 153 ---RQLSlgqrmrceLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVID 229
|
250
....*....|....*.
gi 641957197 255 NGRFKCLGSIQHLKNR 270
Cdd:COG4586 230 HGRIIYDGSLEELKER 245
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
45-253 |
5.00e-33 |
|
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: 119.88 E-value: 5.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGssilKELLRVQQSI 124
Cdd:cd03293 1 LEVRNVSKTYGGGG-GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYAD-MPAgTYSGGNKRKLSTAIALIGYPSLVF 203
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENaYPH-QLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 641957197 204 LDEPTTGMDPKARRFLWNLILDIL-KTGRSVVLTSHSMEECEALCTRLGIM 253
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIWrETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
44-267 |
7.46e-33 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 119.99 E-value: 7.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL----KELLR 119
Cdd:cd03258 1 MIELKNVSKVFGDTG-GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYP 199
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641957197 200 SLVFLDEPTTGMDPKARRFLWNLILDI-LKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHL 267
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
44-257 |
8.14e-33 |
|
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: 119.92 E-value: 8.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQ- 122
Cdd:cd03257 1 LLEVKNLSVSFPTGG-GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 ---SIGYCPQ--FDALFEDLTAREHL-ELYtRLRGIPWKDE--ERVVSWALEKLELSK-YADMPAGTYSGGNKRKLSTAI 193
Cdd:cd03257 80 rrkEIQMVFQdpMSSLNPRMTIGEQIaEPL-RIHGKLSKKEarKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 194 ALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILK-TGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
65-209 |
1.12e-32 |
|
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: 116.98 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 65 VDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLR-VQQSIGYCPQFDALFEDLTAREHL 143
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKsLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 144 ELYTRLRGIPWKDEERVVSWALEKLELSKYAD----MPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTT 209
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
40-269 |
1.44e-32 |
|
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: 119.31 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 40 ADNDMLKIDNLTKVYKSRKmgrILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL----K 115
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRV---VL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 116 ELLRVQQSIGYCPQFDALFEDLTAREHLELYTR-LRGIPWKDEERVVSWALEKLELSKYAD-MPAGTySGGNKRKLSTAI 193
Cdd:COG1127 76 ELYELRRRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADkMPSEL-SGGMRKRVALAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641957197 194 ALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKN 269
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
44-253 |
1.90e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 119.81 E-value: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGssilKELLRVQQS 123
Cdd:COG1116 7 ALELRGVSKRFPTGG-GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVF 203
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 641957197 204 LDEPTTGMDPKARRFLWNLILDIL-KTGRSVVLTSHSMEECEALCTRLGIM 253
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWqETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
45-257 |
5.18e-32 |
|
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: 117.54 E-value: 5.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI--LKELLRVQQ 122
Cdd:cd03224 1 LEVENLNAGY-----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItgLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 SIGYCPQFDALFEDLTAREHLELYTRLRGipwkdeERVVSWALEKL-----ELSKYADMPAGTYSGGNKRKLSTAIALIG 197
Cdd:cd03224 76 GIGYVPEGRRIFPELTVEENLLLGAYARR------RAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 198 YPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
44-257 |
1.91e-31 |
|
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: 116.23 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKelL----R 119
Cdd:COG0410 3 MLEVENLHAGY-----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG--LpphrI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSIGYCPQFDALFEDLTAREHLELYTRLRGipwkdEERVVSWALEKL-----ELSKYADMPAGTYSGGNKRKLSTAIA 194
Cdd:COG0410 76 ARLGIGYVPEGRRIFPSLTVEENLLLGAYARR-----DRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 195 LIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
47-257 |
2.41e-31 |
|
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: 116.28 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 47 IDNLTKVYK----------------SRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGG 110
Cdd:cd03267 3 VSNLSKSYRvyskepgligslkslfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 111 ssilkeLLRVQQSIGYCPQFDALFE-------DLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSG 183
Cdd:cd03267 83 ------LVPWKRRKKFLRRIGVVFGqktqlwwDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 184 GNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILK-TGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
47-259 |
3.23e-31 |
|
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: 115.05 E-value: 3.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 47 IDNLTkvYKSRKMGRILAVDRLCLgvRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI-LKELLRvqqSIG 125
Cdd:cd03226 2 IENIS--FSYKKGTEILDDLSLDL--YAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkAKERRK---SIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 126 YCPQ--FDALFEDlTAREhlELYTRLRGIPwkDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVF 203
Cdd:cd03226 75 YVMQdvDYQLFTD-SVRE--ELLLGLKELD--AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 204 LDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFK 259
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
44-272 |
3.25e-31 |
|
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: 116.06 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKMGRIlAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVqqs 123
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVP-VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 igYCPQFDALFED--------LTAREHLELYTRLRGIPwKDEERVVSwALEKLELSK-YADMPAGTYSGGNKRKLSTAIA 194
Cdd:COG1124 77 --FRRRVQMVFQDpyaslhprHTVDRILAEPLRIHGLP-DREERIAE-LLEQVGLPPsFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641957197 195 LIGYPSLVFLDEPTTGMDPKARRFLWNLILDILK-TGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKNRSE 272
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
48-257 |
8.15e-31 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 121.00 E-value: 8.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 48 DNLTkvyksRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQSIGYC 127
Cdd:NF033858 270 RGLT-----MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 128 PQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEP 207
Cdd:NF033858 345 SQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 641957197 208 TTGMDPKARRFLWNLILDiL--KTGRSVVLTSHSMEECEaLCTRLGIMVNGR 257
Cdd:NF033858 425 TSGVDPVARDMFWRLLIE-LsrEDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
47-269 |
8.64e-31 |
|
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: 114.52 E-value: 8.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 47 IDNLTKVYKSRkmgRILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL----KELLRVQQ 122
Cdd:cd03261 3 LRGLTKSFGGR---TVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 SIGYCPQFDALFEDLTA--------REHLELytrlrgipwkDEERVVSWALEKLE---LSKYAD-MPAgTYSGGNKRKLS 190
Cdd:cd03261 78 RMGMLFQSGALFDSLTVfenvafplREHTRL----------SEEEIREIVLEKLEavgLRGAEDlYPA-ELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 191 TAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKN 269
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
44-257 |
2.02e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 116.35 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKelLRVQQ- 122
Cdd:COG3842 5 ALELENVSKRY-----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG--LPPEKr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 SIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLV 202
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 203 FLDEPTTGMDPKARRFLWNLILDILK-TGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQReLGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
42-257 |
3.24e-30 |
|
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: 118.08 E-value: 3.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLTKVYKSrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTG---DESTTGGEAFIGGSSILK--E 116
Cdd:COG1123 2 TPLLEVRDLSVRYPG---GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLElsE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 117 LLRVQQsIGYCPQ-FDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIAL 195
Cdd:COG1123 79 ALRGRR-IGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 196 IGYPSLVFLDEPTTGMDPKARRFLWNLILDILK-TGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGR 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
42-257 |
7.99e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 111.67 E-value: 7.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI--LKE--- 116
Cdd:COG1136 2 SPLLELRNLTKSYGTGE-GEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIssLSErel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 117 -LLRvQQSIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIAL 195
Cdd:COG1136 81 aRLR-RRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641957197 196 IGYPSLVFLDEPTTGMDPKARRflwnLILDILK-----TGRSVVLTSHSmEECEALCTRLGIMVNGR 257
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGE----EVLELLRelnreLGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
45-263 |
7.03e-29 |
|
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: 109.70 E-value: 7.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKMgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKE-LLRVQQS 123
Cdd:cd03295 1 IEFENVTKRYGGGKK----AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQFDALFEDLTAREHLELYTRLRGipWKdEERVVSWALEKLEL-----SKYADMPAGTYSGGNKRKLSTAIALIGY 198
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLK--WP-KEKIRERADELLALvgldpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 199 PSLVFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGS 263
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
45-263 |
4.59e-28 |
|
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: 107.32 E-value: 4.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKeLLRVQQSI 124
Cdd:cd03300 1 IELENVSKFY-----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-LPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFL 204
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641957197 205 DEPTTGMDPKARRFLwNLILDIL--KTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGS 263
Cdd:cd03300 155 DEPLGALDLKLRKDM-QLELKRLqkELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
45-263 |
3.07e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 105.36 E-value: 3.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKMgrilaVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGS--SILKELLRVQQ 122
Cdd:PRK10895 4 LTAKNLAKAYKGRRV-----VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 SIGYCPQFDALFEDLTAREHLELYTRLR-GIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSL 201
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641957197 202 VFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGS 263
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
44-241 |
3.85e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 104.75 E-value: 3.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKsrkmGRILAVDRLCLGVRPGE-CFgLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK----ELL 118
Cdd:COG2884 1 MIRFENVSKRYP----GGREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 119 RVQQSIGYCPQfDA-LFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIG 197
Cdd:COG2884 76 YLRRRIGVVFQ-DFrLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 641957197 198 YPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSME 241
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
42-264 |
4.48e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 105.16 E-value: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLTKVYK-----------------SRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGG 104
Cdd:COG1134 2 SSMIEVENVSKSYRlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 105 EAFIGG--SSILkELlrvqqSIGycpqFDAlfeDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYS 182
Cdd:COG1134 82 RVEVNGrvSALL-EL-----GAG----FHP---ELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 183 GGNKRKLSTAIALIGYPSLVFLDEPTTGMDP----KARRFlwnlILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRF 258
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLAR----IRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
....*.
gi 641957197 259 KCLGSI 264
Cdd:COG1134 225 VMDGDP 230
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
45-257 |
8.86e-27 |
|
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: 102.65 E-value: 8.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI---LKELLRVQ 121
Cdd:cd03229 1 LELKNVSKRY-----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdlEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYCPQFDALFEDLTAREHLELytrlrgipwkdeervvswALeklelskyadmpagtySGGNKRKLSTAIALIGYPSL 201
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIAL------------------GL----------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 641957197 202 VFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
57-270 |
9.56e-27 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 106.74 E-value: 9.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 57 RKMGRILAVDRLCLGVRPGECFGLLGVNGAG--KTTTFKMLTGDESTTGGEAFIGGSSILKELLRvqqSIG-YCPQFDAL 133
Cdd:NF000106 21 KHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRALRR---TIG*HRPVR*GR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 134 FEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDP 213
Cdd:NF000106 98 RESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 641957197 214 KARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKNR 270
Cdd:NF000106 178 RTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
72-257 |
1.10e-26 |
|
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: 102.63 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 72 VRPGECFGLLGVNGAGKTTTFKMLTG--DESTTGGEAFIGGSSILKELLRvqQSIGYCPQFDALFEDLTAREHLELYTRL 149
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFR--KIIGYVPQDDILHPTLTVRETLMFAAKL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 150 RGIpwkdeervvswaleklelskyadmpagtySGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKT 229
Cdd:cd03213 110 RGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT 160
|
170 180
....*....|....*....|....*....
gi 641957197 230 GRSVVLTSHS-MEECEALCTRLGIMVNGR 257
Cdd:cd03213 161 GRTIICSIHQpSSEIFELFDKLLLLSQGR 189
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
45-262 |
1.86e-26 |
|
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: 102.72 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIlKELLRVQQSI 124
Cdd:cd03301 1 VELENVTKRFGNVT-----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFL 204
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 641957197 205 DEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCTRLGIMVNGRFKCLG 262
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-258 |
1.10e-25 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 105.65 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 29 ASERRRVLRGEADNDMLKIDNLTKVYKSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAF- 107
Cdd:TIGR03269 264 VSEVEKECEVEVGEPIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNv 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 108 -IGGSSI------LKELLRVQQSIGYCPQFDALFedlTAREHLELYTRLRGIPWKDE---------ERVVSWALEKLE-- 169
Cdd:TIGR03269 344 rVGDEWVdmtkpgPDGRGRAKRYIGILHQEYDLY---PHRTVLDNLTEAIGLELPDElarmkavitLKMVGFDEEKAEei 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 170 LSKYADmpagTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCT 248
Cdd:TIGR03269 421 LDKYPD----ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCD 496
|
250
....*....|
gi 641957197 249 RLGIMVNGRF 258
Cdd:TIGR03269 497 RAALMRDGKI 506
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
44-240 |
1.26e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 101.61 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLtkvykSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI---------L 114
Cdd:PRK11300 5 LLSVSGL-----MMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiaR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 115 KELLRVQQSIgycpqfdALFEDLTARE------HLELYTRL----------RGIPWKDEERVVSWaLEKLELSKYADMPA 178
Cdd:PRK11300 80 MGVVRTFQHV-------RLFREMTVIEnllvaqHQQLKTGLfsgllktpafRRAESEALDRAATW-LERVGLLEHANRQA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641957197 179 GTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLIlDILKT--GRSVVLTSHSM 240
Cdd:PRK11300 152 GNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELI-AELRNehNVTVLLIEHDM 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
72-238 |
1.75e-25 |
|
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: 100.42 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 72 VRPGECFGLLGVNGAGKTTTFKMLTG---DESTTGGEAFIGGSSILKELlrVQQSIGYCPQFDALFEDLTAREHLELYTR 148
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPDQ--FQKCVAYVRQDDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 149 LR-GIPWKDEERVVSWalEKLELSKYADMPAGTY-----SGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPkarrFLWNL 222
Cdd:cd03234 108 LRlPRKSSDAIRKKRV--EDVLLRDLALTRIGGNlvkgiSGGERRRVSIAVQLLWDPKVLILDEPTSGLDS----FTALN 181
|
170 180
....*....|....*....|
gi 641957197 223 ILDILK----TGRSVVLTSH 238
Cdd:cd03234 182 LVSTLSqlarRNRIVILTIH 201
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
45-265 |
2.38e-25 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 100.49 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmgrilaVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIlKELLRVQQSI 124
Cdd:cd03299 1 LKVENLSKDWKEFK------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFL 204
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641957197 205 DEPTTGMDPKARRFLWNLILDILKTGRSVVL-TSHSMEECEALCTRLGIMVNGRFKCLGSIQ 265
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
42-257 |
2.85e-25 |
|
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: 100.54 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLTKVYKSRkmgRILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDES-TTGGEAFI-----GGSSILK 115
Cdd:COG1119 1 DPLLELRNVTVRRGGK---TIL--DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPpTYGNDVRLfgerrGGEDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 116 elLRvqQSIGYC-PQFDALF-EDLTARE--------HLELYtrlRGIPWKDEERVVSWaLEKLELSKYADMPAGTYSGGN 185
Cdd:COG1119 76 --LR--KRIGLVsPALQLRFpRDETVLDvvlsgffdSIGLY---REPTDEQRERAREL-LELLGLAHLADRPFGTLSQGE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 186 KRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTG-RSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
67-238 |
3.18e-25 |
|
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: 98.97 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 67 RLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQSIGYCPQFDALFEDLTAREHLELY 146
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 147 TRLRGipwkDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDI 226
Cdd:TIGR01189 98 AAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAH 173
|
170
....*....|..
gi 641957197 227 LKTGRSVVLTSH 238
Cdd:TIGR01189 174 LARGGIVLLTTH 185
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
42-269 |
3.58e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 100.19 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK--ELLR 119
Cdd:COG4674 8 GPILYVEDLTVSFDGFK-----ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGldEHEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSIGYCPQFDALFEDLTAREHLEL-YTRLRGiPWK---------DEERVVSwALEKLELSKYADMPAGTYSGGNKRKL 189
Cdd:COG4674 83 ARLGIGRKFQKPTVFEELTVFENLELaLKGDRG-VFAslfarltaeERDRIEE-VLETIGLTDKADRLAGLLSHGQKQWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 190 STAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTgRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKN 269
Cdd:COG4674 161 EIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGK-HSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQA 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
46-262 |
3.98e-25 |
|
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: 98.28 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 46 KIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI----LKELLRVq 121
Cdd:cd03214 1 EVENLSVGYGGRT-----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLaslsPKELARK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 qsIGYCPQfdalfedltarehlelytrlrgipwkdeervvswALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSL 201
Cdd:cd03214 75 --IAYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 202 VFLDEPTTGMDPKARrflwNLILDILK-----TGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLG 262
Cdd:cd03214 119 LLLDEPTSHLDIAHQ----IELLELLRrlareRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
72-238 |
1.81e-24 |
|
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: 96.93 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 72 VRPGECFGLLGVNGAGKTTTFKMLTG--DESTTGGEAFIGGSSILKELLRvqqSIGYCPQFDALFEDLTAREHLELYTRL 149
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQR---STGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 150 RGIpwkdeervvswaleklelskyadmpagtySGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKT 229
Cdd:cd03232 107 RGL-----------------------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
....*....
