|
Name |
Accession |
Description |
Interval |
E-value |
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-151 |
8.33e-96 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 280.06 E-value: 8.33e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVG 80
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 81 MVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-151 |
2.40e-84 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 251.15 E-value: 2.40e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEefLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVG 80
Cdd:COG3839 1 MAS--LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 81 MVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-151 |
6.79e-80 |
|
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: 235.11 E-value: 6.79e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVFQS 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 86 YALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALA 146
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-151 |
3.23e-77 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 232.73 E-value: 3.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREI-THLKPSQRNVGMVFQ 84
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 85 SYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-151 |
6.26e-77 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 232.23 E-value: 6.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 4 EFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVF 83
Cdd:TIGR03265 3 PYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVF 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 84 QSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:TIGR03265 83 QSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALA 150
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-151 |
1.27e-75 |
|
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: 224.81 E-value: 1.27e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVFQS 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 86 YALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALV 146
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-151 |
1.31e-73 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 220.73 E-value: 1.31e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTF----GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIThlKPSQ 76
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT--GPGP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 77 RnVGMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG1116 81 D-RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-150 |
3.96e-73 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 222.67 E-value: 3.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVG 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDIC 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 81 MVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARAL 151
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-150 |
1.54e-71 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 219.05 E-value: 1.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVFQS 85
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 86 YALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-151 |
2.90e-68 |
|
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: 205.57 E-value: 2.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVFQS 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 86 YALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIV 146
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-151 |
1.13e-66 |
|
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: 201.55 E-value: 1.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTN----TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIThlkPSQRNVGM 81
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT---GPGPDRGY 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 82 VFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALA 147
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-151 |
4.88e-64 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 195.26 E-value: 4.88e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTN----TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQR---- 77
Cdd:COG1136 5 LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 78 --NVGMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG1136 85 rrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-151 |
4.83e-63 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 192.90 E-value: 4.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT----HLKPSQRNVGM 81
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKLRRKVGM 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 82 VFQSYALFPNLNVRDNIGFGL-KVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALA 152
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-151 |
8.39e-63 |
|
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: 191.93 E-value: 8.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTN----TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQR---- 77
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 78 --NVGMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-151 |
4.57e-62 |
|
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: 190.63 E-value: 4.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 9 EAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVFQSYAL 88
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYAL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 89 FPNLNVRDNIGFGLKV----AGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03296 86 FRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-151 |
2.63e-58 |
|
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: 180.95 E-value: 2.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ---- 76
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyel 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 77 -RNVGMVFQSYALFPNLNVRDNIGFGLKV-AGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG1127 81 rRRIGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-150 |
2.24e-57 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 182.35 E-value: 2.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEefLNLEAITKTFGTNT-VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNV 79
Cdd:PRK11650 1 MAG--LKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDI 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 80 GMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAE---MLELIGLpdLGRRYAfELSGGQQQRVALARAL 150
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEaarILELEPL--LDRKPR-ELSGGQRQRVAMGRAI 149
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-151 |
2.72e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 181.43 E-value: 2.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTN----TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ-----RN 78
Cdd:COG1135 4 LENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraarRK 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 79 VGMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALA 156
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-151 |
1.19e-56 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 176.40 E-value: 1.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTN-TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ-----RNVGM 81
Cdd:COG2884 4 FENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRIGV 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 82 VFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG2884 84 VFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-151 |
1.59e-56 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 177.36 E-value: 1.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHlkPSQRNvGMVFQSYALFPNLNVRDNIG 99
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADR-GVVFQKDALLPWLNVLDNVA 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 100 FGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG4525 99 FGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-151 |
1.11e-55 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 178.49 E-value: 1.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVFQS 85
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 86 YALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLA 165
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-151 |
6.82e-54 |
|
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: 177.02 E-value: 6.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTN-----TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS 75
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 76 Q-----RNVGMVFQ--SYALFPNLNVRDNIGFGLKVAGV-PRAKARERVAEMLELIGL-PDLGRRYAFELSGGQQQRVAL 146
Cdd:COG1123 336 SlrelrRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAI 415
|
....*
gi 1956267849 147 ARALA 151
Cdd:COG1123 416 ARALA 420
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-150 |
4.30e-53 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 171.75 E-value: 4.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVFQSYA 87
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYA 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 88 LFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK11000 86 LYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTL 148
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-151 |
1.31e-52 |
|
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: 166.22 E-value: 1.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTN----TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ----- 76
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 77 RNVGMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-151 |
1.53e-52 |
|
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: 166.71 E-value: 1.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTF-GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMV 82
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 83 FQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPD--LGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALA 151
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-151 |
2.44e-52 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 168.44 E-value: 2.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 36 LLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARER 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1956267849 116 VAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALV 116
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-151 |
3.30e-52 |
|
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: 164.62 E-value: 3.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS----QRNVGM 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 82 VFQSYALFPNLNVRDNIGFGL-KVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALA 151
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-151 |
5.92e-52 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 168.34 E-value: 5.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 11 ITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVFQSYALFP 90
Cdd:PRK10851 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALFR 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 91 NLNVRDNIGFGLKVagVPR------AKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK10851 88 HMTVFDNIAFGLTV--LPRrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-151 |
1.93e-51 |
|
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: 163.44 E-value: 1.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ-----RNVGMV 82
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGML 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 83 FQSYALFPNLNVRDNIGFGLKVAGV-PRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALA 152
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-150 |
2.09e-51 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 163.39 E-value: 2.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTntVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVFQS 85
Cdd:COG3840 2 LRLDDLTYRYGD--FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 86 YALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCL 144
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-150 |
1.35e-49 |
|
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: 158.65 E-value: 1.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGtNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVFQS 85
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 86 YALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARAL 144
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-151 |
4.45e-49 |
|
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: 157.11 E-value: 4.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVFQS--YALFpN 91
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQNpdDQLF-A 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 92 LNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG1122 91 PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-151 |
1.14e-48 |
|
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: 155.92 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 23 DLDLSFN-SGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADG------REITHLKPSQRNVGMVFQSYALFPNLNVR 95
Cdd:cd03297 14 TLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 96 DNIGFGLKVAgvPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03297 94 ENLAFGLKRK--RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALA 147
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-151 |
8.48e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.07 E-value: 8.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS-QRNVGMVFQ 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRRIGYVPQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 85 SYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALL 147
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-151 |
9.92e-48 |
|
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: 152.34 E-value: 9.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT----HLKPSQRNVGM 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 82 VFQSYALFPNLNVRDNIGFGlkvagvprakarervaemleliglpdlgrryafeLSGGQQQRVALARALA 151
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALA 116
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-151 |
1.24e-47 |
|
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: 154.19 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGT----NTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITH--LKPSQRNV 79
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrrRKAFRRRV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 80 GMVFQSY--ALFPNLNVRDNIGFGLKVAGVPRAkaRERVAEMLELIGLP-DLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDR--EERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALI 154
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-151 |
2.50e-46 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 149.55 E-value: 2.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKP---TKGRIFADGREITHLKPSQRNVGMV 82
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGIL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 83 FQSYALFPNLNVRDNIGFGLkVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALL 149
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-151 |
6.46e-46 |
|
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: 150.49 E-value: 6.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 9 EAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ------RNVGMV 82
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMV 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 83 FQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALA 176
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-151 |
6.79e-46 |
|
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: 148.38 E-value: 6.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVFQsyalFP--- 90
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVFQ----NPddq 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 91 --NLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03225 88 ffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-151 |
1.04e-45 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 151.42 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTF--------GTNTVIK---DLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREI 69
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 70 THLKPSQ-----RNVGMVFQ-SYA-LFPNLNVRDNIGFGLKVAGV-PRAKARERVAEMLELIGL-PDLGRRYAFELSGGQ 140
Cdd:COG4608 83 TGLSGRElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQ 162
|
170
....*....|.
gi 1956267849 141 QQRVALARALA 151
Cdd:COG4608 163 RQRIGIARALA 173
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-151 |
1.21e-45 |
|
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: 147.94 E-value: 1.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 4 EFLNleaITKTFGTNTV-IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ-----R 77
Cdd:cd03292 2 EFIN---VTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrR 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 78 NVGMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIV 152
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-151 |
2.96e-45 |
|
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: 145.10 E-value: 2.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITH--LKPSQRNVGMVFQSYALFPNLNVRDNI 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 99 GFGLKVAGVPRAKARERVAEMLELIGLPDLG----RRYAFELSGGQQQRVALARALA 151
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALL 137
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-151 |
3.09e-45 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 150.72 E-value: 3.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTN----TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ-----RN 78
Cdd:PRK11153 4 LKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQ 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 79 VGMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-151 |
1.73e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.97 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTF-GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ-----RNV 79
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 80 GMVFQSYALFPNLNVRDNIGFG-LKVAGVPRA-------KARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGrLGRTSTWRSllglfppEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-151 |
2.67e-44 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 146.00 E-value: 2.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIThlKPSQRNvGMVFQS 85
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAER-GVVFQN 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 86 YALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALA 144
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-151 |
3.46e-44 |
|
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: 144.57 E-value: 3.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTF----GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRN--- 78
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 79 --VGMVFQSY--ALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLP---DLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03257 82 keIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARALA 161
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-151 |
3.82e-44 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 145.19 E-value: 3.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVF 83
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 84 QSYALFPNLNVRDNIGFG----LKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG1120 82 QEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-151 |
5.32e-44 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 144.50 E-value: 5.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRN---VGMV 82
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 83 FQSYALFPNLNVRDNI----------GFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-151 |
1.72e-43 |
|
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: 146.40 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 23 DLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGR------EITHLKPSQRNVGMVFQSYALFPNLNVRD 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsaRGIFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 97 NIGFGLKVAgvPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG4148 97 NLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALL 149
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-151 |
2.22e-43 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 142.92 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 4 EFLNleaITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNV---- 79
Cdd:PRK09493 3 EFKN---VSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqea 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 80 GMVFQSYALFPNLNVRDNIGFG-LKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
6-151 |
3.79e-42 |
|
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: 139.49 E-value: 3.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTN----TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQR---- 77
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 78 --NVGMVFQSYALFPNLNVRDNIGFGLKVAGvpRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG4181 89 arHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-151 |
5.62e-42 |
|
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: 139.61 E-value: 5.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS-QRNVGMVFQ 84
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLPD 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 85 SYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALV 148
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-151 |
9.37e-42 |
|
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: 138.47 E-value: 9.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEK-----PTKGRIFADGREITHLKPS----Q 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlelR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 77 RNVGMVFQSYALFPnLNVRDNIGFGLKVAGV-PRAKARERVAEMLELIGLPDLG--RRYAFELSGGQQQRVALARALA 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVkdRLHALGLSGGQQQRLCLARALA 157
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-151 |
5.27e-41 |
|
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: 136.93 E-value: 5.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNT-VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ-----RNV 79
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 80 GMVFQSYALFPNLNVRDNIGFGL--------KVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-151 |
2.36e-40 |
|
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: 134.98 E-value: 2.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQR-NVGMVF- 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRaRLGIGYl 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 84 -QSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03218 81 pQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALA 149
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-151 |
7.03e-40 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 134.54 E-value: 7.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREItHLKPSQR-------- 77
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLKPDRDgelvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 78 --------NVGMVFQSYALFPNLNVRDNIGFG-LKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALAR 148
Cdd:COG4598 88 rqlqrirtRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
...
