|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-214 |
3.35e-62 |
|
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: 192.69 E-value: 3.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASF 91
Cdd:COG4133 6 ENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVVLARLLGIPSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQ 171
Cdd:COG4133 86 LKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1838243270 172 GIQDMERIIAELKASGVTVILATHlIEQGLTLCEErLHLQDGR 214
Cdd:COG4133 166 GVALLAELIAAHLARGGAVLLTTH-QPLELAAARV-LDLGDFK 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
12-217 |
2.84e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 191.05 E-value: 2.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASF 91
Cdd:COG1131 4 RGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVVLARLLGIPSPQDAASA--LLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:COG1131 84 LYPDLTVRENLRFFARLYGLPRKEARERIdeLLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1838243270 170 PQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:COG1131 164 PEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVA 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-217 |
2.20e-51 |
|
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: 166.19 E-value: 2.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASF 91
Cdd:COG4555 5 ENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDERG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVVLARLLGIPSPQDAASA--LLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:COG4555 85 LYDRLTVRENIRYFAELYGLFDEELKKRIeeLIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1838243270 170 PQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:COG4555 165 VMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVA 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-214 |
5.78e-50 |
|
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: 160.26 E-value: 5.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASFL 92
Cdd:cd03230 5 NLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPEEPSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 YEDLTAHQNLvvlarllgipspqdaasalltrvgltrrsdspvrSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQG 172
Cdd:cd03230 85 YENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1838243270 173 IQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:cd03230 131 RREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-199 |
5.78e-46 |
|
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: 151.22 E-value: 5.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASFl 92
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGF- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 YEDLTAHQNLVVLARLLGIPSpqDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQG 172
Cdd:cd03268 84 YPNLTARENLRLLARLLGIRK--KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180
....*....|....*....|....*..
gi 1838243270 173 IQDMERIIAELKASGVTVILATHLIEQ 199
Cdd:cd03268 162 IKELRELILSLRDQGITVLISSHLLSE 188
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
16-218 |
2.49e-44 |
|
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: 149.85 E-value: 2.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 16 KRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASFLYED 95
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 96 LTAHQNLVVLARLLGIPS--PQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGI 173
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKdeAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1838243270 174 QDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAE 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
12-214 |
1.80e-43 |
|
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: 145.03 E-value: 1.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLtGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASF 91
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVVLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:cd03264 83 VYPNFTVREFLDYIAWLKGIPSKEvkARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1838243270 170 PQgiqdmERI-----IAELkASGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:cd03264 163 PE-----ERIrfrnlLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
12-218 |
4.79e-41 |
|
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: 138.57 E-value: 4.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAvadRDAVRRDVALLSHASF 91
Cdd:cd03269 4 ENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL---DIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVVLARLLGIPsPQDAASA---LLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGEL 168
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLK-KEEARRRideWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1838243270 169 DPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-195 |
7.08e-41 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 138.01 E-value: 7.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 26 RLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASFLYEDLTAHQNLVVL 105
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 106 ARLLGIPSPQDAASALlTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKA 185
Cdd:PRK13538 99 QRLHGPGDDEALWEAL-AQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAE 177
|
170
....*....|
gi 1838243270 186 SGVTVILATH 195
Cdd:PRK13538 178 QGGMVILTTH 187
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-218 |
1.33e-40 |
|
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: 137.89 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASFL 92
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 YEDLTAHQNLVVLARLLGIPSPQDA--ASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDP 170
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPGAERRerIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1838243270 171 QGIQDMERIIAELKAS-GVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:cd03265 165 QTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
12-199 |
2.57e-40 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 137.15 E-value: 2.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAvrRDVALLSHASF 91
Cdd:TIGR03740 4 KNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHP-WTRKDL--HKIGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVVLARLLGIPSPQdaASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQ 171
Cdd:TIGR03740 81 LYENLTARENLKVHTTLLGLPDSR--IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPI 158
|
170 180
....*....|....*....|....*...
gi 1838243270 172 GIQDMERIIAELKASGVTVILATHLIEQ 199
Cdd:TIGR03740 159 GIQELRELIRSFPEQGITVILSSHILSE 186
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-195 |
7.97e-39 |
|
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: 132.87 E-value: 7.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASF 91
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVVLARLLGipSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQ 171
Cdd:TIGR01189 84 LKPELSALENLHFWAAIHG--GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....
gi 1838243270 172 GIQDMERIIAELKASGVTVILATH 195
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-214 |
3.86e-38 |
|
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: 131.46 E-value: 3.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYG----RRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV----ADRDAVRRDva 84
Cdd:cd03255 5 NLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklseKELAAFRRR-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 85 llsHASFLY------EDLTAHQNLVVLARLLGIPSPQDA--ASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAP 156
Cdd:cd03255 83 ---HIGFVFqsfnllPDLTALENVELPLLLAGVPKKERRerAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838243270 157 TLALLDEPFGELDPQGIQDMERIIAEL-KASGVTVILATH---LIEqgltLCEERLHLQDGR 214
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHdpeLAE----YADRIIELRDGK 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
12-216 |
6.74e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 130.94 E-value: 6.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGR-RWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAvadRDAVRRDVALL---- 86
Cdd:COG2884 5 ENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL---SRLKRREIPYLrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 87 --SHASF-LYEDLTAHQNlVVLA-RLLGIPSP--QDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLAL 160
Cdd:COG2884 82 gvVFQDFrLLPDRTVYEN-VALPlRVTGKSRKeiRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 161 LDEPFGELDPQGIQDMERIIAELKASGVTVILATH---LIEQgltlCEER-LHLQDGRAV 216
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHdleLVDR----MPKRvLELEDGRLV 216
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-198 |
2.07e-37 |
|
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: 129.55 E-value: 2.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRW--ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHAS 90
Cdd:cd03263 5 NLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQFD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYEDLTAHQNLVVLARLLGIP-SPQDAASALLTR-VGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGEL 168
Cdd:cd03263 85 ALFDELTVREHLRFYARLKGLPkSEIKEEVELLLRvLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190
....*....|....*....|....*....|
gi 1838243270 169 DPQGIQDMERIIAELKaSGVTVILATHLIE 198
Cdd:cd03263 165 DPASRRAIWDLILEVR-KGRSIILTTHSMD 193
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-214 |
5.81e-37 |
|
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: 128.35 E-value: 5.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGR--RWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDvallsHA 89
Cdd:cd03225 3 KNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR-----KV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYEDlTAHQ--NLVVLA------RLLGIPSPQD--AASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLA 159
Cdd:cd03225 78 GLVFQN-PDDQffGPTVEEevafglENLGLPEEEIeeRVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1838243270 160 LLDEPFGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-217 |
6.94e-37 |
|
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: 128.60 E-value: 6.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY-GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-AVADRDAVRRDVALLshas 90
Cdd:COG1122 5 NLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDiTKKNLRELRRKVGLV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 flyedltaHQN----LV---VLA------RLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKA 155
Cdd:COG1122 81 --------FQNpddqLFaptVEEdvafgpENLGLPREEirERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838243270 156 PTLALLDEPFGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-214 |
9.32e-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: 123.51 E-value: 9.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-AVADRDAVRRDVALLshas 90
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDiAKLPLEELRRRIGYV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 flyedltahqnlvvlarllgipsPQdaasalltrvgltrrsdspvrsFSAGMRKRLAIARLLLKAPTLALLDEPFGELDP 170
Cdd:cd00267 79 -----------------------PQ----------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1838243270 171 QGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-218 |
1.49e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 127.15 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDavaDRDAVRRDVALLSHASF 91
Cdd:COG4152 5 KGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---LDPEDRRRIGYLPEERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVVLARLLGIpSPQDA---ASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGEL 168
Cdd:COG4152 82 LYPKMKVGEQLVYLARLKGL-SKAEAkrrADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1838243270 169 DPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:COG4152 161 DPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
12-217 |
2.24e-35 |
|
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: 124.17 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAVRRDVALLSHASF 91
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRD-VTGVPPERRNIGMVFQDYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVVLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:cd03259 83 LFPHLTVAENIAFGLKLRGVPKAEirARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1838243270 170 PQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:cd03259 163 AKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
13-217 |
5.18e-35 |
|
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: 123.63 E-value: 5.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY----GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSH 88
Cdd:cd03266 6 ALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQNLVVLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFG 166
Cdd:cd03266 86 STGLYDRLTARENLEYFAGLYGLKGDEltARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1838243270 167 ELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:cd03266 166 GLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-214 |
1.46e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.89 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAvadrDAVRRDVALLSHASF 91
Cdd:COG1121 10 ENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP----RRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYED--LTAHQnlVVLA------RLLGIPSPQD--AASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALL 161
Cdd:COG1121 86 VDWDfpITVRD--VVLMgrygrrGLFRRPSRADreAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1838243270 162 DEPFGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:COG1121 164 DEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGL 216
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
12-214 |
6.45e-34 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 120.43 E-value: 6.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGR-RWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRD----AVRRDVALL 86
Cdd:TIGR02673 5 HNVSKAYPGgVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGrqlpLLRRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 87 SHASFLYEDLTAHQNLVVLARLLGIPSP--QDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEP 164
Cdd:TIGR02673 85 FQDFRLLPDRTVYENVALPLEVRGKKEReiQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1838243270 165 FGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:TIGR02673 165 TGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-217 |
3.22e-33 |
|
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: 118.79 E-value: 3.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRdavrRDVALLS-HAS 90
Cdd:cd03235 3 EDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER----KRIGYVPqRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYE-DLTAHQnLVVLAR-----LLGIPSPQD--AASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLD 162
Cdd:cd03235 79 IDRDfPISVRD-VVLMGLyghkgLFRRLSKADkaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1838243270 163 EPFGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLqDGRAVA 217
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVA 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-206 |
5.08e-32 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 115.36 E-value: 5.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAvaDRDAVRRDVALLSHASF 91
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVVLARLLGipSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQ 171
Cdd:PRK13539 84 MKPALTVAENLEFWAAFLG--GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1838243270 172 GIQDMERIIAELKASGVTVILATHlIEQGLTLCEE 206
Cdd:PRK13539 162 AVALFAELIRAHLAQGGIVIAATH-IPLGLPGARE 195
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
12-217 |
6.37e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 115.53 E-value: 6.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYG----RRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV----ADRDAVRRDv 83
Cdd:COG1136 8 RNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslseRELARLRRR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 84 allsHASF------LYEDLTAHQNLVVLARLLGIPSPQDAASA--LLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKA 155
Cdd:COG1136 87 ----HIGFvfqffnLLPELTALENVALPLLLAGVSRKERRERAreLLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838243270 156 PTLALLDEPFGELDPQ-GIQDMErIIAEL-KASGVTVILATH---LIEQgltlCEERLHLQDGRAVA 217
Cdd:COG1136 163 PKLILADEPTGNLDSKtGEEVLE-LLRELnRELGTTIVMVTHdpeLAAR----ADRVIRLRDGRIVS 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-218 |
1.00e-31 |
|
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: 115.91 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA-DRDAVRRDVALLSHAS 90
Cdd:COG1120 5 ENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVPQEP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYEDLTAHQnLVVLAR-----LLGIPSPQD--AASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDE 163
Cdd:COG1120 85 PAPFGLTVRE-LVALGRyphlgLFGRPSAEDreAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838243270 164 PFGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:COG1120 164 PTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-196 |
1.68e-31 |
|
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: 113.74 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 19 GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASFLYEDLTA 98
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 99 HQNLVVLARLLGIPSPQDAasalLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMER 178
Cdd:cd03231 91 LENLRFWHADHSDEQVEEA----LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
170
....*....|....*...
gi 1838243270 179 IIAELKASGVTVILATHL 196
Cdd:cd03231 167 AMAGHCARGGMVVLTTHQ 184
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-218 |
2.76e-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: 114.14 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD----AVADRDAVRRDVALLSH 88
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglSEAELYRLRRRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQNLVVLARLLGIPSP---QDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:cd03261 85 SGALFDSLTVFENVAFPLREHTRLSEeeiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1838243270 166 GELDPQGIQDMERIIAELKAS-GVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:cd03261 165 AGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
12-204 |
3.34e-31 |
|
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: 113.72 E-value: 3.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRW----ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVAdrdaVRRDVALLS 87
Cdd:cd03293 4 RNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG----PGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 88 HASFLYEDLTAHQNLVVLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:cd03293 80 QQDALLPWLTVLDNVALGLELQGVPKAEarERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1838243270 166 GELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLC 204
Cdd:cd03293 160 SALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLA 199
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-165 |
1.53e-30 |
|
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: 110.04 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 24 LARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-AVADRDAVRRDVALLSHASFLYEDLTAHQNL 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDlTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838243270 103 VVLARLLGIPSPQDA--ASALLTRVGLT----RRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:pfam00005 81 RLGLLLKGLSKREKDarAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-217 |
2.14e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 113.75 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASF 91
Cdd:PRK13537 11 RNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQFDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVVLARLLGIPSPQDAA--SALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:PRK13537 91 LDPDFTVRENLLVFGRYFGLSAAAARAlvPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1838243270 170 PQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:PRK13537 171 PQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIA 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
12-198 |
4.10e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 111.72 E-value: 4.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRY----GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAvadrDAVRRDVALL- 86
Cdd:COG1116 11 RGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----TGPGPDRGVVf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 87 -SHAsfLYEDLTAHQNLVVLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDE 163
Cdd:COG1116 87 qEPA--LLPWLTVLDNVALGLELRGVPKAErrERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1838243270 164 PFGELDPQGIQDMERIIAEL-KASGVTVILATHLIE 198
Cdd:COG1116 165 PFGALDALTRERLQDELLRLwQETGKTVLFVTHDVD 200
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-218 |
6.29e-30 |
|
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: 110.94 E-value: 6.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAG-RVEVLGRD----AVADrdaVRRDVALL 86
Cdd:COG1119 7 RNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggeDVWE---LRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 87 SHA--SFLYEDLTAHQnlVVLARL---LGI---PSPQDAASA--LLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAP 156
Cdd:COG1119 84 SPAlqLRFPRDETVLD--VVLSGFfdsIGLyrePTDEQRERAreLLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838243270 157 TLALLDEPFGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-217 |
1.12e-29 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 109.93 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 16 KRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAvadrdavrrdvALLSHASFLYED 95
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----------SLLGLGGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 96 LTAHQNLVVLARLLGIpsPQDAASALLTRV----GLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQ 171
Cdd:cd03220 99 LTGRENIYLNGRLLGL--SRKEIDEKIDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1838243270 172 GIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:cd03220 177 FQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
13-195 |
1.74e-29 |
|
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: 109.45 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD--AVADRDAVRRDVALlshaS 90
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitGLPPHEIARLGIGR----T 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 F----LYEDLTAHQNLVVLARLLGIPSP------------QDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLK 154
Cdd:cd03219 81 FqiprLFPELTVLENVMVAAQARTGSGLllararreereaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1838243270 155 APTLALLDEPFGELDPQGIQDMERIIAELKASGVTVILATH 195
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEH 201
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-217 |
2.04e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 111.85 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASFL 92
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 YEDLTAHQNLVVLARLLGIPSPQDAA--SALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDP 170
Cdd:PRK13536 126 DLEFTVRENLLVFGRYFGMSTREIEAviPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1838243270 171 QGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:PRK13536 206 HARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIA 252
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-211 |
4.09e-29 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 108.01 E-value: 4.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 27 LTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV-ADRDavrRDVALLSHASFLYEDLTAHQNLVVL 105
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATrGDRS---RFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 106 ARLLGIpSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKA 185
Cdd:PRK13543 107 CGLHGR-RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLR 185
|
170 180
....*....|....*....|....*.
