|
Name |
Accession |
Description |
Interval |
E-value |
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-317 |
1.73e-148 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 421.81 E-value: 1.73e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 2 DIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSsakkikTSPHERN 81
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG------LPPEKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVFQDFALWPHMNVFENVAFGLRATKQT-NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGLRMRGVPkAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 161 FDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVGK 240
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 241 ANWL-------------VEGKQ-----------------MIRPEHVSWTKNEVCEMYTGEIQHVTYVGERYEMKVNMGAL 290
Cdd:COG3842 239 ANLLpgtvlgdegggvrTGGRTlevpadaglaaggpvtvAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRLGDG 318
|
330 340 350
....*....|....*....|....*....|.
gi 446273968 291 GIWTAY----HNSKLSIGKPVSLYVPKKYIH 317
Cdd:COG3842 319 QELVVRvpnrAALPLEPGDRVGLSWDPEDVV 349
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-317 |
2.31e-133 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 383.27 E-value: 2.31e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 2 DIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMyssakkIKTSPHERN 81
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV------TDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVFQDFALWPHMNVFENVAFGLRATKQT-NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPLKLRKVPkAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 161 FDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVG- 239
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGs 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 240 -----------KANWLVEGKQM-----------------IRPEHVSWTKNEVCEMyTGEIQHVTYVGERYEMKVNMGAlG 291
Cdd:COG3839 237 ppmnllpgtveGGGVRLGGVRLplpaalaaaaggevtlgIRPEHLRLADEGDGGL-EATVEVVEPLGSETLVHVRLGG-Q 314
|
330 340
....*....|....*....|....*...
gi 446273968 292 IWTAY--HNSKLSIGKPVSLYVPKKYIH 317
Cdd:COG3839 315 ELVARvpGDTRLRPGDTVRLAFDPERLH 342
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-244 |
6.40e-121 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 351.37 E-value: 6.40e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYssakkIKTSPHER 80
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-----TNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQDFALWPHMNVFENVAFGLRATKQTN-QLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFI 159
Cdd:COG1118 76 RVGFVFQHYALFPHMTVAENIAFGLRVRPPSKaEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 160 LFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVG 239
Cdd:COG1118 156 LLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG 235
|
....*
gi 446273968 240 KANWL 244
Cdd:COG1118 236 CVNVL 240
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-239 |
8.50e-118 |
|
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: 339.21 E-value: 8.50e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMyssakkIKTSPHERNI 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI------TNLPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGLRaTKQTNQ--LREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLR-LKKLPKaeIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 161 FDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVG 239
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-220 |
4.16e-112 |
|
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: 324.09 E-value: 4.16e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMyssakkIKTSPHERNI 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV------TGVPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGLRATKQTN-QLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILF 161
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKaEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 162 DEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-242 |
6.55e-105 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 311.88 E-value: 6.55e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMyssakkIKTSPHERNI 82
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI------THVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGLRATKQTNQ-LREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILF 161
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAeITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 162 DEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVGKA 241
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEI 248
|
.
gi 446273968 242 N 242
Cdd:PRK09452 249 N 249
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-239 |
1.52e-99 |
|
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: 293.09 E-value: 1.52e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmyssaKKIKTSPHER 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE------DATDVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQDFALWPHMNVFENVAFGLRATKQT-----NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTK 155
Cdd:cd03296 75 NVGFVFQHYALFRHMTVFDNVAFGLRVKPRSerppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 156 PHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVA 235
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVY 234
|
....
gi 446273968 236 KFVG 239
Cdd:cd03296 235 SFLG 238
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-244 |
4.07e-97 |
|
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: 291.17 E-value: 4.07e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGdtcmyssAKKI-KTSPHERN 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQG-------GRDItRLPPQKRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVFQDFALWPHMNVFENVAFGLRATK-QTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:TIGR03265 78 YGIVFQSYALFPNLTVADNIAYGLKNRGmGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 161 FDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVGK 240
Cdd:TIGR03265 158 LDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE 237
|
....
gi 446273968 241 ANWL 244
Cdd:TIGR03265 238 VNWL 241
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-220 |
4.41e-96 |
|
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: 283.38 E-value: 4.41e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMyssakkIKTSPHERNI 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV------TDLPPKDRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGLRATKQTNQ-LREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILF 161
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDeIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 162 DEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-306 |
8.29e-96 |
|
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: 286.70 E-value: 8.29e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 33 LLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMyssakkIKTSPHERNIGMVFQDFALWPHMNVFENVAFGLRATKQTN 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV------TNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 113 -QLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSIGLTA 191
Cdd:TIGR01187 75 aEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 192 LYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVGKANWL--------------------------- 244
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFeatvierkseqvvlagvegrrcdiytd 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446273968 245 --VEGKQ----MIRPEHVSW---TKNEVCEMYTGEIQHVTYVGE--RYEMKVNMGALGIWTAYHNSKLSIGKP 306
Cdd:TIGR01187 235 vpVEKDQplhvVLRPEKIVIeeeDEANSSNAIIGHVIDITYLGMtlEVHVRLETGQKVLVSEFFNEDDPHMSP 307
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-286 |
1.30e-95 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 287.39 E-value: 1.30e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 10 KNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmySSAKKIKTSPHERNIGMVFQDF 89
Cdd:PRK11432 14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI------DGEDVTHRSIQQRDICMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 90 ALWPHMNVFENVAFGLRATKQTN-QLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSAL 168
Cdd:PRK11432 88 ALFPHMSLGENVGYGLKMLGVPKeERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 169 DAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVGKANWL---- 244
Cdd:PRK11432 168 DANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFpatl 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 245 ------VEGKQMIRPEHVSWTKNE-----------VCEMYTGE------IQHVTYVGERYEMKVN 286
Cdd:PRK11432 248 sgdyvdIYGYRLPRPAAFAFNLPDgectvgvrpeaITLSEQGEesqrctIKHVAYMGPQYEVTVD 312
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-239 |
2.40e-94 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 284.04 E-value: 2.40e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF-GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKT-SPHER 80
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG-------RVVNElEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQDFALWPHMNVFENVAFGL--RATKQTnQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHF 158
Cdd:PRK11650 77 DIAMVFQNYALYPHMSVRENMAYGLkiRGMPKA-EIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 159 ILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFV 238
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFI 235
|
.
gi 446273968 239 G 239
Cdd:PRK11650 236 G 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-214 |
4.91e-92 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 274.66 E-value: 4.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF----GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssakKIKTSPH 78
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--------KPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 ERnIGMVFQDFALWPHMNVFENVAFGLRATKQT-NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPH 157
Cdd:COG1116 80 PD-RGVVFQEPALLPWLTVLDNVALGLELRGVPkAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 158 FILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQG 214
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-211 |
1.54e-88 |
|
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: 264.33 E-value: 1.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFG----KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssakKIKTSPH 78
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 eRNIGMVFQDFALWPHMNVFENVAFGLRAT-KQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPH 157
Cdd:cd03293 73 -PDRGYVFQQDALLPWLTVLDNVALGLELQgVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446273968 158 FILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVM 211
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
1-248 |
6.46e-87 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 265.32 E-value: 6.46e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGLEKNFGK----TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcMYSSAKKIKTS 76
Cdd:NF040933 1 VTVRVENVTKIFKKgkkeVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDK-LVASPGKIIVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 77 PHERNIGMVFQDFALWPHMNVFENVAFGLRATK-QTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTK 155
Cdd:NF040933 80 PEDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKvPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 156 PHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVA 235
Cdd:NF040933 160 PQVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVA 239
|
250
....*....|...