gi 1956267849 149 ALA 151
Cdd:COG4598 168 ALA 170
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-151 |
2.42e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.86 E-value: 2.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVF 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 84 QSYALFPNlNVRDNIGFGLKVAGvpRAKARERVAEMLELIGLPD--LGRRYAfELSGGQQQRVALARALA 151
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPPdiLDKPVE-RLSGGERQRLALIRALL 146
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-151 |
5.59e-39 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 131.69 E-value: 5.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHL---KPSQRNVGMV 82
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhKRARLGIGYL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 83 FQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG1137 84 PQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-151 |
1.03e-38 |
|
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: 129.91 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS-QRNVGMVFQ 84
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYLGH 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 85 SYALFPNLNVRDNIGFGLKVAGVPRakARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRA--DREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLL 147
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-151 |
1.09e-38 |
|
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: 133.25 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTN----TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKP---TKGRIFADGREITHLKPSQ-- 76
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 77 ----RNVGMVFQ-SY-ALFPNLNVRDNIGFGLKV-AGVPRAKARERVAEMLELIGLPD---LGRRYAFELSGGQQQRVAL 146
Cdd:COG0444 82 kirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMI 161
|
....*
gi 1956267849 147 ARALA 151
Cdd:COG0444 162 ARALA 166
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-151 |
2.13e-38 |
|
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: 129.89 E-value: 2.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPsQRNVgmVFQSYALFPNLNVRDNIGF 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 101 GLK--VAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALS 130
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-150 |
2.38e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 130.13 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREI---THLKPSQ-----RNV 79
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAirllrQKV 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 80 GMVFQSYALFPNLNVRDN-IGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:COG4161 85 GMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-150 |
9.70e-38 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 128.55 E-value: 9.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 25 DLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVFQSYALFPNLNVRDNIGFGLKV 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1956267849 105 AGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK10771 99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCL 144
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-151 |
1.75e-37 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 128.18 E-value: 1.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNT-VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLK-----PSQRNV 79
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkklrKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 80 GMVFQSYALFPNLNVRDNI--------GFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgrlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-150 |
1.87e-37 |
|
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: 127.22 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 23 DLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVFQSYALFPNLNVRDNIGFGL 102
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1956267849 103 KVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVL 143
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-150 |
2.62e-37 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 127.87 E-value: 2.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFAdGReiTHLKPSQRNVGMVFQS 85
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-GT--APLAEAREDTRLMFQD 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 86 YALFPNLNVRDNIGFGLKvaGVPRAKARervaEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLK--GQWRDAAL----QALAAVGLADRANEWPAALSGGQKQRVALARAL 148
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-150 |
7.51e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 126.28 E-value: 7.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRI--------FA---DGREITHLKpsq 76
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdFSktpSDKAIRELR--- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 77 RNVGMVFQSYALFPNLNVRDN-IGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-151 |
1.16e-36 |
|
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: 125.24 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRN---VGMV 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 83 FQSYALFPNLNVRDNigfgLKVAGVPRAKA--RERVAEMLELigLPDLGRRY---AFELSGGQQQRVALARALA 151
Cdd:cd03224 81 PEGRRIFPELTVEEN----LLLGAYARRRAkrKARLERVYEL--FPRLKERRkqlAGTLSGGEQQMLAIARALM 148
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-151 |
1.93e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 130.79 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPT---KGRIFADGREITHLKPSQR--NVGMVFQS--YAL 88
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgrRIGMVFQDpmTQL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 89 FPnLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG1123 97 NP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-151 |
2.65e-36 |
|
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: 124.15 E-value: 2.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 11 ITKTFG--TNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREI-THLKPSQRNVGMVFQSYA 87
Cdd:cd03263 6 LTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYCPQFDA 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 88 LFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03263 86 LFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALI 149
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
11-151 |
1.10e-35 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 123.79 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 11 ITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS--------------- 75
Cdd:TIGR03005 6 VTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRngplvpadekhlrqm 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 76 QRNVGMVFQSYALFPNLNVRDNIGFG-LKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:TIGR03005 86 RNKIGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALA 162
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-151 |
1.73e-35 |
|
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: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHlkpSQRNVG 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 81 MVFQSYAL---FPnLNVRDNIGFGL----KVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG1121 79 YVPQRAEVdwdFP-ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-151 |
6.37e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 121.76 E-value: 6.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVF 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLP 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 84 QSYAL-FPnLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDL-GRRYAfELSGGQQQRVALARALA 151
Cdd:COG4559 82 QHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLaGRSYQ-TLSGGEQQRVQLARVLA 149
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-151 |
1.75e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 120.65 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVF 83
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLP 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 84 QSYAL-FPnLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13548 83 QHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-151 |
5.10e-34 |
|
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: 117.15 E-value: 5.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQrnvgmvfqsya 87
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----------- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 88 lfpnlnvrdnigfglkvagvpRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03214 71 ---------------------LARKIAYVPQALELLGLAHLADRPFNELSGGERQRVLLARALA 113
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-151 |
8.73e-34 |
|
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: 116.34 E-value: 8.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREI-THLKPSQRNVGMVFQ 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 85 SYALFPNLNVRDNIgfglkvagvprakarervaemleliglpdlgrryafELSGGQQQRVALARALA 151
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALL 111
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
8-151 |
9.99e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 118.70 E-value: 9.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKP--SQRN------- 78
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsQQKGlirqlrq 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 79 -VGMVFQSYALFPNLNVRDNIGFG-LKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK11264 86 hVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-150 |
2.00e-33 |
|
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: 117.39 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRN---VGMV 82
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArlgIGYV 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 83 FQSYALFPNLNVRDNigfgLKVAGVPR---AKARERVAEMLELigLPDLGRR---YAFELSGGQQQRVALARAL 150
Cdd:COG0410 84 PEGRRIFPSLTVEEN----LLLGAYARrdrAEVRADLERVYEL--FPRLKERrrqRAGTLSGGEQQMLAIGRAL 151
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-151 |
3.22e-33 |
|
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: 117.53 E-value: 3.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADG---REITHLKPSQRNVGMVFQsyalfpnlN--- 93
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtLDEENLWEIRKKVGMVFQ--------Npdn 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 94 ------VRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:TIGR04520 89 qfvgatVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA 152
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-151 |
3.53e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.45 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 15 FGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLR-------MIAGFEkpTKGRIFADGREIthLKPSQ------RNVGM 81
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDI--YDPDVdvvelrRRVGM 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 82 VFQSYALFPnLNVRDNIGFGLKVAGV-PRAKARERVAEMLELIGLPD-----LgRRYAFELSGGQQQRVALARALA 151
Cdd:COG1117 97 VFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALWDevkdrL-KKSALGLSGGQQQRLCIARALA 170
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-150 |
8.04e-33 |
|
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: 115.01 E-value: 8.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRNVGMVFQS 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 86 YALFPNLNVRDNIGFGLKVAGVPrakaRERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALAL 141
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
11-150 |
1.08e-32 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 118.29 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 11 ITKTFGTNTVikDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRI------FADGREITHLKPSQRNVGMVFQ 84
Cdd:TIGR02142 5 FSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtLFDSRKGIFLPPEKRRIGYVFQ 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 85 SYALFPNLNVRDNIGFGLKVAGVPRAKARErvAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:TIGR02142 83 EARLFPHLSVRGNLRYGMKRARPSERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRAL 146
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-151 |
2.10e-32 |
|
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: 114.17 E-value: 2.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGReitHLKPSQRNVGMVFQSYA 87
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRRS 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 88 L---FPnLNVRDNIGFGL----KVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03235 79 IdrdFP-ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALV 148
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-151 |
3.34e-32 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 114.90 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTN---------TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ 76
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 77 -----RNVGMVFQ-SYALF-PNLNVRDNIGFGLK-VAGVPRAKARERVAEMLELIGL-PDLGRRYAFELSGGQQQRVALA 147
Cdd:TIGR02769 83 rrafrRDVQLVFQdSPSAVnPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIA 162
|
....
gi 1956267849 148 RALA 151
Cdd:TIGR02769 163 RALA 166
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-151 |
4.40e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.58 E-value: 4.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 2 AEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKP--SQRN- 78
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdAQAAg 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 79 VGMVFQSYALFPNLNVRDNIGFG--LKVAG-VPRAKARERVAEMLELIGLP-DLGRRyAFELSGGQQQRVALARALA 151
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGrePRRGGlIDWRAMRRRARELLARLGLDiDPDTP-VGDLSVAQQQLVEIARALS 156
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-150 |
6.73e-32 |
|
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: 113.23 E-value: 6.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 9 EAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT-HLKPSQRNVGMVFQSYA 87
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVrEPREVRRRIGIVFQDLS 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 88 LFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:cd03265 84 VDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSL 146
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-151 |
9.29e-32 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 114.01 E-value: 9.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 19 TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ-----RNVGMVFQSY--ALFPN 91
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSisAVNPR 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 92 LNVRDNIGFGLK-VAGVPRAKARERVAEMLELIGLPD-LGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK10419 106 KTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALA 167
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-151 |
1.39e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.96 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT------HLKPSQRNVGMVFQ--SYALFPNl 92
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQfpEHQLFEE- 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 93 NVRDNIGFGLKVAGVPRAKARERVAEMLELIGLP-DLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLA 161
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-150 |
1.41e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.44 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ---R 77
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 78 NVGMVFQSYALFPNLNVRDNIGFGL---KVAGVPRAKARERVAEMLELIGLP-DLGRRYAfELSGGQQQRVALARAL 150
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDvDPDAKVE-DLSVGEQQRVEILKAL 156
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-151 |
1.63e-31 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 118.01 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVFQSYALFpNLNVRDN 97
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGTIREN 568
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 98 IGFGLkvAGVPRAKARE--RVAEMLELI-GLPD-----LGRRYAfELSGGQQQRVALARALA 151
Cdd:COG2274 569 ITLGD--PDATDEEIIEaaRLAGLHDFIeALPMgydtvVGEGGS-NLSGGQRQRLAIARALL 627
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-150 |
3.16e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.80 E-value: 3.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVFQSYALFpNLN 93
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 94 VRDNIGFGLKvaGVPRAKARE--RVAEMLELI-GLPD-----LGRRyAFELSGGQQQRVALARAL 150
Cdd:COG1132 430 IRENIRYGRP--DATDEEVEEaaKAAQAHEFIeALPDgydtvVGER-GVNLSGGQRQRIAIARAL 491
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-150 |
1.68e-30 |
|
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: 107.85 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS--QRNVGMVFQSYALFpNLN 93
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslRKNIAYVPQDPFLF-SGT 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 94 VRDNIgfglkvagvprakarervaemleliglpdlgrryafeLSGGQQQRVALARAL 150
Cdd:cd03228 92 IRENI-------------------------------------LSGGQRQRIAIARAL 111
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-151 |
4.40e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 112.05 E-value: 4.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 3 EEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ------ 76
Cdd:PRK10070 26 EQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrr 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 77 RNVGMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK10070 106 KKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALA 180
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-150 |
9.67e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 107.65 E-value: 9.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTF-GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ-----RNV 79
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQI 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 80 GMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAV 152
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-151 |
1.51e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 108.13 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT-------HLK 73
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 74 PSQRN--------VGMVFQSYALFPNLNVRDNIGFG-LKVAGVPRAKARERVAEMLELIGLPDLGR-RYAFELSGGQQQR 143
Cdd:PRK10619 81 VADKNqlrllrtrLTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQR 160
|
....*...
gi 1956267849 144 VALARALA 151
Cdd:PRK10619 161 VSIARALA 168
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-151 |
1.52e-29 |
|
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: 112.09 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 13 KTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTT----VLRMIagfekPTKGRIFADGREITHLKPSQ-----RNVGMVF 83
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRRAlrplrRRMQVVF 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 84 QS-YA-LFPNLNVRDNIGFGLKVAGVPRAKA--RERVAEMLELIGL-PDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG4172 369 QDpFGsLSPRMTVGQIIAEGLRVHGPGLSAAerRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALI 441
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-151 |
2.89e-29 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 105.80 E-value: 2.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNT-VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREItHLKPSQRNVGMVFQS- 85
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-KAKERRKSIGYVMQDv 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 86 -YALFPNlNVRDNIGFGLKVAGvpraKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03226 81 dYQLFTD-SVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALL 142
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-150 |
3.58e-29 |
|
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: 106.47 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 18 NTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVFQSYALFPNlNVR 95
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFDG-TIA 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 96 DNIGFGLKVAGVPRAKARERVAEMLELI-GLPD-----LGRRyAFELSGGQQQRVALARAL 150
Cdd:cd03249 95 ENIRYGKPDATDEEVEEAAKKANIHDFImSLPDgydtlVGER-GSQLSGGQKQRIAIARAL 154
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-151 |
4.50e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 106.32 E-value: 4.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVFQS 85
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 86 YALFPNLNVRDNIGFGL----KvaGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG4604 84 NHINSRLTVRELVAFGRfpysK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLA 151
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-150 |
7.53e-29 |
|
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: 110.23 E-value: 7.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS--QRNVGMVFQSYALFPnLN 93
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAWVPQNPYLFA-GT 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 94 VRDNIGFGLKVAGVPRAKARERVAEMLELI-GLPD-----LGRRyAFELSGGQQQRVALARAL 150
Cdd:COG4988 427 IRENLRLGRPDASDEELEAALEAAGLDEFVaALPDgldtpLGEG-GRGLSGGQAQRLALARAL 488
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-151 |
8.10e-29 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 105.43 E-value: 8.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHL---KPSQRNVGMV 82
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpmhERARLGIGYL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 83 FQSYALFPNLNVRDNIGFGLKVAG-VPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALA 151
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-150 |
1.12e-28 |
|
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: 104.76 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNT----VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLK-PSQRNVG 80
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 81 MVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-151 |
1.50e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 106.35 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKpsQRNVGmvfqs 85
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED--RRRIG----- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 86 Y-----ALFPNLNVRDNIGF--GLKvaGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG4152 75 YlpeerGLYPKMKVGEQLVYlaRLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-150 |
3.61e-28 |
|
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: 103.13 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKpsQRNVGMVFQS 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RNRIGYLPEE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 86 YALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAV 143
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-151 |
4.67e-28 |
|
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: 107.85 E-value: 4.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTN----TVIKDLDLSFNSGEFVSLLGPSGCGKT----TVLRMIAGFEKPTKGRIFADGREITHL 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 73 KPSQ------RNVGMVFQ--SYALFPNLNVRDNIGFGLKV-AGVPRAKARERVAEMLELIGLPDLGRR---YAFELSGGQ 140
Cdd:COG4172 82 SERElrrirgNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQ 161
|
170
....*....|.