gi 1838243270 186 SGVTVILATHLIEQGLTLCEERLHLQ 211
Cdd:PRK13543 186 GGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-217 |
8.51e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 107.86 E-value: 8.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 16 KRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRdaVAdrdavrrdvALLSHASFLYED 95
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR--VS---------ALLELGAGFHPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 96 LTAHQNLVVLARLLGIpSPQDAAsALLTRV----GLTRRSDSPVRSFSAGMRKRL--AIArLLLKAPTLaLLDEPFGELD 169
Cdd:COG1134 103 LTGRENIYLNGRLLGL-SRKEID-EKFDEIvefaELGDFIDQPVKTYSSGMRARLafAVA-TAVDPDIL-LVDEVLAVGD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1838243270 170 PQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:COG1134 179 AAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
12-217 |
4.23e-28 |
|
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: 106.22 E-value: 4.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV----ADRDAVRRDVALLS 87
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseKELYELRRRIGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 88 HASFLYEDLTAHQNLVV-LARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEP 164
Cdd:COG1127 89 QGGALFDSLTVFENVAFpLREHTDLSEAEirELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1838243270 165 FGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:COG1127 169 TAGLDPITSAVIDELIRELrDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
12-214 |
4.93e-28 |
|
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: 104.19 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAV---RRDVALLSH 88
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQNLVvlarllgipspqdaasalltrVGLtrrsdspvrsfSAGMRKRLAIARLLLKAPTLALLDEPFGEL 168
Cdd:cd03229 84 DFALFPHLTVLENIA---------------------LGL-----------SGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1838243270 169 DPQGIQDMERIIAELKA-SGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:cd03229 132 DPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-214 |
5.78e-28 |
|
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: 105.18 E-value: 5.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRW-ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDA----VRRDVALLS 87
Cdd:cd03292 5 NVTKTYPNGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipyLRRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 88 HASFLYEDLTAHQNLVVLARLLGIPsPQDAA---SALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEP 164
Cdd:cd03292 85 QDFRLLPDRNVYENVAFALEVTGVP-PREIRkrvPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1838243270 165 FGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
12-192 |
7.64e-28 |
|
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: 105.89 E-value: 7.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD--AVADRDAVRRDVALlsha 89
Cdd:COG0411 8 RGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitGLPPHRIARLGIAR---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SF----LYEDLTAHQNLVV----------LARLLGIPSP-------QDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAI 148
Cdd:COG0411 84 TFqnprLFPELTVLENVLVaaharlgrglLAALLRLPRArreereaRERAEELLERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1838243270 149 ARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKA-SGVTVIL 192
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILL 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-218 |
8.62e-28 |
|
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: 104.93 E-value: 8.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA---DRDAvRRDVALLSHA 89
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmHKRA-RLGIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYEDLTAHQNLVVLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGE 167
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIRGLSKKEreEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1838243270 168 LDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAE 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-216 |
3.68e-27 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 103.98 E-value: 3.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRY-GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRD----AVRRDVALL 86
Cdd:COG3638 6 RNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrRLRRRIGMI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 87 sHASF-LYEDLTAHQNlvVLA----------RLLGIPSPQD--AASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLL 153
Cdd:COG3638 86 -FQQFnLVPRLSVLTN--VLAgrlgrtstwrSLLGLFPPEDreRALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838243270 154 KAPTLALLDEPFGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:COG3638 163 QEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
12-218 |
2.16e-26 |
|
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: 99.82 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGrdavadrdavrRDVALLSHASf 91
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-----------KDLASLSPKE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 lyedltahqnlvvLARLLGIpSPQdaasaLLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQ 171
Cdd:cd03214 71 -------------LARKIAY-VPQ-----ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1838243270 172 GIQDMERIIAELKAS-GVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:cd03214 132 HQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-216 |
2.97e-26 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 101.22 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY-GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAV--RRDVALLSHA 89
Cdd:cd03295 5 NVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGED-IREQDPVelRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYEDLTAHQNLVVLARLLGIPSPQ--DAASALLTRVGLTRRS--DSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:cd03295 84 IGLFPHMTVEENIALVPKLLKWPKEKirERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1838243270 166 GELDP----QGIQDMERIIAELkasGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:cd03295 164 GALDPitrdQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
13-218 |
4.54e-26 |
|
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: 100.26 E-value: 4.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRrwALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAVRRDVALLSHASFL 92
Cdd:cd03298 5 KIRFSYGE--QPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD-VTAAPPADRPVSMLFQENNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 YEDLTAHQNlVVLARLLGI---PSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:cd03298 82 FAHLTVEQN-VGLGLSPGLkltAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1838243270 170 PQGIQDMERIIAELKA-SGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:cd03298 161 PALRAEMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
12-195 |
1.18e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 101.71 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGR--SLLltGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAVRRDVALL--S 87
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEfvALL--GPSGCGKTTLLRMIAGFETPDSGRILLDGRD-VTGLPPEKRNVGMVfqD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 88 HAsfLYEDLTAHQN----LvvlaRLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALL 161
Cdd:COG3842 86 YA--LFPHLTVAENvafgL----RMRGVPKAEirARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1838243270 162 DEPFGELDPQGIQDMERIIAEL-KASGVTVILATH 195
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLqRELGITFIYVTH 194
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-214 |
1.79e-25 |
|
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: 99.34 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAvADRDAVRRDVALLSHASFL 92
Cdd:cd03296 7 NVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 YEDLTAHQN----LVVLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFG 166
Cdd:cd03296 86 FRHMTVFDNvafgLRVKPRSERPPEAEirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1838243270 167 ELDPQGIQDMERIIAELKAS-GVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:cd03296 166 ALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-218 |
1.89e-25 |
|
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: 103.30 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRY-GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-AVADRDAVRRDVALLSHA 89
Cdd:COG4988 340 EDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDlSDLDPASWRRQIAWVPQN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYEDlTAHQNLvvlarLLGIPSPQDAA-SALLTRVGLTR--RS-----DSPV----RSFSAGMRKRLAIARLLLKAPT 157
Cdd:COG4988 420 PYLFAG-TIRENL-----RLGRPDASDEElEAALEAAGLDEfvAAlpdglDTPLgeggRGLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838243270 158 LALLDEPFGELDPQGIQDMERIIAELkASGVTVILATHLIEQgLTLCEERLHLQDGRAVAA 218
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLAL-LAQADRILVLDDGRIVEQ 552
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
12-216 |
7.14e-25 |
|
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: 7.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVA-----TALSPTAGRVEVLGRDAVA---DRDAVRRDV 83
Cdd:cd03260 4 RDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlndlIPGAPDEGEVLLDGKDIYDldvDVLELRRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 84 ALLSHASFLYeDLTAHQNLVVLARLLGIpSPQDAASAL----LTRVGLTRR--SDSPVRSFSAGMRKRLAIARLLLKAPT 157
Cdd:cd03260 84 GMVFQKPNPF-PGSIYDNVAYGLRLHGI-KLKEELDERveeaLRKAALWDEvkDRLHALGLSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1838243270 158 LALLDEPFGELDPQGIQDMERIIAELKASgVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
12-195 |
9.50e-25 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 96.44 E-value: 9.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADR---DAVRRDVALLSH 88
Cdd:cd03262 4 KNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKkniNELRQKVGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQNLVV-LARLLGIP--SPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:cd03262 84 QFNLFPHLTVLENITLaPIKVKGMSkaEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190
....*....|....*....|....*....|
gi 1838243270 166 GELDPQGIQDMERIIAELKASGVTVILATH 195
Cdd:cd03262 164 SALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-218 |
1.44e-24 |
|
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: 100.61 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRY--GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA-DRDAVRRDVALLSH 88
Cdd:COG4987 337 EDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAVVPQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDlTAHQNLvvlarLLGIPSPQDAA-SALLTRVGLTRRS-------DSPV----RSFSAGMRKRLAIARLLLKAP 156
Cdd:COG4987 417 RPHLFDT-TLRENL-----RLARPDATDEElWAALERVGLGDWLaalpdglDTWLgeggRRLSGGERRRLALARALLRDA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838243270 157 TLALLDEPFGELDPQGIQD-MERIIAELKasGVTVILATHlIEQGLTLCEERLHLQDGRAVAA 218
Cdd:COG4987 491 PILLLDEPTEGLDAATEQAlLADLLEALA--GRTVLLITH-RLAGLERMDRILVLEDGRIVEQ 550
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-218 |
5.98e-24 |
|
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: 94.81 E-value: 5.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 1 MPPLPAPALALHDVSKRYGRRWA----LARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA-D 75
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAlD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 76 RDA---VRRDvallsHASFLYED------LTAHQNLVVLARLLGIPSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRL 146
Cdd:COG4181 81 EDArarLRAR-----HVGFVFQSfqllptLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838243270 147 AIARLLLKAPTLALLDEPFGELD-PQGiqdmERIIAEL----KASGVTVILATHliEQGLTL-CEERLHLQDGRAVAA 218
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDaATG----EQIIDLLfelnRERGTTLVLVTH--DPALAArCDRVLRLRAGRLVED 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-216 |
6.83e-24 |
|
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: 94.94 E-value: 6.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGR-RWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRD----AVRRDVALL 86
Cdd:cd03256 4 ENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrQLRRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 87 SHASFLYEDLTAHQNLVV--LAR------LLGIPSPQD--AASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAP 156
Cdd:cd03256 84 FQQFNLIERLSVLENVLSgrLGRrstwrsLFGLFPKEEkqRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838243270 157 TLALLDEPFGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-198 |
8.14e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 94.77 E-value: 8.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLG---RDAVADRDAVRRDVALLSH 88
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvNDPKVDERLIRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQNLV---VLARLLGIPSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:PRK09493 85 QFYLFPHLTALENVMfgpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190
....*....|....*....|....*....|...
gi 1838243270 166 GELDPQGIQDMERIIAELKASGVTVILATHLIE 198
Cdd:PRK09493 165 SALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-203 |
1.07e-23 |
|
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: 94.23 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAVRRDVALLSHASFLY 93
Cdd:cd03300 6 VSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD-ITNLPPHKRPVNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 94 EDLTAHQNLVVLARLLGIP--SPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQ 171
Cdd:cd03300 85 PHLTVFENIAFGLRLKKLPkaEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190
....*....|....*....|....*....|...
gi 1838243270 172 GIQDMERIIAEL-KASGVTVILATHLIEQGLTL 203
Cdd:cd03300 165 LRKDMQLELKRLqKELGITFVFVTHDQEEALTM 197
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-209 |
1.34e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 93.79 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRY-GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDA----VRRDVALLSH 88
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQNlVVLARLLGIPSPQDA---ASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:PRK10908 87 DHHLLMDRTVYDN-VAIPLIIAGASGDDIrrrVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1838243270 166 GELDPQGIQDMERIIAELKASGVTVILATH---LIEQG----LTLCEERLH 209
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRVGVTVLMATHdigLISRRsyrmLTLSDGHLH 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-195 |
1.43e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.07 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 17 RYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRdavadrdavrRDVALLSHASFLYEDL 96
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----------ARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 97 TAH-QNLVVLAR-----LLGIPSPQD--AASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGEL 168
Cdd:NF040873 71 PLTvRDLVAMGRwarrgLWRRLTRDDraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180
....*....|....*....|....*..
gi 1838243270 169 DPQGIQDMERIIAELKASGVTVILATH 195
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTH 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-217 |
1.47e-23 |
|
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: 97.67 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY--GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTA---GRVEVLGRDAVADRDAVRRdvallS 87
Cdd:COG1123 9 DLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRG-----R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 88 HASFLYEDLTAHQNLVVLA-------RLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTL 158
Cdd:COG1123 84 RIGMVFQDPMTQLNPVTVGdqiaealENLGLSRAEarARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 159 ALLDEPFGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVE 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-214 |
1.72e-23 |
|
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: 92.06 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYG--RRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-AVADRDAVRRDVALLSH 88
Cdd:cd03228 4 KNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlRDLDLESLRKNIAYVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDlTAHQNLvvlarllgipspqdaasalltrvgltrrsdspvrsFSAGMRKRLAIARLLLKAPTLALLDEPFGEL 168
Cdd:cd03228 84 DPFLFSG-TIRENI-----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1838243270 169 DPQGIQDMERIIAELKAsGVTVILATHLIEQgLTLCEERLHLQDGR 214
Cdd:cd03228 128 DPETEALILEALRALAK-GKTVIVIAHRLST-IRDADRIIVLDDGR 171
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-203 |
1.94e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.16 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYG----RRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRdAV----ADRDAVRRDVA 84
Cdd:COG4525 8 HVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-PVtgpgADRGVVFQKDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 85 LLSHasflyedLTAHQNLVVLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLD 162
Cdd:COG4525 87 LLPW-------LNVLDNVAFGLRLRGVPKAErrARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1838243270 163 EPFGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTL 203
Cdd:COG4525 160 EPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFL 201
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
12-214 |
2.01e-23 |
|
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: 93.09 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAVRRDVALLSHASF 91
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-VTDLPPKDRDIAMVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVVLARLLGIPSP------QDAASALltrvGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:cd03301 83 LYPHMTVYDNIAFGLKLRKVPKDeidervREVAELL----QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1838243270 166 GELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
12-206 |
3.89e-23 |
|
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: 92.50 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD--AVADRDAVRRDVALLSHA 89
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDitGLPPHERARAGIGYVPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYEDLTAHQNLVVLARLLGIPSPQ---DAASALLTRvgLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFG 166
Cdd:cd03224 84 RRIFPELTVEENLLLGAYARRRAKRKarlERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1838243270 167 ELDPQGIQDMERIIAELKASGVTVIlathLIEQGLTLCEE 206
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDEGVTIL----LVEQNARFALE 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
39-214 |
4.30e-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: 92.36 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 39 LTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAV-----RRDVALLSHASFLYEDLTAHQNLVVLARLLGIPS 113
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLVFQQYALFPHLNVRENLAFGLKRKRNRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 114 PQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDP----QGIQDMERIIAELKasgVT 189
Cdd:cd03297 108 DRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRalrlQLLPELKQIKKNLN---IP 184
|
170 180
....*....|....*....|....*
gi 1838243270 190 VILATHLIEQGLTLCEERLHLQDGR 214
Cdd:cd03297 185 VIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
13-195 |
1.03e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.98 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAVRRDVALL--SHAs 90
Cdd:COG3839 8 NVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-VTDLPPKDRNIAMVfqSYA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 fLYEDLTAHQNLVVLARLLGIPSPQ-----DAASALLtrvGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:COG3839 86 -LYPHMTVYENIAFPLKLRKVPKAEidrrvREAAELL---GLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190
....*....|....*....|....*....|.
gi 1838243270 166 GELDPQGIQDMERIIAEL-KASGVTVILATH 195
Cdd:COG3839 162 SNLDAKLRVEMRAEIKRLhRRLGTTTIYVTH 192
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-216 |
1.15e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.00 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLG-----RDAVADRD--AVRRDVALL 86
Cdd:COG4161 8 INCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfSQKPSEKAirLLRQKVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 87 SHASFLYEDLTAHQNLV-VLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDE 163
Cdd:COG4161 88 FQQYNLWPHLTVMENLIeAPCKVLGLSKEQarEKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1838243270 164 PFGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:COG4161 168 PTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-215 |
1.78e-22 |
|
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: 89.58 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYG--RRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDA-VADRDAVRRDVALLSHA 89
Cdd:cd03246 5 NVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYEDlTAHQNLvvlarllgipspqdaasalltrvgltrrsdspvrsFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:cd03246 85 DELFSG-SIAENI-----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1838243270 170 PQGIQDMERIIAELKASGVTVILATHLIEQgLTLCEERLHLQDGRA 215
Cdd:cd03246 129 VEGERALNQAIAALKAAGATRIVIAHRPET-LASADRILVLEDGRV 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-217 |
2.56e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 92.90 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLshasF 91
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFV----F 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 ----LYEDLTAHQNLVVLARLLGIPSPQDAASA--LLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:COG1118 82 qhyaLFPHMTVAENIAFGLRVRPPSKAEIRARVeeLLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1838243270 166 GELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:COG1118 162 GALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQ 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-195 |
3.74e-22 |
|
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: 93.81 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRW-----ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD----AVADRDAVRRD 82
Cdd:COG1123 264 RNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklSRRSLRELRRR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 83 VALL--SHASFLYEDLTAHQNLVVLARLLGIPSPQDA---ASALLTRVGLTRRS-DSPVRSFSAGMRKRLAIARLLLKAP 156
Cdd:COG1123 344 VQMVfqDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERrerVAELLERVGLPPDLaDRYPHELSGGQRQRVAIARALALEP 423
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1838243270 157 TLALLDEPFGELDPQGIQDMERIIAELKAS-GVTVILATH 195
Cdd:COG1123 424 KLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISH 463
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-217 |
4.38e-22 |
|
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: 90.25 E-value: 4.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRW----ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRD-AVRRDVALL 86
Cdd:COG1124 5 RNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 87 ---SHASF---------LYEDLTAHqnlvvlarllGIPSPQDAASALLTRVGLTRR-SDSPVRSFSAGMRKRLAIARLLL 153
Cdd:COG1124 85 fqdPYASLhprhtvdriLAEPLRIH----------GLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838243270 154 KAPTLALLDEPFGELDPqGIQD-MERIIAELKA-SGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:COG1124 155 LEPELLLLDEPTSALDV-SVQAeILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVE 219
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
23-198 |
5.47e-22 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 89.02 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRD---AVRRDVALL---SHASFLYEDL 96
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKgllERRQRVGLVfqdPDDQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 97 TahQNLVVLARLLGIPSPQDAASA--LLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQ 174
Cdd:TIGR01166 87 D--QDVAFGPLNLGLSEAEVERRVreALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|....
gi 1838243270 175 DMERIIAELKASGVTVILATHLIE 198
Cdd:TIGR01166 165 QMLAILRRLRAEGMTVVISTHDVD 188
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
12-198 |
9.12e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.30 E-value: 9.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGR--------DAVADRdAVRRDV 83
Cdd:PRK11124 6 NGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpSDKAIR-ELRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 84 ALLSHASFLYEDLTAHQNLV-VLARLLGIPSPQDAASA--LLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLAL 160
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNLIeAPCRVLGLSKDQALARAekLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1838243270 161 LDEPFGELDPQGIQDMERIIAELKASGVTVILATHLIE 198
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVE 202
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-216 |
9.44e-22 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 89.28 E-value: 9.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGR-RWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDA----VRRDVALL 86
Cdd:TIGR02315 5 ENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrkLRRRIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 87 SHASFLYEDLTAHQNLVV--------LARLLGIPSPQDAASAL--LTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAP 156
Cdd:TIGR02315 85 FQHYNLIERLTVLENVLHgrlgykptWRSLLGRFSEEDKERALsaLERVGLADKAYQRADQLSGGQQQRVAIARALAQQP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838243270 157 TLALLDEPFGELDP----QGIQDMERIIAELkasGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:TIGR02315 165 DLILADEPIASLDPktskQVMDYLKRINKED---GITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-214 |
2.17e-21 |
|
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: 92.00 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 18 YGRRwALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASFLYEDLT 97
Cdd:TIGR01257 941 SGRP-AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 98 AHQNLVVLARLLGIP--SPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQD 175
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSweEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190
....*....|....*....|....*....|....*....
gi 1838243270 176 MERIIAELKaSGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:TIGR01257 1100 IWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-213 |
2.66e-21 |
|
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: 87.31 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGR-RWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDavRRDVALLSHAS 90
Cdd:cd03226 3 ENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER--RKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 --FLYEDLTAHQnlvVLARLLGIPSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGEL 168
Cdd:cd03226 81 dyQLFTDSVREE---LLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1838243270 169 DPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDG 213
Cdd:cd03226 158 DYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
14-218 |
2.86e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.60 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV---ADRDAVRRDVALLSHAS 90
Cdd:PRK11248 7 LYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAERGVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLyedltahQNLVVLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGEL 168
Cdd:PRK11248 87 VQ-------DNVAFGLQLAGVEKMQrlEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838243270 169 DPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCE-------------ERLHLQDGRAVAA 218
Cdd:PRK11248 160 DAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATelvllspgpgrvvERLPLNFARRFVA 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
34-215 |
3.21e-21 |
|
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: 87.91 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 34 GRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA---DRDAVRRDVALLSHasflyedLTAHQN--LVVLARL 108
Cdd:TIGR01184 11 GEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpDRMVVFQNYSLLPW-------LTVRENiaLAVDRVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 109 LGIPSPQDAA--SALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDM-ERIIAELKA 185
Cdd:TIGR01184 84 PDLSKSERRAivEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLqEELMQIWEE 163
|
170 180 190
....*....|....*....|....*....|
gi 1838243270 186 SGVTVILATHLIEQGLTLCEERLHLQDGRA 215
Cdd:TIGR01184 164 HRVTVLMVTHDVDEALLLSDRVVMLTNGPA 193
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
13-217 |
3.58e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.50 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTyaLPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAVRRDVALLSHASFL 92
Cdd:COG3840 6 DLTYRYGDFPLRFDLT--IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-LTALPPAERPVSMLFQENNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 YEDLTAHQNLvvlarLLGIpSP--------QDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEP 164
Cdd:COG3840 83 FPHLTVAQNI-----GLGL-RPglkltaeqRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1838243270 165 FGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:COG3840 157 FSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-217 |
4.43e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.64 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDA--VADRDAVRRDVALLSHAS 90
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIslLPLHARARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYEDLTAHQNLVVLARL---LGIPSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGE 167
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIrddLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1838243270 168 LDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-217 |
5.77e-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: 85.17 E-value: 5.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDA--VADRDAVRRDVAllshas 90
Cdd:cd03216 5 GITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVsfASPRDARRAGIA------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 flyedlTAHQnlvvlarllgipspqdaasalltrvgltrrsdspvrsFSAGMRKRLAIARLLLKAPTLALLDEPFGELDP 170
Cdd:cd03216 79 ------MVYQ-------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1838243270 171 QGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:cd03216 116 AEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-217 |
6.11e-21 |
|
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: 87.00 E-value: 6.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDA-VRRDVALLSHASFLYEDLTAHQN 101
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKfLRRIGVVFGQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 102 LVVLARLLGIPSPQ-----DAASALLTrvgLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDM 176
Cdd:cd03267 116 FYLLAAIYDLPPARfkkrlDELSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1838243270 177 ERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:cd03267 193 RNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-217 |
6.19e-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: 90.28 E-value: 6.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRR--WALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-AVADRDAVRRDVALLSH 88
Cdd:COG2274 477 ENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlRQIDPASLRRQIGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDlTAHQNLvvlarLLGIPS-PQDAASALLTRVGLTR--RS-----DSPV----RSFSAGMRKRLAIARLLLKAP 156
Cdd:COG2274 557 DVFLFSG-TIRENI-----TLGDPDaTDEEIIEAARLAGLHDfiEAlpmgyDTVVgeggSNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838243270 157 TLALLDEPFGELDPQGiqdmERIIAE-LK--ASGVTVILATH---LIEqgltLCEERLHLQDGRAVA 217
Cdd:COG2274 631 RILILDEATSALDAET----EAIILEnLRrlLKGRTVIIIAHrlsTIR----LADRIIVLDKGRIVE 689
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
24-195 |
6.74e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 86.16 E-value: 6.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 24 LARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASFLYEDLTAHQNLV 103
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 104 VlarLLGIPSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAEL 183
Cdd:PRK13540 97 Y---DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEH 173
|
170
....*....|..