gi 446273968 236 KFVGKANwLVEGK 248
Cdd:NF040933 240 RLIGDIN-LLEGK 251
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
3-244 |
7.94e-86 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 258.19 E-value: 7.94e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmyssaKKIKTSPHERNI 82
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQ------DATRVHARDRKI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGLRATKQTNQL-REKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILF 161
Cdd:TIGR00968 75 GFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKiKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 162 DEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVGKA 241
Cdd:TIGR00968 155 DEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEV 234
|
...
gi 446273968 242 NWL 244
Cdd:TIGR00968 235 NVL 237
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
3-244 |
3.74e-81 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 250.68 E-value: 3.74e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPD--KGEIYFGDTCMyssakkIKTSPHER 80
Cdd:TIGR03258 6 IRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDL------THAPPHKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQDFALWPHMNVFENVAFGLRATKQTNQL-REKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFI 159
Cdd:TIGR03258 80 GLALLFQNYALFPHLKVEDNVAFGLRAQKMPKADiAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 160 LFDEPLSALDAILREEMRLELMDIVHSI-GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFV 238
Cdd:TIGR03258 160 LLDEPLSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFL 239
|
....*.
gi 446273968 239 GKANWL 244
Cdd:TIGR03258 240 GAANIL 245
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-290 |
4.38e-81 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 250.72 E-value: 4.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 2 DIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSsakkikTSPHERN 81
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND------VPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVFQDFALWPHMNVFENVAFGLR-ATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKlAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 161 FDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVG- 239
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGs 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 240 -KAN------------------------WL-VEGKQM---------IRPEH-VSWTKNEVCemYTGEIQHVTYVGERYEM 283
Cdd:PRK11000 237 pKMNflpvkvtataieqvqvelpnrqqvWLpVEGRGVqvganmslgIRPEHlLPSDIADVT--LEGEVQVVEQLGNETQI 314
|
....*..
gi 446273968 284 KVNMGAL 290
Cdd:PRK11000 315 HIQIPAI 321
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-240 |
7.26e-81 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 248.08 E-value: 7.26e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF-GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKT-SPHE- 79
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDG-------EDIRDlDPVEl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 -RNIGMVFQDFALWPHMNVFENVAFGLRATKQT-NQLREKVEDAIKRVRL--QGMEKRYPHELSGGQQQRVAFARAIVTK 155
Cdd:COG1125 75 rRRIGYVIQQIGLFPHMTVAENIATVPRLLGWDkERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 156 PHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVA 235
Cdd:COG1125 155 PPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVA 234
|
....*
gi 446273968 236 KFVGK 240
Cdd:COG1125 235 DFVGA 239
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-220 |
2.01e-79 |
|
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: 241.05 E-value: 2.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 28 GEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPHERNIGMVFQDFALWPHMNVFENVAFGLRA 107
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 108 tKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSI 187
Cdd:cd03297 103 -KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNL 181
|
170 180 190
....*....|....*....|....*....|...
gi 446273968 188 GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03297 182 NIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-240 |
3.90e-79 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 241.05 E-value: 3.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTspHERNI 82
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINK--LRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGLRATKQTN--QLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPIKVKKMSkaEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 161 FDEPLSALDAILREEMrLELM-DIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVG 239
Cdd:COG1126 160 FDEPTSALDPELVGEV-LDVMrDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237
|
.
gi 446273968 240 K 240
Cdd:COG1126 238 K 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-255 |
1.17e-77 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 241.53 E-value: 1.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYssakkiKTSPHER 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS------RLHARDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQDFALWPHMNVFENVAFGL-----RATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTK 155
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNIAFGLtvlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 156 PHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVA 235
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVL 234
|
250 260
....*....|....*....|....
gi 446273968 236 KFVGKANWL---VEGKQM-IRPEH 255
Cdd:PRK10851 235 EFMGEVNRLqgtIRGGQFhVGAHR 258
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-242 |
1.28e-77 |
|
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: 237.23 E-value: 1.28e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQaLKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmysSAKKIKT-SPHERN 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL-------NGKDITNlPPEKRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVFQDFALWPHMNVFENVAFGLRatkqtNQLREKVEDAiKRVR----LQGME---KRYPHELSGGQQQRVAFARAIVT 154
Cdd:cd03299 73 ISYVPQNYALFPHMTVYKNIAYGLK-----KRKVDKKEIE-RKVLeiaeMLGIDhllNRKPETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 155 KPHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFV 234
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFV 226
|
....*...
gi 446273968 235 AKFVGKAN 242
Cdd:cd03299 227 AEFLGFNN 234
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-215 |
3.69e-77 |
|
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: 234.00 E-value: 3.69e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKtsPHERNI 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELP--PLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGlratkqtnqlrekvedaikrvrlqgmekrypheLSGGQQQRVAFARAIVTKPHFILFD 162
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446273968 163 EPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGE 215
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-238 |
5.70e-77 |
|
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: 235.64 E-value: 5.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYS-SAKKIKtsPHERN 81
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELY--ELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVFQDFALWPHMNVFENVAFGLRA-TKQT-NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFI 159
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREhTDLSeAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 160 LFDEPLSALDAI-LREEMRLeLMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYvKPSHEFVAKFV 238
Cdd:COG1127 164 LYDEPTAGLDPItSAVIDEL-IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL-ASDDPWVRQFL 241
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-238 |
1.00e-76 |
|
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: 236.00 E-value: 1.00e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 8 LEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPHERNIGMVFQ 87
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 88 DFALWPHMNVFENVAFGLRATKQTNQLR-EKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLS 166
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEReERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446273968 167 ALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFV 238
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-247 |
3.11e-76 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 238.58 E-value: 3.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIyfgdtcMYSSAKKIKTSPHERNI 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI------MLDGVDLSHVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGLRATK-QTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILF 161
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDKlPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 162 DEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVGKA 241
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
....*.
gi 446273968 242 NwLVEG 247
Cdd:PRK11607 254 N-VFEG 258
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
3-247 |
6.85e-74 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 231.50 E-value: 6.85e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFgKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKTSPHE-RN 81
Cdd:NF040840 2 IRIENLSKDW-KEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDG-------KDITNLPPEkRG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVFQDFALWPHMNVFENVAFGLRATK-QTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:NF040840 74 IAYVYQNYMLFPHKTVFENIAFGLKLRKvPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 161 FDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVGK 240
Cdd:NF040840 154 LDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGF 233
|
....*..