gi 641957197 230 GRSVVLTSH 238
Cdd:cd03232 158 GQAILCTIH 166
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
45-257 |
2.53e-24 |
|
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: 97.25 E-value: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTG-----DESTTGGEAFIGGSSILK---E 116
Cdd:cd03260 1 IELRDLNVYYGDKH-----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDldvD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 117 LLRVQQSIGYCPQFDALFeDLTAREHLELYTRLRGIPWKDE-ERVVSWALEKLELSKYAD--MPAGTYSGGNKRKLSTAI 193
Cdd:cd03260 76 VLELRRRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEElDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641957197 194 ALIGYPSLVFLDEPTTGMDPKARRFLWNLILDiLKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAE-LKKEYTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
44-263 |
4.82e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.52 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRkmgriLAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSiLKELLRVQQS 123
Cdd:PRK11607 19 LLEIRNLTKSFDGQ-----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVF 203
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641957197 204 LDEPTTGMDPKARRFLWNLILDIL-KTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGS 263
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILeRVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
72-238 |
6.09e-24 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 100.95 E-value: 6.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 72 VRPGECFGLLGVNGAGKTTTFKMLTGDEST---TGGEAFIGGSSILKELlrvQQSIGYCPQFDALFEDLTAREHLELYTR 148
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSF---QRSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 149 LR---GIPWKDEERVVSWALEKLELSKYADMPAGTYSGG----NKRKLSTAIALIGYP-SLVFLDEPTTGMDPKARRFLW 220
Cdd:TIGR00956 863 LRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSIC 942
|
170
....*....|....*...
gi 641957197 221 NLILDILKTGRSVVLTSH 238
Cdd:TIGR00956 943 KLMRKLADHGQAILCTIH 960
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
62-257 |
8.22e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.09 E-value: 8.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 62 ILAVDRLCLG---------VRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIlkELLRVQQS----IGYCP 128
Cdd:COG1129 256 VLEVEGLSVGgvvrdvsfsVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV--RIRSPRDAiragIAYVP 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 129 ---QFDALFEDLTARE-----HLELYTRLRGIPWKDEERVVSWALEKLELsKYADM--PAGTYSGGNKRKLSTAIALIGY 198
Cdd:COG1129 334 edrKGEGLVLDLSIREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRI-KTPSPeqPVGNLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 641957197 199 PSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGR 471
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
45-257 |
1.16e-23 |
|
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: 95.68 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRK-----------------MGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAF 107
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 108 IGG--SSILkellrvqqSIGYcpqfdALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGN 185
Cdd:cd03220 81 VRGrvSSLL--------GLGG-----GFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641957197 186 KRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
45-257 |
1.61e-23 |
|
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: 95.71 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKMgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL----KELLRV 120
Cdd:cd03256 1 IEVENLSKTYPNGKK----ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 121 QQSIGYCPQFDALFEDLTAREHLeLYTRL------RGI--PWKDEERVVSW-ALEKLELSKYADMPAGTYSGGNKRKLST 191
Cdd:cd03256 77 RRQIGMIFQQFNLIERLSVLENV-LSGRLgrrstwRSLfgLFPKEEKQRALaALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641957197 192 AIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
45-263 |
3.83e-23 |
|
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: 94.71 E-value: 3.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRvQQSI 124
Cdd:cd03296 3 IEVRNVSKRF-----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREH----LELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPS 200
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641957197 201 LVFLDEPTTGMDPKARRFLWNLILDIL-KTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGS 263
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
45-264 |
3.87e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.50 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKE---LLRVQ 121
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvkLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYCPQFD--ALFEDlTAREHLELYTRLRGIPWKDEERVVSWALE--KLELSKYADMPAGTYSGGNKRKLSTAIALIG 197
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641957197 198 YPSLVFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSI 264
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
74-257 |
6.73e-23 |
|
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: 93.13 E-value: 6.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 74 PGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGG----SSILKELLRVQQ-SIGYCPQFDALFEDLTAREHLEL-YT 147
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfDSRKKINLPPQQrKIGLVFQQYALFPHLNVRENLAFgLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 148 RLRGIPWKDEERVVswaLEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDIL 227
Cdd:cd03297 102 RKRNREDRISVDEL---LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIK 178
|
170 180 190
....*....|....*....|....*....|.
gi 641957197 228 KT-GRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03297 179 KNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
45-257 |
1.04e-22 |
|
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: 93.86 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSR-------------------KMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGE 105
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgkskeeilkKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 106 AFIGGSSIL----KELLRVQ-QSIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGT 180
Cdd:cd03294 81 VLIDGQDIAamsrKELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641957197 181 YSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDIL-KTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQaELQKTIVFITHDLDEALRLGDRIAIMKDGR 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
41-258 |
1.81e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.24 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 41 DNDMLKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIlkELLRV 120
Cdd:COG1129 1 AEPLLEMRGISKSF-----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV--RFRSP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 121 QQS----IGYCPQFDALFEDLTAREHL---ELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAI 193
Cdd:COG1129 74 RDAqaagIAIIHQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 194 ALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRF 258
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
44-257 |
3.34e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 93.99 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL----KELLR 119
Cdd:COG1135 1 MIELENLSKTFPTKG-GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalseRELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSIGYCPQFDALFEDLTAREHLELYTRLRGIPwKDE--ERVvswaLEKLE---LSKYADmpagTY----SGGNKRKLS 190
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVP-KAEirKRV----AELLElvgLSDKAD----AYpsqlSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641957197 191 TAIALIGYPSLVFLDEPTTGMDPKARRflwnLILDILK-----TGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTR----SILDLLKdinreLGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
49-241 |
3.60e-22 |
|
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: 91.32 E-value: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 49 NLTKVYKsrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK------ELLRvqQ 122
Cdd:cd03292 5 NVTKTYP----NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraiPYLR--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 SIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELS-KYADMPAGtYSGGNKRKLSTAIALIGYPSL 201
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLShKHRALPAE-LSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 641957197 202 VFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSME 241
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKE 197
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
62-258 |
4.06e-22 |
|
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: 90.18 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 62 ILAVDRLCLG---------VRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI--LKELLRVQQSIGYCP-- 128
Cdd:cd03215 4 VLEVRGLSVKgavrdvsfeVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAGIAYVPed 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 129 -QFDALFEDLTAREHLELYTRLrgipwkdeervvswaleklelskyadmpagtySGGNKRKLSTAIALIGYPSLVFLDEP 207
Cdd:cd03215 84 rKREGLVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 641957197 208 TTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRF 258
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
64-272 |
6.90e-22 |
|
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: 94.83 E-value: 6.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 64 AVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIlKELLR--VQQSIGYCPQFDALFEDlTARE 141
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL-RDLDEddLRRRIAVVPQRPHLFDT-TLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 142 HLelytRLrGIPWKDEERVVSwALEKLELSKY-ADMPAG----------TYSGGNKRKLSTAIALIGYPSLVFLDEPTTG 210
Cdd:COG4987 428 NL----RL-ARPDATDEELWA-ALERVGLGDWlAALPDGldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641957197 211 MDPKARRFLWNLILDILKtGRSVVLTSHSMEECEAlCTRLGIMVNGRFKCLGSIQHLKNRSE 272
Cdd:COG4987 502 LDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
19-238 |
1.41e-21 |
|
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: 93.75 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 19 QPIEDDDEDVASERRRvLRGEadndmLKIDNLTKVYKSRKmgrILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGD 98
Cdd:COG2274 454 LPPEREEGRSKLSLPR-LKGD-----IELENVSFRYPGDS---PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 99 ESTTGGEAFIGG---SSILKELLRvqQSIGYCPQFDALFEDlTAREHLELytrlrGIPWKDEERVVsWALEKLELSKY-A 174
Cdd:COG2274 525 YEPTSGRILIDGidlRQIDPASLR--RQIGVVLQDVFLFSG-TIRENITL-----GDPDATDEEII-EAARLAGLHDFiE 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641957197 175 DMPAG----------TYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKtGRSVVLTSH 238
Cdd:COG2274 596 ALPMGydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAH 668
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
62-257 |
2.07e-21 |
|
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: 89.57 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 62 ILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIlKEL----LRvqQSIGYCPQFDALFEDl 137
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI-RQLdpadLR--RNIGYVPQDVTLFYG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 138 TAREHLELytrlrGIPWKDEERVVSwALEKLELSKYA-------DMPAG----TYSGGNKRKLSTAIALIGYPSLVFLDE 206
Cdd:cd03245 93 TLRDNITL-----GAPLADDERILR-AAELAGVTDFVnkhpnglDLQIGergrGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 641957197 207 PTTGMDPKA-RRFLWNliLDILKTGRSVVLTSH--SMEEceaLCTRLGIMVNGR 257
Cdd:cd03245 167 PTSAMDMNSeERLKER--LRQLLGDKTLIIITHrpSLLD---LVDRIIVMDSGR 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
64-257 |
4.46e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 89.75 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 64 AVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI---LKELLRVQQSIGYCPQF--DALFEDlT 138
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydKKSLLEVRKTVGIVFQNpdDQLFAP-T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 139 AREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRF 218
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 641957197 219 LWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK13639 176 IMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGK 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
44-238 |
4.96e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 87.94 E-value: 4.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTkvykSRKMGRILaVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQS 123
Cdd:PRK13538 1 MLEARNLA----CERDERIL-FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQFDALFEDLTAREHLELYTRLRGIPwkDEERVVSwALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVF 203
Cdd:PRK13538 76 LLYLGHQPGIKTELTALENLRFYQRLHGPG--DDEALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*
gi 641957197 204 LDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSH 238
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
45-257 |
7.64e-21 |
|
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: 86.33 E-value: 7.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIlkellrvqqsi 124
Cdd:cd03216 1 LELRGITKRF-----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 gycpQFDALFEdltAREHlelytrlrGIpwkdeeRVVSwaleklelskyadmpagTYSGGNKRKLSTAIALIGYPSLVFL 204
Cdd:cd03216 65 ----SFASPRD---ARRA--------GI------AMVY-----------------QLSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 641957197 205 DEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
47-238 |
1.82e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 47 IDNLTKVYKSRKmgrILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGssilkellrvQQSIGY 126
Cdd:COG0488 1 LENLSKSFGGRP---LL--DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----------GLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 127 CPQFDALFEDLTAREHL--------ELYTRLRGI------PWKDEERVVS----------WALE--------KLELSK-Y 173
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVldgdaelrALEAELEELeaklaePDEDLERLAElqeefealggWEAEaraeeilsGLGFPEeD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 174 ADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTgrsVVLTSH 238
Cdd:COG0488 146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGT---VLVVSH 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
44-257 |
1.82e-20 |
|
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: 88.57 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTG---DESTTGGEAFIGGSSIL----KE 116
Cdd:COG0444 1 LLEVRNLKVYFPTRR-GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLklseKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 117 LLRV-QQSIGYCPQ--FDALfeD--LTAREHL-ELYTRLRGIPWKD-EERVVSwALEKLELS---KYADMPAGTYSGGNK 186
Cdd:COG0444 80 LRKIrGREIQMIFQdpMTSL--NpvMTVGDQIaEPLRIHGGLSKAEaRERAIE-LLERVGLPdpeRRLDRYPHELSGGMR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641957197 187 RKLSTAIALIGYPSLVFLDEPTTGMDP--KARrflwnlILDILK-----TGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVtiQAQ------ILNLLKdlqreLGLAILFITHDLGVVAEIADRVAVMYAGR 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
44-257 |
2.29e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 88.70 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL----KELLR 119
Cdd:PRK11153 1 MIELKNISKVFPQGG-RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalseKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYAD-MPAgTYSGGNKRKLSTAIALIGY 198
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADrYPA-QLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641957197 199 PSLVFLDEPTTGMDPKARRflwnLILDILKT-----GRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK11153 159 PKVLLCDEATSALDPATTR----SILELLKDinrelGLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
64-242 |
2.81e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 64 AVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSilkellrvqqSIGYCPQFDALFEDL--TARE 141
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA----------RVAYVPQRSEVPDSLplTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 142 HLELYTRLRGIPW----KDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARR 217
Cdd:NF040873 77 LVAMGRWARRGLWrrltRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180
....*....|....*....|....*
gi 641957197 218 FLWNLILDILKTGRSVVLTSHSMEE 242
Cdd:NF040873 157 RIIALLAEEHARGATVVVVTHDLEL 181
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
62-258 |
4.92e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.95 E-value: 4.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 62 ILAVDRLC--------LGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI--LKELLRVQQSIGYCP--- 128
Cdd:PRK15439 268 VLTVEDLTgegfrnisLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPedr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 129 QFDALFEDLTAREHLELYTRLRGIPWKDEERvvswalEKLELSKY----------ADMPAGTYSGGNKRKLSTAIALIGY 198
Cdd:PRK15439 348 QSSGLYLDAPLAWNVCALTHNRRGFWIKPAR------ENAVLERYrralnikfnhAEQAARTLSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 199 PSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRF 258
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
44-242 |
7.27e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.71 E-value: 7.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIG-----GSSILKELL 118
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 119 RVQQSIGYCPQF--DALFEDlTAREHLELYTRLRGIPWKDEERVVSWALEKLELSK-YADMPAGTYSGGNKRKLSTAIAL 195
Cdd:PRK13643 81 PVRKKVGVVFQFpeSQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 641957197 196 IGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEE 242
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDD 206
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
44-250 |
9.32e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 85.18 E-value: 9.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKMG--RILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFI--GGSSI-L---- 114
Cdd:COG4778 4 LLEVENLSKTFTLHLQGgkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdLaqas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 115 -KELLRV-QQSIGYCPQF--------------DALFEDLTAREH-----LELYTRLrGIPwkdeERVvsWALeklelsky 173
Cdd:COG4778 84 pREILALrRRTIGYVSQFlrviprvsaldvvaEPLLERGVDREEararaRELLARL-NLP----ERL--WDL-------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641957197 174 admPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRL 250
Cdd:COG4778 149 ---PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRV 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
44-269 |
1.13e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKvyksrKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI--LKELLRVQ 121
Cdd:PRK09700 5 YISMAGIGK-----SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYCPQFDALFEDLTAREHL---ELYTR-LRGIP---WKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIA 194
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLyigRHLTKkVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 195 LIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKN 269
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
44-257 |
1.54e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKMgrilaVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL----KELLR 119
Cdd:PRK11231 2 TLRTENLTVGYGTKRI-----LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmlssRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 vqqSIGYCPQFDALFEDLTARE--------HLELYTRLRGipwKDEERVvSWALEKLELSKYADMPAGTYSGGNKRKLST 191
Cdd:PRK11231 77 ---RLALLPQHHLTPEGITVRElvaygrspWLSLWGRLSA---EDNARV-NQAMEQTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 192 AIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
44-262 |
1.69e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLtkvykSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLR-VQQ 122
Cdd:PRK09536 3 MIDVSDL-----SVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARaASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 SIGYCPQFDALFEDLTAREHLELYT---RLRGIPW-KDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGY 198
Cdd:PRK09536 78 RVASVPQDTSLSFEFDVRQVVEMGRtphRSRFDTWtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 199 PSLVFLDEPTTGMD-PKARRFLwNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLG 262
Cdd:PRK09536 158 TPVLLLDEPTASLDiNHQVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
68-239 |
3.80e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 68 LCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIlkELLRVQQSIGYCPQFDALFEDLTAREHLELYT 147
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 148 RLRGipwkDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDIL 227
Cdd:PRK13539 99 AFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHL 174
|
170
....*....|..