gi 1838243270 184 KASGVTVILATH 195
Cdd:PRK13540 174 RAKGGAVLLTSH 185
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-216 |
8.86e-21 |
|
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: 86.48 E-value: 8.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRW----ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV----ADRDAVRRDVA 84
Cdd:cd03258 6 NVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKARRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 85 LLSHASFLYEDLTAHQNLVVLARLLGIPSPQDAASA--LLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLD 162
Cdd:cd03258 86 MIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVleLLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1838243270 163 EPFGELDPQGIQDMERIIAELKAS-GVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-216 |
1.15e-20 |
|
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: 86.93 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD--AVADRD--AVRRD------ 82
Cdd:cd03294 29 EILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaAMSRKElrELRRKkismvf 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 83 --VALLSHASFLyedltahQNLVVLARLLGIPSPQDAASAL--LTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTL 158
Cdd:cd03294 109 qsFALLPHRTVL-------ENVAFGLEVQGVPRAEREERAAeaLELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1838243270 159 ALLDEPFGELDPQGIQDMERIIAELKA-SGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAeLQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
23-218 |
2.72e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 86.33 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDA-VRRDVALLSH-------ASFLYE 94
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVGLVFQdpddqvfSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 95 DLT-AHQNLVvlarlLGIPSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGI 173
Cdd:PRK13647 100 DVAfGPVNMG-----LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1838243270 174 QDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:PRK13647 175 ETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-195 |
3.31e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 85.08 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA---DRDAvRRDVALLSH 88
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmHKRA-RLGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQNLVVLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFG 166
Cdd:COG1137 86 EASIFRKLTVEDNILAVLELRKLSKKEreERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180
....*....|....*....|....*....
gi 1838243270 167 ELDPQGIQDMERIIAELKASGVTVILATH 195
Cdd:COG1137 166 GVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-195 |
3.74e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.08 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAVRRDVALLSHASFL 92
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED-VTHRSIQQRDICMVFQSYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 YEDLTAHQNLVVLARLLGIPSPQ-----DAASALltrVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGE 167
Cdd:PRK11432 90 FPHMSLGENVGYGLKMLGVPKEErkqrvKEALEL---VDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180
....*....|....*....|....*....
gi 1838243270 168 LDPQGIQDMERIIAELKAS-GVTVILATH 195
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQfNITSLYVTH 195
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-195 |
6.16e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 6.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLG-------------------RDA 72
Cdd:COG0488 2 ENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqeppldddltvLDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 73 VADRDAVRRDV-----ALLSHASFLYEDLTAHQNLVVLARLLGIPSPQDAASALLTRVGLTRRS-DSPVRSFSAGMRKRL 146
Cdd:COG0488 82 VLDGDAELRALeaeleELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDlDRPVSELSGGWRRRV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1838243270 147 AIARLLLKAPTLALLDEPFGELDPQGIQDMERIiaeLKASGVTVILATH 195
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLESIEWLEEF---LKNYPGTVLVVSH 207
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
12-216 |
6.76e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.59 E-value: 6.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEvlgrdaVADRDAVRRDVALLSHASF 91
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH------YRMRDGQLRDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTA----HQN------LVVLA------RLLGIPSP-----QDAASALLTRV--GLTRRSDSPvRSFSAGMRKRLAI 148
Cdd:PRK11701 84 RRLLRTEwgfvHQHprdglrMQVSAggnigeRLMAVGARhygdiRATAGDWLERVeiDAARIDDLP-TTFSGGMQQRLQI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838243270 149 ARLLLKAPTLALLDEPFGELD---PQGIQDMER-IIAELkasGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDvsvQARLLDLLRgLVREL---GLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-204 |
1.37e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 86.61 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASFLYEDLTAHQNL 102
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 103 VVLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERII 180
Cdd:TIGR01257 2034 YLYARLRGVPAEEieKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180
....*....|....*....|....
gi 1838243270 181 AELKASGVTVILATHLIEQGLTLC 204
Cdd:TIGR01257 2114 VSIIREGRAVVLTSHSMEECEALC 2137
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-195 |
1.38e-19 |
|
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: 86.19 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRY-GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-AVADRDAVRRDVALLSHASF 91
Cdd:TIGR02857 327 VSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPlADADADSWRDQIAWVPQHPF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAhqNLVVLARLlgipspqDAASALLTRV---------------GLTRRSDSPVRSFSAGMRKRLAIARLLLKAP 156
Cdd:TIGR02857 407 LFAGTIA--ENIRLARP-------DASDAEIREAleragldefvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190
....*....|....*....|....*....|....*....
gi 1838243270 157 TLALLDEPFGELDPQGIQDMERIIAELkASGVTVILATH 195
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTH 515
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
23-216 |
2.05e-19 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 83.65 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRD----AVRRDVALLshasF------L 92
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkklkDLRKKVGLV----FqfpehqL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 YEDLTAH------QNLVVlarllgipSPQDA---ASALLTRVGLTR--RSDSPVrSFSAGMRKRLAIARLLLKAPTLALL 161
Cdd:TIGR04521 96 FEETVYKdiafgpKNLGL--------SEEEAeerVKEALELVGLDEeyLERSPF-ELSGGQMRRVAIAGVLAMEPEVLIL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838243270 162 DEPFGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:TIGR04521 167 DEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-195 |
2.32e-19 |
|
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: 82.55 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRW----ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV----ADRDAVRRDV 83
Cdd:cd03257 5 KNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsrRLRKIRRKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 84 ALL---SHASF---------LYEDLTAHQNLVVLARLlgipspQDAASALLTRVGL-TRRSDSPVRSFSAGMRKRLAIAR 150
Cdd:cd03257 85 QMVfqdPMSSLnprmtigeqIAEPLRIHGKLSKKEAR------KEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1838243270 151 LLLKAPTLALLDEPFGELDPQgIQDmeRIIAELK----ASGVTVILATH 195
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVS-VQA--QILDLLKklqeELGLTLLFITH 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
34-218 |
3.90e-19 |
|
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: 82.38 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 34 GRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAVRRDVALLSHASFLYEDLTAHQNLVVLARLLGIPS 113
Cdd:cd03299 25 GDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKD-ITNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 114 PQDAA-----SALLtrvGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQgIQdmERIIAELK---- 184
Cdd:cd03299 104 KEIERkvleiAEML---GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR-TK--EKLREELKkirk 177
|
170 180 190
....*....|....*....|....*....|....
gi 1838243270 185 ASGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:cd03299 178 EFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-217 |
4.12e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 18 YGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD--AVADRDAVRRdVALLSHASFLYED 95
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPisMLSSRQLARR-LALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 96 LTAHQnLVVLAR-----LLGIPSPQDAASA--LLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGEL 168
Cdd:PRK11231 91 ITVRE-LVAYGRspwlsLWGRLSAEDNARVnqAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1838243270 169 DPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:PRK11231 170 DINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMA 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
24-195 |
5.85e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.78 E-value: 5.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 24 LARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-AVADRDAV---RRD--------VALLSHasf 91
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvATLDADALaqlRREhfgfifqrYHLLSH--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 lyedLTAHQNLVVLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:PRK10535 101 ----LTAAQNVEVPAVYAGLERKQrlLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
170 180
....*....|....*....|....*.
gi 1838243270 170 PQGIQDMERIIAELKASGVTVILATH 195
Cdd:PRK10535 177 SHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-195 |
6.42e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.59 E-value: 6.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAVRRDVALLSHASFLY 93
Cdd:PRK10851 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTD-VSRLHARDRKVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 94 EDLTAHQN----LVVLARLlgiPSPQDAA-----SALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEP 164
Cdd:PRK10851 87 RHMTVFDNiafgLTVLPRR---ERPNAAAikakvTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1838243270 165 FGELDPQGIQDMERII----AELKASGVTVilaTH 195
Cdd:PRK10851 164 FGALDAQVRKELRRWLrqlhEELKFTSVFV---TH 195
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
12-199 |
8.17e-19 |
|
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: 81.57 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDA---VRRDVALLSH 88
Cdd:COG0410 7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-ITGLPPhriARLGIGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQNLVVLARLLGipsPQDAASALLTRVG-----LTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDE 163
Cdd:COG0410 86 GRRIFPSLTVEENLLLGAYARR---DRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1838243270 164 PFGELDPQGIQDMERIIAELKASGVTVIlathLIEQ 199
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLNREGVTIL----LVEQ 194
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-194 |
2.11e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.86 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVAD---RDAVRRDVAllsh 88
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGD-MADarhRRAVCPRIA---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 asF--------LYEDLTAHQNLVVLARLLGipspQDAA------SALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLK 154
Cdd:NF033858 80 --YmpqglgknLYPTLSVFENLDFFGRLFG----QDAAerrrriDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1838243270 155 APTLALLDEPFGELDPQGIQDMERIIAELKAS--GVTVILAT 194
Cdd:NF033858 154 DPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVAT 195
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-198 |
3.49e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.40 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-----------AVADRDAVR- 80
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlKVADKNQLRl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 81 ---RDVALLSHASfLYEDLTAHQNLV-VLARLLGIpSPQDA---ASALLTRVGLTRRSDS--PVRsFSAGMRKRLAIARL 151
Cdd:PRK10619 90 lrtRLTMVFQHFN-LWSHMTVLENVMeAPIQVLGL-SKQEArerAVKYLAKVGIDERAQGkyPVH-LSGGQQQRVSIARA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1838243270 152 LLKAPTLALLDEPFGELDPQGIQDMERIIAELKASGVTVILATHLIE 198
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
23-216 |
4.14e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.28 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAV---RRDVALL----SHASFlyeD 95
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLmklRESVGMVfqdpDNQLF---S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 96 LTAHQNLVVLARLLGIPSP--QDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGI 173
Cdd:PRK13636 98 ASVYQDVSFGAVNLKLPEDevRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1838243270 174 QDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:PRK13636 178 SEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
12-195 |
5.08e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.68 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSP---TAGRVEVLGRDaVADRDAVRRDVALLSH 88
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRR-LTALPAEQRRIGILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQNLVV-LARLLGIPSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGE 167
Cdd:COG4136 84 DDLLFPHLSVGENLAFaLPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170 180
....*....|....*....|....*....
gi 1838243270 168 LDPQGIQDMER-IIAELKASGVTVILATH 195
Cdd:COG4136 164 LDAALRAQFREfVFEQIRQRGIPALLVTH 192
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-214 |
5.33e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.65 E-value: 5.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVlgrdavadrdAVRRDVALLS-HAS 90
Cdd:COG0488 319 EGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL----------GETVKIGYFDqHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYEDLTAHQNLVVLARLLGIPSpqdaASALLTRVGLTR-RSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:COG0488 389 ELDPDKTVLDELRDGAPGGTEQE----VRGYLGRFLFSGdDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1838243270 170 PQGIQDMERIIAELKasGvTVILATH---LIEqglTLCEERLHLQDGR 214
Cdd:COG0488 465 IETLEALEEALDDFP--G-TVLLVSHdryFLD---RVATRILEFEDGG 506
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
12-214 |
5.55e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.09 E-value: 5.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGR----RWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRV----EVLGRDAVADRDAVR-RD 82
Cdd:PRK11629 9 DNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngQPMSKLSSAAKAELRnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 83 VALLSHASFLYEDLTAHQNlVVLARLLGIPSPQDA---ASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLA 159
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALEN-VAMPLLIGKKKPAEInsrALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838243270 160 LLDEPFGELDPQGIQDMERIIAELKAS-GVTVILATHLIEQGLTLcEERLHLQDGR 214
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRM-SRQLEMRDGR 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-217 |
5.93e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.60 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVAD--RDAVRRDVAL---- 85
Cdd:COG1129 8 RGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRspRDAQAAGIAIihqe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 86 LShasfLYEDLTAHQNLvVLARLLGIPSPQD------AASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLA 159
Cdd:COG1129 88 LN----LVPNLSVAENI-FLGREPRRGGLIDwramrrRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1838243270 160 LLDEPFGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVG 220
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
13-198 |
6.96e-18 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 79.40 E-value: 6.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY--GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRD---AVRRDVALLs 87
Cdd:TIGR04520 5 NVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDEEnlwEIRKKVGMV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 88 hasFlyedltahQN----LVvlARL-----------LGIPSP------QDAasalLTRVGLTRRSDSPVRSFSAGMRKRL 146
Cdd:TIGR04520 83 ---F--------QNpdnqFV--GATveddvafglenLGVPREemrkrvDEA----LKLVGMEDFRDREPHLLSGGQKQRV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1838243270 147 AIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKAS-GVTVILATHLIE 198
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDME 198
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-195 |
6.97e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.87 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 24 LARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADR-----DAVRRDVALLSH--ASFLYEDl 96
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknlKKLRKKVSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 97 TAHQNLVVLARLLGIPSPQDAASAL--LTRVGLTRR--SDSPVrSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQG 172
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEKALkwLKKVGLSEDliSKSPF-ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180
....*....|....*....|...
gi 1838243270 173 IQDMERIIAELKASGVTVILATH 195
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTH 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
41-195 |
1.43e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.55 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 41 GHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASFLYEDLTAHQNLVVLARLLGIPSPQDAA-- 118
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAArv 378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838243270 119 SALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAEL-KASGVTVILATH 195
Cdd:NF033858 379 AEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsREDGVTIFISTH 456
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-214 |
1.63e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.18 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGrvEVL-GRDAVADrdaVRRDVALlshasf 91
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--ELLaGTAPLAE---AREDTRL------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDltahqnlvvlARLLGIPSP------------QDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLA 159
Cdd:PRK11247 86 MFQD----------ARLLPWKKVidnvglglkgqwRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838243270 160 LLDEPFGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
13-214 |
1.72e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.61 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAVRRDV-------AL 85
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD-ITHVPAENRHVntvfqsyAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 86 LSHasflyedLTAHQNLVVLARLLGIPSPQDAASAL--LTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDE 163
Cdd:PRK09452 98 FPH-------MTVFENVAFGLRMQKTPAAEITPRVMeaLRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1838243270 164 PFGELDPQGIQDMEriiAELKA----SGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:PRK09452 171 SLSALDYKLRKQMQ---NELKAlqrkLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
14-213 |
2.11e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.13 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVA---TALSPTAGRVEVLGRdAVADRDAVRRDV-ALLSHA 89
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSgliTGDKSAGSHIELLGR-TVQREGRLARDIrKSRANT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYEDLTAHQNLVVLARLL-----GIP---------SPQDAASAL--LTRVGLTRRSDSPVRSFSAGMRKRLAIARLLL 153
Cdd:PRK09984 89 GYIFQQFNLVNRLSVLENVLigalgSTPfwrtcfswfTREQKQRALqaLTRVGMVHFAHQRVSTLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838243270 154 KAPTLALLDEPFGELDPQGiqdmERIIAEL-----KASGVTVILATHLIEQGLTLCEERLHLQDG 213
Cdd:PRK09984 169 QQAKVILADEPIASLDPES----ARIVMDTlrdinQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
39-198 |
2.80e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 78.25 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 39 LTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA-----DRDAVRRDVALLSH--ASFLYEDlTAHQNLVVLARLLGI 111
Cdd:PRK13649 38 FIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNFGV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 112 pSPQDA---ASALLTRVGLTR--RSDSPVrSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKAS 186
Cdd:PRK13649 117 -SQEEAealAREKLALVGISEslFEKNPF-ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS 194
|
170
....*....|..
gi 1838243270 187 GVTVILATHLIE 198
Cdd:PRK13649 195 GMTIVLVTHLMD 206
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
34-218 |
3.63e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 34 GRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA-DRDAVRRDVALLSHASFLYEDLTAHQNLVV-----LAR 107
Cdd:PRK09536 29 GSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASRRVASVPQDTSLSFEFDVRQVVEMgrtphRSR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 108 LLGIPSPQDAA-SALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD-PQGIQDMErIIAELKA 185
Cdd:PRK09536 109 FDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQVRTLE-LVRRLVD 187
|
170 180 190
....*....|....*....|....*....|...
gi 1838243270 186 SGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:PRK09536 188 DGKTAVAAIHDLDLAARYCDELVLLADGRVRAA 220
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-203 |
5.01e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.34 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAVRRDVALLSHASFL 92
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRPINMMFQSYAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 YEDLTAHQNLVVLARLLGIPSPQDAA--SALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDP 170
Cdd:PRK11607 103 FPHMTVEQNIAFGLKQDKLPKAEIASrvNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
170 180 190
....*....|....*....|....*....|....
gi 1838243270 171 QGIQDME-RIIAELKASGVTVILATHLIEQGLTL 203
Cdd:PRK11607 183 KLRDRMQlEVVDILERVGVTCVMVTHDQEEAMTM 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-199 |
6.52e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.98 E-value: 6.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY--GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGR----DAVADrdaVRRDVALL 86
Cdd:PRK13635 10 HISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseETVWD---VRRQVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 87 shasFLYED-----LTAHQNLVVLARLLGIPSPQ-----DAAsalLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAP 156
Cdd:PRK13635 87 ----FQNPDnqfvgATVQDDVAFGLENIGVPREEmvervDQA---LRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1838243270 157 TLALLDEPFGELDPQGIQDMERIIAELKA-SGVTVILATHLIEQ 199
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDE 203
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
28-216 |
9.17e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.77 E-value: 9.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 28 TYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD--AVAD---RDAVRRDVALLSHASFLYEDLTAHQNL 102
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiaKISDaelREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 103 VVLARLLGIPSPQDAASAL--LTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERII 180
Cdd:PRK10070 128 AFGMELAGINAEERREKALdaLRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190
....*....|....*....|....*....|....*..