gi 1956267849 141 QQRVALARALA 151
Cdd:COG4172 162 RQRVMIAMALA 172
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-150 |
7.98e-28 |
|
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: 102.27 E-value: 7.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVsLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS-QRNVGMVFQ 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlRRRIGYLPQ 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 85 SYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQAL 145
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-151 |
2.19e-27 |
|
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: 99.63 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVFQs 85
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ- 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 86 yalfpnlnvrdnigfglkvagvprakarervaemleliglpdlgrryafeLSGGQQQRVALARALA 151
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALL 96
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
25-151 |
3.95e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.12 E-value: 3.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 25 DLSFN--SGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT--HLKPSQRNVGMVFQSY-ALFPNLNVRDNIG 99
Cdd:PRK13650 25 DVSFHvkQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKIGMVFQNPdNQFVGATVEDDVA 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 100 FGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13650 105 FGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
17-151 |
6.77e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.22 E-value: 6.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 17 TNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT--HLKPSQRNVGMVFQSY-ALFPNLN 93
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLKEIRKKIGIIFQNPdNQFIGAT 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 94 VRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13632 101 VEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-151 |
8.05e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 101.66 E-value: 8.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT----HLKPSQRNVGMVFQ--SYALFPNLNV 94
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIRKKVGLVFQypEYQLFEETIE 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 95 RDnIGFGLKVAGVPRAKARERVAEMLELIGLP--DLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13637 103 KD-IAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVA 160
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-150 |
1.45e-26 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 99.61 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADG---REIThLKPSQRNVGMVFQSYALFpNLNVRD 96
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYT-LASLRRQIGLVSQDVFLF-NDTVAE 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 97 NIGFGLKvaGVPRAKARE--RVAEMLELI-GLPD-----LGRRyAFELSGGQQQRVALARAL 150
Cdd:cd03251 95 NIAYGRP--GATREEVEEaaRAANAHEFImELPEgydtvIGER-GVKLSGGQRQRIAIARAL 153
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-150 |
1.75e-26 |
|
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: 103.69 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVFQSYALFpNLN 93
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQRPHLF-DTT 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 94 VRDNigfgLKVAgVPRAkARERVAEMLELIGLPDL---------------GRRyafeLSGGQQQRVALARAL 150
Cdd:COG4987 425 LREN----LRLA-RPDA-TDEELWAALERVGLGDWlaalpdgldtwlgegGRR----LSGGERRRLALARAL 486
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-150 |
1.78e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.02 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 2 AEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNV 79
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQV 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 80 GMVFQSYALFPNlNVRDNIGFGLKVAGvpRAKARERVAEMLELIGLPD--LGRRYAfELSGGQQQRVALARAL 150
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDtiLTKNIA-ELSGGEKQRISLIRNL 152
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-150 |
2.20e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 99.12 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS------QRNVGMVFQSYALFPNLN 93
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelrNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 94 VRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
6-150 |
2.61e-26 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 99.53 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNT---------VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ 76
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 77 R--NVGMVFQ--SYALFPNLNVRDNIGFGLKVAGVPRAKAR-ERVAEMLELIGL-PDLGRRYAFELSGGQQQRVALARAL 150
Cdd:COG4167 85 RckHIRMIFQdpNTSLNPRLNIGQILEEPLRLNTDLTAEEReERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARAL 164
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
11-151 |
4.28e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 99.78 E-value: 4.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 11 ITKTF--GTNTVIKDLD---LSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRI---FAD----------------- 65
Cdd:PRK13651 8 IVKIFnkKLPTELKALDnvsVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDeknkkktkekekvlekl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 66 ------GREITHLKPSQRNVGMVFQ--SYALFPNlNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLP-DLGRRYAFEL 136
Cdd:PRK13651 88 viqktrFKKIKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFEL 166
|
170
....*....|....*
gi 1956267849 137 SGGQQQRVALARALA 151
Cdd:PRK13651 167 SGGQKRRVALAGILA 181
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-150 |
6.70e-26 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 97.66 E-value: 6.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 18 NTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS--QRNVGMVFQSYALFpNLNVR 95
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGYVPQDVTLF-YGTLR 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 96 DNIGFGLKVAgvprakARERVAEMLELIGLPDLGRRYA-----------FELSGGQQQRVALARAL 150
Cdd:cd03245 96 DNITLGAPLA------DDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARAL 155
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-151 |
1.09e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.16 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTNT--VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITH--LKPSQ 76
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 77 RNVGMVFQSY-ALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13635 81 RQVGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-151 |
2.25e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 97.14 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREI-----THLKPSQRNVGMVFQSYALFP 90
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 91 NLNVRDNIGFGLKV-AGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK11831 98 DMNVFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIA 159
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-150 |
6.43e-25 |
|
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: 95.37 E-value: 6.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVFQSYALFPNlNVRDN 97
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 98 IGFglkvaGVPRAKaRERVAEMLELIGLPDLGRR----YAFE-------LSGGQQQRVALARAL 150
Cdd:cd03254 97 IRL-----GRPNAT-DEEVIEAAKEAGAHDFIMKlpngYDTVlgenggnLSQGERQLLAIARAM 154
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-149 |
7.00e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 95.23 E-value: 7.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 2 AEEFLNLEAITKTFGTN----TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQR 77
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAR 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 78 ------NVGMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARA 149
Cdd:PRK10584 83 aklrakHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-150 |
1.44e-24 |
|
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: 92.66 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVFQSYALFPNlN 93
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLPQDDELFSG-S 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 94 VRDNIgfglkvagvprakarervaemleliglpdlgrryafeLSGGQQQRVALARAL 150
Cdd:cd03246 92 IAENI-------------------------------------LSGGQRQRLGLARAL 111
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-146 |
1.62e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.77 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTF--GT---NTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQR--N 78
Cdd:COG1101 2 LELKNLSKTFnpGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 79 VGMVFQSYAL--FPNLNVRDNI--------GFGLKvAGVPRAKaRERVAEMLELIGLpDLGRRYAFE---LSGGQQQRVA 145
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLalayrrgkRRGLR-RGLTKKR-RELFRELLATLGL-GLENRLDTKvglLSGGQRQALS 158
|
.
gi 1956267849 146 L 146
Cdd:COG1101 159 L 159
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-151 |
2.44e-24 |
|
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: 97.36 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS--QRNVGMVFQSYALFPNlN 93
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 94 VRDNIGFGLKVAgvprakARERVAEMLELIGL----PDLGRRYAFE-------LSGGQQQRVALARALA 151
Cdd:TIGR02857 412 IAENIRLARPDA------SDAEIREALERAGLdefvAALPQGLDTPigeggagLSGGQAQRLALARAFL 474
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-150 |
6.82e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.33 E-value: 6.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTF----GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ----- 76
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlr 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 77 -RNVGMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK10535 85 rEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-151 |
7.09e-24 |
|
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: 92.50 E-value: 7.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTF------GTN-TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIF------------ADG 66
Cdd:COG4778 5 LEVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwvdlaqASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 67 REITHLKpsQRNVGMVFQsyalFpnLNV------RDNIGFGLKVAGVPRAKARERVAEMLELIGLPD-LGRRYAFELSGG 139
Cdd:COG4778 85 REILALR--RRTIGYVSQ----F--LRViprvsaLDVVAEPLLERGVDREEARARARELLARLNLPErLWDLPPATFSGG 156
|
170
....*....|..
gi 1956267849 140 QQQRVALARALA 151
Cdd:COG4778 157 EQQRVNIARGFI 168
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-150 |
8.93e-24 |
|
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: 92.45 E-value: 8.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 3 EEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKG---RIFadGRE-----ITHLKp 74
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERrggedVWELR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 75 sqRNVGMVfqSYALF----PNLNVRDNIGFGL-KVAGVPR---AKARERVAEMLELIGLPDL-GRRYAfELSGGQQQRVA 145
Cdd:COG1119 78 --KRIGLV--SPALQlrfpRDETVLDVVLSGFfDSIGLYReptDEQRERARELLELLGLAHLaDRPFG-TLSQGEQRRVL 152
|
....*
gi 1956267849 146 LARAL 150
Cdd:COG1119 153 IARAL 157
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-150 |
1.05e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.72 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREI-THLKPSQRNV 79
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRV 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 80 GMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-148 |
1.37e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.36 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLkPSQR--N 78
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQiaR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 79 VGMV--FQSYALFPNLNVRDNI----------GF--GL-KVAGVPRA--KARERVAEMLELIGLPDLGRRYAFELSGGQQ 141
Cdd:PRK11300 80 MGVVrtFQHVRLFREMTVIENLlvaqhqqlktGLfsGLlKTPAFRRAesEALDRAATWLERVGLLEHANRQAGNLAYGQQ 159
|
....*..
gi 1956267849 142 QRVALAR 148
Cdd:PRK11300 160 RRLEIAR 166
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-150 |
1.73e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 93.49 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLD-LSFN--SGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ-----RNVGMVFQS-YAlfpN 91
Cdd:PRK11308 28 VKALDgVSFTleRGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYG---S 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 92 LNVRDNIGFGLKV-----AGVPRAKARERVAEMLELIGL-PDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK11308 105 LNPRKKVGQILEEpllinTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARAL 169
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-151 |
2.44e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 91.61 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVF 83
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLP 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 84 QSYALFPNLNVRDNIGFG----LKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
11-150 |
7.41e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 91.86 E-value: 7.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 11 ITKTFGTNTVikDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREI------THLKPSQRNVGMVFQ 84
Cdd:PRK11144 6 FKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekgICLPPEKRRIGYVFQ 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 85 SYALFPNLNVRDNIGFGLKvagvprAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK11144 84 DARLFPHYKVRGNLRYGMA------KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRAL 143
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-150 |
1.33e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 90.92 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQR-----NVGMVFQS--YALFPNLN 93
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMT 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 94 VRDNIGFGLKV--AGVPRAKARERVAEMLELIGL-PDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK15079 117 IGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARAL 176
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-151 |
4.00e-22 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 86.33 E-value: 4.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS---QRNVGMV 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdarRAGIAMV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 83 FQsyalfpnlnvrdnigfglkvagvprakarervaemleliglpdlgrryafeLSGGQQQRVALARALA 151
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALA 98
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-150 |
4.99e-22 |
|
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: 87.67 E-value: 4.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 14 TFGTNT---VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS--QRNVGMVFQSYAL 88
Cdd:cd03253 7 TFAYDPgrpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDslRRAIGVVPQDTVL 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 89 FpNLNVRDNIGFGLKVAGVPRAKARERVAEMLELI-GLPD-----LGRRyAFELSGGQQQRVALARAL 150
Cdd:cd03253 87 F-NDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKImRFPDgydtiVGER-GLKLSGGEKQRVAIARAI 152
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-151 |
6.73e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.61 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKP---SQR 77
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 78 NVGMVFQSYALFPNLNVRDNIGFGL----KVAGVP---RAKARERVAEMLELIGLP-DLGRRYAfELSGGQQQRVALARA 149
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGRhltkKVCGVNiidWREMRVRAAMMLLRVGLKvDLDEKVA-NLSISHKQMLEIAKT 159
|
..
gi 1956267849 150 LA 151
Cdd:PRK09700 160 LM 161
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-151 |
6.79e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 88.35 E-value: 6.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTfGTNTVIKDLD-LSFN--SGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT------H 71
Cdd:PRK13641 1 MSIKFENVDYIYSP-GTPMEKKGLDnISFEleEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 72 LKPSQRNVGMVFQ--SYALFPNlNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLP-DLGRRYAFELSGGQQQRVALAR 148
Cdd:PRK13641 80 LKKLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAG 158
|
...