gi 641957197 228 KTGRSVVLTSHS 239
Cdd:PRK13539 175 AQGGIVIAATHI 186
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
44-253 |
4.97e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 83.76 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKellrvqqs 123
Cdd:COG4525 3 MLTVRHVSVRYPGGG-QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 igycP--------QFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIAL 195
Cdd:COG4525 74 ----PgadrgvvfQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 641957197 196 IGYPSLVFLDEPTTGMDPKARRFLWNLILDIL-KTGRSVVLTSHSMEECEALCTRLGIM 253
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVWqRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
73-238 |
5.56e-19 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 86.44 E-value: 5.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 73 RPGECFGLLGVNGAGKTTTFKMLTGDEstTGGeaFIGGSSILKELLRVQQSI----GYCPQFDALFEDLTAREHL--ELY 146
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRK--TGG--YIEGDIRISGFPKKQETFarisGYCEQNDIHSPQVTVRESLiySAF 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 147 TRLRGIPWKDEE-RVVSWALEKLELSKYAD----MPAGT-YSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLW 220
Cdd:PLN03140 980 LRLPKEVSKEEKmMFVDEVMELVELDNLKDaivgLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
170
....*....|....*...
gi 641957197 221 NLILDILKTGRSVVLTSH 238
Cdd:PLN03140 1060 RTVRNTVDTGRTVVCTIH 1077
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
41-242 |
5.64e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.98 E-value: 5.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 41 DNDMLKIDNLTKVYKSRKMG-RILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGG--SSILKEL 117
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEEStEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 118 LRVQQSIGYCPQ------FDALFEDLTA--REHLelytrlrGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKL 189
Cdd:PRK13633 81 WDIRNKAGMVFQnpdnqiVATIVEEDVAfgPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 641957197 190 STAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEE 242
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEE 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
73-267 |
7.24e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.87 E-value: 7.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 73 RPGECFGLLGVNGAGKTT-----TFKMLTGdeSTTGGEAFIGGSSILKELLRVQQsiGYCPQFDALFEDLTAREHLELYT 147
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTlmnalAFRSPKG--VKGSGSVLLNGMPIDAKEMRAIS--AYVQQDDLFIPTLTVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 148 RLR---GIPWKDEERVVSWALEKLELSKYADMPAGT------YSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPkarrF 218
Cdd:TIGR00955 125 HLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS----F 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 219 LWNLILDILK----TGRSVVLTSH--SMEECEaLCTRLGIMVNGRFKCLGSIQHL 267
Cdd:TIGR00955 201 MAYSVVQVLKglaqKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQA 254
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
42-250 |
7.24e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.89 E-value: 7.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLTKVYKSRKMgrilaVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGgssilkellrVQ 121
Cdd:COG0488 313 KKVLELEGLSKSYGDKTL-----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----------ET 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYCPQ-FDALFEDLTAREHLElytrlRGIPWKDEERVVSWaLEKLELS-KYADMPAGTYSGGNKRKLSTAIALIGYP 199
Cdd:COG0488 378 VKIGYFDQhQEELDPDKTVLDELR-----DGAPGGTEQEVRGY-LGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 641957197 200 SLVFLDEPTTGMDPKARrflwNLILDILKT--GrSVVLTSHSMEECEALCTRL 250
Cdd:COG0488 452 NVLLLDEPTNHLDIETL----EALEEALDDfpG-TVLLVSHDRYFLDRVATRI 499
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
45-257 |
8.83e-19 |
|
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: 80.89 E-value: 8.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmgrILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK---ELLRvq 121
Cdd:cd03228 1 IEFKNVSFSYPGRP---KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDldlESLR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYCPQFDALFEDlTAREHLelytrlrgipwkdeervvswaleklelskyadmpagtYSGGNKRKLSTAIALIGYPSL 201
Cdd:cd03228 76 KNIAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 202 VFLDEPTTGMDPKARRFLWNLILDILKtGRSVVLTSHSMEECEaLCTRLGIMVNGR 257
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
44-257 |
1.89e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.06 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL--KELLR-V 120
Cdd:PRK09493 1 MIEFKNVSKHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERlI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 121 QQSIGYCPQFDALFEDLTAREHLEL-YTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYP 199
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 641957197 200 SLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
45-240 |
3.05e-18 |
|
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: 80.65 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL---KELLRVQ 121
Cdd:cd03262 1 IEIKNLHKSFGDFH-----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYCPQFDALFEDLTAREHLEL-YTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPS 200
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 641957197 201 LVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSM 240
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEM 195
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
60-244 |
3.23e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.02 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 60 GRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLR--VQQSIGYCPQF--DALFE 135
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRraVCPRIAYMPQGlgKNLYP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 136 DLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKA 215
Cdd:NF033858 92 TLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 171
|
170 180 190
....*....|....*....|....*....|.
gi 641957197 216 RRFLWNLILDILKT--GRSVVLTSHSMEECE 244
Cdd:NF033858 172 RRQFWELIDRIRAErpGMSVLVATAYMEEAE 202
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
79-271 |
4.86e-18 |
|
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: 82.47 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 79 GLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRV-----QQSIGYCPQFDALFEDLTAREHLEL-YTRLRGi 152
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppeKRRIGYVFQEARLFPHLSVRGNLRYgMKRARP- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 153 pwkdEERVVSWA--LEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARR----FLWNLILDI 226
Cdd:TIGR02142 106 ----SERRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYeilpYLERLHAEF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 641957197 227 lktGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKNRS 271
Cdd:TIGR02142 182 ---GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
44-257 |
7.81e-18 |
|
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: 82.57 E-value: 7.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKvyksrKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTG--DESTTGGEAFIGGSSILKELLRVQ 121
Cdd:TIGR02633 1 LLEMKGIVK-----TFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKASNIRDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYC--PQFDALFEDLTAREHLELYTR--LRGIPWKDEERVVSWA--LEKLELSKYAD-MPAGTYSGGNKRKLSTAIA 194
Cdd:TIGR02633 76 ERAGIViiHQELTLVPELSVAENIFLGNEitLPGGRMAYNAMYLRAKnlLRELQLDADNVtRPVGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 195 LIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
65-257 |
1.47e-17 |
|
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: 78.03 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 65 VDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGG---SSILKELLRVQqsIGYCPQFDALFEDlTARE 141
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadiSQWDPNELGDH--VGYLPQDDELFSG-SIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 142 HLelytrlrgipwkdeervvswaleklelskyadmpagtYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWN 221
Cdd:cd03246 95 NI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 641957197 222 LILDILKTGRSVVLTSHSMEECEAlCTRLGIMVNGR 257
Cdd:cd03246 138 AIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
64-267 |
1.90e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.89 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 64 AVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI---LKELLRVQQSIGYCPQ------FDA-L 133
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQdpdnqlFSAsV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 134 FEDLTarehlelYTRLR-GIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMD 212
Cdd:PRK13636 101 YQDVS-------FGAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 213 PKARRFLWNLILDILK-TGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHL 267
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKeLGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
45-259 |
2.02e-17 |
|
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: 77.74 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKMgriLAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGS--SILKELLRvqQ 122
Cdd:cd03247 1 LSINNVSFSYPEQEQ---QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvSDLEKALS--S 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 SIGYCPQFDALFeDLTAREHLelytrlrGIPwkdeervvswaleklelskyadmpagtYSGGNKRKLSTAIALIGYPSLV 202
Cdd:cd03247 76 LISVLNQRPYLF-DTTLRNNL-------GRR---------------------------FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 641957197 203 FLDEPTTGMDPKARRFLWNLILDILKtGRSVVLTSHSMEECEALcTRLGIMVNGRFK 259
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
80-272 |
3.76e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.08 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 80 LLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLR-VQQSIGYCPQF--DALFEDlTAREHLELYTRLRGIpwkD 156
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIReVRKFVGLVFQNpdDQIFSP-TVEQDIAFGPINLGL---D 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 157 EERV---VSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKT-GRS 232
Cdd:PRK13652 111 EETVahrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMT 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 641957197 233 VVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKNRSE 272
Cdd:PRK13652 191 VIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
50-269 |
6.72e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 79.69 E-value: 6.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 50 LTKVYKSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK----ELLRVQ-QSI 124
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaELREVRrKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFL 204
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 205 DEPTTGMDPKARRFLWNLILDI-LKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKN 269
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
64-239 |
8.03e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 79.71 E-value: 8.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 64 AVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK----ELLRVqqsIGYCPQFDALFeDLTA 139
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSldqdEVRRR---VSVCAQDAHLF-DTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 140 REHLELytrlrGIPWKDEERVvSWALEKLELSKY-ADMPAG----------TYSGGNKRKLSTAIALIGYPSLVFLDEPT 208
Cdd:TIGR02868 426 RENLRL-----ARPDATDEEL-WAALERVGLADWlRALPDGldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|.
gi 641957197 209 TGMDPKARRFLWNLILDILkTGRSVVLTSHS 239
Cdd:TIGR02868 500 EHLDAETADELLEDLLAAL-SGRTVVLITHH 529
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
44-257 |
9.28e-17 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 77.54 E-value: 9.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKS----RKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKelLR 119
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQ--LD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSIGYCPQFDALFED--------LTAR----EHLELYTRLRGipwKDEERVVSWALEKLEL-SKYADMPAGTYSGGNK 186
Cdd:TIGR02769 80 RKQRRAFRRDVQLVFQDspsavnprMTVRqiigEPLRHLTSLDE---SEQKARIAELLDMVGLrSEDADKLPRQLSGGQL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 187 RKLSTAIALIGYPSLVFLDEPTTGMDpkarRFLWNLILDILKT-----GRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRKlqqafGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
40-241 |
1.15e-16 |
|
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: 79.42 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 40 ADNDMLKIDNLTKVYKSRKmgriLAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGG---SSILKE 116
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGR----PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlSDLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 117 LLRvqQSIGYCPQFDALFEDlTAREHLELYTrlrgiPWKDEERVVSwALEKLELSKY-ADMPAG----------TYSGGN 185
Cdd:COG4988 408 SWR--RQIAWVPQNPYLFAG-TIRENLRLGR-----PDASDEELEA-ALEAAGLDEFvAALPDGldtplgeggrGLSGGQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 186 KRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKtGRSVVLTSHSME 241
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLA 533
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
67-238 |
2.33e-16 |
|
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: 75.22 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 67 RLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQSIGYCPQFDALFEDLTAREHLELY 146
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 147 TRLRGipwkDEErvVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDI 226
Cdd:cd03231 98 HADHS----DEQ--VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170
....*....|..
gi 641957197 227 LKTGRSVVLTSH 238
Cdd:cd03231 172 CARGGMVVLTTH 183
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
42-217 |
3.19e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 77.45 E-value: 3.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLTKvyksrKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRvQ 121
Cdd:PRK11432 4 KNFVVLKNITK-----RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYCPQFDALFEDLTAREHLELYTRLRGIPwKDEERV-VSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPS 200
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVP-KEERKQrVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170
....*....|....*..
gi 641957197 201 LVFLDEPTTGMDPKARR 217
Cdd:PRK11432 157 VLLFDEPLSNLDANLRR 173
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
41-257 |
3.52e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 76.18 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 41 DNDMLKIDNLTKVYKSRKMgriLAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLR- 119
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEN---NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSIGYCPQF-DALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGY 198
Cdd:PRK13632 81 IRKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 199 PSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLT-SHSMEECeALCTRLGIMVNGR 257
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGK 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-241 |
4.66e-16 |
|
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: 77.33 E-value: 4.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 17 SSQPIEDDDEDVASERRRVlrGEADNDMLKIDNLTKVYKsrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLT 96
Cdd:TIGR02857 296 ALFAVLDAAPRPLAGKAPV--TAAPASSLEFSGVSVAYP----GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 97 GDESTTGGEAFIGGSSiLKELLR--VQQSIGYCPQFDALFEDlTAREHLELYTrlrgiPWKDEERVVSwALEKLELSKY- 173
Cdd:TIGR02857 370 GFVDPTEGSIAVNGVP-LADADAdsWRDQIAWVPQHPFLFAG-TIAENIRLAR-----PDASDAEIRE-ALERAGLDEFv 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 174 ADMPAGTY----------SGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARrflwNLILDILK---TGRSVVLTSHSM 240
Cdd:TIGR02857 442 AALPQGLDtpigeggaglSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE----AEVLEALRalaQGRTVLLVTHRL 517
|
.
gi 641957197 241 E 241
Cdd:TIGR02857 518 A 518
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
75-256 |
4.93e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 75 GECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLrvQQSIGYCPQ-------FDALFEDLTAREHLELYT 147
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ--KNLVAYVPQseevdwsFPVLVEDVVMMGRYGHMG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 148 RLRgIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDIL 227
Cdd:PRK15056 111 WLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELR 189
|
170 180
....*....|....*....|....*....
gi 641957197 228 KTGRSVVLTSHSMEECEALCTrLGIMVNG 256
Cdd:PRK15056 190 DEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
42-257 |
1.59e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.76 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK-ELLRV 120
Cdd:PRK11614 3 KVMLSFDKVSAHY-----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 121 -QQSIGYCPQFDALFEDLTAREHLELytrlrGIPWKDEERV---VSWALEKL-ELSKYADMPAGTYSGGNKRKLSTAIAL 195
Cdd:PRK11614 78 mREAVAIVPEGRRVFSRMTVEENLAM-----GGFFAERDQFqerIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641957197 196 IGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
70-264 |
1.88e-15 |
|
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: 73.65 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 70 LGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK---ELLRVQQSIgycpqfdALFEDLTAREHLELY 146
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpDRMVVFQNY-------SLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 147 TR--LRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLIL 224
Cdd:TIGR01184 79 VDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 641957197 225 DILKTGR-SVVLTSHSMEECEALCTRLGIMVNGRFKCLGSI 264
Cdd:TIGR01184 159 QIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
44-218 |
1.91e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 74.00 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRkmgRILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI----LKELLR 119
Cdd:COG4559 1 MLEAENLSVRLGGR---TLL--DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaawsPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 V-----QQSigycpqfdALFEDLTAREHLelytRLRGIPW----KDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLS 190
Cdd:COG4559 76 RravlpQHS--------SLAFPFTVEEVV----ALGRAPHgssaAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQ 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 641957197 191 TAIALI-------GYPSLVFLDEPTTGMDPK--------ARRF 218
Cdd:COG4559 144 LARVLAqlwepvdGGPRWLFLDEPTSALDLAhqhavlrlARQL 186
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
44-269 |
1.96e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.89 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKMgrILAVDrlcLGVRPGECFGLLGVNGAGKTTTFK----MLTGDESTTGGEAFIGGS-----SIL 114
Cdd:PRK09984 4 IIRVEKLAKTFNQHQA--LHAVD---LNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRTvqregRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 115 KELLRVQQSIGYCPQFDALFEDLTAREHLeLYTRLRGIP-WKDeerVVSW-----------ALEKLELSKYADMPAGTYS 182
Cdd:PRK09984 79 RDIRKSRANTGYIFQQFNLVNRLSVLENV-LIGALGSTPfWRT---CFSWftreqkqralqALTRVGMVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 183 GGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCTRLGIMVNGRFKCL 261
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
....*...
gi 641957197 262 GSIQHLKN 269
Cdd:PRK09984 235 GSSQQFDN 242
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
44-240 |
2.02e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.37 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYksrkMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK----ELLR 119
Cdd:PRK10908 1 MIRFEHVSKAY----LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrEVPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYP 199
Cdd:PRK10908 77 LRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 641957197 200 SLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSM 240
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
43-272 |
2.45e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.00 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 43 DMLKIDNLTKVYKSRKMGRILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKE-LLRVQ 121
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQEKYTL--NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYCPQF-DALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPS 200
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 201 LVFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECeALCTRLGIMVNGRFKCLGSIQHLKNRSE 272
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
45-263 |
3.61e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.21 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL------KELL 118
Cdd:PRK09452 15 VELRGISKSFDGKE-----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThvpaenRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 119 RVQQSigYcpqfdALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGY 198
Cdd:PRK09452 90 TVFQS--Y-----ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641957197 199 PSLVFLDEPTTGMDPKARRFLWNLiLDIL--KTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGS 263
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNE-LKALqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-258 |
3.90e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.68 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 26 EDVASERRRVlRGEADNDMLKIDNLTkVYKSRKmgrILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGE 105
Cdd:COG3845 240 REVLLRVEKA-PAEPGEVVLEVENLS-VRDDRG---VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 106 AFIGGSSILKE--LLRVQQSIGYCP---QFDALFEDLTAREHLELyTRLRGIP-----WKDEERVVSWALEKLElsKY-- 173
Cdd:COG3845 315 IRLDGEDITGLspRERRRLGVAYIPedrLGRGLVPDMSVAENLIL-GRYRRPPfsrggFLDRKAIRAFAEELIE--EFdv 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 174 ----ADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTR 249
Cdd:COG3845 392 rtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDR 471
|
....*....