gi 446273968 241 ANwLVEG 247
Cdd:NF040840 234 EN-IIEG 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-240 |
1.46e-72 |
|
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: 224.49 E-value: 1.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQ-ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIK-TSPHE- 79
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG-------EDIReQDPVEl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 -RNIGMVFQDFALWPHMNVFENVAFGLRATK-QTNQLREKVEDAIKRVRL--QGMEKRYPHELSGGQQQRVAFARAIVTK 155
Cdd:cd03295 74 rRKIGYVIQQIGLFPHMTVEENIALVPKLLKwPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 156 PHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVA 235
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
....*
gi 446273968 236 KFVGK 240
Cdd:cd03295 234 EFVGA 238
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-216 |
1.08e-71 |
|
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: 221.59 E-value: 1.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFG----KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPH 78
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 ERNIGMVFQDFALWPHMNVFENVAFGLR-ATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPH 157
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLlAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 158 FILFDEPLSALDAILREE-MRLeLMDIVHSIGLTALYVTHDQTEAmSMSDQIIVMKQGEV 216
Cdd:cd03255 161 IILADEPTGNLDSETGKEvMEL-LRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
10-240 |
1.11e-71 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 226.27 E-value: 1.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 10 KNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GDTCMYSSAKKIKtSPHERNIGMVFQD 88
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIdGENIMKQSPVELR-EVRRKKIGMVFQQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 89 FALWPHMNVFENVAFGLRATKQTNQLR-EKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSA 167
Cdd:TIGR01186 80 FALFPHMTILQNTSLGPELLGWPEQERkEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446273968 168 LDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVGK 240
Cdd:TIGR01186 160 LDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-237 |
3.33e-71 |
|
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: 220.84 E-value: 3.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMySSAKKIKTSPHERNI 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDI-SGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGLRATKQ--TNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLREHTRlsEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 161 FDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIyVKPSHEFVAKF 237
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL-RASDDPLVRQF 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-225 |
5.03e-70 |
|
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: 221.90 E-value: 5.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 31 TTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPHERNIGMVFQDFALWPHMNVFENVAFGLRATKQ 110
Cdd:COG4148 28 TALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEARLFPHLSVRGNLLYGRKRAPR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 111 TNQlREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSIGLT 190
Cdd:COG4148 108 AER-RISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIP 186
|
170 180 190
....*....|....*....|....*....|....*
gi 446273968 191 ALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG4148 187 ILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-232 |
2.40e-69 |
|
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: 224.78 E-value: 2.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF-----GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMySSAKKIKTSP 77
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDL-TKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 78 HERNIGMVFQD-FA-LWPHMNVFENVAFGLRATKQTN--QLREKVEDAIKRVRLQ-GMEKRYPHELSGGQQQRVAFARAI 152
Cdd:COG1123 340 LRRRVQMVFQDpYSsLNPRMTVGDIIAEPLRLHGLLSraERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 153 VTKPHFILFDEPLSALDAILREE-MRLeLMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSH 231
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQiLNL-LRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
.
gi 446273968 232 E 232
Cdd:COG1123 499 P 499
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-216 |
2.87e-69 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 215.68 E-value: 2.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFG----KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPH 78
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 ERNIGMVFQDFALWPHMNVFENVAFGLRATKQT-NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPH 157
Cdd:COG1136 85 RRHIGFVFQFFNLLPELTALENVALPLLLAGVSrKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 158 FILFDEPLSALDAILREE-MRLeLMDIVHSIGLTALYVTHDQtEAMSMSDQIIVMKQGEV 216
Cdd:COG1136 165 LILADEPTGNLDSKTGEEvLEL-LRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-216 |
2.97e-67 |
|
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: 210.08 E-value: 2.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSphERNI 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINEL--RQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGLRATKQTN--QLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPIKVKGMSkaEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 161 FDEPLSALDAILREEMrLELM-DIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:cd03262 159 FDEPTSALDPELVGEV-LDVMkDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
26-239 |
1.68e-66 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 208.46 E-value: 1.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 26 KQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMyssakkIKTSPHERNIGMVFQDFALWPHMNVFENVAFGL 105
Cdd:COG3840 23 AAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL------TALPPAERPVSMLFQENNLFPHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 106 R-ATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIV 184
Cdd:COG3840 97 RpGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELC 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 185 HSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVG 239
Cdd:COG3840 177 RERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-233 |
5.74e-65 |
|
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: 205.42 E-value: 5.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGK----TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKiktsPH 78
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK----AF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 ERNIGMVFQDF--ALWPHMNVFENVAFGLRATKQTNQlREKVEDAIKRVRL-QGMEKRYPHELSGGQQQRVAFARAIVTK 155
Cdd:COG1124 78 RRRVQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDR-EERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 156 PHFILFDEPLSALDAILREE-MRLeLMDIVHSIGLTALYVTHDqTEAMS-MSDQIIVMKQGEVLQKGTPEDIYVKPSHEF 233
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEiLNL-LKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-216 |
1.92e-64 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 202.98 E-value: 1.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF-GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTS---PH 78
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQ----DLSRLKRReipYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 ERNIGMVFQDFALWPHMNVFENVAFGLRAT-KQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPH 157
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTgKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446273968 158 FILFDEPLSALDailrEEMRLELMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:COG2884 158 LLLADEPTGNLD----PETSWEIMELLEEInrrGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-226 |
3.63e-64 |
|
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: 202.56 E-value: 3.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMY-SSAKKIKtspheRNIGMVFQD--- 88
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELR-----RKVGLVFQNpdd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 89 --FAlwphMNVFENVAFGLRATKQT-NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:COG1122 87 qlFA----PTVEEDVAFGPENLGLPrEEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 166 SALDAilreEMRLELMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:COG1122 163 AGLDP----RGRRELLELLKRLnkeGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-225 |
8.52e-64 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 201.83 E-value: 8.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKtspheRNI 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-----RRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAF--GLRATKQtNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFfaRLYGLPR-KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 161 FDEPLSALDAILREEMRLELMDIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-220 |
4.77e-61 |
|
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: 194.65 E-value: 4.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF----GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKtSPH 78
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR-KIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 ERNIGMVFQD--FALWPHMNVFENVAFGLRAtkqtnQLREKVEDAIKRVRLQGME---------KRYPHELSGGQQQRVA 147
Cdd:cd03257 81 RKEIQMVFQDpmSSLNPRMTIGEQIAEPLRI-----HGKLSKKEARKEAVLLLLVgvglpeevlNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 148 FARAIVTKPHFILFDEPLSALDAILREE-MRLeLMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQiLDL-LKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
29-229 |
2.04e-60 |
|
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: 196.87 E-value: 2.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 29 EFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPHERNIGMVFQDFALWPHMNVFENVAFGLRat 108
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMK-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 109 KQTNQLREKVEDAIkrVRLQGME---KRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVH 185
Cdd:TIGR02142 102 RARPSERRISFERV--IELLGIGhllGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446273968 186 SIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKP 229
Cdd:TIGR02142 180 EFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-211 |
7.54e-60 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 192.77 E-value: 7.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 15 TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKTSPHERniGMVFQDFALWPH 94
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-------VPVTGPGADR--GVVFQKDALLPW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 95 MNVFENVAFGLRATKQTNQLREKV-EDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILR 173
Cdd:COG4525 91 LNVLDNVAFGLRLRGVPKAERRARaEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTR 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 446273968 174 EEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVM 211
Cdd:COG4525 171 EQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-225 |
8.24e-59 |
|
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: 189.48 E-value: 8.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKT-SPHE-- 79
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG-------RDLASlSRREla 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 RNIGMVFQDFALWPHMNVFENVAFGLRA-----TKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVT 154
Cdd:COG1120 75 RRIAYVPQEPPAPFGLTVRELVALGRYPhlglfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 155 KPHFILFDEPLSALDaiLReeMRLELMDIVHSI----GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG1120 155 EPPLLLLDEPTSHLD--LA--HQLEVLELLRRLarerGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-237 |
5.49e-58 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 187.22 E-value: 5.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKiktsphERNI 82
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD------ERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 ----GMVFQDFALWPHMNVFENVAFGLRATKQTN--QLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKP 156
Cdd:PRK09493 76 rqeaGMVFQQFYLFPHLTALENVMFGPLRVRGASkeEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 157 HFILFDEPLSALDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAK 236
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEV-LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
.
gi 446273968 237 F 237
Cdd:PRK09493 235 F 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-225 |
6.24e-57 |
|
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: 184.29 E-value: 6.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmyssAKKIKTSPHERNI 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE-----DVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGLRATKQT-NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILF 161
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYFAELYGLFdEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 162 DEPLSALDAILREEMRLELMDIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-225 |
7.87e-57 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 184.49 E-value: 7.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF-GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMySSAKKIKTSPHERN 81
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDV-TALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVFQDFALWPHMNVFENVAFG-------LRAT--KQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAI 152
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGrlgrtstWRSLlgLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 153 VTKPHFILFDEPLSALDAIL-REEMRLeLMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-239 |
1.32e-56 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 186.82 E-value: 1.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF----GKTQALKP--LQIvmKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKT- 75
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDvsLTI--EKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDG-------VDLTAl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 76 SPHE-----RNIGMVFQDFALWPHMNVFENVAFGLRATKQT-NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFA 149
Cdd:COG1135 73 SERElraarRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPkAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 150 RAIVTKPHFILFDEPLSALD-----AILreemRLeLMDIVHSIGLTALYVTHDqteamsMS------DQIIVMKQGEVLQ 218
Cdd:COG1135 153 RALANNPKVLLCDEATSALDpettrSIL----DL-LKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVE 221
|
250 260
....*....|....*....|.