gi 1838243270 181 AELKASGV-TVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:PRK10070 208 VKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-214 |
1.76e-16 |
|
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: 73.89 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYG--RRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHA 89
Cdd:cd03247 4 NNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYedltahqnlvvlarllgipspqdaASALLTRVGltrrsdspvRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:cd03247 84 PYLF------------------------DTTLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1838243270 170 PQGIQDMERIIAELkASGVTVILATHLIeQGLTLCEERLHLQDGR 214
Cdd:cd03247 131 PITERQLLSLIFEV-LKDKTLIWITHHL-TGIEHMDKILFLENGK 173
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
33-195 |
1.80e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.56 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 33 AGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEV------LGRDAVADRDAVRRdvaLLSHASFLYEDLTAHQNLVVLA 106
Cdd:PRK11264 28 PGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLIRQ---LRQHVGFVFQNFNLFPHRTVLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 107 RLLGIP-----SPQDAASA----LLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDME 177
Cdd:PRK11264 105 NIIEGPvivkgEPKEEATArareLLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVL 184
|
170
....*....|....*...
gi 1838243270 178 RIIAELKASGVTVILATH 195
Cdd:PRK11264 185 NTIRQLAQEKRTMVIVTH 202
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-195 |
1.90e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.99 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVAD--RDAVRRDVALLsHAS 90
Cdd:COG3845 10 GITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRspRDAIALGIGMV-HQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 F-LYEDLTAHQNlVVLA---RLLGIPSPQDAA---SALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDE 163
Cdd:COG3845 89 FmLVPNLTVAEN-IVLGlepTKGGRLDRKAARariRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190
....*....|....*....|....*....|..
gi 1838243270 164 PFGELDPQGIQDMERIIAELKASGVTVILATH 195
Cdd:COG3845 168 PTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
12-216 |
1.98e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.92 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDA--VRRDVALLSHA 89
Cdd:PRK11614 9 DKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIVPEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYEDLTAHQNLVvlarLLGIPSPQDAASALLTRV-----GLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEP 164
Cdd:PRK11614 89 RRVFSRMTVEENLA----MGGFFAERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1838243270 165 FGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
23-195 |
2.84e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.11 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDA---VRRDVALLshasFLYED---- 95
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSlleVRKTVGIV----FQNPDdqlf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 96 -LTAHQNLVVLARLLGIPSP--QDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQG 172
Cdd:PRK13639 93 aPTVEEDVAFGPLNLGLSKEevEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180
....*....|....*....|...
gi 1838243270 173 IQDMERIIAELKASGVTVILATH 195
Cdd:PRK13639 173 ASQIMKLLYDLNKEGITIIISTH 195
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-217 |
3.84e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.64 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 18 YGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGR--DAVADRDAVRRdVALLSHASFLYED 95
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiQHYASKEVARR-IGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 96 LTAhQNLVVLARLLGIP-------SPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGEL 168
Cdd:PRK10253 96 ITV-QELVARGRYPHQPlftrwrkEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1838243270 169 DPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:PRK10253 175 DISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-198 |
6.24e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.38 E-value: 6.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEV-----LGRDAVADRDAVRRDVALLSH--ASFLYED 95
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvSSTSKQKEIKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 96 lTAHQNLVVLARLLGIpSPQDA---ASALLTRVGLTRR--SDSPVRsFSAGMRKRLAIARLLLKAPTLALLDEPFGELDP 170
Cdd:PRK13643 101 -TVLKDVAFGPQNFGI-PKEKAekiAAEKLEMVGLADEfwEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180
....*....|....*....|....*...
gi 1838243270 171 QGIQDMERIIAELKASGVTVILATHLIE 198
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTHLMD 205
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
13-206 |
9.90e-16 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 72.94 E-value: 9.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADR--DAVRRDVALLSHAS 90
Cdd:TIGR03410 5 NLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPphERARAGIAYVPQGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYEDLTAHQNLVVLARLLGIPS---PQDAAS------ALLTRVGltrrsdspvRSFSAGMRKRLAIARLLLKAPTLALL 161
Cdd:TIGR03410 85 EIFPRLTVEENLLTGLAALPRRSrkiPDEIYElfpvlkEMLGRRG---------GDLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1838243270 162 DEPFGELDPQGIQDMERIIAELKAS-GVTVIlathLIEQGLTLCEE 206
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAEgGMAIL----LVEQYLDFARE 197
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
12-214 |
1.18e-15 |
|
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: 70.94 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVlgrdavadrdavrrdvalLSHASF 91
Cdd:cd03221 4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW------------------GSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYedltahqnlvvlarllgipspqdaasalltrvgltrrsdspVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQ 171
Cdd:cd03221 66 GY-----------------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1838243270 172 GIqdmERIIAELKASGVTVILATH---LIEQgltLCEERLHLQDGR 214
Cdd:cd03221 105 SI---EALEEALKEYPGTVILVSHdryFLDQ---VATKIIELEDGK 144
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-195 |
1.31e-15 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 73.30 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 1 MPPLPAPALALHDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEV-----------LG 69
Cdd:COG4598 1 MTDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVggeeirlkpdrDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 70 RDAVADRDAVRRDVALLSHA--SF-LYEDLTAHQNlVVLA--RLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGM 142
Cdd:COG4598 81 ELVPADRRQLQRIRTRLGMVfqSFnLWSHMTVLEN-VIEApvHVLGRPKAEaiERAEALLAKVGLADKRDAYPAHLSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1838243270 143 RKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKASGVTVILATH 195
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-216 |
1.34e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.16 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 24 LARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALS------PTAGRVEVLGRDAVA-DRDAVRRDVALLSHASFLYEDL 96
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQiDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 97 TAHQNLVVLARLLGIPSPQDAASAL---LTRVGLTR----RSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKIVeecLRKVGLWKevydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1838243270 170 PQGIQDMERIIAELKASgVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:PRK14246 186 IVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-195 |
1.45e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALS--PTAGRVEVlgrdavaDRDAVRRDVALLSHasf 91
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV-------PDNQFGREASLIDA--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 lyedltahqnlvvlarlLGIPSPQDAASALLTRVGLtrrSD-----SPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFG 166
Cdd:COG2401 106 -----------------IGRKGDFKDAVELLNAVGL---SDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|
gi 1838243270 167 ELDPQGIQDMERIIAEL-KASGVTVILATH 195
Cdd:COG2401 166 HLDRQTAKRVARNLQKLaRRAGITLVVATH 195
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-199 |
1.54e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.20 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 20 RRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDA--VRRDVALLSH-------AS 90
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwdIRNKAGMVFQnpdnqivAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYEDLT-AHQNLvvlarllGIPSPQ-----DAAsalLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEP 164
Cdd:PRK13633 102 IVEEDVAfGPENL-------GIPPEEirervDES---LKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1838243270 165 FGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQ 199
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKELnKKYGITIILITHYMEE 207
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
13-195 |
1.72e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.86 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY-GRRW-ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVeVLGRDAVADRD------------- 77
Cdd:PRK13648 12 NVSFQYqSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNfeklrkhigivfq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 78 ---------AVRRDVAL-LSHASFLYEDLtahqnlvvlarllgipspQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLA 147
Cdd:PRK13648 91 npdnqfvgsIVKYDVAFgLENHAVPYDEM------------------HRRVSEALKQVDMLERADYEPNALSGGQKQRVA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1838243270 148 IARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKAS-GVTVILATH 195
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITH 201
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-217 |
2.65e-15 |
|
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: 71.85 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA-DRDAVRRDVALLSHASFLYEDlTAHQN 101
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFYG-TLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 102 LVvlarlLGIPSPQDA---ASALLTRVG-LTRRS----DSPV----RSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:cd03245 98 IT-----LGAPLADDErilRAAELAGVTdFVNKHpnglDLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1838243270 170 pqgIQDMERIIAELKA--SGVTVILATHLIEQgLTLCEERLHLQDGRAVA 217
Cdd:cd03245 173 ---MNSEERLKERLRQllGDKTLIIITHRPSL-LDLVDRIIVMDSGRIVA 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
13-217 |
3.25e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.11 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA-DRD---AVRRDVALLSH 88
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmSRSrlyTVRKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQNLVV-LARLLGIPSPQDAASAL--LTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:PRK11831 92 SGALFTDMNVFDNVAYpLREHTQLPAPLLHSTVMmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1838243270 166 GELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:PRK11831 172 VGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVA 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-218 |
3.71e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGR--DAVADRDAVRRDVALLSHASF 91
Cdd:PRK09700 11 IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInyNKLDHKLAAQLGIGIIYQELS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVV----LARLLGIP-----SPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLD 162
Cdd:PRK09700 91 VIDELTVLENLYIgrhlTKKVCGVNiidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838243270 163 EPFGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCS 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-216 |
4.60e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 73.30 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVA---------------TALSPTAGRVEVLGRDA----- 72
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmdqyeptsgriiyhVALCEKCGYVERPSKVGepcpv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 73 --------VAD--------RDAVRRDVALLSHASF-LYEDLTAHQNLVVLARLLGIPSPQ--DAASALLTRVGLTRRSDS 133
Cdd:TIGR03269 85 cggtlepeEVDfwnlsdklRRRIRKRIAIMLQRTFaLYGDDTVLDNVLEALEEIGYEGKEavGRAVDLIEMVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 134 PVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQG---IQDMerIIAELKASGVTVILATHLIEQGLTLCEERLHL 210
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTaklVHNA--LEEAVKASGISMVLTSHWPEVIEDLSDKAIWL 242
|
....*.
gi 1838243270 211 QDGRAV 216
Cdd:TIGR03269 243 ENGEIK 248
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
34-214 |
5.81e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.96 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 34 GRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA----DRDAVR-RDVALLSHASFLYEDLTAHQNLVVLARL 108
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKLRaKHVGFVFQSFMLIPTLNALENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 109 LGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAEL-KA 185
Cdd:PRK10584 116 RGESSRQsrNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnRE 195
|
170 180
....*....|....*....|....*....
gi 1838243270 186 SGVTVILATHlIEQGLTLCEERLHLQDGR 214
Cdd:PRK10584 196 HGTTLILVTH-DLQLAARCDRRLRLVNGQ 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-195 |
6.68e-15 |
|
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: 70.76 E-value: 6.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 21 RWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATAL---SPTAGRVEVLGRDAvaDRDAVRRDVALLSHASFLYEDLT 97
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPR--KPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 98 AHQNLVVLARLLGiPSPQD-------AASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDP 170
Cdd:cd03234 98 VRETLTYTAILRL-PRKSSdairkkrVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180
....*....|....*....|....*
gi 1838243270 171 QGIQDMERIIAELKASGVTVILATH 195
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIH 201
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
13-217 |
7.10e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 71.36 E-value: 7.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVeVLGRDAVADRD--AVRRDVALLSHAS 90
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLESWSskAFARKVAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYEDLTAHQnLVVLARL--------LGIPSPQDAASAlLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLD 162
Cdd:PRK10575 95 PAAEGMTVRE-LVAIGRYpwhgalgrFGAADREKVEEA-ISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1838243270 163 EPFGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-195 |
7.23e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.03 E-value: 7.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 18 YGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLV--ATALSPTA---GRVEVLGRDAVA-DRDA--VRRDVALLSHA 89
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEEArveGEVRLFGRNIYSpDVDPieVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYEDLTAHQNLVVLARLLGIPSPQD----------AASALLTRVGlTRRSDSPvRSFSAGMRKRLAIARLLLKAPTLA 159
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLVKSKKeldervewalKKAALWDEVK-DRLNDYP-SNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1838243270 160 LLDEPFGELDPQGIQDMERIIAELKASgVTVILATH 195
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTH 206
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
23-214 |
8.31e-15 |
|
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: 70.54 E-value: 8.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLR-LVATALsPTAGRVEVLGRDAVAD------RD--AVRRDValLSHAS-FL 92
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKcIYGNYL-PDSGSILVRHDGGWVDlaqaspREilALRRRT--IGYVSqFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 Y-------EDLTAHQnlvvlARLLGIPSP--QDAASALLTRVGLTRRS-DSPVRSFSAGMRKRLAIARLLLKAPTLALLD 162
Cdd:COG4778 103 RviprvsaLDVVAEP-----LLERGVDREeaRARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1838243270 163 EPFGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:COG4778 178 EPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-217 |
1.05e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV--ADRDAVRRDVALLSHA 89
Cdd:PRK11288 8 DGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAAGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYEDLTAHQNLVvLARL---LGIPSPQDA---ASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDE 163
Cdd:PRK11288 88 LHLVPEMTVAENLY-LGQLphkGGIVNRRLLnyeAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1838243270 164 PFGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
41-216 |
1.30e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.89 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 41 GHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLS--------------------------HASF-LY 93
Cdd:PRK13651 40 GQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKlviqktrfkkikkikeirrrvgvvfqFAEYqLF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 94 EDlTAHQNLVVLARLLGIPsPQDA---ASALLTRVGLTRR--SDSPVrSFSAGMRKRLAIARLLLKAPTLALLDEPFGEL 168
Cdd:PRK13651 120 EQ-TIEKDIIFGPVSMGVS-KEEAkkrAAKYIELVGLDESylQRSPF-ELSGGQKRRVALAGILAMEPDFLVFDEPTAGL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1838243270 169 DPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:PRK13651 197 DPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-195 |
1.45e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.40 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-------AVADRDAVRrdval 85
Cdd:PRK11300 10 GLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghQIARMGVVR----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 86 lshaSF----LYEDLTAHQNLVV----------LARLLGIPS-------PQDAASALLTRVGLTRRSDSPVRSFSAGMRK 144
Cdd:PRK11300 85 ----TFqhvrLFREMTVIENLLVaqhqqlktglFSGLLKTPAfrraeseALDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1838243270 145 RLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKAS-GVTVILATH 195
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEH 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
23-217 |
1.60e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 70.60 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTA---GRVEVLG----RDAVADrdaVRRDVALLshasFLYED 95
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGitltAKTVWD---IREKVGIV----FQNPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 96 -----LTAHQNLVVLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGEL 168
Cdd:PRK13640 95 nqfvgATVGDDVAFGLENRAVPRPEmiKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1838243270 169 DPQGIQDMERIIAEL-KASGVTVILATHLIEQGlTLCEERLHLQDGRAVA 217
Cdd:PRK13640 175 DPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLA 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
13-198 |
2.06e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.43 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYG-----RRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRD-----AVRRD 82
Cdd:PRK13634 7 KVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklkPLRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 83 VALL----SHAsfLYEDLTAH------QNLVVlarllgipSPQDA---ASALLTRVGLTR--RSDSPVrSFSAGMRKRLA 147
Cdd:PRK13634 87 VGIVfqfpEHQ--LFEETVEKdicfgpMNFGV--------SEEDAkqkAREMIELVGLPEelLARSPF-ELSGGQMRRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1838243270 148 IARLLLKAPTLALLDEPFGELDPQGIQDMERIIAEL-KASGVTVILATHLIE 198
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSME 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-218 |
2.09e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.80 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV---ADRDAVRRdvALLSH 88
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwsPAELARRR--AVLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQnlVVlaRLLGIPSP------QDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLL------KAP 156
Cdd:PRK13548 84 HSSLSFPFTVEE--VV--AMGRAPHGlsraedDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838243270 157 TLALLDEPFGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-218 |
2.44e-14 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 70.51 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 30 ALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGR---DAVADRD---------AVRRDVALLSHasflyedLT 97
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARGIFlpphrrrigYVFQEARLFPH-------LS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 98 AHQNLVVLARLLGIPSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDM- 176
Cdd:COG4148 94 VRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIl 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1838243270 177 ---ERIIAELkasGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:COG4148 174 pylERLRDEL---DIPILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-195 |
3.11e-14 |
|
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: 70.85 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY-GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA-DRDAVRRDVALLSHAS 90
Cdd:TIGR02868 339 DLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYeDLTAHQNLvvlarLLGIP-SPQDAASALLTRVGLTRRSDSPV-----------RSFSAGMRKRLAIARLLLKAPTL 158
Cdd:TIGR02868 419 HLF-DTTVRENL-----RLARPdATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*....
gi 1838243270 159 ALLDEPFGELDPqgiQDMERIIAELKA--SGVTVILATH 195
Cdd:TIGR02868 493 LLLDEPTEHLDA---ETADELLEDLLAalSGRTVVLITH 528
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-216 |
3.26e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.74 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 18 YGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAG-----RVEVLGRDAVADRDAV--RRDVALLSHAS 90
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLefRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYEdLTAHQNLVVLAR---LLGIPSPQDAASALLTRVGL-----TRRSDSPVRsFSAGMRKRLAIARLLLKAPTLALLD 162
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRahkLVPRKEFRGVAQARLTEVGLwdavkDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1838243270 163 EPFGELDPQGIQDMERIIAELkASGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
41-195 |
4.10e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 69.72 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 41 GHNGSGKTTLLRLVaTAL-SPTAGRVEVLGRD--AVADRD--AVRRDV-------ALLSHAsflyedlTAHQNlVVLA-R 107
Cdd:COG1135 38 GYSGAGKSTLIRCI-NLLeRPTSGSVLVDGVDltALSERElrAARRKIgmifqhfNLLSSR-------TVAEN-VALPlE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 108 LLGIPSPQDAASA--LLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQD----MERIIA 181
Cdd:COG1135 109 IAGVPKAEIRKRVaeLLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSildlLKDINR 188
|
170
....*....|....
gi 1838243270 182 ELkasGVTVILATH 195
Cdd:COG1135 189 EL---GLTIVLITH 199
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-195 |
4.19e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.19 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRY-GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVAD--RDAVRRDVALLSH 88
Cdd:COG1132 343 ENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD-IRDltLESLRRQIGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDlTAHQNLvvlarLLGIPSPQD------AASALLTRV------GLtrrsDSPV----RSFSAGMRKRLAIARLL 152
Cdd:COG1132 422 DTFLFSG-TIRENI-----RYGRPDATDeeveeaAKAAQAHEFiealpdGY----DTVVgergVNLSGGQRQRIAIARAL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1838243270 153 LKAPTLALLDEPFGELDPQG---IQD-MERIIAelkasGVTVILATH 195
Cdd:COG1132 492 LKDPPILILDEATSALDTETealIQEaLERLMK-----GRTTIVIAH 533
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-217 |
9.57e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 68.29 E-value: 9.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY-GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV-ADRDAVRRDVALLshas 90
Cdd:PRK13652 8 DLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENIREVRKFVGLV---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYED-----LTAHQNLVVLARLLGIPSPQDA--ASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDE 163
Cdd:PRK13652 84 FQNPDdqifsPTVEQDIAFGPINLGLDEETVAhrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1838243270 164 PFGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-216 |
1.33e-13 |
|
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: 69.06 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY-----GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVAD--------RDAV 79
Cdd:TIGR03269 284 NVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDmtkpgpdgRGRA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 80 RRDVALLSHASFLYEDLTAHQNLVvlaRLLGIPSPQD----AASALLTRVGLTRRSDSPV-----RSFSAGMRKRLAIAR 150
Cdd:TIGR03269 364 KRYIGILHQEYDLYPHRTVLDNLT---EAIGLELPDElarmKAVITLKMVGFDEEKAEEIldkypDELSEGERHRVALAQ 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838243270 151 LLLKAPTLALLDEPFGELDP-QGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-195 |
1.36e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.05 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-AVADRDAVRRDVALLSHASF 91
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDiSTLKPEIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDlTAHQNLVVLARLLGIPSPQDAASALLTRVGLTRRS-DSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDP 170
Cdd:PRK10247 92 LFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180
....*....|....*....|....*.