gi 641957197 250 LGIMVNGRF 258
Cdd:COG3845 472 IAVMYEGRI 480
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
68-241 |
4.84e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.12 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 68 LCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI---LKELLRVQQSIGYC---PQFDALFEDLTARE 141
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVfqdPEQQIFYTDIDSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 142 HLELytRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWN 221
Cdd:PRK13638 100 AFSL--RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIA 177
|
170 180
....*....|....*....|
gi 641957197 222 LILDILKTGRSVVLTSHSME 241
Cdd:PRK13638 178 IIRRIVAQGNHVIISSHDID 197
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
45-258 |
5.14e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.18 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGG---------SSILK 115
Cdd:PRK11288 5 LSFDGIGKTFPGVK-----ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfasttAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 116 ELLRVQQSIGYCPqfdalfeDLTAREHL---ELYTRLrgiPWKDEERVVSWALEKLE---LSKYADMPAGTYSGGNKRKL 189
Cdd:PRK11288 80 GVAIIYQELHLVP-------EMTVAENLylgQLPHKG---GIVNRRLLNYEAREQLEhlgVDIDPDTPLKYLSIGQRQMV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641957197 190 STAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRF 258
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
44-212 |
7.14e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.77 E-value: 7.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKMGRILAVDrLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGG------SSILKEL 117
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHN-VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 118 LRVQQsIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIG 197
Cdd:PRK11629 84 LRNQK-LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170
....*....|....*
gi 641957197 198 YPSLVFLDEPTTGMD 212
Cdd:PRK11629 163 NPRLVLADEPTGNLD 177
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
47-263 |
7.32e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.73 E-value: 7.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 47 IDNLTKVYKSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI------LKELLRV 120
Cdd:PRK13645 9 LDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 121 QQSIGYCPQFD--ALFEDLTARE------HLElytrlrgipwKDEERVVSWALEKLEL----SKYADMPAGTYSGGNKRK 188
Cdd:PRK13645 89 RKEIGLVFQFPeyQLFQETIEKDiafgpvNLG----------ENKQEAYKKVPELLKLvqlpEDYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641957197 189 LSTA--IALIGypSLVFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGS 263
Cdd:PRK13645 159 VALAgiIAMDG--NTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
77-239 |
7.46e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 72.18 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 77 CFGLLGVNGAGKTT---TFKMLT--GDESTTGGEAFIGGSSILKE---LLRVQQSIGYCPQFDALFEDLTAREHLELYTR 148
Cdd:PRK14267 32 VFALMGPSGCGKSTllrTFNRLLelNEEARVEGEVRLFGRNIYSPdvdPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 149 LRGI--PWKDEERVVSWALEKLEL-----SKYADMPaGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWN 221
Cdd:PRK14267 112 LNGLvkSKKELDERVEWALKKAALwdevkDRLNDYP-SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEE 190
|
170
....*....|....*...
gi 641957197 222 LILDiLKTGRSVVLTSHS 239
Cdd:PRK14267 191 LLFE-LKKEYTIVLVTHS 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
60-238 |
8.41e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 71.87 E-value: 8.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 60 GRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTG-----DESTTGGEAFIGGSSILK----ELLRVQQSIGYCPQf 130
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKmdviELRRRVQMVFQIPN- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 131 daLFEDLTAREHLELYTRL-RGIPWKDE-ERVVSWALEKLEL----SKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFL 204
Cdd:PRK14247 93 --PIPNLSIFENVALGLKLnRLVKSKKElQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190
....*....|....*....|....*....|....
gi 641957197 205 DEPTTGMDPKARRFLWNLILDiLKTGRSVVLTSH 238
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLE-LKKDMTIVLVTH 203
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
70-259 |
8.80e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.73 E-value: 8.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 70 LGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI--LKELLRVQ---QSIGYCPQFDALFEDLTAREHLE 144
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqMDEEARAKlraKHVGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 145 LYTRLRGIPWKDEERVVSWALEKLELSKYAD-MPAgTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLI 223
Cdd:PRK10584 111 LPALLRGESSRQSRNGAKALLEQLGLGKRLDhLPA-QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 641957197 224 LDILKT-GRSVVLTSHSmEECEALCTRLGIMVNGRFK 259
Cdd:PRK10584 190 FSLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
45-238 |
1.13e-14 |
|
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: 69.40 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKmgrILAVDRLclGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSsilkellrvqQSI 124
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISL--TINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------VKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFdalfedltarehlelytrlrgipwkdeervvswaleklelskyadmpagtySGGNKRKLSTAIALIGYPSLVFL 204
Cdd:cd03221 66 GYFEQL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190
....*....|....*....|....*....|....
gi 641957197 205 DEPTTGMDPKARRFLWNLILDilkTGRSVVLTSH 238
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKE---YPGTVILVSH 125
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
41-241 |
1.33e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.19 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 41 DNDMLKIDNLTKVYKSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTT---FKML--------------TGDESTTG 103
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLvthFNGLikskygtiqvgdiyIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 104 GEAFIGGSSILKELLRVQQSIGYCPQFD--ALFEDlTAREHLELYTRLRGIPWKDEERVVSWALEKLEL-SKYADMPAGT 180
Cdd:PRK13631 98 ELITNPYSKKIKNFKELRRRVSMVFQFPeyQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFG 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641957197 181 YSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSME 241
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
72-256 |
2.66e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 72 VRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI--LKELLRVQQSIGYCPQFDALFEDLTAREHLelytrL 149
Cdd:PRK15439 34 LHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarLTPAKAHQLGIYLVPQEPLLFPNLSVKENI-----L 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 150 RGIPWK-DEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILK 228
Cdd:PRK15439 109 FGLPKRqASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA 188
|
170 180
....*....|....*....|....*...
gi 641957197 229 TGRSVVLTSHSMEECEALCTRLGIMVNG 256
Cdd:PRK15439 189 QGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
44-257 |
2.91e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.50 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI--LKE----- 116
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtkLPEykrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 117 -LLRVQQ--SIGYCPqfdalfeDLTAREHLEL-YTR------LRGIPWKDEERVVSwALEKLELS--KYADMPAGTYSGG 184
Cdd:COG1101 81 yIGRVFQdpMMGTAP-------SMTIEENLALaYRRgkrrglRRGLTKKRRELFRE-LLATLGLGleNRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641957197 185 NKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRsvvLTS----HSMEECEALCTRLGIMVNGR 257
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENN---LTTlmvtHNMEQALDYGNRLIMMHEGR 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
44-218 |
3.30e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.57 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRkmgRILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI----LKELLR 119
Cdd:PRK13548 2 MLEARNLSVRLGGR---TLL--DDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadwsPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 vqqSIGYCPQFDALFEDLTAREhlelYTRLRGIPW----KDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIAL 195
Cdd:PRK13548 77 ---RRAVLPQHSSLSFPFTVEE----VVAMGRAPHglsrAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 641957197 196 I------GYPSLVFLDEPTTGMDPK--------ARRF 218
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAhqhhvlrlARQL 186
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
44-257 |
4.68e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.60 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSsilkellRVQQS 123
Cdd:COG3845 5 ALELRGITKRF-----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK-------PVRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 ---------IGYCPQ-FdALFEDLTAREHLELY---TRLRGIPWKDEERVVSWALEKLELS-----KYADMPAGTysggn 185
Cdd:COG3845 73 sprdaialgIGMVHQhF-MLVPNLTVAENIVLGlepTKGGRLDRKAARARIRELSERYGLDvdpdaKVEDLSVGE----- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 186 KRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLwnliLDILKT----GRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEADEL----FEILRRlaaeGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
45-242 |
6.68e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.86 E-value: 6.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL-----KELLR 119
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSIGYCPQF--DALFEDlTAREHLELYTRLRGIPWKD-EERVVSWaLEKLELSK-YADMPAGTYSGGNKRKLSTAIAL 195
Cdd:PRK13641 83 LRKKVSLVFQFpeAQLFEN-TVLKDVEFGPKNFGFSEDEaKEKALKW-LKKVGLSEdLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 641957197 196 IGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEE 242
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDD 207
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
74-238 |
8.66e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 8.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 74 PGECFGLLGVNGAGKTTTFKMLTGDESTTG--GEAFIGGSSILKELLRvqqSIGYCPQFDALFEDLTAREHLELYTRLR- 150
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK---RTGFVTQDDILYPHLTVRETLVFCSLLRl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 151 --GIPWKDEERVVSWALEKLELSKYADMPAGT-----YSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLI 223
Cdd:PLN03211 170 pkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170
....*....|....*
gi 641957197 224 LDILKTGRSVVLTSH 238
Cdd:PLN03211 250 GSLAQKGKTIVTSMH 264
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
39-246 |
1.03e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.39 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 39 EADNDMLKIDNLTKVYKSRKMgriLAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI----L 114
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDAS---FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 115 KELLR---------VQQSIGYCPQFDALFedltareHLELYTrlrgIPWKDEERVVSWALEKLELSKYADMPAGTYSGGN 185
Cdd:PRK13648 79 EKLRKhigivfqnpDNQFVGSIVKYDVAF-------GLENHA----VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641957197 186 KRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDiLKTGRSVVLTSHSMEECEAL 246
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRK-VKSEHNITIISITHDLSEAM 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
45-256 |
1.30e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.04 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL-----KELLR 119
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSIGYCPQF--DALFEDLTAREhLELYTRLRGIpwkDEERVVSWALEKL-ELSKYAD-MPAGTY--SGGNKRKLSTAI 193
Cdd:PRK13646 83 VRKRIGMVFQFpeSQLFEDTVERE-IIFGPKNFKM---NLDEVKNYAHRLLmDLGFSRDvMSQSPFqmSGGQMRKIAIVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641957197 194 ALIGYPSLVFLDEPTTGMDPKARRFLWNLILDI-LKTGRSVVLTSHSMEECEALCTRLGIMVNG 256
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
39-267 |
1.77e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.85 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 39 EADNDMLKIDNLTKVYKSRKMgriLAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK--- 115
Cdd:PRK11160 333 AADQVSLTLNNVSFTYPDQPQ---PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyse 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 116 ELLRvqQSIGYCPQFDALFEDlTAREHLELytrlrGIPWKDEERVVSwALEKLELSKYADMPAG----------TYSGGN 185
Cdd:PRK11160 410 AALR--QAISVVSQRVHLFSA-TLRDNLLL-----AAPNASDEALIE-VLQQVGLEKLLEDDKGlnawlgeggrQLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 186 KRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKtGRSVVLTSH---SMEECEALCtrlgIMVNGRFKCLG 262
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHrltGLEQFDRIC----VMDNGQIIEQG 555
|
....*
gi 641957197 263 SIQHL 267
Cdd:PRK11160 556 THQEL 560
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
44-247 |
2.00e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKvyksrKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTG--DESTTGGEAFIGGSSI----LKEL 117
Cdd:PRK13549 5 LLEMKNITK-----TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFEGEELqasnIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 118 LRVQQSIGYcpQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWA---LEKLELSKYADMPAGTYSGGNKRKLSTAIA 194
Cdd:PRK13549 80 ERAGIAIIH--QELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAqklLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 641957197 195 LIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALC 247
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAIS 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
70-257 |
2.10e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 68.62 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 70 LGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL-----KELLRVQQSIGYCPQF--DALFEDlTAREH 142
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknKDIKQIRKKVGLVFQFpeSQLFEE-TVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 143 LELYTRLRGIPWKDEERVvswALEKLEL----SKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRF 218
Cdd:PRK13649 107 VAFGPQNFGVSQEEAEAL---AREKLALvgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 641957197 219 LWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK13649 184 LMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
41-257 |
2.42e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.03 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 41 DNDMLKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEA-FIGGSSILKELLR 119
Cdd:PRK11701 3 DQPLLSVRGLTKLY-----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSI---------GYCPQF--DALFEDLTAREHL-ElytRLRGIPWKD----EERVVSWaLEKLEL--SKYADMPAgTY 181
Cdd:PRK11701 78 LSEAErrrllrtewGFVHQHprDGLRMQVSAGGNIgE---RLMAVGARHygdiRATAGDW-LERVEIdaARIDDLPT-TF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 182 SGGNKRKLSTAIALIGYPSLVFLDEPTTGMD--PKARrflwnlILDILKT-----GRSVVLTSHSMEECEALCTRLGIMV 254
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQAR------LLDLLRGlvrelGLAVVIVTHDLAVARLLAHRLLVMK 226
|
...
gi 641957197 255 NGR 257
Cdd:PRK11701 227 QGR 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
39-259 |
2.70e-13 |
|
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: 69.47 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 39 EADNDMLKIDNLTKVYKSRKmgRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGD-ESTTGGEAFIGGS--SILK 115
Cdd:TIGR02633 252 EIGDVILEARNLTCWDVINP--HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKpvDIRN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 116 ELLRVQQSIGYCPQ---FDALFEDLTAREHLEL-----YTRLRGIPWKDEERVVSWALEKLELSKYA-DMPAGTYSGGNK 186
Cdd:TIGR02633 330 PAQAIRAGIAMVPEdrkRHGIVPILGVGKNITLsvlksFCFKMRIDAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 187 RKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFK 259
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
45-257 |
2.95e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.78 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRkmgRILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEaFIGGSSILKEllrvqqsi 124
Cdd:PRK11247 13 LLLNAVSKRYGER---TVL--NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPLAE-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 gycpqfdalfedltAREHlelyTRL-----RGIPWKdeeRVV---------SW---ALEKLE---LSKYA-DMPAgTYSG 183
Cdd:PRK11247 79 --------------ARED----TRLmfqdaRLLPWK---KVIdnvglglkgQWrdaALQALAavgLADRAnEWPA-ALSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 184 GNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDI-LKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK11247 137 GQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-257 |
3.05e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 10 YNRRVPVSSQPIEDDDEDVAsERRRVLRGEAdndMLKIDNLTKVYKSRK--MGRIL----AVDRLCLGVRPGECFGLLGV 83
Cdd:PRK10261 283 YPRRFPLISLEHPAKQEPPI-EQDTVVDGEP---ILQVRNLVTRFPLRSglLNRVTrevhAVEKVSFDLWPGETLSLVGE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 84 NGAGKTTTFKMLTGDESTTGGEAFIGGSSI-------LKELLRVQQSIgycpqFDALFEDLTAR--------EHLELYTR 148
Cdd:PRK10261 359 SGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspgkLQALRRDIQFI-----FQDPYASLDPRqtvgdsimEPLRVHGL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 149 LRGipwKDEERVVSWALEKLEL-SKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDIL 227
Cdd:PRK10261 434 LPG---KAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQ 510
|
250 260 270
....*....|....*....|....*....|.