gi 446273968 219 KGTPEDIYVKPSHEFVAKFVG 239
Cdd:COG1135 222 QGPVLDVFANPQSELTRRFLP 242
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
18-211 |
1.38e-56 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 182.30 E-value: 1.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPD---KGEIYFGDTCMYSSAkkiktsPHERNIGMVFQDFALWPH 94
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALP------AEQRRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 95 MNVFENVAFGLRATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILRE 174
Cdd:COG4136 91 LSVGENLAFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 446273968 175 EMRLELMDIVHSIGLTALYVTHDQTEAMSMSdQIIVM 211
Cdd:COG4136 171 QFREFVFEQIRQRGIPALLVTHDEEDAPAAG-RVLDL 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
13-215 |
1.48e-56 |
|
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: 182.28 E-value: 1.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTspheRNIGMVFQD---- 88
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQNpddq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 89 -FALwphmNVFENVAFGLRATKQTN-QLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLS 166
Cdd:cd03225 88 fFGP----TVEEEVAFGLENLGLPEeEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446273968 167 ALDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGE 215
Cdd:cd03225 164 GLDPAGRREL-LELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-228 |
9.44e-56 |
|
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: 181.23 E-value: 9.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFG-KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMySSAKKIKTSPHERN 81
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDI-NKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVFQDFALWPHMNVFENVAFGLRATKQTNQL---------REKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAI 152
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSlfglfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 153 VTKPHFILFDEPLSALDAILREE-MRLeLMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVK 228
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-225 |
3.83e-54 |
|
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: 176.60 E-value: 3.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEE-----PDKGEIYFGDTCMYSSAKKIKTsp 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 78 HERNIGMVFQDFALWPhMNVFENVAFGLRA--TKQTNQLREKVEDAIKRVRLQGMEKR--YPHELSGGQQQRVAFARAIV 153
Cdd:cd03260 79 LRRRVGMVFQKPNPFP-GSIYDNVAYGLRLhgIKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446273968 154 TKPHFILFDEPLSALDAILREEMRLELMDIVHSIglTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-225 |
4.15e-54 |
|
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: 176.86 E-value: 4.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKT-SPHERN 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG-------EDITGlPPHEIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 ---IGMVFQDFALWPHMNVFENVAFGLRATKQTN-----------QLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVA 147
Cdd:cd03219 74 rlgIGRTFQIPRLFPELTVLENVMVAAQARTGSGlllararreerEARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 148 FARAIVTKPHFILFDEPLsaldAILREEMRLELMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPED 224
Cdd:cd03219 154 IARALATDPKLLLLDEPA----AGLNPEETEELAELIRELrerGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
.
gi 446273968 225 I 225
Cdd:cd03219 230 V 230
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-238 |
3.19e-53 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 175.18 E-value: 3.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEE-----PDKGEIYFGDTCMYSsaKKIKTSP 77
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYD--KKIDVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 78 HERNIGMVFQDFALWPhMNVFENVAFGLRA--TKQTNQLREKVEDAIKRVRLQGMEK----RYPHELSGGQQQRVAFARA 151
Cdd:TIGR00972 80 LRRRVGMVFQKPNPFP-MSIYDNIAYGPRLhgIKDKKELDEIVEESLKKAALWDEVKdrlhDSALGLSGGQQQRLCIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 152 IVTKPHFILFDEPLSALDAILREEMrLELMDIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSH 231
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIATGKI-EELIQELKK-KYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKE 236
|
....*..
gi 446273968 232 EFVAKFV 238
Cdd:TIGR00972 237 KRTEDYI 243
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-214 |
7.86e-52 |
|
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: 171.11 E-value: 7.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmysSAKKIKTSPHERNIgmVFQDFALWPHMNV 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL-------EGKQITEPGPDRMV--VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 98 FENVAFGL---RATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILRE 174
Cdd:TIGR01184 72 RENIALAVdrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446273968 175 EMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQG 214
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-237 |
8.87e-52 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 171.35 E-value: 8.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKkiktsPHE- 79
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQK-----PSEk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 ------RNIGMVFQDFALWPHMNVFEN-VAFGLRATKQT-NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARA 151
Cdd:COG4161 76 airllrQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSkEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 152 IVTKPHFILFDEPLSALDAilreEMRLELMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEdIYVK 228
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDP----EITAQVVEIIRELsqtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQ 230
|
....*....
gi 446273968 229 PSHEFVAKF 237
Cdd:COG4161 231 PQTEAFAHY 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-229 |
9.36e-52 |
|
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: 178.56 E-value: 9.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF--GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPD---KGEIYFGDTCMYssakkiKTSP 77
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLL------ELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 78 HER--NIGMVFQDF--ALWPhMNVFENVAFGLRATKQT-NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAI 152
Cdd:COG1123 79 ALRgrRIGMVFQDPmtQLNP-VTVGDQIAEALENLGLSrAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 153 VTKPHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKP 229
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-216 |
1.05e-51 |
|
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: 170.28 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMySSAKKIKTSPHERNIGMVFQDFALW 92
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-SDLRGRAIPYLRRKIGVVFQDFRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 93 PHMNVFENVAFGLRATKQTNQL-REKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAI 171
Cdd:cd03292 91 PDRNVYENVAFALEVTGVPPREiRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446273968 172 LREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:cd03292 171 TTWEI-MNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-230 |
2.02e-51 |
|
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: 170.07 E-value: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFG----KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMySSAKKIKTSPH 78
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDL-TLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 ERNIGMVFQDFALWPHMNVFENVAFGLRATKQT-NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPH 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPkAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 158 FILFDEPLSALDAILREEMrLELM-DIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPS 230
Cdd:cd03258 161 VLLCDEATSALDPETTQSI-LALLrDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-237 |
2.13e-51 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 170.75 E-value: 2.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GDTCMYSSAKKIKTSPHER- 80
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVgGEEIRLKPDRDGELVPADRr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 -------NIGMVFQDFALWPHMNVFENVAFG----LRATKQtnQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFA 149
Cdd:COG4598 89 qlqrirtRLGMVFQSFNLWSHMTVLENVIEApvhvLGRPKA--EAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 150 RAIVTKPHFILFDEPLSALDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKP 229
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEV-LKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
|
....*...