gi 1838243270 171 QGIQDMERIIAEL-KASGVTVILATH 195
Cdd:PRK10247 171 SNKHNVNEIIHRYvREQNIAVLWVTH 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
22-218 |
1.37e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.34 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 22 WALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEV----LGRDAVADRDA-------------VRRDVA 84
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELItnpyskkiknfkeLRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 85 LLSHasF----LYEDlTAHQNLVVLARLLGIPSPQDA--ASALLTRVGL--TRRSDSPVrSFSAGMRKRLAIARLLLKAP 156
Cdd:PRK13631 120 MVFQ--FpeyqLFKD-TIEKDIMFGPVALGVKKSEAKklAKFYLNKMGLddSYLERSPF-GLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838243270 157 TLALLDEPFGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
53-217 |
1.52e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.22 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 53 LVATALSPTAGRVEVLGRDAVADRDAVRRDVALLSHASF-LYEDLTAHQNLVVLARLLGIpSPQDA---ASALLTRVGLT 128
Cdd:NF000106 57 LPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPVR*gRRESFSGRENLYMIGR*LDL-SRKDArarADELLERFSLT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 129 RRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERL 208
Cdd:NF000106 136 EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELT 215
|
....*....
gi 1838243270 209 HLQDGRAVA 217
Cdd:NF000106 216 VIDRGRVIA 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
41-205 |
2.34e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 41 GHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLshasF-----LYEDLTAHQNLVVLARLLGIPsPQ 115
Cdd:COG4586 55 GPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVV----FgqrsqLWWDLPAIDSFRLLKAIYRIP-DA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 116 DAASAL--LTRV-GLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDP---QGIQDMeriIAELKAS-GV 188
Cdd:COG4586 130 EYKKRLdeLVELlDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVvskEAIREF---LKEYNRErGT 206
|
170 180
....*....|....*....|
gi 1838243270 189 TVILATHL---IEQgltLCE 205
Cdd:COG4586 207 TILLTSHDmddIEA---LCD 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-169 |
2.38e-13 |
|
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: 66.49 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYG--RRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDA--VRRDVALLSH 88
Cdd:cd03251 5 NVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD-VRDYTLasLRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDlTAHQNLVVLARLLGIPSPQDAASA-------------LLTRVGltrrsDSPVRsFSAGMRKRLAIARLLLKA 155
Cdd:cd03251 84 DVFLFND-TVAENIAYGRPGATREEVEEAARAanahefimelpegYDTVIG-----ERGVK-LSGGQRQRIAIARALLKD 156
|
170
....*....|....
gi 1838243270 156 PTLALLDEPFGELD 169
Cdd:cd03251 157 PPILILDEATSALD 170
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-195 |
3.25e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.93 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA-DRDAVRRDVALLSHASFLYEDlTAHQN 101
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQAISVVSQRVHLFSA-TLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 102 LvvlarLLGIPSPQDAA-SALLTRVGLTRRSDSPV----------RSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDP 170
Cdd:PRK11160 434 L-----LLAAPNASDEAlIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
170 180
....*....|....*....|....*
gi 1838243270 171 QGIQDMERIIAELkASGVTVILATH 195
Cdd:PRK11160 509 ETERQILELLAEH-AQNKTVLMITH 532
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-214 |
8.72e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.99 E-value: 8.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 26 RLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAvRRDVALLSHASFLYEDLTAHQNLVvl 105
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-RRPVSMLFQENNLFSHLTVAQNIG-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 106 arlLGI-------PSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMER 178
Cdd:PRK10771 94 ---LGLnpglklnAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1838243270 179 IIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:PRK10771 171 LVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
39-198 |
1.03e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 39 LTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRD---AVRRDVALL---SHASFLYEDLTAhqNLVVLARLLGIP 112
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllALRQQVATVfqdPEQQIFYTDIDS--DIAFSLRNLGVP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 113 SPQDA--ASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKASGVTV 190
Cdd:PRK13638 110 EAEITrrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHV 189
|
....*...
gi 1838243270 191 ILATHLIE 198
Cdd:PRK13638 190 IISSHDID 197
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-195 |
1.20e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRdVALLSHASFL 92
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKR-TGFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 YEDLTAHQNLVVLArLLGIP---SPQD---AASALLTRVGLTR-----RSDSPVRSFSAGMRKRLAIARLLLKAPTLALL 161
Cdd:PLN03211 152 YPHLTVRETLVFCS-LLRLPkslTKQEkilVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190
....*....|....*....|....*....|....
gi 1838243270 162 DEPFGELDPQGIQDMERIIAELKASGVTVILATH 195
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
29-195 |
2.15e-12 |
|
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: 63.34 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 29 YALPaGRSLLLTGHNGSGKTTLLRLVATALSPTA--GRVEVLGRDAvaDRDAVRRDVALLSHASFLYEDLTAHQNLVVLA 106
Cdd:cd03213 31 KAKP-GELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPL--DKRSFRKIIGYVPQDDILHPTLTVRETLMFAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 107 RLlgipspqdaasalltrvgltrrsdspvRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKAS 186
Cdd:cd03213 108 KL---------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT 160
|
....*....
gi 1838243270 187 GVTVILATH 195
Cdd:cd03213 161 GRTIICSIH 169
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-198 |
2.39e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.30 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDA----VRRDVALLshasF------L 92
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVD-ITDKKVklsdIRKKVGLV----FqypeyqL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 YEDlTAHQNLVVLARLLGIPSPQ--DAASALLTRVGLTR---RSDSPVrSFSAGMRKRLAIARLLLKAPTLALLDEPFGE 167
Cdd:PRK13637 97 FEE-TIEKDIAFGPINLGLSEEEieNRVKRAMNIVGLDYedyKDKSPF-ELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190
....*....|....*....|....*....|..
gi 1838243270 168 LDPQGIQDMERIIAEL-KASGVTVILATHLIE 198
Cdd:PRK13637 175 LDPKGRDEILNKIKELhKEYNMTIILVSHSME 206
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-205 |
2.59e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAvadRDAVRRD-VALLSHA-----SF--LYE 94
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNlVAYVPQSeevdwSFpvLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 95 DLtahqnlVVLAR-----LLGIPSPQDAA--SALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGE 167
Cdd:PRK15056 99 DV------VMMGRyghmgWLRRAKKRDRQivTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1838243270 168 LDpqgIQDMERIIA---ELKASGVTVILATHLIEQGLTLCE 205
Cdd:PRK15056 173 VD---VKTEARIISllrELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
23-169 |
3.38e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.22 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV-ADRDAV---RRDVALL---SHASF---- 91
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkADPEAQkllRQKIQIVfqnPYGSLnprk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 -----LYEDLTAHQNLVVLARllgipspQDAASALLTRVGL-TRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:PRK11308 110 kvgqiLEEPLLINTSLSAAER-------REKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
....
gi 1838243270 166 GELD 169
Cdd:PRK11308 183 SALD 186
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-199 |
5.93e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.01 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLV--ATALSPTA---GRVEVLGRDAVA-DRDAVRRDVALL 86
Cdd:PRK14247 8 DLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEArvsGEVYLDGQDIFKmDVIELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 87 SHASFLYEDLTAHQNLVV---LARLLGIPSP-QDAASALLTRVGL----TRRSDSPVRSFSAGMRKRLAIARLLLKAPTL 158
Cdd:PRK14247 88 FQIPNPIPNLSIFENVALglkLNRLVKSKKElQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1838243270 159 ALLDEPFGELDPQGIQDMERIIAELKASgVTVILATHLIEQ 199
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQ 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
39-217 |
6.53e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 6.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 39 LTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVAD--RDAVRRDVALLS---HASFLYEDLTAHQN--LVVLARL--L 109
Cdd:COG1129 283 IAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRspRDAIRAGIAYVPedrKGEGLVLDLSIRENitLASLDRLsrG 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 110 GIPSPQ---DAASALLTRVGL-TRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFgeldpQGI-----QDMERII 180
Cdd:COG1129 363 GLLDRRrerALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT-----RGIdvgakAEIYRLI 437
|
170 180 190
....*....|....*....|....*....|....*..
gi 1838243270 181 AELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:COG1129 438 RELAAEGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-216 |
7.14e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 63.28 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRY--GRRW--ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD--AVADRD--AVRRDV 83
Cdd:PRK11153 5 KNISKVFpqGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltALSEKElrKARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 84 A-------LLSHAsflyedlTAHQNlVVLA-RLLGIPSPQDAA--SALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLL 153
Cdd:PRK11153 85 GmifqhfnLLSSR-------TVFDN-VALPlELAGTPKAEIKArvTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838243270 154 KAPTLALLDEPFGELDPQGIQDMERIIAEL-KASGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-217 |
7.80e-12 |
|
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: 63.69 E-value: 7.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRlVATALSPTA---GRVEVLGRDAVAD--RDAVRRDVALLSH 88
Cdd:TIGR02633 7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHGtwdGEIYWSGSPLKASniRDTERAGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQNlVVLARLLGIPSPQDA-------ASALLTRVGLTRRSDS-PVRSFSAGMRKRLAIARLLLKAPTLAL 160
Cdd:TIGR02633 86 ELTLVPELSVAEN-IFLGNEITLPGGRMAynamylrAKNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1838243270 161 LDEPFGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVA 221
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-169 |
8.73e-12 |
|
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: 63.58 E-value: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRYG--RRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVeVLGRDAVADR--DAVRRDVALLSHA 89
Cdd:TIGR02203 336 VTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI-LLDGHDLADYtlASLRRQVALVSQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYEDLTAhqNLVVLARLLGIPSPQ---DAASALLTRV--GLTRRSDSPVRS----FSAGMRKRLAIARLLLKAPTLAL 160
Cdd:TIGR02203 415 VVLFNDTIA--NNIAYGRTEQADRAEierALAAAYAQDFvdKLPLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILI 492
|
....*....
gi 1838243270 161 LDEPFGELD 169
Cdd:TIGR02203 493 LDEATSALD 501
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
23-169 |
1.13e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.83 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV----ADRDAVRRDVALL---SHASF---- 91
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITglsgRELRPLRRRMQMVfqdPYASLnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 -----LYEDLTAHqnlvvlaRLLGIPSPQDAASALLTRVGLtrRSDSPVR---SFSAGMRKRLAIARLLLKAPTLALLDE 163
Cdd:COG4608 113 tvgdiIAEPLRIH-------GLASKAERRERVAELLELVGL--RPEHADRyphEFSGGQRQRIGIARALALNPKLIVCDE 183
|
....*.
gi 1838243270 164 PFGELD 169
Cdd:COG4608 184 PVSALD 189
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-195 |
2.58e-11 |
|
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: 60.96 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRYG--RRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-AVADRDAVRRDVALLSHAS 90
Cdd:cd03252 6 VRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWLRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLY-----EDLTAHQNLVVLARLLGIPSPQDAASALLT-RVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEP 164
Cdd:cd03252 86 VLFnrsirDNIALADPGMSMERVIEAAKLAGAHDFISElPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190
....*....|....*....|....*....|....*
gi 1838243270 165 FGELDPQG----IQDMERIIAelkasGVTVILATH 195
Cdd:cd03252 166 TSALDYESehaiMRNMHDICA-----GRTVIIIAH 195
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-216 |
2.60e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 61.33 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVAD-RDA----VRRDVALLSH--ASFLYED 95
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtKDKyirpVRKRIGMVFQfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 96 lTAHQNLVVLARLLGIPSPQ--DAASALLTRVGLTRR--SDSPVRSFSAGMRKrLAIARLLLKAPTLALLDEPFGELDPQ 171
Cdd:PRK13646 102 -TVEREIIFGPKNFKMNLDEvkNYAHRLLMDLGFSRDvmSQSPFQMSGGQMRK-IAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1838243270 172 GIQDMERIIAELKA-SGVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:PRK13646 180 SKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
39-195 |
2.62e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 39 LTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDvallshasfLYEDLTAHQNLV--------------V 104
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAE---------LDPEKTVMDNLAegkqevmvngrprhV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 105 LARLlgipspQDAasaLLTrvglTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELK 184
Cdd:PRK11147 421 LGYL------QDF---LFH----PKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQ 487
|
170
....*....|.
gi 1838243270 185 AsgvTVILATH 195
Cdd:PRK11147 488 G---TVLLVSH 495
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
13-217 |
3.60e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.77 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGR--RWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADrdavrrdvallshas 90
Cdd:PRK13632 12 NVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKE--------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 flyedltahqNLVVLARLLGI----PSPQ--------DAASAL-----------------LTRVGLTRRSDSPVRSFSAG 141
Cdd:PRK13632 77 ----------NLKEIRKKIGIifqnPDNQfigatvedDIAFGLenkkvppkkmkdiiddlAKKVGMEDYLDKEPQNLSGG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838243270 142 MRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKASGV-TVILATHLIEQGLtLCEERLHLQDGRAVA 217
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIA 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
34-195 |
4.19e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.60 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 34 GRSLLLTGHNGSGKTTLLRLVATALSP---TAGRVEVLGRdaVADRDAVRRDVALLSHASFLYEDLTAHQNLVVLARL-L 109
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGM--PIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLrM 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 110 GIPSPQD----AASALLTRVGLTRRSDS------PVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERI 179
Cdd:TIGR00955 129 PRRVTKKekreRVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208
|
170
....*....|....*.
gi 1838243270 180 IAELKASGVTVILATH 195
Cdd:TIGR00955 209 LKGLAQKGKTIICTIH 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-195 |
8.20e-11 |
|
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: 59.55 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYG-RRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-AVADRDAVRRDVALLSHAS 90
Cdd:cd03253 5 NVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDiREVTLDSLRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYED----------LTAHQNLVVLA--------RLLGIPSPQDaasallTRVGltrrsDSPVRsFSAGMRKRLAIARLL 152
Cdd:cd03253 85 VLFNDtigynirygrPDATDEEVIEAakaaqihdKIMRFPDGYD------TIVG-----ERGLK-LSGGEKQRVAIARAI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1838243270 153 LKAPTLALLDEPFGELDPQGIQDMERIIAELkASGVTVILATH 195
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAH 194
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-196 |
9.21e-11 |
|
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: 59.16 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGR-RWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA-DRDAVRRDVALLSHAS 90
Cdd:cd03254 7 NVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYEDlTAHQNLvvlarLLGIPSPQDA-ASALLTRVGLT---RRS----DSPVR----SFSAGMRKRLAIARLLLKAPTL 158
Cdd:cd03254 87 FLFSG-TIMENI-----RLGRPNATDEeVIEAAKEAGAHdfiMKLpngyDTVLGenggNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1838243270 159 ALLDEPFGELDPQGIQDMERIIAELKASGVTVILATHL 196
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRL 198
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
41-196 |
1.03e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 58.73 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 41 GHNGSGKTTLLRLVATALSPTAGRVEVLGRDAvadRDAVRRDVALLSHASFLYEDLTAHQNLVVLARLLGIPSPQDAAsa 120
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI---NNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAA-- 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838243270 121 lLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKASGVTVILATHL 196
Cdd:PRK13541 108 -IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHL 182
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-199 |
1.14e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 59.28 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLR-------LVATALspTAGRVEVLGRDaVADRD----AVRR 81
Cdd:COG1117 16 NLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGED-IYDPDvdvvELRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 82 DVALLshasF---------LYEdltahqNLVVLARLLGIPSPQDAASAL---LTRVGL----TRRSDSPVRSFSAGMRKR 145
Cdd:COG1117 93 RVGMV----FqkpnpfpksIYD------NVAYGLRLHGIKSKSELDEIVeesLRKAALwdevKDRLKKSALGLSGGQQQR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1838243270 146 LAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKASgVTVILATHLIEQ 199
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQ 215
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
31-199 |
1.84e-10 |
|
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: 57.37 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 31 LPAGRSLLLTGHNGSGKTTLLRlvATALsptagrveVLGRDAVADRdavRRDVALLshasflyedltahqnlvvlarllG 110
Cdd:cd03227 18 FGEGSLTIITGPNGSGKSTILD--AIGL--------ALGGAQSATR---RRSGVKA-----------------------G 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 111 IPSPQDAASALLTRVGLtrrsdspvrsfSAGMRKRLAIARLL----LKAPTLALLDEPFGELDPQGIQDMERIIAELKAS 186
Cdd:cd03227 62 CIVAAVSAELIFTRLQL-----------SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK 130
|
170
....*....|...
gi 1838243270 187 GVTVILATHLIEQ 199
Cdd:cd03227 131 GAQVIVITHLPEL 143
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-200 |
2.57e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.57 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 24 LARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRD-AVRRDVALL-SHASFLYEDLTAHQN 101
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVfQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 102 LVVLARLLGIPSPQ---DAASALLTRVGLTRRSDSPVRsFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMER 178
Cdd:PRK13642 103 VAFGMENQGIPREEmikRVDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180
....*....|....*....|...
gi 1838243270 179 IIAELKAS-GVTVILATHLIEQG 200
Cdd:PRK13642 182 VIHEIKEKyQLTVLSITHDLDEA 204
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-169 |
3.07e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.20 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRY-GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVAD--RDAVRRDVALLSH 88
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTD-IRTvtRASLRRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYeDLTAHQNLVVlarllGIPSPQDA--------ASAL----------LTRVGltRRSdspvRSFSAGMRKRLAIAR 150
Cdd:PRK13657 417 DAGLF-NRSIEDNIRV-----GRPDATDEemraaaerAQAHdfierkpdgyDTVVG--ERG----RQLSGGERQRLAIAR 484
|
170
....*....|....*....
gi 1838243270 151 LLLKAPTLALLDEPFGELD 169
Cdd:PRK13657 485 ALLKDPPILILDEATSALD 503
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-199 |
3.47e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.25 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLV--ATALSPTA---GRVEVLGRDAVA---DRDAVRRDVA 84
Cdd:PRK14243 15 NLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFrveGKVTFHGKNLYApdvDPVEVRRRIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 85 LLSHASFLYEDlTAHQNLVVLARLLGIPSPQDA-------ASALLTRVGLTRRSDSpvRSFSAGMRKRLAIARLLLKAPT 157
Cdd:PRK14243 95 MVFQKPNPFPK-SIYDNIAYGARINGYKGDMDElverslrQAALWDEVKDKLKQSG--LSLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1838243270 158 LALLDEPFGELDPQGIQDMERIIAELKASgVTVILATHLIEQ 199
Cdd:PRK14243 172 VILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQ 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-195 |
3.86e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 58.67 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 24 LARLTYALPAGRSLLLTGHNGSGKTTLLRLVAtALSPTA-GRVEVLGRDavadrdavrrDVALLSHASFLyedltahqNL 102
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIA-GLWPYGsGRIARPAGA----------RVLFLPQRPYL--------PL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 103 VVLARLLGIPSPQDAAS-----ALLTRVGLTR---RSDSPV---RSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQ 171
Cdd:COG4178 440 GTLREALLYPATAEAFSdaelrEALEAVGLGHlaeRLDEEAdwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180
....*....|....*....|....*
gi 1838243270 172 GIQDM-ERIIAELKasGVTVILATH 195
Cdd:COG4178 520 NEAALyQLLREELP--GTTVISVGH 542
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-213 |
5.26e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.36 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 22 WALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGrdavadrdavrrDVALLSHASFLYEDLTAHQN 101
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------------SAALIAISSGLNGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 102 LVVLARLLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERI 179
Cdd:PRK13545 106 IELKGLMMGLTKEKikEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180 190
....*....|....*....|....*....|....