gi 641957197 228 KT-GRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK10261 511 RDfGIAYLFISHDMAVVERISHRVAVMYLGQ 541
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
45-265 |
3.80e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.19 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQsI 124
Cdd:PRK10851 3 IEIANIKKSF-----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLELytRLRGIPWKDE------ERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGY 198
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAF--GLTVLPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641957197 199 PSLVFLDEPTTGMDPKA----RRFLWNLILDILKTGrsvVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQ 265
Cdd:PRK10851 155 PQILLLDEPFGALDAQVrkelRRWLRQLHEELKFTS---VFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
44-238 |
3.98e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.51 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRkmgriLAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQS 123
Cdd:PRK13540 1 MLDVIELDFDYHDQ-----PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQFDALFEDLTAREH--LELYTRLRGIPWKDEERVVSwalekleLSKYADMPAGTYSGGNKRKLSTAIALIGYPSL 201
Cdd:PRK13540 76 LCFVGHRSGINPYLTLRENclYDIHFSPGAVGITELCRLFS-------LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 641957197 202 VFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSH 238
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
44-258 |
4.48e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGE-AFIGGSSILKELLRVQQ 122
Cdd:PRK10762 4 LLQLKGIDKAFPGVK-----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSiLYLGKEVTFNGPKSSQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 S-IGYCPQFDALFEDLTAREHL----ELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIG 197
Cdd:PRK10762 79 AgIGIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641957197 198 YPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRF 258
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
44-245 |
5.74e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.97 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKMgrilaVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDES---TTGGEAFIGGSSILKelLRV 120
Cdd:COG4136 1 MLSLENLTITLGGRPL-----LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTA--LPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 121 QQ-SIGYCPQFDALFEDLTAREHLELYTRlRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYP 199
Cdd:COG4136 74 EQrRIGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 641957197 200 SLVFLDEPTTGMDP----KARRFLWNLILDilkTGRSVVLTSHSMEECEA 245
Cdd:COG4136 153 RALLLDEPFSKLDAalraQFREFVFEQIRQ---RGIPALLVTHDEEDAPA 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
54-257 |
6.62e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.01 E-value: 6.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 54 YKSRKMGRI-LAVDRL---------CLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLR--VQ 121
Cdd:PRK11288 248 YRPRPLGEVrLRLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdaIR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYCPQ---FDALFEDLTAREHLELYTRLRGIPW------KDEERVVSWALEKLEL-SKYADMPAGTYSGGNKRK--- 188
Cdd:PRK11288 328 AGIMLCPEdrkAEGIIPVHSVADNINISARRHHLRAgclinnRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKail 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641957197 189 ---LSTAIALIgypslvFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK11288 408 grwLSEDMKVI------LLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
63-240 |
7.41e-13 |
|
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: 66.36 E-value: 7.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 63 LAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGG---SSILKELLRVQqsIGYCPQFDALFeDLTA 139
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlALADPAWLRRQ--VGVVLQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 140 REHLELytrlrGIPWKDEERVVswaleklELSKYAD-------MPAG----------TYSGGNKRKLSTAIALIGYPSLV 202
Cdd:cd03252 93 RDNIAL-----ADPGMSMERVI-------EAAKLAGahdfiseLPEGydtivgeqgaGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 641957197 203 FLDEPTTGMDPKARRFLWNLILDILKtGRSVVLTSHSM 240
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRL 197
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
45-257 |
8.52e-13 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 65.57 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGssilkellrvqqSI 124
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDlTAREHLelytrLRGIPWkDEER----VVSWALEK-LELskyadMPAG----------TYSGGNKRKL 189
Cdd:cd03250 69 AYVSQEPWIQNG-TIRENI-----LFGKPF-DEERyekvIKACALEPdLEI-----LPDGdlteigekgiNLSGGQKQRI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641957197 190 STAIALIGYPSLVFLDEPTTGMDPKARRFLW-NLILDILKTGRSVVLTSHSMEECEAlCTRLGIMVNGR 257
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
75-269 |
9.11e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.19 E-value: 9.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 75 GECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI-------LKELLRVQQSIGYCPQFDALFEDLTAREHL-ELY 146
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktpsDKAIRELRRNVGMVFQQYNLWPHLTVQQNLiEAP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 147 TRLRGIpwkDEERVVSWA---LEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLI 223
Cdd:PRK11124 108 CRVLGL---SKDQALARAeklLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSII 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 641957197 224 LDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKN 269
Cdd:PRK11124 185 RELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
44-263 |
9.24e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.55 E-value: 9.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKMgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGG--SSILKELLRVQ 121
Cdd:PRK13644 1 MIRLENVSYSYPDGTP----ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidTGDFSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYCPQF-DALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPS 200
Cdd:PRK13644 77 KLVGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 201 LVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEAlCTRLGIMVNGRFKCLGS 263
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
42-270 |
1.28e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.30 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLTKVYKSRKMgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLR-V 120
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTK----ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 121 QQSIGYCPQF--DALFEDlTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGY 198
Cdd:PRK13647 78 RSKVGLVFQDpdDQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 199 PSLVFLDEPTTGMDPKARRFLWNlILDIL-KTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKNR 270
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLME-ILDRLhNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
45-257 |
1.33e-12 |
|
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: 65.21 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKMGRILAVDRlclgvrpGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGssilkellrvqQSI 124
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFAQ-------GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-----------VDV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCP----------QFDALFEDLTAREH--LELYTRLRGIPwKDEERVVSwALEKLELSKYADMPAGTYSGGNKRKLSTA 192
Cdd:cd03298 63 TAAPpadrpvsmlfQENNLFAHLTVEQNvgLGLSPGLKLTA-EDRQAIEV-ALARVGLAGLEKRLPGELSGGERQRVALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 193 IALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILK-TGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
74-257 |
1.56e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 65.42 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 74 PGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI-------LKELLRVQQSIGYCPQFDALFEDLTAREHL-EL 145
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLRQKVGMVFQQYNLWPHLTVMENLiEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 146 YTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILD 225
Cdd:COG4161 107 PCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRE 186
|
170 180 190
....*....|....*....|....*....|..
gi 641957197 226 ILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:COG4161 187 LSQTGITQVIVTHEVEFARKVASQVVYMEKGR 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
44-240 |
1.81e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.54 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKMgrILAVDrlcLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI--------LK 115
Cdd:PRK11264 3 AIEVKNLVKKFHGQTV--LHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 116 ELLR-VQQSIGYCPQFDALFEDLTAREH-LELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAI 193
Cdd:PRK11264 78 GLIRqLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 641957197 194 ALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSM 240
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
42-256 |
1.95e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.88 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLtkVYKSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKE-LLRV 120
Cdd:PRK13642 2 NKILEVENL--VFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 121 QQSIGYCPQF-DALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYP 199
Cdd:PRK13642 80 RRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 641957197 200 SLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLT-SHSMEECeALCTRLGIMVNG 256
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAG 216
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
72-250 |
2.08e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.87 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 72 VRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK-ELLRVQQSIGYCPqfdALFEDLTAREHLELYTRLR 150
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMAYLGHLP---GLKADLSTLENLHFLCGLH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 151 GipwKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTG 230
Cdd:PRK13543 111 G---RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGG 187
|
170 180
....*....|....*....|
gi 641957197 231 RSVVLTSHSMEECEALCTRL 250
Cdd:PRK13543 188 GAALVTTHGAYAAPPVRTRM 207
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
70-262 |
3.40e-12 |
|
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: 65.92 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 70 LGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI---LKELLRvqQSIGYCPQFDALFEDlTAREHLely 146
Cdd:COG4618 353 FSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwDREELG--RHIGYLPQDVELFDG-TIAENI--- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 147 TRLRGIpwkDEERVVSWAleklelsKYAD-------MPAGtY-----------SGGNKRKLSTAIALIGYPSLVFLDEPT 208
Cdd:COG4618 427 ARFGDA---DPEKVVAAA-------KLAGvhemilrLPDG-YdtrigeggarlSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 209 TGMDPKARRFLWNLILDILKTGRSVVLTSHSMeecEAL--CTRLGIMVNGRFKCLG 262
Cdd:COG4618 496 SNLDDEGEAALAAAIRALKARGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFG 548
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
42-238 |
4.25e-12 |
|
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: 65.73 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLTKVYKSRkmgriLAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSsilkellrVQ 121
Cdd:TIGR03719 320 DKVIEAENLTKAFGDK-----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET--------VK 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 qsIGYCPQFdalfedltaREHLElytrlrgiPWKDEERVVSWALEKLELSKYaDMPAGTY------------------SG 183
Cdd:TIGR03719 387 --LAYVDQS---------RDALD--------PNKTVWEEISGGLDIIKLGKR-EIPSRAYvgrfnfkgsdqqkkvgqlSG 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 184 GNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDIlktGRSVVLTSH 238
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF---AGCAVVISH 498
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
42-257 |
6.75e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 64.27 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLTKVYKSRKMgriLAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSsILKE--LLR 119
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAT---YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM-VLSEetVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSIGYCPQF-DALFEDLTAREHLELYTRLRGIPwKDE--ERVvSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALI 196
Cdd:PRK13635 79 VRRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVP-REEmvERV-DQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641957197 197 GYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLT-SHSMEECeALCTRLGIMVNGR 257
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGE 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
32-257 |
7.02e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 7.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 32 RRRVLRGEADNDMLKIDNLTkvykSRKMGRilaVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGS 111
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVT----SRDRKK---VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 112 SIL--KELLRVQQSIGYCPQF---DALFEDLTAREHLELYTRLRGIPWK---------DEERVVSWALEKLELSKYA-DM 176
Cdd:PRK09700 326 DISprSPLDAVKKGMAYITESrrdNGFFPNFSIAQNMAISRSLKDGGYKgamglfhevDEQRTAENQRELLALKCHSvNQ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 177 PAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNG 256
Cdd:PRK09700 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
.
gi 641957197 257 R 257
Cdd:PRK09700 486 R 486
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
70-238 |
8.66e-12 |
|
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: 63.01 E-value: 8.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 70 LGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGG---SSILKELLRvqQSIGYCPQFDALFEDlTAREHLELy 146
Cdd:cd03254 24 FSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDISRKSLR--SMIGVVLQDTFLFSG-TIMENIRL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 147 trlrGIPWKDEERVVSWA--------LEKLE--LSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKAR 216
Cdd:cd03254 100 ----GRPNATDEEVIEAAkeagahdfIMKLPngYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETE 175
|
170 180
....*....|....*....|..
gi 641957197 217 RFLWNLILDILKtGRSVVLTSH 238
Cdd:cd03254 176 KLIQEALEKLMK-GRTSIIIAH 196
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
43-240 |
9.04e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 9.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 43 DMLKIDNLTKVYKSRKMgrilaVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGeafiggsSILKEllrVQQ 122
Cdd:PRK09544 3 SLVSLENVSVSFGQRRV-----LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-------VIKRN---GKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 SIGYCPQfdALFEDLTAREHLELYTRLR-GIPWKDeervVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSL 201
Cdd:PRK09544 68 RIGYVPQ--KLYLDTTLPLTVNRFLRLRpGTKKED----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 641957197 202 VFLDEPTTGMDPKARRFLWNLIlDILKT--GRSVVLTSHSM 240
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLI-DQLRRelDCAVLMVSHDL 181
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
78-263 |
9.82e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.53 E-value: 9.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 78 FGLLGVNGAGKTTTFKMLT------GDESTTGGEAFIGGSSILK-ELLRVQQSIGYCPQFDALFEDLTAREHLELYTRLR 150
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLNrlieiyDSKIKVDGKVLYFGKDIFQiDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 151 GIPWKDE-ERVVSWALEKLELSKYA----DMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILD 225
Cdd:PRK14246 119 GIKEKREiKKIVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITE 198
|
170 180 190
....*....|....*....|....*....|....*...
gi 641957197 226 iLKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGS 263
Cdd:PRK14246 199 -LKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
44-250 |
9.90e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.57 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL---KELLRV 120
Cdd:PRK11248 1 MLQISHLYADYGGKP-----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 121 QQSIGYCPQFDALfedltarEHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPS 200
Cdd:PRK11248 76 FQNEGLLPWRNVQ-------DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 641957197 201 LVFLDEPTTGMDPKARRFLWNLILDIL-KTGRSVVLTSHSMEECEALCTRL 250
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWqETGKQVLLITHDIEEAVFMATEL 199
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
45-263 |
1.07e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.47 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYksrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLR-VQQS 123
Cdd:PRK10253 8 LRGEQLTLGY-----GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQFDALFEDLTARE--------HLELYTRLRgipwKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIAL 195
Cdd:PRK10253 83 IGLLAQNATTPGDITVQElvargrypHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641957197 196 IGYPSLVFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGS 263
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
72-212 |
1.85e-11 |
|
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: 61.89 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 72 VRPGECFGLLGVNGAGKTTTFKMLTGDESTTG---GEAFIGGSSILKELLRVQQSIGYCPQFDALFEDLTAREHLELYTR 148
Cdd:cd03233 30 VKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALR 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641957197 149 LRGipwKDEERVVswaleklelskyadmpagtySGGNKRKLSTAIALIGYPSLVFLDEPTTGMD 212
Cdd:cd03233 110 CKG---NEFVRGI--------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
42-244 |
2.56e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.51 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLTKVYKSRKMGrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTG----DESTTGGEAFIGGSSILKEL 117
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKP---ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpDDNPNSKITVDGITLTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 118 LRVQQSIGYCPQF-DALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALI 196
Cdd:PRK13640 80 WDIREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 641957197 197 GYPSLVFLDEPTTGMDPKARRFLWNLILDILK-TGRSVVLTSHSMEECE 244
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEAN 208
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
65-257 |
3.18e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 65 VDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL----KELLRvqQSIGYCPQ---FDALFEDL 137
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspQDGLA--NGIVYISEdrkRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 138 TAREHLELyTRLR-------GIPWKDEERVVSWALEKLEL-SKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTT 209
Cdd:PRK10762 346 SVKENMSL-TALRyfsraggSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 641957197 210 GMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
47-265 |
4.41e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.60 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 47 IDNLTKVYKSRKMGRI-LAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILkellrVQQSIG 125
Cdd:PRK13545 21 FDKLKDLFFRSKDGEYhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL-----IAISSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 126 ycpqfdaLFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLD 205
Cdd:PRK13545 96 -------LNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVID 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 206 EPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQ 265
Cdd:PRK13545 169 EALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIK 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
44-257 |
1.14e-10 |
|
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: 60.14 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI--LKE--LLR 119
Cdd:COG4181 8 IIELRGLTKTVGTGA-GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaLDEdaRAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 V-QQSIGYCPQFDALFEDLTAREHLELYTRLRGIPwKDEERVVSWaLEKLELSKYADMPAGTYSGGNKRKLSTAIALIGY 198
Cdd:COG4181 87 LrARHVGFVFQSFQLLPTLTALENVMLPLELAGRR-DARARARAL-LERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641957197 199 PSLVFLDEPTTGMDPKARRflwnLILDIL-----KTGRSVVLTSHSmEECEALCTRLGIMVNGR 257
Cdd:COG4181 165 PAILFADEPTGNLDAATGE----QIIDLLfelnrERGTTLVLVTHD-PALAARCDRVLRLRAGR 223
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
42-264 |
1.98e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.83 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLTKVYK---------------SRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEA 106
Cdd:PRK13546 2 NVSVNIKNVTKEYRiyrtnkermkdalipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 107 FIGGssilkELLRVQQSIGYCPQfdalfedLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNK 186
Cdd:PRK13546 82 DRNG-----EVSVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641957197 187 RKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSI 264
Cdd:PRK13546 150 AKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEL 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
45-263 |
3.31e-10 |
|
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: 60.20 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKMGRILAVDrlclgVRPGECFGLLGVNGAGKTTTFKMLTGDES--TTGGEaFIGGSSILKELLRV-- 120
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFT-----IEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGR-IIYHVALCEKCGYVer 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 121 QQSIGY-CP-------QFDALFEDLTAREHLELYTRL-----RGIPWKDEERVVSWALEKLELSKYA------------D 175
Cdd:TIGR03269 75 PSKVGEpCPvcggtlePEEVDFWNLSDKLRRRIRKRIaimlqRTFALYGDDTVLDNVLEALEEIGYEgkeavgravdliE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 176 MP---------AGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILK-TGRSVVLTSHSMEECEA 245
Cdd:TIGR03269 155 MVqlshrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKaSGISMVLTSHWPEVIED 234
|
250
....*....|....*...