gi 446273968 230 SHEFVAKF 237
Cdd:COG4598 246 KSERLRQF 253
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-216 |
1.05e-50 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 166.03 E-value: 1.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKtspheRNI 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-----RRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVafglratkqtnqlrekvedaikrvrlqgmekryphELSGGQQQRVAFARAIVTKPHFILFD 162
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446273968 163 EPLSALDAILREEMRLELMDIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-221 |
1.23e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 168.27 E-value: 1.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEI-----YFgDTCMYSSAKKIKT 75
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHF-DFSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 76 SphERNIGMVFQDFALWPHMNVFENV------AFGLraTKQtnQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFA 149
Cdd:PRK11124 80 L--RRNVGMVFQQYNLWPHLTVQQNLieapcrVLGL--SKD--QALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 150 RAIVTKPHFILFDEPLSALDAilreEMRLELMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGT 221
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDP----EITAQIVSIIRELaetGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-216 |
1.99e-50 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 168.32 E-value: 1.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 5 ISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMySSAKKiktspherNIGM 84
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-AEARE--------DTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 85 VFQDFALWPHMNVFENVAFGLRAtkqtnQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEP 164
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLGLKG-----QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 165 LSALDAILREEMRlelmDIVHSI----GLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:PRK11247 161 LGALDALTRIEMQ----DLIESLwqqhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-230 |
2.93e-50 |
|
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: 167.99 E-value: 2.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF--GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFG--DTCMYSSAKKIKtsph 78
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDglDTLDEENLWEIR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 eRNIGMVFQDfalwPHmNVF------ENVAFGL--RATKqTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFAR 150
Cdd:TIGR04520 77 -KKVGMVFQN----PD-NQFvgatveDDVAFGLenLGVP-REEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 151 AIVTKPHFILFDEPLSALDAILREemrlELMDIVHSI----GLTALYVTHDQTEAMsMSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRK----EVLETIRKLnkeeGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIF 224
|
....
gi 446273968 227 VKPS 230
Cdd:TIGR04520 225 SQVE 228
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-226 |
5.59e-50 |
|
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: 166.70 E-value: 5.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGK-TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GDTCMYSSAKKIKTspHER 80
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLeGTDITKLRGKKLRK--LRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQDFALWPHMNVFENVAFGLRATKQTNQL---------REKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARA 151
Cdd:TIGR02315 80 RIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSllgrfseedKERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 152 IVTKPHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-220 |
5.69e-50 |
|
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: 165.36 E-value: 5.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 27 QGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSakkiktSPHERNIGMVFQDFALWPHMNVFENVAFGLR 106
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA------PPADRPVSMLFQENNLFAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 107 AT-KQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVH 185
Cdd:cd03298 97 PGlKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176
|
170 180 190
....*....|....*....|....*....|....*
gi 446273968 186 SIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03298 177 ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-214 |
6.02e-50 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 166.80 E-value: 6.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGdtcmyssAKKIKTSPHERni 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLD-------GKPVEGPGAER-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGLR-ATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILF 161
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGLQlAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446273968 162 DEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQG 214
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-216 |
4.79e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 163.06 E-value: 4.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSakkiktSPHE--R 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM------PPPEwrR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQDFALWPhMNVFENVAFGLRATKQTNQlREKVEDAIKRVRLQG--MEKRYpHELSGGQQQRVAFARAIVTKPHF 158
Cdd:COG4619 75 QVAYVPQEPALWG-GTVRDNLPFPFQLRERKFD-RERALELLERLGLPPdiLDKPV-ERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 159 ILFDEPLSALDAILREemRLE--LMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:COG4619 152 LLLDEPTSALDPENTR--RVEelLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-240 |
5.16e-49 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 164.15 E-value: 5.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFG----DTCMYSSAKKIKTSPH 78
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditiDTARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 ERNIGMVFQDFALWPHMNVFENVAFGLRATKqtnqlREKVEDAIKRVR-------LQGMEKRYPHELSGGQQQRVAFARA 151
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVK-----GEPKEEATARARellakvgLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 152 IVTKPHFILFDEPLSALDAilreEMRLELMDIVHSIG---LTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVK 228
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDP----ELVGEVLNTIRQLAqekRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
250
....*....|....*.
gi 446273968 229 PSHE----FVAKFVGK 240
Cdd:PRK11264 235 PQQPrtrqFLEKFLLQ 250
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-231 |
2.67e-48 |
|
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: 164.46 E-value: 2.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF----GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEP---DKGEIYFGDTCMyssakkIKT 75
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDL------LKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 76 SPHE------RNIGMVFQDF--ALWPHMNVFENVAFGLRATKQTN--QLREKVEDAIKRVRLQGMEKR---YPHELSGGQ 142
Cdd:COG0444 76 SEKElrkirgREIQMIFQDPmtSLNPVMTVGDQIAEPLRIHGGLSkaEARERAIELLERVGLPDPERRldrYPHELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 143 QQRVAFARAIVTKPHFILFDEPLSALDAILREE-MRLeLMDIVHSIGLTALYVTHDqteaMS----MSDQIIVMKQGEVL 217
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQiLNL-LKDLQRELGLAILFITHD----LGvvaeIADRVAVMYAGRIV 230
|
250
....*....|....
gi 446273968 218 QKGTPEDIYVKPSH 231
Cdd:COG0444 231 EEGPVEELFENPRH 244
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-225 |
6.35e-48 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 161.74 E-value: 6.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 4 KISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKI-KTSPHERN- 81
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG-------RDItGLPPHRIAr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMV--FQDFALWPHMNVFENVAFGL----------------RATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQ 143
Cdd:COG0411 79 LGIArtFQNPRLFPELTVLENVLVAAharlgrgllaallrlpRARREEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 144 QRVAFARAIVTKPHFILFDEPLSALDAilrEEMRlELMDIVHSI----GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQK 219
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNP---EETE-ELAELIRRLrderGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
....*.
gi 446273968 220 GTPEDI 225
Cdd:COG0411 235 GTPAEV 240
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-237 |
7.30e-48 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 165.59 E-value: 7.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 8 LEKNfGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPHERNIGMVFQ 87
Cdd:PRK10070 35 LEKT-GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 88 DFALWPHMNVFENVAFGLR-ATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLS 166
Cdd:PRK10070 114 SFALMPHMTVLDNTAFGMElAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446273968 167 ALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKF 237
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-232 |
1.02e-47 |
|
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: 167.94 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 12 FGKTQ----ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEePDKGEIYFGDTCMYS-SAKKIKtsPHERNIGMVF 86
Cdd:COG4172 292 FRRTVghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGlSRRALR--PLRRRMQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 87 QD-FA-LWPHMNVFENVAFGLRA-----TKQtnQLREKVEDAIKRVRLQ-GMEKRYPHELSGGQQQRVAFARAIVTKPHF 158
Cdd:COG4172 369 QDpFGsLSPRMTVGQIIAEGLRVhgpglSAA--ERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 159 ILFDEPLSALDAILREEMrLELM-DIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHE 232
Cdd:COG4172 447 LVLDEPTSALDVSVQAQI-LDLLrDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHP 520
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-215 |
1.17e-47 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 159.72 E-value: 1.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF-GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEI-YFGDTCMYSSAKKIktsPH-E 79
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVrIAGEDVNRLRGRQL---PLlR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 RNIGMVFQDFALWPHMNVFENVAFGLRAT-KQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHF 158
Cdd:TIGR02673 79 RRIGVVFQDFRLLPDRTVYENVALPLEVRgKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 159 ILFDEPLSALDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGE 215
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERI-LDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-238 |
2.28e-47 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 160.20 E-value: 2.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLL----RMIAglEEPD---KGEIYFGDTCMYSSakkiKT 75
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMND--LIPGarvEGEILLDGEDIYDP----DV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 76 SPHE--RNIGMVFQD---FAlwphMNVFENVAFGLRA--TKQTNQLREKVEDAIKRV--------RLqgmeKRYPHELSG 140
Cdd:COG1117 86 DVVElrRRVGMVFQKpnpFP----KSIYDNVAYGLRLhgIKSKSELDEIVEESLRKAalwdevkdRL----KKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 141 GQQQRVAFARAIVTKPHFILFDEPLSALDAI--LR-EEMRLEL---MDIVhsIgltalyVTHDQTEAMSMSDQIIVMKQG 214
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPIstAKiEELILELkkdYTIV--I------VTHNMQQAARVSDYTAFFYLG 229
|
250 260
....*....|....*....|....