gi 1838243270 180 IAELKASGVTVILATHLIEQGLTLCEERLHLQDG 213
Cdd:PRK13545 186 MNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYG 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
41-195 |
5.80e-10 |
|
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: 58.02 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 41 GHNGSGKTTLLRLVA---------TALSP--TAGRVE----------VLG--RDAVAD-RDAVRR--DV-ALLSHASFLY 93
Cdd:TIGR03719 38 GLNGAGKSTLLRIMAgvdkdfngeARPQPgiKVGYLPqepqldptktVREnvEEGVAEiKDALDRfnEIsAKYAEPDADF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 94 EDLTAHQnlvvlARLLGIPSPQD----------AASALLTRVGltrrsDSPVRSFSAGMRKRLAIARLLLKAPTLALLDE 163
Cdd:TIGR03719 118 DKLAAEQ-----AELQEIIDAADawdldsqleiAMDALRCPPW-----DADVTKLSGGERRRVALCRLLLSKPDMLLLDE 187
|
170 180 190
....*....|....*....|....*....|..
gi 1838243270 164 PFGELDPQGIQDMERIIAELKAsgvTVILATH 195
Cdd:TIGR03719 188 PTNHLDAESVAWLERHLQEYPG---TVVAVTH 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-199 |
6.04e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 57.69 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDA--VADRDAVRRDVALL-SHASFLYEDLTAH 99
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGIVfQNPETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 100 QNLVVLARLLGIPSPQ-----DAAsalLTRVGLTR-RSDSPvRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQ-G 172
Cdd:PRK13644 97 EDLAFGPENLCLPPIEirkrvDRA---LAEIGLEKyRHRSP-KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDsG 172
|
170 180
....*....|....*....|....*..
gi 1838243270 173 IQDMERiIAELKASGVTVILATHLIEQ 199
Cdd:PRK13644 173 IAVLER-IKKLHEKGKTIVYITHNLEE 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-197 |
8.20e-10 |
|
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: 57.64 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEV-----LG-----RDAVADRDAVrr 81
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvkLAyvdqsRDALDPNKTV-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 82 dvallshasflYEDLTAHQNLVVLARlLGIPSpqdaaSALLTRVGLtRRSDS--PVRSFSAGMRKRLAIARLLLKAPTLA 159
Cdd:TIGR03719 404 -----------WEEISGGLDIIKLGK-REIPS-----RAYVGRFNF-KGSDQqkKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1838243270 160 LLDEPFGELDPQGIQDMERIIAELKASGVtVI---------LATHLI 197
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLNFAGCAV-VIshdrwfldrIATHIL 511
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-195 |
8.45e-10 |
|
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: 55.62 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 24 LARLTYALPAGRSLLLTGHNGSGKTTLLRLVAtALSP-TAGRVEVLGRdavadrdavrRDVALLSHASFLyedltahqNL 102
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALA-GLWPwGSGRIGMPEG----------EDLLFLPQRPYL--------PL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 103 VVLARLLGIPspqdaasalLTRVgltrrsdspvrsFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPqgiqDMERIIAE 182
Cdd:cd03223 78 GTLREQLIYP---------WDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESEDRLYQ 132
|
170
....*....|....
gi 1838243270 183 -LKASGVTVILATH 195
Cdd:cd03223 133 lLKELGITVISVGH 146
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-197 |
8.85e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.87 E-value: 8.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEV-----LGRDAVADRDAVRRDVALLSH 88
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLakgikLGYFAQHQLEFLRADESPLQH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQnlvvLARLLGipspqdaasalltrvGLTRRSDS---PVRSFSAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:PRK10636 398 LARLAPQELEQK----LRDYLG---------------GFGFQGDKvteETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
170 180 190
....*....|....*....|....*....|..
gi 1838243270 166 GELDPQGIQDMERIIAELKASGVTVILATHLI 197
Cdd:PRK10636 459 NHLDLDMRQALTEALIDFEGALVVVSHDRHLL 490
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-199 |
1.37e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.32 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLV--ATALSP---TAGRVEVLGRDAVADR-DAV--RRDVA 84
Cdd:PRK14239 10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYSPRtDTVdlRKEIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 85 LLSHASFLYEdLTAHQNLVVLARLLGIPSPQ--DAA-------SALLTRVGlTRRSDSPVrSFSAGMRKRLAIARLLLKA 155
Cdd:PRK14239 90 MVFQQPNPFP-MSIYENVVYGLRLKGIKDKQvlDEAvekslkgASIWDEVK-DRLHDSAL-GLSGGQQQRVCIARVLATS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1838243270 156 PTLALLDEPFGELDPQGIQDMERIIAELKASgVTVILATHLIEQ 199
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQ 209
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-214 |
1.47e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.28 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 21 RWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVAD-----RD----------------AV 79
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnvwdiRHkigmvfqnpdnqfvgaTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 80 RRDVAL-LSHASFLYEDLtahQNLVVLArllgipspqdaasalLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTL 158
Cdd:PRK13650 100 EDDVAFgLENKGIPHEEM---KERVNEA---------------LELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1838243270 159 ALLDEPFGELDPQGIQDMERIIAELKAS-GVTVILATHLIEQgLTLCEERLHLQDGR 214
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQ 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
33-218 |
1.51e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 33 AGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVAD--RDAVRRDVALLSHASFLYEDLTAHQNlVVLAR--- 107
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpKSSQEAGIGIIHQELNLIPQLTIAEN-IFLGRefv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 108 --LLGIPSPQ--DAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAEL 183
Cdd:PRK10762 108 nrFGRIDWKKmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1838243270 184 KASGVTVILATHLIEQGLTLCEERLHLQDG-----RAVAA 218
Cdd:PRK10762 188 KSQGRGIVYISHRLKEIFEICDDVTVFRDGqfiaeREVAD 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
41-214 |
1.74e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.58 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 41 GHNGSGKTTLLRLVATALSPTAGRVeVLGRDAVADRDAVRRDVALLSHASFLYEDLTAHQNLVVLARLLGIPSPQ----- 115
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMNDVPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEinqrv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 116 DAASALLTRVGLTRRSdsPvRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAEL-KASGVTVILAT 194
Cdd:PRK11000 115 NQVAEVLQLAHLLDRK--P-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVT 191
|
170 180
....*....|....*....|
gi 1838243270 195 HLIEQGLTLCEERLHLQDGR 214
Cdd:PRK11000 192 HDQVEAMTLADKIVVLDAGR 211
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
44-214 |
1.77e-09 |
|
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: 55.13 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 44 GSGKTTLLRLVATALSPTAGRVEVLGRDAVAD--RDAVRRDVALLS---HASFLYEDLTAHQNLVvLARLLgipspqdaa 118
Cdd:cd03215 36 GNGQTELAEALFGLRPPASGEITLDGKPVTRRspRDAIRAGIAYVPedrKREGLVLDLSVAENIA-LSSLL--------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 119 salltrvgltrrsdspvrsfSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKASGVTVILATHLIE 198
Cdd:cd03215 106 --------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELD 165
|
170
....*....|....*.
gi 1838243270 199 QGLTLCEERLHLQDGR 214
Cdd:cd03215 166 ELLGLCDRILVMYEGR 181
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
32-195 |
1.94e-09 |
|
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: 55.23 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 32 PAGRSLLLTGHNGSGKTTLLRLVA--TALSPTAGRVEVLGrdavadrdavrrdvallshasflyEDLTahqNLvvlarll 109
Cdd:cd03217 24 KKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKG------------------------EDIT---DL------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 110 gipSPQDAAsalltRVGLTRRSDSPVR---------------SFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQ 174
Cdd:cd03217 70 ---PPEERA-----RLGIFLAFQYPPEipgvknadflryvneGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180
....*....|....*....|.
gi 1838243270 175 DMERIIAELKASGVTVILATH 195
Cdd:cd03217 142 LVAEVINKLREEGKSVLIITH 162
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-195 |
2.68e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV--ADRDAVRRDVALLSHA 89
Cdd:PRK15439 15 RSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArlTPAKAHQLGIYLVPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYEDLTAHQNLvvlarLLGIPSPQDAAS---ALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFG 166
Cdd:PRK15439 95 PLLFPNLSVKENI-----LFGLPKRQASMQkmkQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180
....*....|....*....|....*....
gi 1838243270 167 ELDPQGIQDMERIIAELKASGVTVILATH 195
Cdd:PRK15439 170 SLTPAETERLFSRIRELLAQGVGIVFISH 198
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
14-195 |
4.35e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEvlgrdavadRDAVRRdVALLSHAsfLY 93
Cdd:PRK09544 10 VSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR-IGYVPQK--LY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 94 EDLTAHQNLVVLARLLGIPSPQDAASAlLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGI 173
Cdd:PRK09544 78 LDTTLPLTVNRFLRLRPGTKKEDILPA-LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|...
gi 1838243270 174 QDMERIIAELKAS-GVTVILATH 195
Cdd:PRK09544 157 VALYDLIDQLRRElDCAVLMVSH 179
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-216 |
5.52e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.50 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRR---WALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA-DRDAVRRDVALLSH 88
Cdd:TIGR00958 483 DVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQNLVVLARllgIPSPQDAASALLTRV-----GLTRRSDSPV----RSFSAGMRKRLAIARLLLKAPTLA 159
Cdd:TIGR00958 563 EPVLFSGSVRENIAYGLTD---TPDEEIMAAAKAANAhdfimEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838243270 160 LLDEPFGELDPQgiqdMERIIAELKAS-GVTVILATH---LIEQgltlCEERLHLQDGRAV 216
Cdd:TIGR00958 640 ILDEATSALDAE----CEQLLQESRSRaSRTVLLIAHrlsTVER----ADQILVLKKGSVV 692
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
41-216 |
7.39e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.63 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 41 GHNGSGKTTLLRLVATALSPTAGRVEV------LGRDAVADRDAVRRDVALLSH--ASFLYEDlTAHQNLVVLARLLGiP 112
Cdd:PRK13645 44 GTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKIKEVKRLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLG-E 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 113 SPQDA---ASALLTRVGLTRR--SDSPVRsFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAEL-KAS 186
Cdd:PRK13645 122 NKQEAykkVPELLKLVQLPEDyvKRSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEY 200
|
170 180 190
....*....|....*....|....*....|
gi 1838243270 187 GVTVILATHLIEQGLTLCEERLHLQDGRAV 216
Cdd:PRK13645 201 KKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-195 |
1.06e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 17 RYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRV------------------EVLGRDAVADRDA 78
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlawvnqetpalPQPALEYVIDGDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 79 VRRDV-ALLSHASflyEDLTAHQNLVVLARLLGIP--SPQDAASALLTRVGLTRRS-DSPVRSFSAGMRKRLAIARLLLK 154
Cdd:PRK10636 90 EYRQLeAQLHDAN---ERNDGHAIATIHGKLDAIDawTIRSRAASLLHGLGFSNEQlERPVSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1838243270 155 APTLALLDEPFGELDPQGIQDMERIiaeLKASGVTVILATH 195
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLDAVIWLEKW---LKSYQGTLILISH 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-216 |
2.21e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.56 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 19 GRRWALARLTYALPAGRSLLLTGHNGSGKTT----LLRLVAT-----------------ALSPTAGRVEVLGRD---AVA 74
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSqgeiwfdgqplhnlnrrQLLPVRHRIQVVFQDpnsSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 75 DRDAVRRDVAllshasflyEDLTAHQnlvvlaRLLGIPSPQDAASALLTRVGL--TRRSDSPVrSFSAGMRKRLAIARLL 152
Cdd:PRK15134 377 PRLNVLQIIE---------EGLRVHQ------PTLSAAQREQQVIAVMEEVGLdpETRHRYPA-EFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838243270 153 LKAPTLALLDEPFGELDpQGIQdmERIIAELKASGVTVILATHLIEQGL----TLCEERLHLQDGRAV 216
Cdd:PRK15134 441 ILKPSLIILDEPTSSLD-KTVQ--AQILALLKSLQQKHQLAYLFISHDLhvvrALCHQVIVLRQGEVV 505
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-169 |
2.94e-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: 52.41 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 37 LLLTGHNGSGKTTLLRLVATALSPTAGrvevlgrDAVADRDAVrrdvallshaSFLYEDLTAHQNLVVLARLLGIPSPQD 116
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEG-------DIEIELDTV----------SYKPQYIKADYEGTVRDLLSSITKDFY 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1838243270 117 AASALLTRV----GLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:cd03237 91 THPYFKTEIakplQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
30-169 |
2.99e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 53.15 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 30 ALPAGRSLLLTGHNGSGKTTL----LRLVatalsPTAGRVEVLGRDaVADRD-----AVRRDV---------AL---LSH 88
Cdd:COG4172 308 TLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQD-LDGLSrralrPLRRRMqvvfqdpfgSLsprMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ASFLYEDLTAHQnlvvlaRLLGIPSPQDAASALLTRVGLtrrsDSPVRS-----FSAGMRKRLAIARLLLKAPTLALLDE 163
Cdd:COG4172 382 GQIIAEGLRVHG------PGLSAAERRARVAEALEEVGL----DPAARHrypheFSGGQRQRIAIARALILEPKLLVLDE 451
|
....*.
gi 1838243270 164 PFGELD 169
Cdd:COG4172 452 PTSALD 457
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-217 |
3.10e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 14 VSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRlVATALSPTA---GRVEVLGRDAVAD--RDAVRRDVALLsh 88
Cdd:PRK13549 11 ITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMK-VLSGVYPHGtyeGEIIFEGEELQASniRDTERAGIAII-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 asflYEDLTAHQNLVVLARL-LGI-PSPQ-----DA----ASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPT 157
Cdd:PRK13549 88 ----HQELALVKELSVLENIfLGNeITPGgimdyDAmylrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 158 LALLDEPFGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-218 |
3.64e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 52.15 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 24 LARLTYALPAGRSLLLTGHNGSGKTTLLRLVAtALSPTAGRVEVLGR---DAVADRDAVRRdvALLSH---ASFL---YE 94
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMA-GLLPGQGEILLNGRplsDWSAAELARHR--AYLSQqqsPPFAmpvFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 95 DLTAHQnlvvlARLLGIPSPQDAASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLK-------APTLALLDEPFGE 167
Cdd:COG4138 89 YLALHQ-----PAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1838243270 168 LDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGRAVAA 218
Cdd:COG4138 164 LDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVAS 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-195 |
3.97e-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: 51.77 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRR---WALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDavaDRD----AVRRDVA 84
Cdd:cd03249 4 KNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD---IRDlnlrWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 85 LLSHASFLYeDLTAHQNLvvlarLLGIPSPQD--------AASALLTRVGLTRRSDSPV----RSFSAGMRKRLAIARLL 152
Cdd:cd03249 81 LVSQEPVLF-DGTIAENI-----RYGKPDATDeeveeaakKANIHDFIMSLPDGYDTLVgergSQLSGGQKQRIAIARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1838243270 153 LKAPTLALLDEPFGELDPQGiqdmERIIAEL--KAS-GVTVILATH 195
Cdd:cd03249 155 LRNPKILLLDEATSALDAES----EKLVQEAldRAMkGRTTIVIAH 196
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
132-195 |
4.21e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 4.21e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838243270 132 DSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKAsgvTVILATH 195
Cdd:PRK11819 158 DAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG---TVVAVTH 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-216 |
4.55e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.54 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 27 LTYALPAGRSLLLTGHNGSGKTTLLRLVATALsPTAGRVEVLGRD-AVADRDAVRRDVALLSHASFLYEDlTAHQNLvvl 105
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIElRELDPESWRKHLSWVGQNPQLPHG-TLRDNV--- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 106 arLLGIPSPQDAA-SALLTRVG-------LTRRSDSPVRSFSAGMR----KRLAIARLLLKAPTLALLDEPFGELDPQGI 173
Cdd:PRK11174 444 --LLGNPDASDEQlQQALENAWvseflplLPQGLDTPIGDQAAGLSvgqaQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1838243270 174 QdmeRIIAELK--ASGVTVILATHLIEQgLTLCEERLHLQDGRAV 216
Cdd:PRK11174 522 Q---LVMQALNaaSRRQTTLMVTHQLED-LAQWDQIWVMQDGQIV 562
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-214 |
4.83e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 22 WALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGrdavadrdavrrDVALLSHASFLYEDLTAHQN 101
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------------EVSVIAISAGLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 102 LVVLARLLGIPSPQdaASALLTRV----GLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDME 177
Cdd:PRK13546 106 IEFKMLCMGFKRKE--IKAMTPKIiefsELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1838243270 178 RIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:PRK13546 184 DKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGK 220
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-192 |
5.00e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVaTALSPT--AGRVEVLGR-----DAVADrdaVRRDVA 84
Cdd:PRK10938 264 NNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-TGDHPQgySNDLTLFGRrrgsgETIWD---IKKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 85 LLShaSFLYEDLTAHQNL--VVLARL---LGI----PSPQDA-ASALLTRVGLTRR-SDSPVRSFSAGMRKRLAIARLLL 153
Cdd:PRK10938 340 YVS--SSLHLDYRVSTSVrnVILSGFfdsIGIyqavSDRQQKlAQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALV 417
|
170 180 190
....*....|....*....|....*....|....*....