gi 641957197 246 LCTRLGIMVNGRFKCLGS 263
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGT 252
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
44-259 |
3.56e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.94 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLT---KVYKSRKMgrilaVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGdeSTTG---GEAFIGGS--SILK 115
Cdd:PRK13549 259 ILEVRNLTawdPVNPHIKR-----VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGrweGEIFIDGKpvKIRN 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 116 ELLRVQQSIGYCPQ---FDALFEDLTAREHLEL-----YTRLRGIPWKDEERVVSWALEKLEL-SKYADMPAGTYSGGNK 186
Cdd:PRK13549 332 PQQAIAQGIAMVPEdrkRDGIVPVMGVGKNITLaaldrFTGGSRIDDAAELKTILESIQRLKVkTASPELAIARLSGGNQ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 187 RKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRFK 259
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
44-257 |
3.96e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.93 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKS----RKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKelLR 119
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK--LN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSIGYCPQFDALFED-LTA-----------REHLELYTRLrgipwkDEERVVSWALEKLEL----SKYADMPAGTYSG 183
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDsISAvnprktvreiiREPLRHLLSL------DKAERLARASEMLRAvdldDSVLDKRPPQLSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641957197 184 GNKRKLSTAIALIGYPSLVFLDEPTTGMDpkarRFLWNLILDILK-----TGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLD----LVLQAGVIRLLKklqqqFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
66-272 |
4.00e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.01 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 66 DRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK----ELLRVQQSIGYCPQFDALFEDLTA-- 139
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsRLYTVRKRMSMLFQSGALFTDMNVfd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 140 ------REHlelyTRLrgiPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRK--LSTAIALigYPSLVFLDEPTTGM 211
Cdd:PRK11831 104 nvayplREH----TQL---PAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRaaLARAIAL--EPDLIMFDEPFVGQ 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641957197 212 DPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHLKNRSE 272
Cdd:PRK11831 175 DPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-238 |
5.19e-10 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 59.34 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 19 QPIEDDDEDVASERrrvLRGEadndmLKIDNLTKVYKSRKmgrILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGD 98
Cdd:TIGR02203 313 SPPEKDTGTRAIER---ARGD-----VEFRNVTFRYPGRD---RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRF 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 99 ESTTGGEAFIGGSSILKELLR-VQQSIGYCPQFDALFEDLTAREhlELYTRLRGIpwkDEERVVSwALEKLELSKYAD-M 176
Cdd:TIGR02203 382 YEPDSGQILLDGHDLADYTLAsLRRQVALVSQDVVLFNDTIANN--IAYGRTEQA---DRAEIER-ALAAAYAQDFVDkL 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641957197 177 PAGTY----------SGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRfLWNLILDILKTGRSVVLTSH 238
Cdd:TIGR02203 456 PLGLDtpigengvllSGGQRQRLAIARALLKDAPILILDEATSALDNESER-LVQAALERLMQGRTTLVIAH 526
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
64-238 |
8.52e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 59.02 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 64 AVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI----LKELLRvqqSIGYCPQfDA-LFEDlT 138
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrdltLESLRR---QIGVVPQ-DTfLFSG-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 139 AREHLelytRLrGIPWKDEERVVsWALEKLELSKY-ADMPAG----------TYSGGNKRKLSTAIALIGYPSLVFLDEP 207
Cdd:COG1132 430 IRENI----RY-GRPDATDEEVE-EAAKAAQAHEFiEALPDGydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190
....*....|....*....|....*....|.
gi 641957197 208 TTGMDPKARRFLWNLILDILKtGRSVVLTSH 238
Cdd:COG1132 504 TSALDTETEALIQEALERLMK-GRTTIVIAH 533
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-247 |
1.33e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.18 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 7 CVFYNRRVPVSSQPIEdddedvaSERRRVLRGEADND----------MLKIDNLTKVYKSRK--MGRIL----AVDRLCL 70
Cdd:PRK15134 235 CVEQNRAATLFSAPTH-------PYTQKLLNSEPSGDpvplpepaspLLDVEQLQVAFPIRKgiLKRTVdhnvVVKNISF 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 71 GVRPGECFGLLGVNGAGKTTT-FKMLTGDESTtgGEAFIGGSSIlkELLRVQQSIGYCPQFDALFED----LTAR----- 140
Cdd:PRK15134 308 TLRPGETLGLVGESGSGKSTTgLALLRLINSQ--GEIWFDGQPL--HNLNRRQLLPVRHRIQVVFQDpnssLNPRlnvlq 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 141 ---EHLELYTRLRGiPWKDEERVVSwALEKLELS-----KYadmPAgTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMD 212
Cdd:PRK15134 384 iieEGLRVHQPTLS-AAQREQQVIA-VMEEVGLDpetrhRY---PA-EFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 641957197 213 pkarRFLWNLILDILKT-----GRSVVLTSHSMEECEALC 247
Cdd:PRK15134 458 ----KTVQAQILALLKSlqqkhQLAYLFISHDLHVVRALC 493
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
72-267 |
2.15e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.95 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 72 VRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL-----KELLRVQQSIGYCPQF--DALFEDlTAREHLE 144
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknKKLKPLRKKVGIVFQFpeHQLFEE-TVEKDIC 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 145 LYTRLRGIPWKDEERVVSWALEKLELS-KYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLI 223
Cdd:PRK13634 109 FGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMF 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 641957197 224 LDILKT-GRSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSIQHL 267
Cdd:PRK13634 189 YKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
44-271 |
2.31e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 56.13 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKMgrilavdRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGS------------ 111
Cdd:PRK10771 1 MLKLTDITWLYHHLPM-------RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 112 SILKellrvqqsigycpQFDALFEDLTAREH--LELYTRLRGIPwkDEERVVSWALEKLELSKYADMPAGTYSGGNKRKL 189
Cdd:PRK10771 74 SMLF-------------QENNLFSHLTVAQNigLGLNPGLKLNA--AQREKLHAIARQMGIEDLLARLPGQLSGGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 190 STAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVL-TSHSMEECEALCTRLGIMVNGRFKCLGSIQHLK 268
Cdd:PRK10771 139 ALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLmVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
...
gi 641957197 269 NRS 271
Cdd:PRK10771 219 SGK 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
179-257 |
2.37e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 2.37e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641957197 179 GTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
64-238 |
3.10e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 57.29 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 64 AVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRvqqsiGYCPQFDALFEDLtareHl 143
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE-----DYRKLFSAVFTDF----H- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 144 eLYTRL---RGIPwKDEERVVSWaLEKLELSKYADMPAGT-----YSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKA 215
Cdd:PRK10522 408 -LFDQLlgpEGKP-ANPALVEKW-LERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF 484
|
170 180
....*....|....*....|....
gi 641957197 216 RRFLWNLILDILK-TGRSVVLTSH 238
Cdd:PRK10522 485 RREFYQVLLPLLQeMGKTIFAISH 508
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
42-225 |
3.35e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.10 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 42 NDMLKIDNLTKVYKSRkmgriLAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEafIGGSSILKellrvq 121
Cdd:PRK10636 310 NPLLKMEKVSAGYGDR-----IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE--IGLAKGIK------ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 qsIGYCP--QFDALFEDLTAREHL------ELYTRLR----GIPWKDEervvswaleklelsKYADmPAGTYSGGNKRKL 189
Cdd:PRK10636 377 --LGYFAqhQLEFLRADESPLQHLarlapqELEQKLRdylgGFGFQGD--------------KVTE-ETRRFSGGEKARL 439
|
170 180 190
....*....|....*....|....*....|....*.
gi 641957197 190 STAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILD 225
Cdd:PRK10636 440 VLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID 475
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
47-212 |
6.00e-09 |
|
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: 56.10 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 47 IDNLTKVYKSRKmgRILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAfiggssilkellRVQQSI-- 124
Cdd:TIGR03719 7 MNRVSKVVPPKK--EIL--KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA------------RPQPGIkv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDLTAREHLE--------LYTRLRGI------PWKD-----------EERVVS---WALE-KLELSKYA- 174
Cdd:TIGR03719 71 GYLPQEPQLDPTKTVRENVEegvaeikdALDRFNEIsakyaePDADfdklaaeqaelQEIIDAadaWDLDsQLEIAMDAl 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 641957197 175 -----DMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMD 212
Cdd:TIGR03719 151 rcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
70-238 |
8.17e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 70 LGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKellRVQQSigycPQ-------FDALFEDLTAR-E 141
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVA---RLQQD----PPrnvegtvYDFVAEGIEEQaE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 142 HLELY-------------------TRLRGI-----PWKDEERVVSwALEKLELSkyADMPAGTYSGGNKRKLSTAIALIG 197
Cdd:PRK11147 97 YLKRYhdishlvetdpseknlnelAKLQEQldhhnLWQLENRINE-VLAQLGLD--PDAALSSLSGGWLRKAALGRALVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 641957197 198 YPSLVFLDEPTTGMDPKARRFLWNLILDIlktGRSVVLTSH 238
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETIEWLEGFLKTF---QGSIIFISH 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
48-238 |
8.24e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 48 DNLTKVYKSRkmgriLAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSsilkellrVQqsIGYC 127
Cdd:PRK11819 328 ENLSKSFGDR-----LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET--------VK--LAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 128 PQFdalfedltaREHLElytrlrgiPWKDEERVVSWALEKLELSKYaDMP------------------AGTYSGGNKRKL 189
Cdd:PRK11819 393 DQS---------RDALD--------PNKTVWEEISGGLDIIKVGNR-EIPsrayvgrfnfkggdqqkkVGVLSGGERNRL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 641957197 190 STAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDIlktGRSVVLTSH 238
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEF---PGCAVVISH 500
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
72-212 |
8.86e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 72 VRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEafiggssILKELlrvqqSIGYCPQFDALFEDLTAREHLE-LYTRLR 150
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE-------VDPEL-----KISYKPQYIKPDYDGTVEDLLRsITDDLG 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641957197 151 GIPWKDEervvswALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMD 212
Cdd:PRK13409 430 SSYYKSE------IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
29-257 |
9.17e-09 |
|
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: 55.85 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 29 ASERRRVLRGEADND--MLKIDNLTKVYKSRK------MGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDES 100
Cdd:COG4172 258 AAEPRGDPRPVPPDAppLLEARDLKVWFPIKRglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 101 tTGGEAFIGGSSIL----KELLRVQQSIgycpQfdALFED--------LTAREHLELYTRLRGIPWKDEERV--VSWALE 166
Cdd:COG4172 338 -SEGEIRFDGQDLDglsrRALRPLRRRM----Q--VVFQDpfgslsprMTVGQIIAEGLRVHGPGLSAAERRarVAEALE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 167 KLELSkyADMpAGTY----SGGNKRKLSTAIALIGYPSLVFLDEPTTGMDpkarRFLWNLILDILKT-----GRSVVLTS 237
Cdd:COG4172 411 EVGLD--PAA-RHRYphefSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQILDLLRDlqrehGLAYLFIS 483
|
250 260
....*....|....*....|
gi 641957197 238 HSMEECEALCTRLGIMVNGR 257
Cdd:COG4172 484 HDLAVVRALAHRVMVMKDGK 503
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
72-212 |
9.61e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 9.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 72 VRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEafiggssilkelLRVQQSIGYCPQFDALFEDLTAREHLE--LYTRL 149
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE------------VDEDLKISYKPQYISPDYDGTVEEFLRsaNTDDF 430
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 150 RGIPWKDEervvswALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMD 212
Cdd:COG1245 431 GSSYYKTE------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
45-263 |
1.46e-08 |
|
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: 53.30 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTkVYKSRKmgRILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDEST--TGGEAFIGGSSILkELL---R 119
Cdd:cd03217 1 LEIKDLH-VSVGGK--EIL--KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDIT-DLPpeeR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSIGYCPQFDALFEDLTAREHlelytrLRGIpwkDEervvswaleklelskyadmpagTYSGGNKRKLSTAIALIGYP 199
Cdd:cd03217 75 ARLGIFLAFQYPPEIPGVKNADF------LRYV---NE----------------------GFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 200 SLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEAL-CTRLGIMVNGRFKCLGS 263
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
70-238 |
1.88e-08 |
|
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: 53.77 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 70 LGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIlKEL----LRvqQSIGYCPQFDALFEDlTAREHLEl 145
Cdd:cd03253 22 FTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI-REVtldsLR--RAIGVVPQDTVLFND-TIGYNIR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 146 YTRLRGipwkDEERVVswaleklELSKYAD-------MPAGtY-----------SGGNKRKLSTAIALIGYPSLVFLDEP 207
Cdd:cd03253 97 YGRPDA----TDEEVI-------EAAKAAQihdkimrFPDG-YdtivgerglklSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190
....*....|....*....|....*....|.
gi 641957197 208 TTGMDPKARRFLWNLILDILKtGRSVVLTSH 238
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSK-GRTTIVIAH 194
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
44-256 |
2.05e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.63 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmgrilAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLT--GD---ESTTGGEAFIGGSSILK--- 115
Cdd:PRK14239 5 ILQVSDLSVYYNKKK-----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDlnpEVTITGSIVYNGHNIYSprt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 116 ELLRVQQSIGYCPQFDALFEdLTAREHLELYTRLRGIpwKDEErVVSWALEKL--------ELSKYADMPAGTYSGGNKR 187
Cdd:PRK14239 80 DTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGI--KDKQ-VLDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641957197 188 KLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDiLKTGRSVVLTSHSMEECEALCTRLGIMVNG 256
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG-LKDDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-267 |
2.07e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.95 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 28 VASERRRVLRGEADNDM----LKIDNLTKVYKSRKMgrilaVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTG-DESTT 102
Cdd:PRK14271 1 MACERLGGQSGAADVDAaapaMAAVNLTLGFAGKTV-----LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 103 G----GEAFIGGSSIL--KELLRVQQSIGYC-----PQFDALFEDLTA--REH-LELYTRLRGIPWKDEERVVSWALEKL 168
Cdd:PRK14271 76 GyrysGDVLLGGRSIFnyRDVLEFRRRVGMLfqrpnPFPMSIMDNVLAgvRAHkLVPRKEFRGVAQARLTEVGLWDAVKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 169 ELSkyaDMPAgTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDiLKTGRSVVLTSHSMEECEALCT 248
Cdd:PRK14271 156 RLS---DSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS-LADRLTVIIVTHNLAQAARISD 230
|
250
....*....|....*....
gi 641957197 249 RLGIMVNGRFKCLGSIQHL 267
Cdd:PRK14271 231 RAALFFDGRLVEEGPTEQL 249
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
44-216 |
2.44e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 54.08 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKsrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSsilkellRVQQ- 122
Cdd:PRK11650 3 GLKLQAVRKSYD----GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR-------VVNEl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 -----SIGYCPQFDALFEDLTAREHLELYTRLRGIPwKDE-ERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALI 196
Cdd:PRK11650 72 epadrDIAMVFQNYALYPHMSVRENMAYGLKIRGMP-KAEiEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIV 150
|
170 180
....*....|....*....|.
gi 641957197 197 GYPSlVFL-DEPTTGMDPKAR 216
Cdd:PRK11650 151 REPA-VFLfDEPLSNLDAKLR 170
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
64-212 |
3.05e-08 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 54.36 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 64 AVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGG---SSILKELLRvqQSIGYCPQFDALFeDLTAR 140
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslKDIDRHTLR--QFINYLPQEPYIF-SGSIL 565
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641957197 141 EHLELYTRlRGIPWKDEERVVSWA-----LEKLELSKYADMP--AGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMD 212
Cdd:TIGR01193 566 ENLLLGAK-ENVSQDEIWAACEIAeikddIENMPLGYQTELSeeGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
70-216 |
3.13e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 53.88 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 70 LGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSiLKELLRVQQSIGYCPQFDALFEDLTAREHLELYTRL 149
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR-MNDVPPAERGVGMVFQSYALYPHLSVAENMSFGLKL 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641957197 150 RGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKAR 216
Cdd:PRK11000 103 AGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
72-216 |
3.40e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 53.18 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 72 VRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEafiggssILKELlrvqQSIGYCPQFDALFEDLTAREHLELYTRLRG 151
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGD-------IEIEL----DTVSYKPQYIKADYEGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641957197 152 IP--WKDEervvswALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKAR 216
Cdd:cd03237 91 THpyFKTE------IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
35-257 |
3.53e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.57 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 35 VLRGEADNDMLKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTG---DESTTGGEAFIGGS 111
Cdd:PRK09473 3 PLAQQQADALLDVKDLRVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllaANGRIGGSATFNGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 112 SIL----KELLRVQQSigycpQFDALFED-LTArehLELYTRL-----------RGIPWKD--EERVVSW-ALEKLELSK 172
Cdd:PRK09473 82 EILnlpeKELNKLRAE-----QISMIFQDpMTS---LNPYMRVgeqlmevlmlhKGMSKAEafEESVRMLdAVKMPEARK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 173 YADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLiLDILKT--GRSVVLTSHSMEECEALCTRL 250
Cdd:PRK09473 154 RMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTL-LNELKRefNTAIIMITHDLGVVAGICDKV 232
|
....*..