gi 1956267849 149 ALA 151
Cdd:PRK13641 159 VMA 161
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-151 |
7.29e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 87.91 E-value: 7.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGF-----EKPTKGRIFADGREI----TH 71
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 72 LKPSQRNVGMVFQSYALFPnLNVRDNIGFGLKVAGVpraKARERVAEMLE--LIG------LPDLGRRYAFELSGGQQQR 143
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGI---KDKQVLDEAVEksLKGasiwdeVKDRLHDSALGLSGGQQQR 156
|
....*...
gi 1956267849 144 VALARALA 151
Cdd:PRK14239 157 VCIARVLA 164
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-150 |
1.00e-21 |
|
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: 87.16 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS--QRNVGMVFQSYALFpNLNVRDN 97
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 98 IGFGLKVAGVPRAKARERVAEMLELI-GLPD-----LGRRYAfELSGGQQQRVALARAL 150
Cdd:cd03252 96 IALADPGMSMERVIEAAKLAGAHDFIsELPEgydtiVGEQGA-GLSGGQRQRIAIARAL 153
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-148 |
1.10e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 86.26 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS-QRNVGMVFQ 84
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGH 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 85 SYALFPNLNVRDNIGFGLKVAGvpraKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALAR 148
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALAR 140
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-151 |
1.31e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.87 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHL---KPSQRNVGMV 82
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRGIGYL 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 83 FQSYALFPNLNVRDNIGFGLKV-AGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-150 |
1.57e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFadgreithlKPSQRNVGMVFQSYA 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS---------IPKGLRIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 88 LFPNLNVRDNIGFGLKVAGVPRAKARE--------------------------------RVAEMLELIGLP--DLGRRYA 133
Cdd:COG0488 72 LDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPeeDLDRPVS 151
|
170
....*....|....*..
gi 1956267849 134 fELSGGQQQRVALARAL 150
Cdd:COG0488 152 -ELSGGWRRRVALARAL 167
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-150 |
2.05e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.99 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGF---EKPTKGRIFADGREITH-------LKPS 75
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQRegrlardIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 76 QRNVGMVFQSYALFPNLNVRDNIGFGlKVAGVP---------RAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVAL 146
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
....
gi 1956267849 147 ARAL 150
Cdd:PRK09984 164 ARAL 167
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-151 |
2.26e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 5 FLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHL--KPSQRNVGMV 82
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsaRAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 83 FQSYALFPNLNVRDNIGFGlkvagvpRAKARER-----------VAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMG-------RTPHRSRfdtwtetdraaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-151 |
2.27e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 87.06 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS----QRNVGMVFQSY--ALFPNlN 93
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevRKTVGIVFQNPddQLFAP-T 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 94 VRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-151 |
2.85e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.12 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 14 TFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVL----RMIAGFEKP-TKGRIFADGREITHLKPSQ--RNVGMVFQSY 86
Cdd:PRK14247 12 SFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfnRLIELYPEArVSGEVYLDGQDIFKMDVIElrRRVQMVFQIP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 87 ALFPNLNVRDNIGFGLKVAGVPRAKA--RERVAEMLELIGLPDLGRRY----AFELSGGQQQRVALARALA 151
Cdd:PRK14247 92 NPIPNLSIFENVALGLKLNRLVKSKKelQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALA 162
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-151 |
3.97e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 86.29 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 19 TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADG---REITHLKPSQRNVGMVFQSyalfPNlN-- 93
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PD-Nqi 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 94 ----VRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLgRRYAFE-LSGGQQQRVALARALA 151
Cdd:PRK13633 99 vatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEY-RRHAPHlLSGGQKQRVAIAGILA 160
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-151 |
4.80e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 85.66 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 15 FGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGF-----EKPTKGRIFADGREITHLKPS----QRNVGMVFQS 85
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDpievRREVGMVFQY 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 86 YALFPNLNVRDNIGFGLKVAGVPRAKAR--ERVAEMLELIGL----PDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALA 165
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-150 |
4.97e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 4.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 13 KTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTT----VLRMIAgfekpTKGRIFADGREITHLKPSQ-----RNVGMVF 83
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVF 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 84 Q--SYALFPNLNVRDNIGFGLKV--AGVPRAKARERVAEMLELIGL-PDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK15134 369 QdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARAL 440
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-151 |
8.28e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.22 E-value: 8.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLR-------MIAGFEkpTKGRIFADGREI--THLKPSQ 76
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 77 --RNVGMVFQSYALFPNlNVRDNIGFGLKVAGVpRAKARERVAEMLELIGL----PDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK14243 89 vrRRIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAI 166
|
.
gi 1956267849 151 A 151
Cdd:PRK14243 167 A 167
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-150 |
9.79e-21 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 87.11 E-value: 9.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVFQSYALFPNlN 93
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 94 VRDNIG-FGlkvaGVPRAKARE--RVAEMLELI-GLPD-----LGRRYAFeLSGGQQQRVALARAL 150
Cdd:COG4618 422 IAENIArFG----DADPEKVVAaaKLAGVHEMIlRLPDgydtrIGEGGAR-LSGGQRQRIGLARAL 482
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-150 |
1.03e-20 |
|
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: 84.06 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS--QRNVGMVFQSYALFPNlNVRDN 97
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 98 IGFGLKVAGVPRAKARERVAEMLELI-GLP-----DLGRRYAfELSGGQQQRVALARAL 150
Cdd:cd03248 108 IAYGLQSCSFECVKEAAQKAHAHSFIsELAsgydtEVGEKGS-QLSGGQKQRVAIARAL 165
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-151 |
3.14e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.61 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ-------RNvgmvfqsyAL 88
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEachylghRN--------AM 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 89 FPNLNVRDNIGFGLKVAGvpraKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13539 85 KPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLV 143
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-151 |
3.46e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 83.64 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 23 DLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITH------LKPSQRNVGMVFQsyalFPNLN--- 93
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQIRKKVGLVFQ----FPESQlfe 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 94 --VRDNIGFGLKVAGVPRAKARERVAEMLELIGLP-DLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13649 101 etVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILA 161
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
6-151 |
4.03e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.01 E-value: 4.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNT-----VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT------HLKP 74
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 75 SQRNVGMVFQ--SYALFPNLNVRDnIGFGLKVAGVPRAKARERVAEMLELIGLP-DLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKD-VAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILA 160
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
20-151 |
6.45e-20 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 85.01 E-value: 6.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS--QRNVGMVFQSYALFPNlNVRDN 97
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQavRRQLGVVLQNGRLMSG-SIFEN 546
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 98 IgfglkVAGVPRAKarERVAEMLELIGLPDLGRRYAF-----------ELSGGQQQRVALARALA 151
Cdd:TIGR03797 547 I-----AGGAPLTL--DEAWEAARMAGLAEDIRAMPMgmhtvisegggTLSGGQRQRLLIARALV 604
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
31-151 |
7.75e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.52 E-value: 7.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 31 GEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ-----RNVGMVFQS-YA-LFPNLNVRDNIGFGLK 103
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1956267849 104 VAGVPRAK-ARERVAEMLELIGL-PDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK10261 430 VHGLLPGKaAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALA 479
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-151 |
7.97e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.73 E-value: 7.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 9 EAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHL--KPSQRNVGMVFQSY 86
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYasKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 87 ALFPNLNVRDNIGFGlKVAGVP-----RAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK10253 91 TTPGDITVQELVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
25-151 |
1.45e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.11 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 25 DLSFN--SGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT--HLKPSQRNVGMVFQS-YALFPNLNVRDNIG 99
Cdd:PRK13648 27 DVSFNipKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddNFEKLRKHIGIVFQNpDNQFVGSIVKYDVA 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 100 FGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13648 107 FGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLA 158
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-151 |
1.54e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.06 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT--HLKPSQRNVGMVFQSY-ALFPNLNVRDN 97
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 98 IGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
15-151 |
4.21e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.37 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 15 FGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNvGMVF-----QSYA 87
Cdd:COG1129 262 LSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaiRA-GIAYvpedrKGEG 340
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 88 LFPNLNVRDNI---------GFGLkvagVPRAKARERVAEMLELIGL--PDLGRRyAFELSGGQQQRVALARALA 151
Cdd:COG1129 341 LVLDLSIRENItlasldrlsRGGL----LDRRRERALAEEYIKRLRIktPSPEQP-VGNLSGGNQQKVVLAKWLA 410
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-124 |
5.31e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS---QRNVGMV 82
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkahQLGIYLV 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1956267849 83 FQSYALFPNLNVRDNIGFGLkvagvPR-AKARERVAEMLELIG 124
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGL-----PKrQASMQKMKQLLAALG 129
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-148 |
6.24e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.08 E-value: 6.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 23 DLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSqrnvgmvFQSYALF--------PNLNV 94
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDLLYlghqpgikTELTA 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 95 RDNIGFGLKVAGVPRakaRERVAEMLELIGLpdLGRRY--AFELSGGQQQRVALAR 148
Cdd:PRK13538 92 LENLRFYQRLHGPGD---DEALWEALAQVGL--AGFEDvpVRQLSAGQQRRVALAR 142
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-151 |
8.08e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 80.21 E-value: 8.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITH------LKPSQRNVGMVFQ--SYALFPNl 92
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQfpESQLFED- 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 93 NVRDNIGFGLKVAGVPRAKARERVAEMLELIGLP-DLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13646 102 TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILA 161
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-151 |
8.35e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 79.71 E-value: 8.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 2 AEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVL----RMIAGFEKPTK--GRIFADGREITHLKPS 75
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLkvlnRLIEIYDSKIKvdGKVLYFGKDIFQIDAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 76 Q--RNVGMVFQSYALFPNLNVRDNIGFGLKVAGVP-RAKARERVAEMLELIGL----PDLGRRYAFELSGGQQQRVALAR 148
Cdd:PRK14246 87 KlrKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIAR 166
|
...
gi 1956267849 149 ALA 151
Cdd:PRK14246 167 ALA 169
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-151 |
1.17e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.84 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKP---TKGRIFADGREITH--LKPSQRNVGMVFQSY-ALFPNLN 93
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAktVWDIREKVGIVFQNPdNQFVGAT 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 94 VRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-150 |
1.84e-18 |
|
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: 78.53 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 19 TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADG-----REITHLkpsqRNVGMVF-QSYALFPNL 92
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkRRKKFL----RRIGVVFgQKTQLWWDL 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 93 NVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAAL 168
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-150 |
2.24e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 80.62 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 19 TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRI-FADGREITHLkpSQRnvgmvfqSYalFPNLNVRDN 97
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIaRPAGARVLFL--PQR-------PY--LPLGTLREA 445
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 98 IGFglkvAGVPRAKARERVAEMLELIGLPDLGRRYAFE------LSGGQQQRVALARAL 150
Cdd:COG4178 446 LLY----PATAEAFSDAELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLL 500
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-151 |
2.32e-18 |
|
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: 78.08 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAG---FEKPTKGRIFADGREItHLKPSQRNVGMVFQSYALFPNLNVRD 96
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPR-KPDQFQKCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 97 NIGFGLKVAGvPRAKA----RERVAEM-LELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03234 101 TLTYTAILRL-PRKSSdairKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLL 159
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-151 |
2.78e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.74 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITH----LKPSQRNVGMVFQS--YALFpNLNV 94
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkgLMKLRESVGMVFQDpdNQLF-SASV 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 95 RDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-150 |
2.79e-18 |
|
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: 80.25 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 19 TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS--QRNVGMVFQSYALFpNLNVRD 96
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIGIVPQDTVLF-NDTIAY 450
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 97 NIGFGLkvAGVPRAKARE--RVAEMLELI-GLPD-----LGRRyAFELSGGQQQRVALARAL 150
Cdd:COG5265 451 NIAYGR--PDASEEEVEAaaRAAQIHDFIeSLPDgydtrVGER-GLKLSGGEKQRVAIARTL 509
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-151 |
2.94e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.12 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 19 TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRI------------------FADGREITHLKPSQRNVG 80
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnhelitNPYSKKIKNFKELRRRVS 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 81 MVFQ--SYALFPNlNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPD-LGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13631 120 MVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILA 192
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-150 |
3.91e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.77 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHL--KPSQRNVGMVFQSYALFpNLNVRDN 97
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYdhHYLHRQVALVGQEPVLF-SGSVREN 574
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 98 IGFGLK-------VAGVPRAKARERVAEMLELIGlPDLGRRYAFeLSGGQQQRVALARAL 150
Cdd:TIGR00958 575 IAYGLTdtpdeeiMAAAKAANAHDFIMEFPNGYD-TEVGEKGSQ-LSGGQKQRIAIARAL 632
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-151 |
4.03e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.51 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNT-----VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGR-------IFADGREITHLKPS 75
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaIPANLKKIKEVKRL 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 76 QRNVGMVFQ--SYALFPNlNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLP-DLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIA 166
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-151 |
7.46e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.47 E-value: 7.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 18 NTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT--HLKPSQRNVGMVFQSY--ALFPNlN 93
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaeNEKWVRSKVGLVFQDPddQVFSS-T 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 94 VRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13647 97 VWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-151 |
1.02e-17 |
|
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: 78.69 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFE--KPTKGRIF----------------ADGR 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 68 ------------EITHLKPS--------QRNVGMVFQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPD 127
Cdd:TIGR03269 81 pcpvcggtlepeEVDFWNLSdklrrrirKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180
....*....|....*....|....