gi 446273968 215 EVLQKGTPEDIYVKPSHEFVAKFV 238
Cdd:COG1117 230 ELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-209 |
2.88e-47 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 158.16 E-value: 2.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 5 ISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcMYSSAKKIKTSPHERN-IG 83
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQ-ETPPLNSKKASKFRREkLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 84 MVFQDFALWPHMNVFENVAFGLRATKQT-NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFD 162
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLSkKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446273968 163 EPLSALDailrEEMRLELMDIVHSI---GLTALYVTHDqTEAMSMSDQII 209
Cdd:TIGR03608 160 EPTGSLD----PKNRDEVLDLLLELndeGKTIIIVTHD-PEVAKQADRVI 204
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
33-231 |
2.43e-46 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 159.51 E-value: 2.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 33 LLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMySSAKKIKTSPHERNIGMVFQD-FA-LWPHMNVFENVAFGLR---- 106
Cdd:COG4608 49 LVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI-TGLSGRELRPLRRRMQMVFQDpYAsLNPRMTVGDIIAEPLRihgl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 107 ATKQtnQLREKVEDAIKRVRL-QGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALD-AI------LREEMRL 178
Cdd:COG4608 128 ASKA--ERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvSIqaqvlnLLEDLQD 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 179 ELmdivhsiGLTALYVTHDqteaMSM----SDQIIVMKQGEVLQKGTPEDIYVKPSH 231
Cdd:COG4608 206 EL-------GLTYLFISHD----LSVvrhiSDRVAVMYLGKIVEIAPRDELYARPLH 251
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-220 |
5.68e-46 |
|
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: 154.13 E-value: 5.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 4 KISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKT-SPHE--R 80
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-------KDLASlSPKElaR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQdfalwphmnvfenvafglratkqtnqlrekvedAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:cd03214 74 KIAYVPQ---------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 161 FDEPLSALDaiLReeMRLELMDIV----HSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03214 121 LDEPTSHLD--IA--HQIELLELLrrlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
28-220 |
1.38e-45 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 154.25 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 28 GEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAkkiktsPHERNIGMVFQDFALWPHMNVFENVAFGLRA 107
Cdd:TIGR01277 24 GEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA------PYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 108 TKQTNQL-REKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHS 186
Cdd:TIGR01277 98 GLKLNAEqQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 446273968 187 IGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-201 |
7.40e-45 |
|
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: 152.25 E-value: 7.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmyssAKKIKTSPHER 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE-----PIRDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQDFALWPHMNVFENVAFgLRATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:COG4133 76 RLAYLGHADGLKPELTVRENLRF-WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446273968 161 FDEPLSALD----AILREEMRLELMDivhsiGLTALYVTHDQTEA 201
Cdd:COG4133 155 LDEPFTALDaagvALLAELIAAHLAR-----GGAVLLTTHQPLEL 194
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-166 |
7.79e-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: 150.11 E-value: 7.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIktspHERNIGMVFQDFALWPHMNV 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS----LRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 98 FENVAFGLRATK-QTNQLREKVEDAIKRVRLQGMEKR----YPHELSGGQQQRVAFARAIVTKPHFILFDEPLS 166
Cdd:pfam00005 77 RENLRLGLLLKGlSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-239 |
9.70e-45 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 155.73 E-value: 9.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF----GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYS-SAKKIKTSp 77
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlSEKELRKA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 78 hERNIGMVFQDFALWPHMNVFENVAFGLR-ATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKP 156
Cdd:PRK11153 81 -RRQIGMIFQHFNLLSSRTVFDNVALPLElAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 157 HFILFDEPLSALD-----AIlreemrLELM-DIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPS 230
Cdd:PRK11153 160 KVLLCDEATSALDpattrSI------LELLkDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
....*....
gi 446273968 231 HEFVAKFVG 239
Cdd:PRK11153 234 HPLTREFIQ 242
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-225 |
1.08e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.94 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKTSPHErnI 82
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-------KPPRRARRR--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFAL-W--PhMNVFENVAFGL--------RATKQtnqLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARA 151
Cdd:COG1121 78 GYVPQRAEVdWdfP-ITVRDVVLMGRygrrglfrRPSRA---DREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 152 IVTKPHFILFDEPLSALDAilreEMRLELMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGeVLQKGTPEDI 225
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDA----ATEEALYELLRELrreGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEV 225
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
3-258 |
1.22e-44 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 153.45 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF---------GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKI 73
Cdd:COG4167 5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 74 KTspheRNIGMVFQD--FALWPHMNVFENVAFGLR-ATKQTNQLR-EKVEDAIKRVrlqGM--EKR--YPHELSGGQQQR 145
Cdd:COG4167 85 RC----KHIRMIFQDpnTSLNPRLNIGQILEEPLRlNTDLTAEEReERIFATLRLV---GLlpEHAnfYPHMLSSGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 146 VAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEV 237
|
250 260 270
....*....|....*....|....*....|...
gi 446273968 226 YVKPSHEFVAKfvgkanwLVEGKQMIRPEHVSW 258
Cdd:COG4167 238 FANPQHEVTKR-------LIESHFGEALTADAW 263
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-226 |
1.90e-44 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 155.42 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 31 TTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPHERNIGMVFQDFALWPHMNVFENVAFGLRATKQ 110
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKSMV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 111 TNQlrekveDAIkrVRLQGME---KRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSI 187
Cdd:PRK11144 107 AQF------DKI--VALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREI 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 446273968 188 GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVW 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-225 |
3.76e-44 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 151.27 E-value: 3.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 26 KQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GDTCMyssakkiKTSPHERNIGMVFQDFALWPHMNVFENVAFG 104
Cdd:PRK10771 23 ERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDHT-------TTPPSRRPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 105 LR-ATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMrLELMD- 182
Cdd:PRK10771 96 LNpGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM-LTLVSq 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446273968 183 IVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-226 |
1.09e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 151.06 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 15 TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPHeRNIGMVFQD-----F 89
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQFpehqlF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 90 ALwphmNVFENVAFGLRATKQTNQ-LREKVEDAIKRVRL-QGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSA 167
Cdd:TIGR04521 97 EE----TVYKDIAFGPKNLGLSEEeAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 168 LDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:TIGR04521 173 LDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-225 |
1.12e-43 |
|
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: 149.51 E-value: 1.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKI-KTSPHERN 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG-------RDItGLPPHERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 ---IGMVFQDFALWPHMNVFENVAFGLRAtkqtnQLREKVEDAIKRV-----RLQGMEKRYPHELSGGQQQRVAFARAIV 153
Cdd:cd03224 74 ragIGYVPEGRRIFPELTVEENLLLGAYA-----RRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 154 TKPHFILFDEPLSALDAILREemrlELMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVE----EIFEAIRELrdeGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-215 |
1.20e-43 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 147.39 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 4 KISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPHERNIG 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK----DIAKLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 84 MVFQdfalwphmnvfenvafglratkqtnqlrekvedaikrvrlqgmekrypheLSGGQQQRVAFARAIVTKPHFILFDE 163
Cdd:cd00267 77 YVPQ--------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446273968 164 PLSALDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGE 215
Cdd:cd00267 107 PTSGLDPASRERL-LELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
17-225 |
1.28e-43 |
|
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: 159.23 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIktSPHE--RNIGMVFQDFALWpH 94
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI----DLRQI--DPASlrRQIGVVLQDVFLF-S 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 95 MNVFENVAFG-LRATkqtnqlREKVEDAIKRVRL----QGMEKRYPHE-------LSGGQQQRVAFARAIVTKPHFILFD 162
Cdd:COG2274 563 GTIRENITLGdPDAT------DEEIIEAARLAGLhdfiEALPMGYDTVvgeggsnLSGGQRQRLAIARALLRNPRILILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446273968 163 EPLSALDAILREEMRLELMDIVHsiGLTALYVTHDqTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG2274 637 EATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
3-240 |
2.25e-43 |
|
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: 149.59 E-value: 2.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GDTCMYSSAKKIKTSP---- 77
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEQLYHMPGRNGPLVPadek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 78 HER----NIGMVFQDFALWPHMNVFENVAFGLRATK--QTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARA 151
Cdd:TIGR03005 81 HLRqmrnKIGMVFQSFNLFPHKTVLDNVTEAPVLVLgmARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 152 IVTKPHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSH 231
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
....*....