gi 641957197 251 GIMVNGR 257
Cdd:PRK09473 233 LVMYAGR 239
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
72-238 |
4.64e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.75 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 72 VRPGECFGLLGVNGAGKTTTFKMLTG------------DESTTGGEAFIGG------SSILKELLRVQQSIGYCPQFDAL 133
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddpPDWDEILDEFRGSelqnyfTKLLEGDVKVIVKPQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 134 FEDLTarehLELYTRlrgipwKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDP 213
Cdd:cd03236 103 VKGKV----GELLKK------KDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*
gi 641957197 214 KARRFLWNLILDILKTGRSVVLTSH 238
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
124-241 |
4.91e-08 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 53.16 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSwaLEKLELSKYADMPAGTYSGGNKRKLSTAIALI---GYPS 200
Cdd:pfam13304 182 KELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERG--LILLENGGGGELPAFELSDGTKRLLALLAALLsalPKGG 259
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 641957197 201 LVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSME 241
Cdd:pfam13304 260 LLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
45-269 |
5.06e-08 |
|
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: 53.76 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRkmGRILAVDrLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRVQQSI 124
Cdd:TIGR01271 1218 MDVQGLTAKYTEA--GRAVLQD-LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 125 GYCPQFDALFEDlTAREHLELYTRlrgipWKDEE--RVVSWALEKLELSKYAD-----MPAGTY--SGGNKRKLSTAIAL 195
Cdd:TIGR01271 1295 GVIPQKVFIFSG-TFRKNLDPYEQ-----WSDEEiwKVAEEVGLKSVIEQFPDkldfvLVDGGYvlSNGHKQLMCLARSI 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 196 IGYPSLVFLDEPTTGMDPkarrFLWNLILDILKTGRS---VVLTSHSME---ECEALctrlgIMVNG-RFKCLGSIQHLK 268
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDP----VTLQIIRKTLKQSFSnctVILSEHRVEallECQQF-----LVIEGsSVKQYDSIQKLL 1439
|
.
gi 641957197 269 N 269
Cdd:TIGR01271 1440 N 1440
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
65-217 |
5.27e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.41 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 65 VDRLCLGVRPGEcFGLL-GVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK---ELLRVQQSigYCPQFDALFEDlTAR 140
Cdd:PRK10247 23 LNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlkpEIYRQQVS--YCAQTPTLFGD-TVY 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641957197 141 EHLELYTRLRGIpwKDEERVVSWALEKLELSKYA-DMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARR 217
Cdd:PRK10247 99 DNLIFPWQIRNQ--QPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
45-249 |
5.34e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKMgrilaVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEafiggssilkellrVQQS- 123
Cdd:PRK15064 320 LEVENLTKGFDNGPL-----FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT--------------VKWSe 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 ---IGYCPQ-----FDalfEDLTAREHLELYTRLrgipwKDEERVVSWALEKLELSK-YADMPAGTYSGGNKRKLSTAIA 194
Cdd:PRK15064 381 nanIGYYAQdhaydFE---NDLTLFDWMSQWRQE-----GDDEQAVRGTLGRLLFSQdDIKKSVKVLSGGEKGRMLFGKL 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 195 LIGYPSLVFLDEPTTGMDPKARRFLwNLILDILKTgrSVVLTSHSMEECEALCTR 249
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMESIESL-NMALEKYEG--TLIFVSHDREFVSSLATR 504
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
45-244 |
5.43e-08 |
|
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: 52.09 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKMGRILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL----KELLRV 120
Cdd:cd03248 12 VKFQNVTFAYPTRPDTLVL--QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyehKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 121 QQSIGYCPQfdaLFEDlTAREHLELytrlrGIPWKDEERVVSWA--------LEKLELSKYADM--PAGTYSGGNKRKLS 190
Cdd:cd03248 90 VSLVGQEPV---LFAR-SLQDNIAY-----GLQSCSFECVKEAAqkahahsfISELASGYDTEVgeKGSQLSGGQKQRVA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 641957197 191 TAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILkTGRSVVLTSHSMEECE 244
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWP-ERRTVLVIAHRLSTVE 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
54-238 |
5.55e-08 |
|
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: 52.16 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 54 YKSRKMGRILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIlKEL----LRVQqsIGYCPQ 129
Cdd:cd03249 10 YPSRPDVPIL--KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI-RDLnlrwLRSQ--IGLVSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 130 FDALFeDLTAREHLELytrlrGIPWKDEERVVSwALEKLELSKY-ADMPAG----------TYSGGNKRKLSTAIALIGY 198
Cdd:cd03249 85 EPVLF-DGTIAENIRY-----GKPDATDEEVEE-AAKKANIHDFiMSLPDGydtlvgergsQLSGGQKQRIAIARALLRN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 641957197 199 PSLVFLDEPTTGMDPKARRflwnLI---LDILKTGRSVVLTSH 238
Cdd:cd03249 158 PKILLLDEATSALDAESEK----LVqeaLDRAMKGRTTIVIAH 196
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
68-239 |
7.29e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.41 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 68 LCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKellrVQQS-IGYCPQFDALFEDLTAREHLELY 146
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN----IAKPyCTYIGHNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 147 TRLRgipwkDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDI 226
Cdd:PRK13541 95 SEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMK 169
|
170
....*....|...
gi 641957197 227 LKTGRSVVLTSHS 239
Cdd:PRK13541 170 ANSGGIVLLSSHL 182
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
44-238 |
1.01e-07 |
|
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: 52.38 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTF----KMLTGDESTTGGEAFIGGSSIL----K 115
Cdd:COG4172 6 LLSVEDLSVAFGQGG-GTVEAVKGVSFDIAAGETLALVGESGSGKSVTAlsilRLLPDPAAHPSGSILFDGQDLLglseR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 116 ELLRVQ-QSIGYCPQfdalfEDLTA-----------REHLELYTRLRGIPWkdEERVVSWaLEKLELSKyADMPAGTY-- 181
Cdd:COG4172 85 ELRRIRgNRIAMIFQ-----EPMTSlnplhtigkqiAEVLRLHRGLSGAAA--RARALEL-LERVGIPD-PERRLDAYph 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641957197 182 --SGGNKRKLSTAIALIGYPSLVFLDEPTTGMDP--KARrflwnlILDILK-----TGRSVVLTSH 238
Cdd:COG4172 156 qlSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvQAQ------ILDLLKdlqreLGMALLLITH 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
45-241 |
1.36e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.63 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTG------------------DESTTGGEA 106
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAlllpdtgtiewifkdeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 107 FIGGSSILKELLR-------VQQSIGYCPQFD--ALFEDlTAREHLELYTRLRGIPwKDE--ERvvswALEKLEL----S 171
Cdd:PRK13651 83 VLEKLVIQKTRFKkikkikeIRRRVGVVFQFAeyQLFEQ-TIEKDIIFGPVSMGVS-KEEakKR----AAKYIELvgldE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 172 KYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSME 241
Cdd:PRK13651 157 SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
44-226 |
1.69e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.94 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSR----KMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFI-------GGSS 112
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddhplhfGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 113 ILKELLRVqqsigycpqfdaLFED----LTAREH--------LELYTRLRGipwKDEERVVSWALEKLEL-----SKYAD 175
Cdd:PRK15112 84 YRSQRIRM------------IFQDpstsLNPRQRisqildfpLRLNTDLEP---EQREKQIIETLRQVGLlpdhaSYYPH 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 641957197 176 MPAgtysGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDI 226
Cdd:PRK15112 149 MLA----PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL 195
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
45-213 |
2.12e-07 |
|
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: 50.18 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSrkmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTT----FKMLtgdeSTTGGEAFIGG---SSILKEL 117
Cdd:cd03244 3 IEFKNVSLRYRP---NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGvdiSKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 118 LRvqQSIGYCPQFDALFEDlTAREHLELYTRlrgipWKDEERvvsW-ALEKLELSKY-ADMPAG----------TYSGGN 185
Cdd:cd03244 76 LR--SRISIIPQDPVLFSG-TIRSNLDPFGE-----YSDEEL---WqALERVGLKEFvESLPGGldtvveeggeNLSVGQ 144
|
170 180
....*....|....*....|....*...
gi 641957197 186 KRKLSTAIALIGYPSLVFLDEPTTGMDP 213
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDP 172
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
73-238 |
2.67e-07 |
|
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: 51.32 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 73 RPGECFGLLGVNGAGKTTTFKMLTGD--------ESTTGGEAFI---GGSSI---LKEL----LRVQQSIGYCPQFDALF 134
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGElkpnlgdyDEEPSWDEVLkrfRGTELqdyFKKLangeIKVAHKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 135 eDLTAREHLELYtrlrgipwkDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPK 214
Cdd:COG1245 177 -KGTVRELLEKV---------DERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180
....*....|....*....|....
gi 641957197 215 ARRFLWNLILDILKTGRSVVLTSH 238
Cdd:COG1245 247 QRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
60-212 |
2.87e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.56 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 60 GRILaVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSIL----KELLRvqqSIGYCPQFDALFE 135
Cdd:PRK10575 23 GRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswssKAFAR---KVAYLPQQLPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 136 DLTAREhlelytrLRGI---PW---------KDEERVVSwALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVF 203
Cdd:PRK10575 99 GMTVRE-------LVAIgryPWhgalgrfgaADREKVEE-AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
....*....
gi 641957197 204 LDEPTTGMD 212
Cdd:PRK10575 171 LDEPTSALD 179
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
70-241 |
4.07e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.97 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 70 LGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI---------LK-------ELLRVQQSIGYcpQFDAL 133
Cdd:PRK10619 26 LQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqLKvadknqlRLLRTRLTMVF--QHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 134 FEDLTAREH-LELYTRLRGIPWKD-EERVVSWaLEKLELSKYADmpaGTY----SGGNKRKLSTAIALIGYPSLVFLDEP 207
Cdd:PRK10619 104 WSHMTVLENvMEAPIQVLGLSKQEaRERAVKY-LAKVGIDERAQ---GKYpvhlSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190
....*....|....*....|....*....|....
gi 641957197 208 TTGMDPKARRFLWNLILDILKTGRSVVLTSHSME 241
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
45-238 |
4.17e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.35 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRK-----MGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK---- 115
Cdd:PRK11308 6 LQAIDLKKHYPVKRglfkpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 116 --ELLRvqQSIgycpQ--FDALFEDLTAR--------EHLELYTRLRGipwkdEERV--VSWALEKLEL-----SKYADM 176
Cdd:PRK11308 86 aqKLLR--QKI----QivFQNPYGSLNPRkkvgqileEPLLINTSLSA-----AERRekALAMMAKVGLrpehyDRYPHM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641957197 177 pagtYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSH 238
Cdd:PRK11308 155 ----FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISH 213
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
44-212 |
4.56e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.83 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKvykSRKMGRILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGD---ESTTGGEAFIGGSSILKELL-- 118
Cdd:PRK13547 1 MLTADHLHV---ARRHRAIL--RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgGGAPRGARVTGDVTLNGEPLaa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 119 ----RVQQSIGYCPQFDALFEDLTAREHLEL----YTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLS 190
Cdd:PRK13547 76 idapRLARLRAVLPQAAQPAFAFSAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQ 155
|
170 180 190
....*....|....*....|....*....|.
gi 641957197 191 TAIAL---------IGYPSLVFLDEPTTGMD 212
Cdd:PRK13547 156 FARVLaqlwpphdaAQPPRYLLLDEPTAALD 186
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
72-212 |
5.14e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 72 VRPGECFGLLGVNGAGKTTTFKMLTG--DESTTGGEAFIGGSSILKELLRVQ--QSIGYCPQFDALFEDLTAREHLELYT 147
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASntDGFHIGVEGVITYDGITPEEIKKHyrGDVVYNAETDVHFPHLTVGETLDFAA 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641957197 148 RLRGIPWKDE--------ERVVSWALEKLELSKYADMPAGT-----YSGGNKRKLSTAIALIGYPSLVFLDEPTTGMD 212
Cdd:TIGR00956 164 RCKTPQNRPDgvsreeyaKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
44-238 |
5.43e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.49 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI-------LKE 116
Cdd:PRK10535 4 LLELKDIRRSYPSGE-EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldadaLAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 117 LLRvqQSIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALI 196
Cdd:PRK10535 83 LRR--EHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 641957197 197 GYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSH 238
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
61-223 |
6.38e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 61 RILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGD-------ESTTGGEAFIGGSSILKellrVQQSIGYcpqfdal 133
Cdd:PRK10938 274 PIL--HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysnDLTLFGRRRGSGETIWD----IKKHIGY------- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 134 fedLTAREHLE--LYTRLR-----------GI--PWKDEERVVS--WaLEKLELSKY-ADMPAGTYSGGNKRKLSTAIAL 195
Cdd:PRK10938 341 ---VSSSLHLDyrVSTSVRnvilsgffdsiGIyqAVSDRQQKLAqqW-LDILGIDKRtADAPFHSLSWGQQRLALIVRAL 416
|
170 180 190
....*....|....*....|....*....|..
gi 641957197 196 IGYPSLVFLDEPTTGMDPKAR----RFLWNLI 223
Cdd:PRK10938 417 VKHPTLLILDEPLQGLDPLNRqlvrRFVDVLI 448
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
38-238 |
7.83e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.81 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 38 GEADNDMLKIDNLTkVYKSRkmGRILaVDRLCLGVRPGEcfGLL--GVNGAGKTTTFKMLTG-DESTTGgeafiggssil 114
Cdd:COG4178 356 ETSEDGALALEDLT-LRTPD--GRPL-LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGlWPYGSG----------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 115 kellrvqqSIGYCPQFDALFedLTAREHLELYTrLRGI--------PWKDEErvVSWALEKLELSKYADMP------AGT 180
Cdd:COG4178 419 --------RIARPAGARVLF--LPQRPYLPLGT-LREAllypataeAFSDAE--LREALEAVGLGHLAERLdeeadwDQV 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 641957197 181 YSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKtGRSVVLTSH 238
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELP-GTTVISVGH 542
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
64-238 |
8.45e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.57 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 64 AVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGG---SSILKELLRvqQSIGYCPQfDALFEDLTAR 140
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASLR--RNIAVVFQ-DAGLFNRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 141 EHLELytrlrGIPWKDEERVVSwALEKLELSKYADMPAGTY-----------SGGNKRKLSTAIALIGYPSLVFLDEPTT 209
Cdd:PRK13657 427 DNIRV-----GRPDATDEEMRA-AAERAQAHDFIERKPDGYdtvvgergrqlSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180
....*....|....*....|....*....
gi 641957197 210 GMDPKARRFLwNLILDILKTGRSVVLTSH 238
Cdd:PRK13657 501 ALDVETEAKV-KAALDELMKGRTTFIIAH 528
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
68-244 |
9.52e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 49.72 E-value: 9.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 68 LCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK-ELLRVQQSIGYCPQFDALFEDlTAREHLely 146
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFSG-SVRENI--- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 147 trLRGIPWKDEERVVSWALEKLELSKYADMPAGTY----------SGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKAR 216
Cdd:TIGR00958 576 --AYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDtevgekgsqlSGGQKQRIAIARALVRKPRVLILDEATSALDAECE 653
|
170 180
....*....|....*....|....*...
gi 641957197 217 RFLWNlilDILKTGRSVVLTSHSMEECE 244
Cdd:TIGR00958 654 QLLQE---SRSRASRTVLLIAHRLSTVE 678
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
64-258 |
9.89e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 64 AVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGG----------------SSILKELLRVQQS---- 123
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeidfksskealengiSMVHQELNLVLQRsvmd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 ---IGYCPQfDALFEDltareHLELYTRLRGIpwkdeervvswaLEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPS 200
Cdd:PRK10982 93 nmwLGRYPT-KGMFVD-----QDKMYRDTKAI------------FDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 641957197 201 LVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVNGRF 258
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQW 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
45-242 |
1.70e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.11 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSRKMgrilaVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLT------GDESTTGGEAFIGGSSILKEL- 117
Cdd:PRK14258 8 IKVNNLSFYYDTQKI-----LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRVEGRVEFFNQNIYERRVn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 118 ---LRVQQSIGYcPQFDaLFEdLTAREHLELYTRLRGIPWKDE-ERVVSWALEKLEL----SKYADMPAGTYSGGNKRKL 189
Cdd:PRK14258 83 lnrLRRQVSMVH-PKPN-LFP-MSVYDNVAYGVKIVGWRPKLEiDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 641957197 190 STAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDI-LKTGRSVVLTSHSMEE 242
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQ 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
64-238 |
3.84e-06 |
|
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: 46.84 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 64 AVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSI----LKELLRvqqSIGYCPQFDALFEDlTA 139
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdytLASLRR---QIGLVSQDVFLFND-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 140 REHLeLYtrlrGIPWKDEERVVSwALEKLELSKYAD-MPAG----------TYSGGNKRKLSTAIALIGYPSLVFLDEPT 208
Cdd:cd03251 93 AENI-AY----GRPGATREEVEE-AARAANAHEFIMeLPEGydtvigergvKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190
....*....|....*....|....*....|...