gi 1956267849 128 LGRRYAFELSGGQQQRVALARALA 151
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLA 184
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-150 |
2.19e-17 |
|
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: 74.84 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS-QRNVGMVFQSYALFPNLNV 94
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 95 RDNIGFglkvagVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:cd03231 91 LENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLL 140
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-150 |
2.32e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 77.40 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVFQSYALFpNLN 93
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 94 VRDNIGFGLKVAgvprakARERVAEMLELIGLPDLGRRY-----------AFELSGGQQQRVALARAL 150
Cdd:TIGR02868 425 VRENLRLARPDA------TDEELWAALERVGLADWLRALpdgldtvlgegGARLSGGERQRLALARAL 486
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-150 |
2.45e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.79 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREI-THLKPSQRNVGMVFQ 84
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLARARIGVVPQ 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 85 SYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-150 |
3.57e-17 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 73.89 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTN--TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQRN-VGMV 82
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 83 FQSYALFpNLNVRDNigfglkvagvprakarervaemleliglpdLGRRyafeLSGGQQQRVALARAL 150
Cdd:cd03247 81 NQRPYLF-DTTLRNN------------------------------LGRR----FSGGERQRLALARIL 113
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-151 |
5.59e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRI-FADGREITHLkpSQRNVgmvfq 84
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVkLGETVKIGYF--DQHQE----- 388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 85 syALFPNLNVRDNIgfglkvAGVPRAKARERVAEMLELIGL-PDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG0488 389 --ELDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLL 448
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-151 |
6.11e-17 |
|
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: 74.11 E-value: 6.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLkpsqrNVGMVFQsyalfPNLNVR 95
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN-----PELTGR 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 96 DNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03220 103 ENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATA 158
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-150 |
9.80e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.44 E-value: 9.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 3 EEFLNLEAITKTFGTNT---------VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT--- 70
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 71 HLKPSQRnVGMVFQSYAlfPNLNVRDNIG----FGLKVAGVPRAKARE-RVAEMLELIGL-PDLGRRYAFELSGGQQQRV 144
Cdd:PRK15112 82 YSYRSQR-IRMIFQDPS--TSLNPRQRISqildFPLRLNTDLEPEQREkQIIETLRQVGLlPDHASYYPHMLAPGQKQRL 158
|
....*.
gi 1956267849 145 ALARAL 150
Cdd:PRK15112 159 GLARAL 164
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-121 |
1.00e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.96 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 13 KTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGReITHLkpsqRNVGMVFQsyalfPNL 92
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSAL----LELGAGFH-----PEL 103
|
90 100
....*....|....*....|....*....
gi 1956267849 93 NVRDNIGFGLKVAGVPRAKARERVAEMLE 121
Cdd:COG1134 104 TGRENIYLNGRLLGLSRKEIDEKFDEIVE 132
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-150 |
1.03e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 75.63 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ--RNVGMVFQSYALFpNLNVRDN 97
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAISVVSQRVHLF-SATLRDN 433
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 98 igfgLKVAGvPRAkARERVAEMLELIGLPDL--------------GRryafELSGGQQQRVALARAL 150
Cdd:PRK11160 434 ----LLLAA-PNA-SDEALIEVLQQVGLEKLleddkglnawlgegGR----QLSGGEQRRLGIARAL 490
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-150 |
1.17e-16 |
|
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: 75.61 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLD-LSFN--SGEFVSLLGPSGCGKTTVLRMIAGFEKPTKG----RIFADGREITHLKPSQRN-----VGMVFQSYA 87
Cdd:TIGR03269 296 VVKAVDnVSLEvkEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvRVGDEWVDMTKPGPDGRGrakryIGILHQEYD 375
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 88 LFPNLNVRDNI--GFGLKvagVPRAKARERVAEMLELIGLPD-----LGRRYAFELSGGQQQRVALARAL 150
Cdd:TIGR03269 376 LYPHRTVLDNLteAIGLE---LPDELARMKAVITLKMVGFDEekaeeILDKYPDELSEGERHRVALAQVL 442
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-151 |
1.73e-16 |
|
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: 72.08 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQR-NVGMVF-----QSYALFPNLN 93
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiRAGIAYvpedrKREGLVLDLS 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 94 VRDNIGfglkvagvprakarervaemleligLPDLgrryafeLSGGQQQRVALARALA 151
Cdd:cd03215 95 VAENIA-------------------------LSSL-------LSGGNQQKVVLARWLA 120
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-151 |
1.78e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.53 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 14 TFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGF-----EKPTKGRIFADGREI----THLKPSQRNVGMVFQ 84
Cdd:PRK14258 16 YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIyerrVNLNRLRRQVSMVHP 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 85 SYALFPnLNVRDNIGFGLKVAG-VPRAKARERVAEMLELIGLPDLGR----RYAFELSGGQQQRVALARALA 151
Cdd:PRK14258 96 KPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKhkihKSALDLSGGQQQRLCIARALA 166
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-100 |
1.80e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 72.56 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 18 NTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFE--KPTKGRIFADGREITHLKPSQR---NVGMVFQSYALFPNL 92
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIPGV 92
|
90
....*....|...
gi 1956267849 93 NVRD-----NIGF 100
Cdd:cd03217 93 KNADflryvNEGF 105
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-150 |
2.28e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.97 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADG-----REITHLkpsqRNVGMVF-QSYALFPNLNV 94
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkRRKEFA----RRIGVVFgQRSQLWWDLPA 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 95 RDNigFGL--KVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:COG4586 114 IDS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAAL 169
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-150 |
2.71e-16 |
|
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: 72.12 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 17 TNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGReithlkpsqrnVGMVFQSyALFPNLNVRD 96
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQE-PWIQNGTIRE 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 97 NIGFGLKVagvprakARERVAEMLELIGL-PDL-----------GRRyAFELSGGQQQRVALARAL 150
Cdd:cd03250 85 NILFGKPF-------DEERYEKVIKACALePDLeilpdgdlteiGEK-GINLSGGQKQRISLARAV 142
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-151 |
3.32e-16 |
|
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: 71.43 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 19 TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAG--FEKPTKGRIFADGREItHLKPSQRNVGMVFQSYALFPNLNVRD 96
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL-DKRSFRKIIGYVPQDDILHPTLTVRE 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 97 NIGFGLKVAGvprakarervaemleliglpdlgrryafeLSGGQQQRVALARALA 151
Cdd:cd03213 102 TLMFAAKLRG-----------------------------LSGGERKRVSIALELV 127
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
34-151 |
7.25e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.14 E-value: 7.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 34 VSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT--HLKPSQRNVGMVFQSY--ALFpNLNVRDNIGFGLKVAGVPR 109
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGLVFQNPddQIF-SPTVEQDIAFGPINLGLDE 111
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1956267849 110 AKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13652 112 ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-151 |
1.07e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.56 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNT-VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGR---EITHLKPSQRNVGM 81
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 82 VFQS-YALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-150 |
1.12e-15 |
|
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: 73.12 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 7 NLEAITKTFGTNTVIKdLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREI-THLKPSQRNVGMVFQS 85
Cdd:TIGR01257 933 NLVKIFEPSGRPAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQH 1011
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 86 YALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-150 |
2.07e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.29 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ---R 77
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 78 NVGMVFQSYALFPNLNVRDNIGFGLKVAgvPRAKARERVAEMLELigLPDLGRR---YAFELSGGQQQRVALARAL 150
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYEL--FPRLHERriqRAGTMSGGEQQMLAIGRAL 152
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-150 |
3.21e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.39 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGF--EKPTKGRIFADGREI--THLKPSQR-NVG 80
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkaSNIRDTERaGIV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 81 MVFQSYALFPNLNVRDNIGFG----LKVAGVPRAKARERVAEMLELIGLPDLG-RRYAFELSGGQQQRVALARAL 150
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNvTRPVGDYGGGQQQLVEIAKAL 156
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-151 |
5.68e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.74 E-value: 5.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 11 ITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRM-------IAGFEkpTKGRIFADGREITHLKPS---QRNVG 80
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYR--YSGDVLLGGRSIFNYRDVlefRRRVG 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 81 MVFQSYALFPnLNVRDNIGFGLKVAG-VPRAKARERVAEMLELIGLPDLGR----RYAFELSGGQQQRVALARALA 151
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDAVKdrlsDSPFRLSGGQQQLLCLARTLA 179
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-62 |
9.29e-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: 66.70 E-value: 9.29e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRI 62
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV 57
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-150 |
1.21e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.88 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS----QRNVGMVFQ--SYALFPNlN 93
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllalRQQVATVFQdpEQQIFYT-D 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 94 VRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGAL 151
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
8-148 |
2.89e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.80 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNT--VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGReitHLKPSQRNVGMVFQS 85
Cdd:PRK13543 12 LAAHALAFSRNEepVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRFMAYLG 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 86 Y--ALFPNLNVRDNIGFglkVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALAR 148
Cdd:PRK13543 89 HlpGLKADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR 150
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-151 |
4.00e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.84 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAeeFLNLEAITKTFG-TNTVIKDLD---LSFNSGEFVSLLGPSGCGKTTVLRMIAGF-EKPtkGRIFAD-----GREIT 70
Cdd:PRK11022 1 MA--LLNVDKLSVHFGdESAPFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYP--GRVMAEklefnGQDLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 71 HLKPSQR------NVGMVFQS--YALFPNLNVRDNIGFGLKV-AGVPRAKARERVAEMLELIGLPDLGRR---YAFELSG 138
Cdd:PRK11022 77 RISEKERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSG 156
|
170
....*....|...
gi 1956267849 139 GQQQRVALARALA 151
Cdd:PRK11022 157 GMSQRVMIAMAIA 169
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-150 |
5.50e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.68 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 25 DLSFN--SGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT--HLKPSQRNVGMVFQSYALFpNLNVRDNIGF 100
Cdd:PRK13657 353 DVSFEakPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvTRASLRRNIAVVFQDAGLF-NRSIEDNIRV 431
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 101 GLKVAG---VPRAKARERVAEMLE--------LIGlpDLGRRyafeLSGGQQQRVALARAL 150
Cdd:PRK13657 432 GRPDATdeeMRAAAERAQAHDFIErkpdgydtVVG--ERGRQ----LSGGERQRLAIARAL 486
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-151 |
1.50e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.49 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAG------FEkptkGRIFADGREIT--HL 72
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtYE----GEIIFEGEELQasNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 73 KPSQRN-VGMVFQSYALFPNLNVRDNIGFG--LKVAGVPR-AKARERVAEMLELIGL---PDLGRRyafELSGGQQQRVA 145
Cdd:PRK13549 77 RDTERAgIAIIHQELALVKELSVLENIFLGneITPGGIMDyDAMYLRAQKLLAQLKLdinPATPVG---NLGLGQQQLVE 153
|
....*.