gi 1838243270 154 KAPTLALLDEPFGELDPQGIQDMERIIAELKASGVTVIL 192
Cdd:PRK10938 418 KHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLL 456
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-195 |
5.88e-08 |
|
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: 51.98 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY----GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSP---TAGRVEVLGRDAV----ADRDAVR- 80
Cdd:COG0444 6 NLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLklseKELRKIRg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 81 RDVALL---SHASF---------LYEDLTAHQNLvvlarllgipSPQDA---ASALLTRVGLT---RRSDS-PVRsFSAG 141
Cdd:COG0444 86 REIQMIfqdPMTSLnpvmtvgdqIAEPLRIHGGL----------SKAEArerAIELLERVGLPdpeRRLDRyPHE-LSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1838243270 142 MRKRLAIARLLLKAPTLALLDEPFGELDP----QGIQDMERIIAELkasGVTVILATH 195
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVtiqaQILNLLKDLQREL---GLAILFITH 209
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-213 |
7.91e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.40 E-value: 7.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 24 LARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDA------VRRDVAL-LSHASFLYEDl 96
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSwimpgtIKENIIFgVSYDEYRYKS- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 97 tahqnlVVLARLL--GIPSPQDAASALLTRVGLTrrsdspvrsFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQ 174
Cdd:cd03291 132 ------VVKACQLeeDITKFPEKDNTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1838243270 175 DM-ERIIAELKASGvTVILATHLIEQgLTLCEERLHLQDG 213
Cdd:cd03291 197 EIfESCVCKLMANK-TRILVTSKMEH-LKKADKILILHEG 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
23-216 |
8.63e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.94 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAvadRD----AVRRDVALLSHASFLYEDLTA 98
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDytlaSLRNQVALVSQNVHLFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 99 hqNLVVLAR-----LLGIPSPQDAASALLTRVGLTRRSDSPV----RSFSAGMRKRLAIARLLLK-APTLaLLDEPFGEL 168
Cdd:PRK11176 435 --NNIAYARteqysREQIEEAARMAYAMDFINKMDNGLDTVIgengVLLSGGQRQRIAIARALLRdSPIL-ILDEATSAL 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1838243270 169 DPQGiqdmERII----AELKASGVTVILATHL--IEQGltlcEERLHLQDGRAV 216
Cdd:PRK11176 512 DTES----ERAIqaalDELQKNRTSLVIAHRLstIEKA----DEILVVEDGEIV 557
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
31-195 |
8.92e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 51.72 E-value: 8.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 31 LPAGRSLLLTGHNGSGKTTLLRLVaTAL-SPTAGRVEVLGRdAVADrdavrrdvallshasflyEDLTAHQNL--VVLA- 106
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLL-TGLyRPESGEILLDGQ-PVTA------------------DNREAYRQLfsAVFSd 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 107 -----RLLGIPSPQDA--ASALLTRVGLT--------RRSDspvRSFSAGMRKRLA-IARLLLKAPTLaLLDEPFGELDP 170
Cdd:COG4615 415 fhlfdRLLGLDGEADParARELLERLELDhkvsvedgRFST---TDLSQGQRKRLAlLVALLEDRPIL-VFDEWAADQDP 490
|
170 180
....*....|....*....|....*..
gi 1838243270 171 QgIQDM--ERIIAELKASGVTVILATH 195
Cdd:COG4615 491 E-FRRVfyTELLPELKARGKTVIAISH 516
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-197 |
1.53e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 27 LTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVevlGRDAvadrdAVRRDVALLSHASFLyeDLTAHQNLVVLA 106
Cdd:PLN03073 528 LNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV---FRSA-----KVRMAVFSQHHVDGL--DLSSNPLLYMMR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 107 RLLGIPspQDAASALLTRVGLT-RRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKA 185
Cdd:PLN03073 598 CFPGVP--EQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG 675
|
170
....*....|..
gi 1838243270 186 SGVTVILATHLI 197
Cdd:PLN03073 676 GVLMVSHDEHLI 687
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-199 |
1.63e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.06 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 24 LARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADR------DAVRRDVAL-LSHASFLYEDL 96
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQtswimpGTIKDNIIFgLSYDEYRYTSV 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 97 TA----HQNLVVLARLLGIPspqdaasalLTRVGLTrrsdspvrsFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQG 172
Cdd:TIGR01271 522 IKacqlEEDIALFPEKDKTV---------LGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180
....*....|....*....|....*...
gi 1838243270 173 IQDM-ERIIAELKASGvTVILATHLIEQ 199
Cdd:TIGR01271 584 EKEIfESCLCKLMSNK-TRILVTSKLEH 610
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
12-198 |
2.59e-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: 49.41 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRY--GRRWALARLTYALPAGRSLLLTGHNGSGKTT----LLRLVatalSPTAGRVEVLGRD-AVADRDAVRRDVA 84
Cdd:cd03244 6 KNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDiSKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 85 LLSHASFLYEDlTAHQNLvvlaRLLGIPSPQDAASALlTRVGLTRRS-------DSPV----RSFSAGMRKRLAIARLLL 153
Cdd:cd03244 82 IIPQDPVLFSG-TIRSNL----DPFGEYSDEELWQAL-ERVGLKEFVeslpgglDTVVeeggENLSVGQRQLLCLARALL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1838243270 154 KAPTLALLDEPFGELDPQGIQDMERIIAElKASGVTVILATHLIE 198
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLD 199
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-195 |
3.79e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.76 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 38 LLTGHNGSGKTTLLRLVATALSPTAGRVevlGRDAVADRD-----AVRRDVAL-LSHASflYEDLTAHQNLVVLarLLGI 111
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYALTGELPPN---SKGGAHDPKliregEVRAQVKLaFENAN--GKKYTITRSLAIL--ENVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 112 PSPQDAASALLTRvgltrrsdsPVRSFSAGMRK------RLAIARLL-LKAPTLAlLDEPFGELDPQGI-QDMERIIAEL 183
Cdd:cd03240 99 FCHQGESNWPLLD---------MRGRCSGGEKVlasliiRLALAETFgSNCGILA-LDEPTTNLDEENIeESLAEIIEER 168
|
170
....*....|...
gi 1838243270 184 KASGV-TVILATH 195
Cdd:cd03240 169 KSQKNfQLIVITH 181
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
41-203 |
5.51e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.93 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 41 GHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAVRRdvallshASFL-----------YEDLTAHQNLvVLARL- 108
Cdd:COG1101 39 GSNGAGKSTLLNAIAGSLPPDSGSILIDGKD-VTKLPEYKR-------AKYIgrvfqdpmmgtAPSMTIEENL-ALAYRr 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 109 -------LGIPSPQ-DAASALLTRV--GLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQG---IQD 175
Cdd:COG1101 110 gkrrglrRGLTKKRrELFRELLATLglGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTaalVLE 189
|
170 180
....*....|....*....|....*....
gi 1838243270 176 M-ERIIAELKasgVTVILATHLIEQGLTL 203
Cdd:COG1101 190 LtEKIVEENN---LTTLMVTHNMEQALDY 215
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
28-217 |
5.94e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 28 TYALPAGRSLLLTGHNGSGKTTLLRLVAT-ALS--PTAGRV-----EVLGRDA-----VADRDaVRRDVALLSHASFL-- 92
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRYMAMhAIDgiPKNCQIlhveqEVVGDDTtalqcVLNTD-IERTQLLEEEAQLVaq 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 -----YEDLTAHQNL---------VVLARLLGI---------PSPQDAASALLTrvGLTRRSDSPVR---SFSAGMRKRL 146
Cdd:PLN03073 276 qreleFETETGKGKGankdgvdkdAVSQRLEEIykrlelidaYTAEARAASILA--GLSFTPEMQVKatkTFSGGWRMRI 353
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838243270 147 AIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKAsgvTVILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:PLN03073 354 ALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK---TFIVVSHAREFLNTVVTDILHLHGQKLVT 421
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-198 |
6.88e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVE-----VLGRDAvadRDavrrdvalls 87
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsenaNIGYYA---QD---------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 88 HASFLYEDLT-----------AHQNLVV---LARLLGipSPQDAasalltrvgltrrsDSPVRSFSAGMRKRLAIARLLL 153
Cdd:PRK15064 391 HAYDFENDLTlfdwmsqwrqeGDDEQAVrgtLGRLLF--SQDDI--------------KKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 154 KAPTLALLDEPFGELdpqgiqDMERI----IAELKASGvTVI-----------LATHLIE 198
Cdd:PRK15064 455 QKPNVLVMDEPTNHM------DMESIeslnMALEKYEG-TLIfvshdrefvssLATRIIE 507
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
39-199 |
7.02e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.49 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 39 LTGHNGSGKTTLLRLV-----ATALSPTAGRVEVLGRDAVADR---DAVRRDVALLSHASFLYEdLTAHQNLVVLARLLG 110
Cdd:PRK14258 38 IIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIYERRvnlNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 111 ---------IPSPQDAASALLTRVglTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIA 181
Cdd:PRK14258 117 wrpkleiddIVESALKDADLWDEI--KHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQ 194
|
170
....*....|....*....
gi 1838243270 182 ELK-ASGVTVILATHLIEQ 199
Cdd:PRK14258 195 SLRlRSELTMVIVSHNLHQ 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
32-214 |
1.06e-06 |
|
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: 47.46 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 32 PAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRdavadrdavrrdVALLSHASFLYEDlTAHQNLvvlarLLGi 111
Cdd:cd03250 29 PKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQEPWIQNG-TIRENI-----LFG- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 112 pSPQDA--------ASAL-----------LTRVGltrrsdspVR--SFSAGMRKRLAIARLLLKAPTLALLDEPFGELDP 170
Cdd:cd03250 90 -KPFDEeryekvikACALepdleilpdgdLTEIG--------EKgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1838243270 171 Q-GIQDMERIIAELKASGVTVILATHLIeQGLTLCEERLHLQDGR 214
Cdd:cd03250 161 HvGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-196 |
1.47e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.18 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGR-RWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDavadrdavrrdVALLSHASF 91
Cdd:PRK10790 345 NVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRP-----------LSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVVLAR------LLGIPSPQDAASALLTRV-----------GLTRRSDSPVRSFSAGMRKRLAIARLLLK 154
Cdd:PRK10790 414 RQGVAMVQQDPVVLADtflanvTLGRDISEEQVWQALETVqlaelarslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1838243270 155 APTLALLDEPFGELDPQGIQDMERIIAELKASGVTVILATHL 196
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRL 535
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-169 |
1.75e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 47.37 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRY---------GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD----AVADRDA 78
Cdd:PRK10419 7 SGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlaklNRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 79 VRRDVALLSHASF------------LYEDLTAHQNLVVLARllgipspQDAASALLTRVGLTRR-SDSPVRSFSAGMRKR 145
Cdd:PRK10419 87 FRRDIQMVFQDSIsavnprktvreiIREPLRHLLSLDKAER-------LARASEMLRAVDLDDSvLDKRPPQLSGGQLQR 159
|
170 180
....*....|....*....|....
gi 1838243270 146 LAIARLLLKAPTLALLDEPFGELD 169
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLD 183
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-195 |
2.03e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.23 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 24 LARLTYALPAGRSLLLTGHNGSGKTTLLRLVAtALSPTAGRVEVLGR---DAVADRDAVRRdvALLSHAS--------FL 92
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMA-GLLPGSGSIQFAGQpleAWSAAELARHR--AYLSQQQtppfampvFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 YEDLTAHQNLVVLArllgipsPQDAASALLTRVGLTRRSDSPVRSFSAG--MRKRLAiARLLLKAPT------LALLDEP 164
Cdd:PRK03695 89 YLTLHQPDKTRTEA-------VASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLA-AVVLQVWPDinpagqLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|.
gi 1838243270 165 FGELDPQGIQDMERIIAELKASGVTVILATH 195
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSH 191
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
13-195 |
2.11e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYG-RRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-AVADRDAVRrdvallSHAS 90
Cdd:PRK10522 327 NVTFAYQdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPvTAEQPEDYR------KLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYEDLtaHqnlvVLARLLGiPSPQDAASAL----LTRVGLTRR---SDSPVR--SFSAGMRKRLAIARLLLKAPTLALL 161
Cdd:PRK10522 401 AVFTDF--H----LFDQLLG-PEGKPANPALvekwLERLKMAHKlelEDGRISnlKLSKGQKKRLALLLALAEERDILLL 473
|
170 180 190
....*....|....*....|....*....|....*
gi 1838243270 162 DEPFGELDPQGIQDMER-IIAELKASGVTVILATH 195
Cdd:PRK10522 474 DEWAADQDPHFRREFYQvLLPLLQEMGKTIFAISH 508
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
41-169 |
2.31e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 41 GHNGSGKTTLLRLVATALSPTAGRVEVlgrdavadrdavrrDVALlshaSFLYEDLTAHQNLVVLARLLGIPSPQDAA-- 118
Cdd:PRK13409 372 GPNGIGKTTFAKLLAGVLKPDEGEVDP--------------ELKI----SYKPQYIKPDYDGTVEDLLRSITDDLGSSyy 433
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1838243270 119 -SALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:PRK13409 434 kSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
31-195 |
2.40e-06 |
|
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: 46.16 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 31 LPAGRSLLLTGHNGSGKTTLLRlvatalsptagrvevlgrdAVADRDAVRRDVALLSHASflyedltaHQNLVVLARLlg 110
Cdd:cd03238 18 IPLNVLVVVTGVSGSGKSTLVN-------------------EGLYASGKARLISFLPKFS--------RNKLIFIDQL-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 111 ipspqdaasALLTRVGLTR-RSDSPVRSFSAGMRKRLAIARLLLKAP--TLALLDEPFGELDPQGIQDMERIIAELKASG 187
Cdd:cd03238 69 ---------QFLIDVGLGYlTLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDLG 139
|
....*...
gi 1838243270 188 VTVILATH 195
Cdd:cd03238 140 NTVILIEH 147
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
136-197 |
3.14e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 3.14e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838243270 136 RSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELK-ASGVTVILATHLI 197
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRI 1419
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-213 |
3.55e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 46.17 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 24 LARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRV----EVLGRDAVADRDAVRR-DVALLSHASFLYeDLTA 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRySVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 99 HQNLVvlarlLGIPSPQDAASALLTRVGLtrRSDSPVRSF-------------SAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:cd03290 96 EENIT-----FGSPFNKQRYKAVTDACSL--QPDIDLLPFgdqteigerginlSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1838243270 166 GELDPQgIQD---MERIIAELKASGVTVILATHLIeQGLTLCEERLHLQDG 213
Cdd:cd03290 169 SALDIH-LSDhlmQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-192 |
3.61e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 30 ALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV----------ADRDAVRRDVALLSH---------AS 90
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITrlsfeqlqklVSDEWQRNNTDMLSPgeddtgrttAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 91 FLYEDLTAHQNLVVLARLLGIpspqdaaSALLTRvgltrrsdsPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDP 170
Cdd:PRK10938 105 IIQDEVKDPARCEQLAQQFGI-------TALLDR---------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180
....*....|....*....|..
gi 1838243270 171 QGIQDMERIIAELKASGVTVIL 192
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLVL 190
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
13-169 |
9.31e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.60 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY-GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVADRDAVRRDVALLSHASF 91
Cdd:PRK11650 8 AVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV-VNELEPADRDIAMVFQNYA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 92 LYEDLTAHQNLVVLARLLGIPSPQ------DAASALLTRVGLTRRsdsPvRSFSAGMRKRLAIARLLLKAPTLALLDEPF 165
Cdd:PRK11650 87 LYPHMSVRENMAYGLKIRGMPKAEieervaEAARILELEPLLDRK---P-RELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
....
gi 1838243270 166 GELD 169
Cdd:PRK11650 163 SNLD 166
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
38-198 |
1.10e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 44.57 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 38 LLTGHNGSGKTTLLRLVATAL---SPTAGRVEVLGRDAVADRDAVRrdVAL---LSHASFLYE-----DLTAHQNLVVLa 106
Cdd:cd03279 32 LICGPTGAGKSTILDAITYALygkTPRYGRQENLRSVFAPGEDTAE--VSFtfqLGGKKYRVErsrglDYDQFTRIVLL- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 107 rllgipsPQDAASALLTRvgltrrsdsPVRSFSAGMR------KRLAIARLL---LKAPTLAL-LDEPFGELDPQGIQDM 176
Cdd:cd03279 109 -------PQGEFDRFLAR---------PVSTLSGGETflaslsLALALSEVLqnrGGARLEALfIDEGFGTLDPEALEAV 172
|
170 180
....*....|....*....|..
gi 1838243270 177 ERIIAELKASGVTVILATHLIE 198
Cdd:cd03279 173 ATALELIRTENRMVGVISHVEE 194
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-169 |
1.20e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 45.25 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 41 GHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAV------RR------DVALLSHAS----FLY---EDLTAHQN 101
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppekRRigyvfqDARLFPHYKvrgnLRYgmaKSMVAQFD 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838243270 102 LVVlaRLLGIpspqdaaSALLTRVGLTrrsdspvrsFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:PRK11144 111 KIV--ALLGI-------EPLLDRYPGS---------LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
23-195 |
1.46e-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: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-AVADRDAVRRDVALLSHASFLYeDLTAHQN 101
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDiSTIPLEDLRSSLTIIPQDPTLF-SGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 102 LVVLARLlgipSPQDAASAL-LTRVGLtrrsdspvrSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERII 180
Cdd:cd03369 102 LDPFDEY----SDEEIYGALrVSEGGL---------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI 168
|
170
....*....|....*
gi 1838243270 181 AELkASGVTVILATH 195
Cdd:cd03369 169 REE-FTNSTILTIAH 182
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
31-198 |
1.70e-05 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 44.16 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 31 LPAGRSLLLTGHNGSGKTTLLRLVATAlsptagrvevlgrdavadrdavrrdvALLSHAsflyedltahqnlvvlarllG 110
Cdd:cd03243 26 LGSGRLLLITGPNMGGKSTYLRSIGLA--------------------------VLLAQI--------------------G 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 111 IPSPQDAAS-----ALLTRVGltrRSDSPVRSFSAGMRKRLAIARLLLKAP--TLALLDEPF---GELDPQGIqdMERII 180
Cdd:cd03243 60 CFVPAESASiplvdRIFTRIG---AEDSISDGRSTFMAELLELKEILSLATprSLVLIDELGrgtSTAEGLAI--AYAVL 134
|
170
....*....|....*...
gi 1838243270 181 AELKASGVTVILATHLIE 198
Cdd:cd03243 135 EHLLEKGCRTLFATHFHE 152
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
39-186 |
2.45e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 39 LTGHNGSGKTTLLRLVATALSPTAGRVeVLGRDAVADR--------------DAVRRDVALLS-------HASFLYEDLT 97
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDLIVARlqqdpprnvegtvyDFVAEGIEEQAeylkryhDISHLVETDP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 98 AHQNLVVLARLLGIPSPQDA------ASALLTRVGLTrrSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQ 171
Cdd:PRK11147 113 SEKNLNELAKLQEQLDHHNLwqlenrINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE 190
|
170
....*....|....*
gi 1838243270 172 GIQDMERIIAELKAS 186
Cdd:PRK11147 191 TIEWLEGFLKTFQGS 205
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-198 |
2.46e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 34 GRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALLshasflyedltahqnlvvlarllgips 113
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 114 pqdaasalltrvgltrrsDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDP------QGIQDMERIIAELKASG 187
Cdd:smart00382 55 ------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqeallLLLEELRLLLLLKSEKN 116
|
170
....*....|.