gi 641957197 209 TGMDPKARRflwnLI---LDILKTGRSVVLTSH 238
Cdd:cd03251 167 SALDTESER----LVqaaLERLMKNRTTFVIAH 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
60-239 |
5.70e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 45.61 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 60 GRILaVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGD-ESTTGgeafiggssilkellrvqqSIGYCPQFDALFedLT 138
Cdd:cd03223 13 GRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwPWGSG-------------------RIGMPEGEDLLF--LP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 139 AREHLELYTrLRGI---PWKDEervvswaleklelskyadmpagtYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKA 215
Cdd:cd03223 71 QRPYLPLGT-LREQliyPWDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180
....*....|....*....|....
gi 641957197 216 RRFLWNLILDILKTgrsVVLTSHS 239
Cdd:cd03223 127 EDRLYQLLKELGIT---VISVGHR 147
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
49-212 |
6.24e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 49 NLTKVYKSRKmgRILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAfiggssilkellRVQQ--SIGY 126
Cdd:PRK11819 11 RVSKVVPPKK--QIL--KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA------------RPAPgiKVGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 127 CPQFDALFEDLTAREHLE--------LYTRLRGI------PWKD-----------EERVVS---WALE-KLELSKYA--- 174
Cdd:PRK11819 75 LPQEPQLDPEKTVRENVEegvaevkaALDRFNEIyaayaePDADfdalaaeqgelQEIIDAadaWDLDsQLEIAMDAlrc 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 641957197 175 ---DMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMD 212
Cdd:PRK11819 155 ppwDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
61-255 |
6.82e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 61 RILAVDRLCLgvRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGE---AFIGGSSILKELLrvQQSIGYCPQ---FDALF 134
Cdd:PRK10938 17 KTLQLPSLTL--NAGDSWAFVGANGSGKSALARALAGELPLLSGErqsQFSHITRLSFEQL--QKLVSDEWQrnnTDMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 135 ED-----LTAREHLELYTrlrgipwKDEERVVSWAlEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTT 209
Cdd:PRK10938 93 PGeddtgRTTAEIIQDEV-------KDPARCEQLA-QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 641957197 210 GMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMVN 255
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
72-238 |
6.92e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 72 VRPGECFGLLGVNGAGKTTTFKMLTG--------DESTTGGEAFI---GGSSI---LKEL----LRVQQSIGYCPQFDAL 133
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVLkrfRGTELqnyFKKLyngeIKVVHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 134 FeDLTAREHLELYtrlrgipwkDEERVVSWALEKLELSKYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDP 213
Cdd:PRK13409 176 F-KGKVRELLKKV---------DERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180
....*....|....*....|....*
gi 641957197 214 KARRFLWNLILDILKtGRSVVLTSH 238
Cdd:PRK13409 246 RQRLNVARLIRELAE-GKYVLVVEH 269
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
65-257 |
8.12e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.85 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 65 VDRLCLGVRPGECFGLLGVNGAGKTTT----FKMLTGDESTTGGEAFIGGSSILKELLR------VQQSigycPQ--FDA 132
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCALRgrkiatIMQN----PRsaFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 133 LfedLTAREHLELYTRLRGIPwkDEERVVSWALEKLELS---KYADMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTT 209
Cdd:PRK10418 95 L---HTMHTHARETCLALGKP--ADDATLTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 641957197 210 GMDPKAR-RFLwNLILDILKT-GRSVVLTSHSMEECEALCTRLGIMVNGR 257
Cdd:PRK10418 170 DLDVVAQaRIL-DLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGR 218
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
75-241 |
1.01e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 75 GECFGLLGVNGAGKTTTFKMLT---------------------GDESTTGG---EAFIGGSSILKELLRVQQ-------- 122
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilhveqevvGDDTTALQcvlNTDIERTQLLEEEAQLVAqqrelefe 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 123 ---SIGYCPQFDALFEDLTAREHLELYTRLRGIPWKDEERVVSWALEKLELSkyADM---PAGTYSGGNKRKLSTAIALI 196
Cdd:PLN03073 283 tetGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFT--PEMqvkATKTFSGGWRMRIALARALF 360
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 641957197 197 GYPSLVFLDEPTTGMDPKArrFLWnLILDILKTGRSVVLTSHSME 241
Cdd:PLN03073 361 IEPDLLLLDEPTNHLDLHA--VLW-LETYLLKWPKTFIVVSHARE 402
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
65-269 |
1.10e-05 |
|
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: 45.62 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 65 VDRLCLGVRPGECFGLLGVNGAGKTTTF----KMLtgdesTTGGEAFIGGSSILK-ELLRVQQSIGYCPQFDALFEDlTA 139
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLsaflRLL-----NTEGDIQIDGVSWNSvPLQKWRKAFGVIPQKVFIFSG-TF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 140 REHLELYTRlrgipWKDEE--RVVSWALEKLELSKYAD-----MPAGTY--SGGNKRKLSTAIALIGYPSLVFLDEPTTG 210
Cdd:cd03289 94 RKNLDPYGK-----WSDEEiwKVAEEVGLKSVIEQFPGqldfvLVDGGCvlSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641957197 211 MDPkarrFLWNLILDILK---TGRSVVLTSHSMeecEAL--CTRLGIMVNGRFKCLGSIQHLKN 269
Cdd:cd03289 169 LDP----ITYQVIRKTLKqafADCTVILSEHRI---EAMleCQRFLVIEENKVRQYDSIQKLLN 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
175-258 |
1.21e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 175 DMPAGTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSMEECEALCTRLGIMV 254
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMN 478
|
....
gi 641957197 255 NGRF 258
Cdd:NF040905 479 EGRI 482
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
182-238 |
1.74e-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: 43.89 E-value: 1.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641957197 182 SGGNKRKLSTAIAL----IGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSH 238
Cdd:cd03227 79 SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
44-238 |
2.35e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.63 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmgrILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTG--DESTTGGEAFIGGSSILKEL--LR 119
Cdd:CHL00131 7 ILEIKNLHASVNENE---IL--KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEpeER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 VQQSIGYCPQFDALFEDLTAREHLEL-YT---RLRGIPWKDEERVVSWALEKLELskyADMPAG--------TYSGGNKR 187
Cdd:CHL00131 82 AHLGIFLAFQYPIEIPGVSNADFLRLaYNskrKFQGLPELDPLEFLEIINEKLKL---VGMDPSflsrnvneGFSGGEKK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 641957197 188 K---LSTAIAligYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSH 238
Cdd:CHL00131 159 RneiLQMALL---DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
68-238 |
2.37e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.54 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 68 LCLGVRPGECFGLLGVNGAGKTTTFKMLTGdeSTTG-GEAFIGGSSI----LKELLRVQqsiGY-CPQFDALFEdLTARE 141
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG--LLPGsGSIQFAGQPLeawsAAELARHR---AYlSQQQTPPFA-MPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 142 HLELYtRLRGIPWKDEERVVSWALEKLELSKYADMPAGTYSGGN-KRKLSTAIALIGYPS------LVFLDEPTTGMDPK 214
Cdd:PRK03695 89 YLTLH-QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEwQRVRLAAVVLQVWPDinpagqLLLLDEPMNSLDVA 167
|
170 180
....*....|....*....|....
gi 641957197 215 ARRFLWNLILDILKTGRSVVLTSH 238
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSSH 191
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
45-212 |
2.46e-05 |
|
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: 44.33 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 45 LKIDNLTKVYKSrKMGRILavDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK-ELLRVQQS 123
Cdd:cd03369 7 IEVENLSVRYAP-DLPPVL--KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQFDALFeDLTAREHLELYTRlrgipWKDEErvvswALEKLELSKYADmpagTYSGGNKRKLSTAIALIGYPSLVF 203
Cdd:cd03369 84 LTIIPQDPTLF-SGTIRSNLDPFDE-----YSDEE-----IYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLV 148
|
....*....
gi 641957197 204 LDEPTTGMD 212
Cdd:cd03369 149 LDEATASID 157
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
44-257 |
3.46e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.41 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKmGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGdesttggeafiggssILKELLRVQQS 123
Cdd:PRK15093 3 LLDIRNLTIEFKTSD-GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG---------------VTKDNWRVTAD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 124 IGYCPQFDALfeDLTAREHLELYTR-----------------------LRGIP-WKDEER---VVSW----ALEKLELSK 172
Cdd:PRK15093 67 RMRFDDIDLL--RLSPRERRKLVGHnvsmifqepqscldpservgrqlMQNIPgWTYKGRwwqRFGWrkrrAIELLHRVG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 173 YAD----MPAGTY--SGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILK-TGRSVVLTSHSMEECEA 245
Cdd:PRK15093 145 IKDhkdaMRSFPYelTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQ 224
|
250
....*....|..
gi 641957197 246 LCTRLGIMVNGR 257
Cdd:PRK15093 225 WADKINVLYCGQ 236
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
47-212 |
3.57e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 44.71 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 47 IDNLTKVYKSRKmgriLAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGG---SSILKELLR---- 119
Cdd:PRK10790 343 IDNVSFAYRDDN----LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplSSLSHSVLRqgva 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 -VQQSigycPQF--DALFEDLTAREHLelytrlrgipwkDEERVvsW-ALEKLELSKYA-DMPAGTY----------SGG 184
Cdd:PRK10790 419 mVQQD----PVVlaDTFLANVTLGRDI------------SEEQV--WqALETVQLAELArSLPDGLYtplgeqgnnlSVG 480
|
170 180
....*....|....*....|....*...
gi 641957197 185 NKRKLSTAIALIGYPSLVFLDEPTTGMD 212
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANID 508
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
44-257 |
4.46e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.31 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKMGRiLAVDRLCLGVRPGECFGLLGVNGAGKTTT----FKML-TGDESTTGGEAFIGGSSILK--- 115
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVR-TVVNDVSLQIEAGETLALVGESGSGKSVTalsiLRLLpSPPVVYPSGDIRFHGESLLHase 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 116 -ELLRVQQSigycpQFDALFEDLTAR------------EHLELYTRLRGIPWKDE-----ERV-VSWALEKLelskyADM 176
Cdd:PRK15134 84 qTLRGVRGN-----KIAMIFQEPMVSlnplhtlekqlyEVLSLHRGMRREAARGEilnclDRVgIRQAAKRL-----TDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 177 PAgTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRflwnLILDILKT-----GRSVVLTSHSMEECEALCTRLG 251
Cdd:PRK15134 154 PH-QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQA----QILQLLRElqqelNMGLLFITHNLSIVRKLADRVA 228
|
....*.
gi 641957197 252 IMVNGR 257
Cdd:PRK15134 229 VMQNGR 234
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
44-270 |
1.52e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 42.59 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSrKMGRILAVDRLCLGVRPGECFGLLGVNGAGKTTTFKMLTG--DEST--TGGEAFIGGssilKELLR 119
Cdd:COG4170 3 LLDIRNLTIEIDT-PQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGitKDNWhvTADRFRWNG----IDLLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 120 ---------VQQSIGYCPQ------------FDALFEDLTAREhlelytrLRGIPWK----DEERVVSWaLEKLELSKYA 174
Cdd:COG4170 78 lsprerrkiIGREIAMIFQepsscldpsakiGDQLIEAIPSWT-------FKGKWWQrfkwRKKRAIEL-LHRVGIKDHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 175 D-MPAGTY--SGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKT-GRSVVLTSHSMEECEALCTRL 250
Cdd:COG4170 150 DiMNSYPHelTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTI 229
|
250 260
....*....|....*....|
gi 641957197 251 GIMVNGRFKCLGSIQHLKNR 270
Cdd:COG4170 230 TVLYCGQTVESGPTEQILKS 249
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
155-238 |
1.72e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 155 KDEERVVSWA-----LEKLElSKYaDMPAGTY----SGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILD 225
Cdd:PTZ00265 1326 EDVKRACKFAaidefIESLP-NKY-DTNVGPYgkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1403
|
90
....*....|....
gi 641957197 226 IL-KTGRSVVLTSH 238
Cdd:PTZ00265 1404 IKdKADKTIITIAH 1417
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
80-239 |
1.74e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 42.26 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 80 LLGVNGAGKTTTFKMLTGDESTTGgeAFIGGS-----SILKELLRVQQSIGYCPQFDALFedltarehLELYTRLRGIPW 154
Cdd:COG4938 25 LIGPNGSGKSTLIQALLLLLQSNF--IYLPAErsgpaRLYPSLVRELSDLGSRGEYTADF--------LAELENLEILDD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 155 KDE---ERVVSWaLEKLELSKY---ADMPAG-----TYSGGNKRKLS-------------TAIALIGYP-SLVFLDEPTT 209
Cdd:COG4938 95 KSKellEQVEEW-LEKIFPGKVevdASSDLVrlvfrPSGNGKRIPLSnvgsgvsellpilLALLSAAKPgSLLIIEEPEA 173
|
170 180 190
....*....|....*....|....*....|
gi 641957197 210 GMDPKARRFLWNLILDILKTGRSVVLTSHS 239
Cdd:COG4938 174 HLHPKAQSALAELLAELANSGVQVIIETHS 203
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
177-239 |
1.78e-04 |
|
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: 41.15 E-value: 1.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641957197 177 PAGTYSGGNKR--KLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHS 239
Cdd:cd03238 84 KLSTLSGGELQrvKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
44-238 |
1.96e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 44 MLKIDNLTKVYKSRKMGRILAVDrlclgVRPGECFGLLGVNGAGKTTTFKMLTGDE--STTGGEAFIGGSSILKELLRVQ 121
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLE-----VRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 122 QSIGYCPQFDALFEDLTAREHLELYTRL------RGIPWKDEERVVSWALEKLELSKyadMPAGT--------YSGGNKR 187
Cdd:PRK09580 76 AGEGIFMAFQYPVEIPGVSNQFFLQTALnavrsyRGQEPLDRFDFQDLMEEKIALLK---MPEDLltrsvnvgFSGGEKK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 641957197 188 KLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSH 238
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
68-212 |
3.71e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.89 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 68 LCLGVRPGECFGLLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILK-ELLRVQQSIGYCPQFDALFEDlTAREHLELY 146
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLFSG-TVRFNIDPF 1333
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 147 TRLRGIP-WKDEERV-VSWALEKLELSKYADMPAG--TYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMD 212
Cdd:PLN03232 1334 SEHNDADlWEALERAhIKDVIDRNPFGLDAEVSEGgeNFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
162-240 |
5.79e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 162 SWALEKLELSKyadmPAGTYSGGNKRKLSTAIALIG---YPSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSH 238
Cdd:PRK00635 795 SLGLDYLPLGR----PLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
..
gi 641957197 239 SM 240
Cdd:PRK00635 871 NM 872
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
80-264 |
1.22e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 39.86 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 80 LLGVNGAGKTTTFKMLTGDESTTGGEAFIGGSSILKELLRV-----QQSIGYCPQfDA-LFEDLTAREHLeLYtrlrGIP 153
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRIGYVFQ-DArLFPHYKVRGNL-RY----GMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641957197 154 WKDEE---RVVSW-ALEKLeLSKYadmPAgTYSGGNKRKLSTAIALIGYPSLVFLDEPTTGMD-PKARR---FLWNLILD 225
Cdd:PRK11144 103 KSMVAqfdKIVALlGIEPL-LDRY---PG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKREllpYLERLARE 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 641957197 226 IlKTgrSVVLTSHSMEECEALCTRLGIMVNGRFKCLGSI 264
Cdd:PRK11144 178 I-NI--PILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
199-241 |
1.67e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.22 E-value: 1.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 641957197 199 PSLVFLDEPTTGMDPKARRFLWNLILDILKTGRSVVLTSHSME 241
Cdd:COG3593 188 NPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPH 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
182-242 |
5.35e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 37.45 E-value: 5.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641957197 182 SGGNKRKLSTAIALIGYPSLVFLDEPTTGMDPKARRFLWNLILDiLKTGRSVVLTSHSMEE 242
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHE-LKEQYTIIIVTHNMQQ 212
|
|
|