gi 1956267849 146 LARALA 151
Cdd:PRK13549 154 IAKALN 159
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
19-151 |
1.84e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.58 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 19 TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT--HLKPSQRNVGMVFQSYALFPNLNVRD 96
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 97 NIGFGL----KVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK10575 105 LVAIGRypwhGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
8-150 |
1.96e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIfadgreithLKPSQRNVGMVFQSYA 87
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGYVPQKLY 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 88 LFPNLNvrdnigfgLKVAGVPRAKARERVAEMleligLPDLGRRYAF--------ELSGGQQQRVALARAL 150
Cdd:PRK09544 78 LDTTLP--------LTVNRFLRLRPGTKKEDI-----LPALKRVQAGhlidapmqKLSGGETQRVLLARAL 135
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-150 |
1.99e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 65.25 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 24 LDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEkPTKGRIFADGREITHLKP----------SQRNV---GM-VFQSYALF 89
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAaelarhraylSQQQSppfAMpVFQYLALH 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 90 -PnlnvrdnigfglkvAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:COG4138 94 qP--------------AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVL 141
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-151 |
2.11e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.09 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 5 FLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHlkPSQRN-----V 79
Cdd:PRK11288 4 YLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRF--ASTTAalaagV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 80 GMVFQSYALFPNLNVRDNIGFGL---KVAGVPRAKARERVAEMLELIGL---PDLGRRYafeLSGGQQQRVALARALA 151
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQlphKGGIVNRRLLNYEAREQLEHLGVdidPDTPLKY---LSIGQRQMVEIAKALA 156
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-151 |
2.18e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.20 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 19 TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQ-RNVGMVF-----QSYALFPNL 92
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErRRLGVAYipedrLGRGLVPDM 351
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 93 NVRDNIGFG------LKVAGVPRAKARERVAEmlELIglpdlgRRY----------AFELSGGQQQRVALARALA 151
Cdd:COG3845 352 SVAENLILGryrrppFSRGGFLDRKAIRAFAE--ELI------EEFdvrtpgpdtpARSLSGGNQQKVILARELS 418
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-149 |
2.48e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 9 EAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKG--RIFadGREIThlkPS----QRNVGMV 82
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeaWLF--GQPVD---AGdiatRRRVGYM 344
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 83 FQSYALFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARA 149
Cdd:NF033858 345 SQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVA 411
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-150 |
3.97e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.51 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS--QRNVGMVFQSYALFPNlNVRDN 97
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPVVLAD-TFLAN 434
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 98 IGFGlkvagvpRAKARERVAEMLELIGLPDLGRRY-----------AFELSGGQQQRVALARAL 150
Cdd:PRK10790 435 VTLG-------RDISEEQVWQALETVQLAELARSLpdglytplgeqGNNLSVGQKQLLALARVL 491
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-150 |
4.61e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 65.25 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 24 LDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFeKPTKGRIFADGREITHLKPSQ--RNVGMVFQSYALFPNlNVRDNIGFG 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESwrKHLSWVGQNPQLPHG-TLRDNVLLG 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 102 LKVAG---VPRAKARERVAEMLELigLPD-----LGRRYAfELSGGQQQRVALARAL 150
Cdd:PRK11174 447 NPDASdeqLQQALENAWVSEFLPL--LPQgldtpIGDQAA-GLSVGQAQRLALARAL 500
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-150 |
4.76e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.34 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKT----TVLRMI-AGFEKpTKGRIFADGREITHLKPSQRNVGMVFQS--YALFPNLN 93
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHT 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 94 VRDNIGFGLKVAGVPRAKARerVAEMLELIGLPDLGR---RYAFELSGGQQQRVALARAL 150
Cdd:PRK10418 98 MHTHARETCLALGKPADDAT--LTAALEAVGLENAARvlkLYPFEMSGGMLQRMMIALAL 155
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-150 |
1.31e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.59 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTN----TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTkGRI-----FaDGREITH 71
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPdgdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIggsatF-NGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 72 LKPSQRN------VGMVFQS--YALFPNLNVRDNIGFGLKV-AGVPRAKARERVAEMLELIGLPDLGRR---YAFELSGG 139
Cdd:PRK09473 86 LPEKELNklraeqISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGG 165
|
170
....*....|.
gi 1956267849 140 QQQRVALARAL 150
Cdd:PRK09473 166 MRQRVMIAMAL 176
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
12-150 |
2.89e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.97 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 12 TKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPT--KGRIFADGREIThlKPSQRNVGMVFQSYALF 89
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT--KQILKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 90 PNLNVRDNIGFgLKVAGVPRAKARE---RVAE-MLELIGLPD-----LGRRYAFELSGGQQQRVALARAL 150
Cdd:PLN03211 153 PHLTVRETLVF-CSLLRLPKSLTKQekiLVAEsVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEM 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-151 |
3.82e-12 |
|
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: 61.66 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 27 SFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHlKPSQrnVGMVFQSyalfpnlNVRDNIGFGLKVAG 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY-KPQY--IKADYEG-------TVRDLLSSITKDFY 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1956267849 107 VpRAKARERVAEMLELIGLPDlgrRYAFELSGGQQQRVALARALA 151
Cdd:cd03237 91 T-HPYFKTEIAKPLQIEQILD---REVPELSGGELQRVAIAACLS 131
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-151 |
4.68e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.82 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTF-GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIThlKPSQRN- 78
Cdd:PRK15056 2 MQQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR--QALQKNl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 79 VGMVFQSYAL---FPNLnVRDNIGFG----LKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK15056 80 VAYVPQSEEVdwsFPVL-VEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-150 |
1.18e-11 |
|
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: 61.10 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 9 EAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADgrEITHLkpsqrnvGMVFQSY-A 87
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVKL-------AYVDQSRdA 396
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 88 LFPNLNVRDNIGFG---LKVAGVpRAKARERVAemleliglpdlgrRYAF----------ELSGGQQQRVALARAL 150
Cdd:TIGR03719 397 LDPNKTVWEEISGGldiIKLGKR-EIPSRAYVG-------------RFNFkgsdqqkkvgQLSGGERNRVHLAKTL 458
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-151 |
1.25e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 60.69 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLD---LSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKP----TKGRIFADGREITHLKPSQR------NVGMVFQ--S 85
Cdd:COG4170 20 VKAVDrvsLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQepS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 86 YALFPNLNVRDNIgfglkVAGVP----------RAKAR-ERVAEMLELIGLPD---LGRRYAFELSGGQQQRVALARALA 151
Cdd:COG4170 100 SCLDPSAKIGDQL-----IEAIPswtfkgkwwqRFKWRkKRAIELLHRVGIKDhkdIMNSYPHELTEGECQKVMIAMAIA 174
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-150 |
1.81e-11 |
|
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: 60.72 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 11 ITKTFGTN-TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGR-IFADGreithlkpsqRNVGMVFQSYAL 88
Cdd:TIGR03719 10 VSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEaRPQPG----------IKVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 89 FPNLNVRDNIGFGlkVAGVPRAKAR-------------------ERVAEMLELI---GLPDLGRRY-------------- 132
Cdd:TIGR03719 80 DPTKTVRENVEEG--VAEIKDALDRfneisakyaepdadfdklaAEQAELQEIIdaaDAWDLDSQLeiamdalrcppwda 157
|
170
....*....|....*....
gi 1956267849 133 -AFELSGGQQQRVALARAL 150
Cdd:TIGR03719 158 dVTKLSGGERRRVALCRLL 176
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-150 |
1.85e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.42 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS--QRNVGMVFQSYALFpNLNVRDNI 98
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAslRNQVALVSQNVHLF-NDTIANNI 437
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 99 GFGLKvAGVPRAKArERVAEM---LELI-----GLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK11176 438 AYART-EQYSREQI-EEAARMayaMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARAL 495
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
6-151 |
2.60e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.46 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAG-FEKP-------TKGRIFADGREITHLKPSQ- 76
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaprgarVTGDVTLNGEPLAAIDAPRl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 77 --RNVGMVFQSYALFPnLNVRDNIGFG----LKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK13547 82 arLRAVLPQAAQPAFA-FSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
.
gi 1956267849 151 A 151
Cdd:PRK13547 161 A 161
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-151 |
2.86e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 19 TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADgreithlkpsqrnvgmvFQSYALFPNLNVRDNI 98
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----------------VPDNQFGREASLIDAI 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 99 gfglkvagvPRAKARERVAEMLELIGLPD---LGRRYAfELSGGQQQRVALARALA 151
Cdd:COG2401 107 ---------GRKGDFKDAVELLNAVGLSDavlWLRRFK-ELSTGQKFRFRLALLLA 152
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-150 |
4.82e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.37 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRI------FADGREITHLKPS-----Q 76
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevlggdMADARHRRAVCPRiaympQ 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 77 ---RNvgmvfqsyaLFPNLNVRDNIGFGLKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:NF033858 84 glgKN---------LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCAL 151
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-148 |
6.02e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 25 DLSFN--SGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITH-LKPSQRNVGMVFQSYALFPNLNVRDNIGFG 101
Cdd:PRK13540 19 QISFHlpAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSGINPYLTLRENCLYD 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1956267849 102 LKVAGVprakarerVAEMLELIGLPDLGRRYAFE---LSGGQQQRVALAR 148
Cdd:PRK13540 99 IHFSPG--------AVGITELCRLFSLEHLIDYPcglLSSGQKRQVALLR 140
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-62 |
8.48e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 8.48e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRI 62
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-143 |
1.01e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 4 EFLNLEAitkTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFE--KPTKGRIFADGREITHLKP---SQRN 78
Cdd:CHL00131 9 EIKNLHA---SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPeerAHLG 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 79 VGMVFQSYALFPNLNvrdNIGFgLKVAGVPRAKAR-----------ERVAEMLELIGL-PDLGRRYAFE-LSGGQQQR 143
Cdd:CHL00131 86 IFLAFQYPIEIPGVS---NADF-LRLAYNSKRKFQglpeldpleflEIINEKLKLVGMdPSFLSRNVNEgFSGGEKKR 159
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-151 |
1.10e-10 |
|
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: 58.27 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 24 LDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREIT-HLKPSQRN---VgmVFQSYALFPNLnvrdnig 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTaDNREAYRQlfsA--VFSDFHLFDRL------- 421
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 100 fglkvAGVPRAKARERVAEMLELIGLPDL-----GRRYAFELSGGQQQRVALARALA 151
Cdd:COG4615 422 -----LGLDGEADPARARELLERLELDHKvsvedGRFSTTDLSQGQRKRLALLVALL 473
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-150 |
1.72e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 12 TKTFGTNTVI-KDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGR-IFADGreithlkpsqRNVGMVFQSYALF 89
Cdd:PRK11819 13 SKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPG----------IKVGYLPQEPQLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 90 PNLNVRDNI--GFGLKVAGVPR-----AKARERVAEMLELI-------------GLPDLGRRY--AFE------------ 135
Cdd:PRK11819 83 PEKTVRENVeeGVAEVKAALDRfneiyAAYAEPDADFDALAaeqgelqeiidaaDAWDLDSQLeiAMDalrcppwdakvt 162
|
170
....*....|....*.