gi 446273968 232 EFVAKFVGK 240
Cdd:TIGR03005 241 ERTREFLSK 249
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-222 |
2.08e-42 |
|
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: 146.11 E-value: 2.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQ--ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKtspheR 80
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR-----Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQDFALWPHMNVFENVAF-----GLRATkqtnQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTK 155
Cdd:cd03263 76 SLGYCPQFDALFDELTVREHLRFyarlkGLPKS----EIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 156 PHFILFDEPLSALDAILREEMrlelMDIVHSI--GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTP 222
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAI----WDLILEVrkGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-225 |
7.96e-42 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 146.06 E-value: 7.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GDTCMYSSAKKIKTSphERN 81
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIPAMSRSRLYTV--RKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVFQDFALWPHMNVFENVAFGLRATKQTNQ--LREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFI 159
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYPLREHTQLPAplLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 160 LFDEPLSALDAILREEMrLELMD-IVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:PRK11831 166 MFDEPFVGQDPITMGVL-VKLISeLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-224 |
3.41e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 151.09 E-value: 3.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmyssakKIKTSPHE---RNIGMVFQDF 89
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV-------DIRDLTLEslrRQIGVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 90 ALWpHMNVFENVAFG-LRATkqtnqlREKVEDAIKRVRL----QGMEKRYPHE-------LSGGQQQRVAFARAIVTKPH 157
Cdd:COG1132 424 FLF-SGTIRENIRYGrPDAT------DEEVEEAAKAAQAhefiEALPDGYDTVvgergvnLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 158 FILFDEPLSALD----AILREEMRlELMDivhsiGLTALYVTHdqteamSMS-----DQIIVMKQGEVLQKGTPED 224
Cdd:COG1132 497 ILILDEATSALDteteALIQEALE-RLMK-----GRTTIVIAH------RLStirnaDRILVLDDGRIVEQGTHEE 560
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-226 |
1.97e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.85 E-value: 1.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 14 KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssakkIKTSPH-----ERNIGMVFQD 88
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---------MVLSEEtvwdvRRQVGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 89 falwPHmNVF------ENVAFGLRatkqtNQ------LREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKP 156
Cdd:PRK13635 90 ----PD-NQFvgatvqDDVAFGLE-----NIgvpreeMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 157 HFILFDEPLSALDAILREEMrlelMDIVHSI----GLTALYVTHDQTEAMSmSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREV----LETVRQLkeqkGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-225 |
7.67e-40 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 140.60 E-value: 7.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKTSPHE--- 79
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG-------LDVATTPSRela 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 RNIGMVFQDfalwPHMN----VFENVAFGL------RATKQTnqlREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFA 149
Cdd:COG4604 75 KRLAILRQE----NHINsrltVRELVAFGRfpyskgRLTAED---REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 150 RAIVTKPHFILFDEPLSALD---AilREEMRLeLMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDmkhS--VQMMKL-LRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
14-214 |
1.10e-39 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 139.08 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 14 KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFG--DTCMYSSAKKIktSPHERNIGMVFQDFAL 91
Cdd:NF038007 17 KTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAgkEVTNLSYSQKI--ILRRELIGYIFQSFNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 92 WPHMNVFENVAFGL--RATKQTNQLrEKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALD 169
Cdd:NF038007 95 IPHLSIFDNVALPLkyRGVAKKERI-ERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446273968 170 AILREEMrLELMDIVHSIGLTALYVTHDQtEAMSMSDQIIVMKQG 214
Cdd:NF038007 174 SKNARAV-LQQLKYINQKGTTIIMVTHSD-EASTYGNRIINMKDG 216
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-241 |
1.19e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 140.10 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGD---TCMYSSAKKIKTSPHE 79
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtiNLVRDKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 R------NIGMVFQDFALWPHMNVFENVafgLRATKQTNQL--REKVEDAIKRVRLQGMEKR----YPHELSGGQQQRVA 147
Cdd:PRK10619 86 QlrllrtRLTMVFQHFNLWSHMTVLENV---MEAPIQVLGLskQEARERAVKYLAKVGIDERaqgkYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 148 FARAIVTKPHFILFDEPLSALDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYV 227
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEV-LRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
250
....*....|....
gi 446273968 228 KPSHEFVAKFVGKA 241
Cdd:PRK10619 242 NPQSPRLQQFLKGS 255
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-215 |
2.34e-39 |
|
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: 136.74 E-value: 2.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPHERNIGMVFQDFALW 92
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGV----DLRDLDLESLRKNIAYVPQDPFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 93 pHMNVFENVafglratkqtnqlrekvedaikrvrlqgmekrypheLSGGQQQRVAFARAIVTKPHFILFDEPLSALDAIL 172
Cdd:cd03228 89 -SGTIRENI------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446273968 173 REEMRLELMDIvhSIGLTALYVTHDqTEAMSMSDQIIVMKQGE 215
Cdd:cd03228 132 EALILEALRAL--AKGKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-218 |
2.67e-39 |
|
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: 138.34 E-value: 2.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF----GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMyssakkikTSPH 78
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL--------FALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 E--------RNIGMVFQDFALWPHMNVFENVA-----FGLRatkqtnQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQR 145
Cdd:COG4181 81 EdararlraRHVGFVFQSFQLLPTLTALENVMlplelAGRR------DARARARALLERVGLGHRLDHYPAQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 146 VAFARAIVTKPHfILF-DEPLSALDAILREEMrLELM-DIVHSIGLTALYVTHDQTEAmSMSDQIIVMKQGEVLQ 218
Cdd:COG4181 155 VALARAFATEPA-ILFaDEPTGNLDAATGEQI-IDLLfELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-220 |
1.43e-38 |
|
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: 135.78 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGeFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmySSAKKIKTSPHERnI 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG----QDVLKQPQKLRRR-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAF-----GLRATKQtnqlREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPH 157
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYiawlkGIPSKEV----KARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 158 FILFDEPLSALDAilreEMRLELMDIVHSIGLTALYV--THDQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03264 151 ILIVDEPTAGLDP----EERIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-214 |
1.50e-38 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 136.16 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 12 FGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMySSAKKIKTSPHERNIGMVFQDFAL 91
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI-TRLKNREVPFLRRQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 92 WPHMNVFENVAFGLR-ATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDA 170
Cdd:PRK10908 91 LMDRTVYDNVAIPLIiAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446273968 171 ILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQG 214
Cdd:PRK10908 171 ALSEGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-232 |
3.49e-38 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 136.06 E-value: 3.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEE--PD---KGEIYFGDTCMYSsaKKIKTSP 77
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYS--PRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 78 HERNIGMVFQDFALWPhMNVFENVAFGLR--ATKQTNQLREKVEDAIKRVRLQGMEKRYPHE----LSGGQQQRVAFARA 151
Cdd:PRK14239 84 LRKEIGMVFQQPNPFP-MSIYENVVYGLRlkGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 152 IVTKPHFILFDEPLSALDAILR---EEMRLELMDivhsiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVK 228
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAgkiEETLLGLKD-----DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMN 237
|
....