gi 1838243270 188 VTVILATHLIE 198
Cdd:smart00382 117 LTVILTTNDEK 127
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-169 |
2.61e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEV-----LG-----RDAVADRDAVrr 81
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvkLAyvdqsRDALDPNKTV-- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 82 dvallshasflYEDLTAHQNLVVLARlLGIPSpqdaaSALLTRVGLtRRSDS--PVRSFSAGMRKRLAIARLLLKAPTLA 159
Cdd:PRK11819 406 -----------WEEISGGLDIIKVGN-REIPS-----RAYVGRFNF-KGGDQqkKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
170
....*....|
gi 1838243270 160 LLDEPFGELD 169
Cdd:PRK11819 468 LLDEPTNDLD 477
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
38-195 |
2.94e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 43.80 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 38 LLTGHNGSGKTTLLRLVATALSptaGRVEVLGrdavADRDAVRRDVALL--------SHASFLYEDLTAHQNLVV----- 104
Cdd:COG4938 24 LLIGPNGSGKSTLIQALLLLLQ---SNFIYLP----AERSGPARLYPSLvrelsdlgSRGEYTADFLAELENLEIlddks 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 105 ------LARLLGIPSPQDA---ASALLTRVGLTRRSDSPVRSF---SAGMRKRLAI---ARLLLKAPTLALLDEPfgE-- 167
Cdd:COG4938 97 kelleqVEEWLEKIFPGKVevdASSDLVRLVFRPSGNGKRIPLsnvGSGVSELLPIllaLLSAAKPGSLLIIEEP--Eah 174
|
170 180
....*....|....*....|....*...
gi 1838243270 168 LDPQGIQDMERIIAELKASGVTVILATH 195
Cdd:COG4938 175 LHPKAQSALAELLAELANSGVQVIIETH 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-169 |
4.32e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.69 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTT----LLRLVATalspTAGRVEVLGR--DAVADR--DAVRRDVALLSHASFLYE 94
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVES----QGGEIIFNGQriDTLSPGklQALRRDIQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 95 D--LTAHQNLVVLARLLGIPSPQDAA---SALLTRVGLtrRSDSPVR---SFSAGMRKRLAIARLLLKAPTLALLDEPFG 166
Cdd:PRK10261 415 DprQTVGDSIMEPLRVHGLLPGKAAAarvAWLLERVGL--LPEHAWRyphEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
...
gi 1838243270 167 ELD 169
Cdd:PRK10261 493 ALD 495
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-196 |
4.66e-05 |
|
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: 42.84 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRYGRRWA---LARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVA-DRDAVRRDVALLSh 88
Cdd:cd03248 16 NVTFAYPTRPDtlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSKVSLVG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 asflyedltahQNLVVLARLL------GIPS--------PQDAASALLTRVGLTRRSDSPV----RSFSAGMRKRLAIAR 150
Cdd:cd03248 95 -----------QEPVLFARSLqdniayGLQScsfecvkeAAQKAHAHSFISELASGYDTEVgekgSQLSGGQKQRVAIAR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1838243270 151 LLLKAPTLALLDEPFGELDPQGIQDMERIIAELKASGVTVILATHL 196
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRL 209
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
37-65 |
4.78e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 43.06 E-value: 4.78e-05
10 20
....*....|....*....|....*....
gi 1838243270 37 LLLTGHNGSGKTTLLRLVATALSPTAGRV 65
Cdd:COG3950 28 TVLVGENGSGKTTLLEAIALALSGLLSRL 56
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-195 |
4.80e-05 |
|
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: 43.52 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKT----TLLRLVATALSPTAGRVEVLGRDAV----ADRDAVR-RDVA--------- 84
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLglseRELRRIRgNRIAmifqepmts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 85 ---LLSHASFLYEDLTAHQNLvvlarllgipSPQDA---ASALLTRVGLtRRSDSPVRSF----SAGMRKRLAIARLLLK 154
Cdd:COG4172 105 lnpLHTIGKQIAEVLRLHRGL----------SGAAArarALELLERVGI-PDPERRLDAYphqlSGGQRQRVMIAMALAN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1838243270 155 APTLALLDEPFGELDPQgIQ-DMERIIAELKAS-GVTVILATH 195
Cdd:COG4172 174 EPDLLIADEPTTALDVT-VQaQILDLLKDLQRElGMALLLITH 215
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-192 |
5.56e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.45 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 28 TYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVAD--RDAVRRDVALLShasflyED---------- 95
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspQDGLANGIVYIS------EDrkrdglvlgm 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 96 -------LTAhqnLVVLARLLGIPSPQDAASALLTRVGL----TRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEP 164
Cdd:PRK10762 346 svkenmsLTA---LRYFSRAGGSLKHADEQQAVSDFIRLfnikTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180
....*....|....*....|....*...
gi 1838243270 165 FGELDPQGIQDMERIIAELKASGVTVIL 192
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAEGLSIIL 450
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
41-169 |
8.68e-05 |
|
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: 42.85 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 41 GHNGSGKTTLLRLVATALSPTAGRVEV----------LGRDA---VAD--RDAVRRDVAllshASFLYEDLtahqnlvvl 105
Cdd:COG1245 373 GPNGIGKTTFAKILAGVLKPDEGEVDEdlkisykpqyISPDYdgtVEEflRSANTDDFG----SSYYKTEI--------- 439
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838243270 106 arllgipspqdaasalLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:COG1245 440 ----------------IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-208 |
9.21e-05 |
|
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: 42.98 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY--GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSpTAGRVEVlgrDAVAdRDAV-----RRDVAL 85
Cdd:TIGR01271 1222 GLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQI---DGVS-WNSVtlqtwRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 86 LSHASFLYEDlTAHQNLVVLARLlgipSPQDAASaLLTRVGLTrrsdSPVRSF---------------SAGMRKRLAIAR 150
Cdd:TIGR01271 1297 IPQKVFIFSG-TFRKNLDPYEQW----SDEEIWK-VAEEVGLK----SVIEQFpdkldfvlvdggyvlSNGHKQLMCLAR 1366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1838243270 151 LLLKAPTLALLDEPFGELDPQGIQDMERIIAElKASGVTVILATHLIEQGLTlCEERL 208
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVEALLE-CQQFL 1422
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
38-184 |
9.45e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 38 LLTGHNGSGKTTLLRLVATALSPTAGRVEVLgRDAVADRDAVRRDVAL-LSHASFLYE------------DLTAHQNLVV 104
Cdd:COG0419 27 LIVGPNGAGKSTILEAIRYALYGKARSRSKL-RSDLINVGSEEASVELeFEHGGKRYRierrqgefaeflEAKPSERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 105 LARLLGIPSPQDAASAL-------------------LTRVGLTRRSD-SPVRSFSAGMRKRLAIARLLlkaptLALLDep 164
Cdd:COG0419 106 LKRLLGLEIYEELKERLkeleealesaleelaelqkLKQEILAQLSGlDPIETLSGGERLRLALADLL-----SLILD-- 178
|
170 180
....*....|....*....|
gi 1838243270 165 FGELDPQGIQDMERIIAELK 184
Cdd:COG0419 179 FGSLDEERLERLLDALEELA 198
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
118-195 |
1.05e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 1.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838243270 118 ASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKASGVTVILATH 195
Cdd:NF040905 120 ARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISH 197
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-169 |
1.15e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 33 AGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVE-VLGRDAVADRDAVRR---DVALLSHASFLYEDLTAHQNLVVLARL 108
Cdd:TIGR00956 86 PGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEgVITYDGITPEEIKKHyrgDVVYNAETDVHFPHLTVGETLDFAARC 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838243270 109 LGipsPQD-------------AASALLTRVGL-----TRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELD 169
Cdd:TIGR00956 166 KT---PQNrpdgvsreeyakhIADVYMATYGLshtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
39-217 |
1.17e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 39 LTGHNGSGKTTLLRLVATALSPTAGRVEVLGR--DAVADRDAVRRDVALLSHASFLYEDLTAHQNLVvLAR--LLGIPSP 114
Cdd:PRK10982 29 LMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSKEALENGISMVHQELNLVLQRSVMDNMW-LGRypTKGMFVD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 115 QDA----ASALLTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKASGVTV 190
Cdd:PRK10982 108 QDKmyrdTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGI 187
|
170 180
....*....|....*....|....*..
gi 1838243270 191 ILATHLIEQGLTLCEERLHLQDGRAVA 217
Cdd:PRK10982 188 VYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-195 |
1.32e-04 |
|
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: 41.46 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 34 GRSLLLTGHNGSGKTTLLRLVAtaLSPTAGRVEvlGRDAVADRdavrrdvallshasflyedltahQNLVVLARLLGIPS 113
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLA--GRKTAGVIT--GEILINGR-----------------------PLDKNFQRSTGYVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 114 PQDAASALLT-RVGLtrRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKASGVTVIL 192
Cdd:cd03232 86 QQDVHSPNLTvREAL--RFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILC 163
|
...
gi 1838243270 193 ATH 195
Cdd:cd03232 164 TIH 166
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
41-195 |
1.42e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.55 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 41 GHNGSGKTTLLRLVA--TALSPTAGRVEVLGRDaVADRDAVRR-------------DVALLSHASFL---YEDLTAHQNL 102
Cdd:CHL00131 40 GPNGSGKSTLSKVIAghPAYKILEGDILFKGES-ILDLEPEERahlgiflafqypiEIPGVSNADFLrlaYNSKRKFQGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 103 VVLARL--LGIPSPQdaasalLTRVG-----LTRRSDSpvrSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDpqgIqD 175
Cdd:CHL00131 119 PELDPLefLEIINEK------LKLVGmdpsfLSRNVNE---GFSGGEKKRNEILQMALLDSELAILDETDSGLD---I-D 185
|
170 180
....*....|....*....|....
gi 1838243270 176 MERIIAE----LKASGVTVILATH 195
Cdd:CHL00131 186 ALKIIAEginkLMTSENSIILITH 209
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-214 |
2.01e-04 |
|
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: 41.73 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 12 HDVSKRYGRRwaLARLTYALPAGRSLLLTGHNGSGKTTLLR-LVATALSPTAGRVEVLGR--DAVADRDAVRRDVALLSH 88
Cdd:TIGR02633 266 WDVINPHRKR--VDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKpvDIRNPAQAIRAGIAMVPE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 89 ---ASFLYEDLTAHQN--LVVLARLLGIPSPQDAASALLTRVGLTRRS------DSPVRSFSAGMRKRLAIARLLLKAPT 157
Cdd:TIGR02633 344 drkRHGIVPILGVGKNitLSVLKSFCFKMRIDAAAELQIIGSAIQRLKvktaspFLPIGRLSGGNQQKAVLAKMLLTNPR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1838243270 158 LALLDEPFGELDPQGIQDMERIIAELKASGVTVILATHLIEQGLTLCEERLHLQDGR 214
Cdd:TIGR02633 424 VLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
34-81 |
2.05e-04 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 40.39 E-value: 2.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838243270 34 GRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAV------------ADRDA-VRR 81
Cdd:PRK00889 4 GVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVrtnlskglgfskEDRDTnIRR 64
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-216 |
3.04e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.50 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY--GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRD-AVADRDAVRRDVALLSHA 89
Cdd:PLN03232 1239 DVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDvAKFGLTDLRRVLSIIPQS 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYE-------DLTAHQNLVVLARLLGIPSPQDAASAllTRVGLTRRSDSPVRSFSAGMRKRLAIARLLLKAPTLALLD 162
Cdd:PLN03232 1319 PVLFSgtvrfniDPFSEHNDADLWEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1838243270 163 EPFGELDPQGIQDMERIIAELKASGVTVILATHLieQGLTLCEERLHLQDGRAV 216
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREEFKSCTMLVIAHRL--NTIIDCDKILVLSSGQVL 1448
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
138-195 |
3.12e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.86 E-value: 3.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838243270 138 FSAGMRKRLAIARLLLKAPTLALLDEPFGELDP--QGiQDMErIIAELKAS-GVTVILATH 195
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvQA-QIMT-LLNELKREfNTAIIMITH 220
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
139-214 |
3.30e-04 |
|
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: 40.61 E-value: 3.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838243270 139 SAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAElKASGVTVILATHLIEQGLTlCEERLHLQDGR 214
Cdd:cd03289 140 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENK 213
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-182 |
3.49e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 40.96 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 13 DVSKRY-GRRWALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDaVAD--RDAVRRDVALLSHA 89
Cdd:COG5265 362 NVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD-IRDvtQASLRAAIGIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 90 SFLYED----------LTAHQNLVV----LARLLG-IPS-PQdaasALLTRVG-----LtrrsdspvrsfSAGMRKRLAI 148
Cdd:COG5265 441 TVLFNDtiayniaygrPDASEEEVEaaarAAQIHDfIESlPD----GYDTRVGerglkL-----------SGGEKQRVAI 505
|
170 180 190
....*....|....*....|....*....|....*..
gi 1838243270 149 ARLLLKAPTLALLDEPFGELDP---QGIQDMERIIAE 182
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSrteRAIQAALREVAR 542
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-192 |
4.66e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.42 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 27 LTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADRDAVRRDVALL-----SHASFLYEDLTAHQN 101
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedRQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 102 LVVLAR-LLGIPSPQDAASALLTRVgltRRS--------DSPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQG 172
Cdd:PRK15439 362 VCALTHnRRGFWIKPARENAVLERY---RRAlnikfnhaEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180
....*....|....*....|
gi 1838243270 173 IQDMERIIAELKASGVTVIL 192
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLF 458
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
23-125 |
4.71e-04 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 40.16 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSL-LLTGHNGSGKTTLLRLVATALSPtagrvevlgrdavadrdavRRDVALLSHASflyedLTAHQN 101
Cdd:COG3267 31 ALARLEYALAQGGGFvVLTGEVGTGKTTLLRRLLERLPD-------------------DVKVAYIPNPQ-----LSPAEL 86
|
90 100
....*....|....*....|....
gi 1838243270 102 LVVLARLLGIPSPQDAASALLTRV 125
Cdd:COG3267 87 LRAIADELGLEPKGASKADLLRQL 110
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-216 |
8.17e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 39.70 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVEVLGRDAVADR-DAVRRDVALLSHASFLYEDLTAhQN 101
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRSRLAVVSQTPFLFSDTVA-NN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 102 LVvlarlLGIPspqDAASALLTRVG-LTRRSDSPVR--------------SFSAGMRKRLAIARLLLKAPTLALLDEPFG 166
Cdd:PRK10789 409 IA-----LGRP---DATQQEIEHVArLASVHDDILRlpqgydtevgergvMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1838243270 167 ELDPqgiQDMERIIAELK--ASGVTVILATHLIeQGLTLCEERLHLQDGRAV 216
Cdd:PRK10789 481 AVDG---RTEHQILHNLRqwGEGRTVIISAHRL-SALTEASEILVMQHGHIA 528
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
134-195 |
1.61e-03 |
|
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: 38.52 E-value: 1.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838243270 134 PVRSFSAGMRK---RLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKASGVTVILATH 195
Cdd:pfam13304 233 PAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
23-169 |
1.86e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 38.23 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 23 ALARLTYALPAGRSLLLTGHNGSGKTTLLRLVATALSPTAG-------------------RVEVLGRDAVADRDAVRRDV 83
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGelliddhplhfgdysyrsqRIRMIFQDPSTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 84 ALLSHASFLYEDLTAhqnlvvlarllgiPSPQDAASALLTRVGLTRRSDS--PvRSFSAGMRKRLAIARLLLKAPTLALL 161
Cdd:PRK15112 108 QILDFPLRLNTDLEP-------------EQREKQIIETLRQVGLLPDHASyyP-HMLAPGQKQRLGLARALILRPKVIIA 173
|
....*...
gi 1838243270 162 DEPFGELD 169
Cdd:PRK15112 174 DEALASLD 181
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
18-191 |
2.36e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 37.48 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 18 YGRRWALARLTYAL-----PAGRSLLLTGHNGSGKTTLLRLVATALSPTAGRVevlgrdavadrdaVRRDVALLSHASFL 92
Cdd:pfam13191 3 VGREEELEQLLDALdrvrsGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYF-------------LRGKCDENLPYSPL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 93 YEDLTAHQNLVVLARLLGIPSPQDAASALLTRVGLTRR-SDSPVRSFSAGMRKRLAIARlLLKAPTLALLDEpFGELDPQ 171
Cdd:pfam13191 70 LEALTREGLLRQLLDELESSLLEAWRAALLEALAPVPElPGDLAERLLDLLLRLLDLLA-RGERPLVLVLDD-LQWADEA 147
|
170 180
....*....|....*....|
gi 1838243270 172 GIQDMERIIAELKASGVTVI 191
Cdd:pfam13191 148 SLQLLAALLRLLESLPLLVV 167
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
133-196 |
2.85e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.47 E-value: 2.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838243270 133 SPVRSFSAGMRKRLAIARLLLKAPTLALLDEPFGELDPQGIQDMERIIAELKASG--VTVILATHL 196
Cdd:PTZ00265 575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnrITIIIAHRL 640
|
|
| DLIC |
pfam05783 |
Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein ... |
31-64 |
2.91e-03 |
|
Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein light intermediate chain proteins. The light intermediate chains (LICs) of cytoplasmic dynein consist of multiple isoforms, which undergo post-translational modification to produce a large number of species. DLIC1 is known to be involved in assembly, organization, and function of centrosomes and mitotic spindles when bound to pericentrin. DLIC2 is a subunit of cytoplasmic dynein 2 that may play a role in maintaining Golgi organization by binding cytoplasmic dynein 2 to its Golgi-associated cargo.
Pssm-ID: 368612 Cd Length: 468 Bit Score: 38.28 E-value: 2.91e-03
10 20 30
....*....|....*....|....*....|....
gi 1838243270 31 LPAGRSLLLTGHNGSGKTTLLRLVATALSPTAGR 64
Cdd:pfam05783 22 LPSGKNVLVLGEDGSGKTTLIAKLQGVEHPKKGR 55
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
38-195 |
3.75e-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: 37.67 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 38 LLTGHNGSGKTTLLRLVATALSPTAGR-------------------VEV-----LGR-----DAVADRDAVRRDVALLS- 87
Cdd:COG3593 27 VLVGENNSGKSSILEALRLLLGPSSSRkfdeedfylgddpdlpeieIELtfgslLSRllrllLKEEDKEELEEALEELNe 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838243270 88 --HASF--LYEDLTAHQNLVVLARLLGIPSPQDAASALLT--RVGLTRRSDSPVRSFSAGMRKRLAIA--RLLL-----K 154
Cdd:COG3593 107 elKEALkaLNELLSEYLKELLDGLDLELELSLDELEDLLKslSLRIEDGKELPLDRLGSGFQRLILLAllSALAelkraP 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1838243270 155 APTLALLDEPfgE--LDPQGIQDMERIIAELKASGVTVILATH 195
Cdd:COG3593 187 ANPILLIEEP--EahLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-195 |
4.37e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 4.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838243270 134 PVRSFSAGMRKRLAIARLLL---KAPTLALLDEPFGELDPQGIQDMERIIAELKASGVTVILATH 195
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
31-59 |
4.90e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 36.36 E-value: 4.90e-03
10 20
....*....|....*....|....*....
gi 1838243270 31 LPAGRSLLLTGHNGSGKTTLLRLVATALS 59
Cdd:cd00009 16 LPPPKNLLLYGPPGTGKTTLARAIANELF 44
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
32-60 |
8.93e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 36.82 E-value: 8.93e-03
10 20
....*....|....*....|....*....
gi 1838243270 32 PAGRSLLLTGHNGSGKTTLLRLVATALSP 60
Cdd:COG4913 22 FDGRGTLLTGDNGSGKSTLLDAIQTLLVP 50
|
|
| |