gi 1956267849 136 -LSGGQQQRVALARAL 150
Cdd:PRK11819 163 kLSGGERRRVALCRLL 178
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
18-151 |
1.94e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.42 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 18 NTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHL-KPSQRNVGmvfQSYALFPNLNVRD 96
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIaKPYCTYIG---HNLGLKLEMTVFE 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 97 NIGFGLKVagvprAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13541 90 NLKFWSEI-----YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIA 139
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-150 |
3.06e-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: 55.24 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 18 NTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIfadgreithLKPSQRNVGMVFQ-SYalFPNLNVRD 96
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPEGEDLLFLPQrPY--LPLGTLRE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 97 NIgfglkvagvprakarervaemleliglpdlgrRYAF--ELSGGQQQRVALARAL 150
Cdd:cd03223 83 QL--------------------------------IYPWddVLSGGEQQRLAFARLL 106
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
7-147 |
3.34e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.98 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 7 NLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAgFEKPT----KGRIFADGREIThLKPSQRNVGMV 82
Cdd:TIGR00955 27 LRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPID-AKEMRAISAYV 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 83 FQSYALFPNLNVRDNIGFGLKV---AGVPRAKARERVAEMLE----------LIGLPDLGRryafELSGGQQQRVALA 147
Cdd:TIGR00955 105 QQDDLFIPTLTVREHLMFQAHLrmpRRVTKKEKRERVDEVLQalglrkcantRIGVPGRVK----GLSGGERKRLAFA 178
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-151 |
5.96e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.13 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTV-IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS--QRNVGMV 82
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyRKLFSAV 402
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 83 FQSYALFPNLnvRDNIGFGLKVAGVPRAKARERVAEMLELIGlpdlGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK10522 403 FTDFHLFDQL--LGPEGKPANPALVEKWLERLKMAHKLELED----GRISNLKLSKGQKKRLALLLALA 465
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-147 |
8.04e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.32 E-value: 8.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 24 LDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFeKPTKGRIFADGREITHLKPS------------QRNVGM--VFQSYALF 89
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAelarhraylsqqQTPPFAmpVFQYLTLH 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 90 pnlnvrdnigfglKVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALA 147
Cdd:PRK03695 94 -------------QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLA 138
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-150 |
9.75e-10 |
|
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: 55.79 E-value: 9.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 4 EFLNLEAITKTF-GTNTVIKD-LDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREI-THLKPSQRNVG 80
Cdd:TIGR01257 1936 DILRLNELTKVYsGTSSPAVDrLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQNMG 2015
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 81 MVFQSYALFPNLNVRDNIGFGLKVAGVPrAKARERVAEM-LELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREHLYLYARLRGVP-AEEIEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-151 |
1.39e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.06 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 22 KDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQR-NVGMVF-----QSYALFPNLNVR 95
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 96 DNI--------GFGLKVAGVPRAKARERVAEMLELIGLPDLGRRyafeLSGGQQQRVALARALA 151
Cdd:PRK15439 360 WNVcalthnrrGFWIKPARENAVLERYRRALNIKFNHAEQAART----LSGGNQQKVLIAKCLE 419
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-62 |
1.48e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 1.48e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 9 EAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRI 62
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-150 |
1.64e-09 |
|
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: 55.30 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGReithlkpsqrnVGMVFQSYALFPNlNVRDNIG 99
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNII 508
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 100 FGL-----KVAGVPRA-KARERVAEMLELIGLPdLGRRyAFELSGGQQQRVALARAL 150
Cdd:TIGR01271 509 FGLsydeyRYTSVIKAcQLEEDIALFPEKDKTV-LGEG-GITLSGGQRARISLARAV 563
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-150 |
2.16e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.95 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 10 AITKTFGTNTVIKD-------LDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIfadgreitHLKPSqrnVGMV 82
Cdd:TIGR00957 636 SITVHNATFTWARDlpptlngITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV--------HMKGS---VAYV 704
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 83 FQSyALFPNLNVRDNIGFGlKVAGVPRAKAR-ERVAEMLELIGLP-----DLGRRyAFELSGGQQQRVALARAL 150
Cdd:TIGR00957 705 PQQ-AWIQNDSLRENILFG-KALNEKYYQQVlEACALLPDLEILPsgdrtEIGEK-GVNLSGGQKQRVSLARAV 775
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
26-151 |
2.47e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.42 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 26 LSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKP----TKGRIFADGREITHLKPSQR------NVGMVFQSyalfPN--LN 93
Cdd:PRK15093 28 MTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERrklvghNVSMIFQE----PQscLD 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 94 VRDNIGFGLkVAGVP----------RAKARERVA-EMLELIGLPD---LGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK15093 104 PSERVGRQL-MQNIPgwtykgrwwqRFGWRKRRAiELLHRVGIKDhkdAMRSFPYELTEGECQKVMIAIALA 174
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-151 |
2.84e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 2 AEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIA----GFEKPTKGRIFADGREITHLKPSQR 77
Cdd:TIGR00956 58 LTRGFRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 78 -NVGMVFQSYALFPNLNVRDNIGF-------GLKVAGVPRAKARERVAEM-LELIGL-----PDLGRRYAFELSGGQQQR 143
Cdd:TIGR00956 138 gDVVYNAETDVHFPHLTVGETLDFaarcktpQNRPDGVSREEYAKHIADVyMATYGLshtrnTKVGNDFVRGVSGGERKR 217
|
....*...
gi 1956267849 144 VALARALA 151
Cdd:TIGR00956 218 VSIAEASL 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-128 |
4.47e-09 |
|
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: 52.63 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKP--TKGRIFADGREIThlKPSQRNVGMVFQSYALFPNLN 93
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLD--KNFQRSTGYVEQQDVHSPNLT 95
|
90 100 110
....*....|....*....|....*....|....*
gi 1956267849 94 VRDNIGFGLKVAGVpRAKARERVAEMLELIGLPDL 128
Cdd:cd03232 96 VREALRFSALLRGL-SVEQRKRLTIGVELAAKPSI 129
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-150 |
5.37e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTF-GtntvIKDLD---LSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKP--SQR-N 78
Cdd:PRK10762 5 LQLKGIDKAFpG----VKALSgaaLNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPksSQEaG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 79 VGMVFQSYALFPNLNVRDNIGFGL----KVAGVPRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARAL 150
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGRefvnRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-150 |
6.22e-09 |
|
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: 52.94 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 18 NTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGReithlkpsqrnVGMVFQSYALFPNlNVRDN 97
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 98 IGFGLKVAGVpRAKARERVAEMLE-LIGLPDLGRRYAFE----LSGGQQQRVALARAL 150
Cdd:cd03291 118 IIFGVSYDEY-RYKSVVKACQLEEdITKFPEKDNTVLGEggitLSGGQRARISLARAV 174
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-150 |
6.75e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 4 EFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFA-DGREI--THLKPSQRNVG 80
Cdd:PTZ00265 384 QFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLkdINLKWWRSKIG 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 81 MVFQSYALFPNlNVRDNIGF------------------------GLKVAGVPRAKARERVAEML------ELI------- 123
Cdd:PTZ00265 464 VVSQDPLLFSN-SIKNNIKYslyslkdlealsnyynedgndsqeNKNKRNSCRAKCAGDLNDMSnttdsnELIemrknyq 542
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 124 ---------------------GLPD----LGRRYAFELSGGQQQRVALARAL 150
Cdd:PTZ00265 543 tikdsevvdvskkvlihdfvsALPDkyetLVGSNASKLSGGQKQRISIARAI 594
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-151 |
6.92e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 31 GEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADgreithlkpsqrnvgmvfqsyalfpnlnvrdnigfgLKVAGVP-- 108
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------------------------------------LKISYKPqy 408
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1956267849 109 -RAKARERVAEML--------------ELI---GLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK13409 409 iKPDYDGTVEDLLrsitddlgssyyksEIIkplQLERLLDKNVKDLSGGELQRVAIAACLS 469
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-150 |
8.45e-09 |
|
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: 52.11 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTV----LRMIagfeKPTKGRIFADGREITHLKPSQ--RNVGMVFQSYALF 89
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLF 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 90 PNlNVRDNIG-FG----------LKvagvpRAKARERVAEMLELIGLPDL--GRryafELSGGQQQRVALARAL 150
Cdd:cd03244 91 SG-TIRSNLDpFGeysdeelwqaLE-----RVGLKEFVESLPGGLDTVVEegGE----NLSVGQRQLLCLARAL 154
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-150 |
9.18e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.79 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 17 TNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPS--QRNVGMVFQSYALFPNlNV 94
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 95 RDNIGFGLkvagvPRAKAR--ERVAEML----ELIGLP-----DLGRRyAFELSGGQQQRVALARAL 150
Cdd:PRK10789 406 ANNIALGR-----PDATQQeiEHVARLAsvhdDILRLPqgydtEVGER-GVMLSGGQKQRISIARAL 466
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-150 |
1.02e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 52.24 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGR-----EITHLKPS 75
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 76 QRNV------GMVFQSYA--LFPNLNVRDNIGFGLKVAGVpR--AKARERVAEMLELIGLP-----DLGRRYafelSGGQ 140
Cdd:PRK11701 82 ERRRllrtewGFVHQHPRdgLRMQVSAGGNIGERLMAVGA-RhyGDIRATAGDWLERVEIDaaridDLPTTF----SGGM 156
|
170
....*....|
gi 1956267849 141 QQRVALARAL 150
Cdd:PRK11701 157 QQRLQIARNL 166
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-151 |
1.64e-08 |
|
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: 52.09 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 1 MAEEFLNLEAITKTFGtntvikDLDLSFNSG-----EFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGReITHlKPs 75
Cdd:COG1245 337 EEETLVEYPDLTKSYG------GFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-ISY-KP- 407
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 76 QRnvgmVFQSYalfpNLNVRDNIGFGLKVAgVPRAKARERVAEMLeliGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:COG1245 408 QY----ISPDY----DGTVEEFLRSANTDD-FGSSYYKTEIIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLS 471
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-151 |
6.09e-08 |
|
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: 50.55 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 30 SGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFAdgreithlKPSQRNV-----GMVFQSYalFPNLnvRDNigfGLKV 104
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDE--------EPSWDEVlkrfrGTELQDY--FKKL--ANG---EIKV 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 105 A-------GVPRA----------KARER-----VAEMLELIGLPDlgrRYAFELSGGQQQRVALARALA 151
Cdd:COG1245 163 AhkpqyvdLIPKVfkgtvrelleKVDERgkldeLAEKLGLENILD---RDISELSGGELQRVAIAAALL 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-150 |
9.68e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 9.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 17 TNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGfekptkgrifadgrEITHLKPS----QRNVGMVFQSYALFpNL 92
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG--------------ELSHAETSsvviRGSVAYVPQVSWIF-NA 693
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 93 NVRDNIGFGLKVAGVPRAKARERVAEMLELIGLP-----DLGRRyAFELSGGQQQRVALARAL 150
Cdd:PLN03232 694 TVRENILFGSDFESERYWRAIDVTALQHDLDLLPgrdltEIGER-GVNISGGQKQRVSMARAV 755
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-150 |
1.75e-07 |
|
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: 48.48 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 14 TFGTN-TVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIF---ADGREITHLKPSQRNVGMVfqSYA-- 87
Cdd:cd03290 9 SWGSGlATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnKNESEPSFEATRSRNRYSV--AYAaq 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 88 --LFPNLNVRDNIGFG-----LKVAGVPRAKARERVAEMLELIGLPDLGRRyAFELSGGQQQRVALARAL 150
Cdd:cd03290 87 kpWLLNATVEENITFGspfnkQRYKAVTDACSLQPDIDLLPFGDQTEIGER-GINLSGGQRQRICVARAL 155
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-150 |
1.88e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 17 TNTVIKDLDLSFNSGEFVSLLGPSGCGKT----TVLRMIagfekPT------KGRIF--------ADGREITHLKPSQrn 78
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRfhgesllhASEQTLRGVRGNK-- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 79 VGMVFQS--YALFPNLNVRDNIGFGLKV-AGVPRAKARERVAEMLELIGLPDLGRR---YAFELSGGQQQRVALARAL 150
Cdd:PRK15134 94 IAMIFQEpmVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMAL 171
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-151 |
1.92e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 48.03 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 13 KTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAG----FEKPTkGRIFADGREITHLKPS-QRNVGMVFQSYA 87
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSVE-GDIHYNGIPYKEFAEKyPGEIIYVSEEDV 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 88 LFPNLNVRDNIGFGLKVagvprakarervaemleliglpdLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03233 94 HFPTLTVRETLDFALRC-----------------------KGNEFVRGISGGERKRVSIAEALV 134
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-151 |
1.93e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAG------FEkptkGRIFADG--REITHLKPSQR 77
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsYE----GEILFDGevCRFKDIRDSEA 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 78 nVGMVF--QSYALFPNLNVRDNIGFGLKVA--GV-PRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:NF040905 78 -LGIVIihQELALIPYLSIAENIFLGNERAkrGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-151 |
1.98e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.52 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 30 SGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRI-----------FADGREI----THLKPSQRNVGMVFQSYALFPNlNV 94
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELqnyfTKLLEGDVKVIVKPQYVDLIPK-AV 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 95 RDNIGFGLKvagvpRAKARERVAEMLELIGLPDLGRRYAFELSGGQQQRVALARALA 151
Cdd:cd03236 104 KGKVGELLK-----KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALA 155
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
18-143 |
4.34e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 18 NTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFE--KPTKGRIFADGREITHLKPSQR---NVGMVFQSYALFPNL 92
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAFQYPVEIPGV 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 93 NVRdnigFGLKVAGVPRAKARER-----------VAEMLELIGLPD--LGRRYAFELSGGQQQR 143
Cdd:PRK09580 94 SNQ----FFLQTALNAVRSYRGQepldrfdfqdlMEEKIALLKMPEdlLTRSVNVGFSGGEKKR 153
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-150 |
4.63e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQR-NVGMVFQSY-----ALFPNLNV 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 95 RDNIG------FGLKVAGVPRAKARERVAEMLEL--IGLPDLGRRYAFeLSGGQQQRVALARAL 150
Cdd:PRK10762 348 KENMSltalryFSRAGGSLKHADEQQAVSDFIRLfnIKTPSMEQAIGL-LSGGNQQKVAIARGL 410
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-150 |
6.74e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIfadgREITHLKPSqrnvgmVFQSY- 86
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVA------YFDQHr 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 87 -ALFPNLNVRDNIGFGLK---VAGVPR-------------AKARERVAemleliglpdlgrryafELSGGQQQRVALARA 149
Cdd:PRK11147 392 aELDPEKTVMDNLAEGKQevmVNGRPRhvlgylqdflfhpKRAMTPVK-----------------ALSGGERNRLLLARL 454
|
.
gi 1956267849 150 L 150
Cdd:PRK11147 455 F 455
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-148 |
1.20e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 46.67 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGF--------EKPTKGRIFadgreithLKPsQRnvgmvfqsyALFPN 91
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLF--------YVP-QR---------PYMTL 528
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 92 LNVRDNIGFGLKVAGVPRAKARERVAE-MLELIGLPDLGRR---------YAFELSGGQQQRVALAR 148
Cdd:TIGR00954 529 GTLRDQIIYPDSSEDMKRRGLSDKDLEqILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMAR 595
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
60-150 |
1.48e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 60 GRIFADGREIT--HLKPSQRNVGMVFQSYALFpNLNVRDNIGFGLKVAGVPRAKARERVAEMLELI-GLPD-----LGRr 131
Cdd:PTZ00265 1277 GKILLDGVDICdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFIeSLPNkydtnVGP- 1354
|
90
....*....|....*....
gi 1956267849 132 YAFELSGGQQQRVALARAL 150
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARAL 1373
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-149 |
1.64e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 23 DLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGfEKPTKgrifADGREIThlkpsQRNVGMVFQSYALFpNLNVRDNIGFGL 102
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPPR----SDASVVI-----RGTVAYVPQVSWIF-NATVRDNILFGS 703
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 103 KVAGVPRAKARERVAEMLELIGLP-----DLGRRyAFELSGGQQQRVALARA 149
Cdd:PLN03130 704 PFDPERYERAIDVTALQHDLDLLPggdltEIGER-GVNISGGQKQRVSMARA 754
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-150 |
1.76e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADgREITHLkPSQrnvgmvfqsyALFPNLNVRDNIG 99
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIAYV-PQQ----------AWIMNATVRGNIL 742
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 100 F-----GLKVAGVPRAKARErvAEMLELIG--LPDLGRRyAFELSGGQQQRVALARAL 150
Cdd:PTZ00243 743 FfdeedAARLADAVRVSQLE--ADLAQLGGglETEIGEK-GVNLSGGQKARVSLARAV 797
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
9-74 |
2.71e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 2.71e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1956267849 9 EAITKTFGTNTVIKDLDlSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHlKP 74
Cdd:cd03222 4 PDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVY-KP 67
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-150 |
3.01e-06 |
|
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: 45.10 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITH--LKPSQRNVGMVFQSYALFPNlNVRDN 97
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTipLEDLRSSLTIIPQDPTLFSG-TIRSN 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1956267849 98 IGfglkvagvPRAKARERvaEMLELIGLPDLGRryafELSGGQQQRVALARAL 150
Cdd:cd03369 102 LD--------PFDEYSDE--EIYGALRVSEGGL----NLSQGQRQLLCLARAL 140
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-151 |
4.05e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.23 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKT-TVLRMIAGFEKpTKGRIFADG-------REITHLKPSQR---------NVGMVF 83
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKmllrrrsRQVIELSEQSAaqmrhvrgaDMAMIF 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1956267849 84 QS--YALFPNLNVRDNIGFGLKV-AGVPRAKARERVAEMLELIGLPD---LGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK10261 111 QEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALS 184
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-148 |
5.97e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGReITHLKPSQRNV-GMVFQSYAL------ 88
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK-VRMAVFSQHHVdGLDLSSNPLlymmrc 598
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 89 FPnlnvrdnigfglkvaGVPRAKARERVAEmLELIGlpDLGRRYAFELSGGQQQRVALAR 148
Cdd:PLN03073 599 FP---------------GVPEQKLRAHLGS-FGVTG--NLALQPMYTLSGGQKSRVAFAK 640
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-87 |
7.23e-06 |
|
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: 43.13 E-value: 7.23e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 30 SGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGR-IFADGREITHLKPSQRNVGMVFQSYA 87
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLIIVGGKKA 59
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-151 |
1.32e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.75 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 26 LSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKPSQR-NVGMVF-----QSYALFPNLNVRDNIG 99
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAiRAGIMLcpedrKAEGIIPVHSVADNIN 353
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 100 ---------FGLKV-AGVPRAKARERVAEMleLIGLPDlGRRYAFELSGGQQQRVALARALA 151
Cdd:PRK11288 354 isarrhhlrAGCLInNRWEAENADRFIRSL--NIKTPS-REQLIMNLSGGNQQKAILGRWLS 412
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-150 |
1.84e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 15 FGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGfEKPTK--------GRIFADGREITHLKpsqRNVGMVFQSY 86
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfGRRRGSGETIWDIK---KHIGYVSSSL 345
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1956267849 87 AL--FPNLNVRDNI--GFgLKVAGVPRA---KARERVAEMLELIGLPDLGRRYAFE-LSGGQQQRVALARAL 150
Cdd:PRK10938 346 HLdyRVSTSVRNVIlsGF-FDSIGIYQAvsdRQQKLAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRAL 416
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-151 |
2.61e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.85 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITHLKP---SQRNVGMVFQSY---ALFPNLNV 94
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldaVKKGMAYITESRrdnGFFPNFSI 358
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1956267849 95 RDNIGF-------GLKVA-GVPRAKARERVAE-MLELIGLP--DLGRRYAfELSGGQQQRVALARALA 151
Cdd:PRK09700 359 AQNMAIsrslkdgGYKGAmGLFHEVDEQRTAEnQRELLALKchSVNQNIT-ELSGGNQQKVLISKWLC 425
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-101 |
5.71e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 8 LEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREItHLKPS----QRNVGMVF 83
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSkealENGISMVH 79
|
90
....*....|....*...
gi 1956267849 84 QSYALFPNLNVRDNIGFG 101
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLG 97
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-150 |
7.62e-05 |
|
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: 41.35 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 3 EEFLNLEAITKTFGTNTVIK---DLDLSFNSGEFVSLLGPSGCGKTTVLRMIAG-FEKPTKGRIFADGREITHLKPSQ-- 76
Cdd:TIGR02633 255 DVILEARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNPAQai 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 77 -RNVGMVFQS---YALFPNLNVRDNIGFGL--KVAGVPRAKARERVAEMLELI-------GLPDL--GRryafeLSGGQQ 141
Cdd:TIGR02633 335 rAGIAMVPEDrkrHGIVPILGVGKNITLSVlkSFCFKMRIDAAAELQIIGSAIqrlkvktASPFLpiGR-----LSGGNQ 409
|
....*....
gi 1956267849 142 QRVALARAL 150
Cdd:TIGR02633 410 QKAVLAKML 418
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-62 |
1.39e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 1.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 6 LNLEAITKTFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRI 62
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-150 |
2.33e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.34 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITH--LKPSQRNVGMVFQSYALFPNlNVRDN 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSG-TVRFN 1329
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 98 IGfglkvagvPRAKARER-VAEMLELIGLPDLGRRYAFEL-----------SGGQQQRVALARAL 150
Cdd:PLN03232 1330 ID--------PFSEHNDAdLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARAL 1386
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-150 |
4.49e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 39.54 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 16 GTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGREITH--LKPSQRNVGMVFQSYALFPNlN 93
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKigLHDLRFKITIIPQDPVLFSG-S 1375
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1956267849 94 VRDNIG-FGlkvagvprAKARERVAEMLELIGLPD----LGRRYAFE-------LSGGQQQRVALARAL 150
Cdd:TIGR00957 1376 LRMNLDpFS--------QYSDEEVWWALELAHLKTfvsaLPDKLDHEcaeggenLSVGQRQLVCLARAL 1436
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-150 |
8.57e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 38.61 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 20 VIKDLDLSFNSGEFVSLLGPSGCGKTTVL----RMIagfeKPTKGRIFADGREITH--LKPSQRNVGMVFQSYALFPNlN 93
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG-T 1399
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1956267849 94 VRDNIGFGLKV--AGVPRA----KARERVAEMLELIGLPDL--GRRYafelSGGQQQRVALARAL 150
Cdd:PTZ00243 1400 VRQNVDPFLEAssAEVWAAlelvGLRERVASESEGIDSRVLegGSNY----SVGQRQLMCMARAL 1460
|
|
| SpoIIIAA |
COG3854 |
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ... |
36-66 |
1.52e-03 |
|
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443063 Cd Length: 309 Bit Score: 37.44 E-value: 1.52e-03
10 20 30
....*....|....*....|....*....|.
gi 1956267849 36 LLGPSGCGKTTVLRMIAgfekptkgRIFADG 66
Cdd:COG3854 145 IISPPGCGKTTLLRDIA--------RVLSDG 167
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-150 |
1.97e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 37.22 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 3 EEFLNLEAITKTFGTNTVIK---DLDLSFNSGEFVSLLGPSGCGKTTVLRMIAG-FEKPTKGRIFADGREITHLKPSQ-- 76
Cdd:PRK13549 257 EVILEVRNLTAWDPVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKIRNPQQai 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 77 -RNVGMVFQS---YALFPNLNVRDNI---------GFGLKVAGVPRAKARERVAEMLELIGLPDL--GRryafeLSGGQQ 141
Cdd:PRK13549 337 aQGIAMVPEDrkrDGIVPVMGVGKNItlaaldrftGGSRIDDAAELKTILESIQRLKVKTASPELaiAR-----LSGGNQ 411
|
....*....
gi 1956267849 142 QRVALARAL 150
Cdd:PRK13549 412 QKAVLAKCL 420
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-121 |
1.98e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 37.10 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAGFEKPTKGRIFADGreithlkpsqrNVGMVFQSYALFPNLNVRDNIGF 100
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIAISAGLSGQLTGIENIEF 108
|
90 100
....*....|....*....|.
gi 1956267849 101 GLKVAGVPRAKARERVAEMLE 121
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIE 129
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-66 |
2.06e-03 |
|
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: 37.58 E-value: 2.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 14 TFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTV----LRMIAgfekpTKGRIFADG 66
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLS-----TEGEIQIDG 1279
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-62 |
3.39e-03 |
|
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: 36.15 E-value: 3.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1956267849 21 IKDLDLSFNSGEFVSLLGPSGCGKTTVLRmiAGFEKPTKGRI 62
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARL 50
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-128 |
4.32e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 36.63 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 31 GEFVSLLGPSGCGKTTVLRMIAgfEKPTKGRIFAD-----GREIThlKPSQRNVGMVFQSYALFPNLNVRDNIGFGLKV- 104
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGdrlvnGRPLD--SSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLr 864
|
90 100
....*....|....*....|....*.
gi 1956267849 105 --AGVPRAKARERVAEMLELIGLPDL 128
Cdd:TIGR00956 865 qpKSVSKSEKMEYVEEVIKLLEMESY 890
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
70-147 |
4.40e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 36.53 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 70 THLKPSQRNVGMVFQSYALFPNLNVRDNIGF--GLKVAGVPRAKARERVAEMLELIG-LPDLGRRY------AFELSGGQ 140
Cdd:TIGR00630 414 TRLKPEALAVTVGGKSIADVSELSIREAHEFfnQLTLTPEEKKIAEEVLKEIRERLGfLIDVGLDYlslsraAGTLSGGE 493
|
....*..
gi 1956267849 141 QQRVALA 147
Cdd:TIGR00630 494 AQRIRLA 500
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-150 |
4.66e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 36.08 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 15 FGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTVLRMIAG----------FEK----------PTK---GRIF---ADG-- 66
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevllddgriiYEQdlivarlqqdPPRnveGTVYdfvAEGie 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1956267849 67 ---------REITHL---KPSQRNVGMVFQSYALFPNLNvrdniGFGLKvagvprakarERVAEMLELIGL-PD--LGrr 131
Cdd:PRK11147 93 eqaeylkryHDISHLvetDPSEKNLNELAKLQEQLDHHN-----LWQLE----------NRINEVLAQLGLdPDaaLS-- 155
|
170
....*....|....*....
gi 1956267849 132 yafELSGGQQQRVALARAL 150
Cdd:PRK11147 156 ---SLSGGWLRKAALGRAL 171
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-66 |
5.89e-03 |
|
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: 35.60 E-value: 5.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1956267849 14 TFGTNTVIKDLDLSFNSGEFVSLLGPSGCGKTTV----LRMIAgfekpTKGRIFADG 66
Cdd:cd03289 13 TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDG 64
|
|
| |