gi 446273968 229 PSHE 232
Cdd:PRK14239 238 PKHK 241
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-224 |
4.02e-38 |
|
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: 142.20 E-value: 4.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmyssakKIKTSPHE---RNIGMVFQDf 89
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV-------DLSDLDPAswrRQIAWVPQN- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 90 ALWPHMNVFENVAFGLR-ATkqtnqlREKVEDAIKRVRLQGMEKRYPH-------E----LSGGQQQRVAFARAIVTKPH 157
Cdd:COG4988 420 PYLFAGTIRENLRLGRPdAS------DEELEAALEAAGLDEFVAALPDgldtplgEggrgLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 158 FILFDEPLSALDAilreEMRLELMDIVHSI--GLTALYVTHDqTEAMSMSDQIIVMKQGEVLQKGTPED 224
Cdd:COG4988 494 LLLLDEPTAHLDA----ETEAEILQALRRLakGRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-214 |
1.71e-37 |
|
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: 133.04 E-value: 1.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 12 FGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIY-FGdtcmyssaKKIKTSPHErnIGMVFQDF- 89
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvFG--------KPLEKERKR--IGYVPQRRs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 90 ALW--PhMNVFENVAFGLRAT-----KQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFD 162
Cdd:cd03235 79 IDRdfP-ISVRDVVLMGLYGHkglfrRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446273968 163 EPLSALDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQG 214
Cdd:cd03235 158 EPFAGVDPKTQEDI-YELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-220 |
3.93e-37 |
|
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: 132.49 E-value: 3.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGK----TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmysSAKKIKTSPH 78
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-------DGFDVVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 E--RNIGMVFQDFALWPHMNVFENVAF--GLRATKQTnQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVT 154
Cdd:cd03266 75 EarRRLGFVSDSTGLYDRLTARENLEYfaGLYGLKGD-ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 155 KPHFILFDEPLSALD----AILREEMRlELMDivhsIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03266 154 DPPVLLLDEPTTGLDvmatRALREFIR-QLRA----LGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-223 |
4.07e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 134.09 E-value: 4.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 15 TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIY-FGDTCMYSSAKKIKTspherNIGMVFQD----- 88
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvMGREVNAENEKWVRS-----KVGLVFQDpddqv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 89 FAlwphMNVFENVAFG---LRATKQtnQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:PRK13647 93 FS----STVWDDVAFGpvnMGLDKD--EVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 166 SALDAILREEMRlELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPE 223
Cdd:PRK13647 167 AYLDPRGQETLM-EILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-216 |
1.19e-36 |
|
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: 130.84 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKTSPHERNIGMVFQDfalw 92
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-------KPIKAKERRKSIGYVMQD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 93 phMN-------VFENVAFGLRATKQTNqlrEKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:cd03226 80 --VDyqlftdsVREELLLGLKELDAGN---EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446273968 166 SALDailREEMRL--ELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:cd03226 155 SGLD---YKNMERvgELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
26-230 |
1.38e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 132.93 E-value: 1.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 26 KQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GDTCMYSSAKKIKtspheRNIGMVFQDfalwPH-----MNVFE 99
Cdd:PRK13650 31 KQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVWDIR-----HKIGMVFQN----PDnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 100 NVAFGLRATKQTNQ-LREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAilreEMRL 178
Cdd:PRK13650 102 DVAFGLENKGIPHEeMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP----EGRL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 179 ELMDIVHSI----GLTALYVTHDQTEaMSMSDQIIVMKQGEVLQKGTPEDIYVKPS 230
Cdd:PRK13650 178 ELIKTIKGIrddyQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
12-231 |
1.55e-36 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 134.06 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 12 FGKTQALKPLQIV---MKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEI-YFGDTCMYSSAKKIKTSphERNIGMVFQ 87
Cdd:PRK15079 28 WQPPKTLKAVDGVtlrLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLGKDLLGMKDDEWRAV--RSDIQMIFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 88 D--FALWPHMNVFENVAFGLRA-----TKQtnQLREKVEDAIKRVRL-QGMEKRYPHELSGGQQQRVAFARAIVTKPHFI 159
Cdd:PRK15079 106 DplASLNPRMTIGEIIAEPLRTyhpklSRQ--EVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446273968 160 LFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSH 231
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLH 255
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-216 |
2.42e-36 |
|
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: 128.70 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIK-TSPHERN 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-------KEVSfASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 ---IGMVFQdfalwphmnvfenvafglratkqtnqlrekvedaikrvrlqgmekrypheLSGGQQQRVAFARAIVTKPHF 158
Cdd:cd03216 74 ragIAMVYQ--------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 159 ILFDEPLSALDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:cd03216 104 LILDEPTAALTPAEVERL-FKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-238 |
3.35e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 130.80 E-value: 3.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEE--PD---KGEIYFGDTCMYssakKIKTSP 77
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIF----KMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 78 HERNIGMVFQDFALWPHMNVFENVAFGL---RATKQTNQLREKVEDAIKRVRL-QGMEKRY---PHELSGGQQQRVAFAR 150
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALGLklnRLVKSKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 151 AIVTKPHFILFDEPLSALDAILR---EEMRLELMDivhsiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYV 227
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTakiESLFLELKK-----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
250
....*....|.
gi 446273968 228 KPSHEFVAKFV 238
Cdd:PRK14247 235 NPRHELTEKYV 245
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-229 |
3.44e-36 |
|
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: 130.36 E-value: 3.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmyssakKIKTSP-HER- 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ-------DITKLPmHKRa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 --NIGMVFQDFALWPHMNVFENVAFGLRATKQTN-QLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPH 157
Cdd:cd03218 74 rlGIGYLPQEASIFRKLTVEENILAVLEIRGLSKkEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446273968 158 FILFDEPLSALDAILREEMRlELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKP 229
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQ-KIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-224 |
9.20e-36 |
|
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: 136.05 E-value: 9.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmyssakKIKTSPHE---RNIGMVFQDF 89
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGV-------DLRDLDEDdlrRRIAVVPQRP 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 90 ALWpHMNVFENVAFGL-RATkqtnqlREKVEDAIKRVRLQGMEKRYPH-------E----LSGGQQQRVAFARAIVTKPH 157
Cdd:COG4987 419 HLF-DTTLRENLRLARpDAT------DEELWAALERVGLGDWLAALPDgldtwlgEggrrLSGGERRRLALARALLRDAP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 158 FILFDEPLSALDAILREEMRLELMDivHSIGLTALYVTHDQTEAMSMsDQIIVMKQGEVLQKGTPED 224
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLE--ALAGRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEE 555
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-216 |
1.73e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 134.38 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIK-TSPHE-- 79
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG-------EPVRfRSPRDaq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 -RNIGMVFQDFALWPHMNVFENVAFGLRATK----QTNQLREKVEDAIKRVrlqGMEKRyPH----ELSGGQQQRVAFAR 150
Cdd:COG1129 78 aAGIAIIHQELNLVPNLSVAENIFLGREPRRggliDWRAMRRRARELLARL---GLDID-PDtpvgDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 151 AIVTKPHFILFDEPLSALDAilRE-EMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:COG1129 154 ALSRDARVLILDEPTASLTE--REvERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-225 |
2.31e-35 |
|
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: 128.66 E-value: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 12 FGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKG-EIY-FGDtcmyssaKKIKTSPHE--RNIGMVFQ 87
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlFGE-------RRGGEDVWElrKRIGLVSP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 88 DFALW--PHMNVFENVAFGLRAT-----KQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:COG1119 86 ALQLRfpRDETVLDVVLSGFFDSiglyrEPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 161 FDEPLSALDAILREEMrLELMDIVHSIGLTAL-YVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG1119 166 LDEPTAGLDLGARELL-LALLDKLAAEGAPTLvLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-225 |
2.33e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 129.34 E-value: 2.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 14 KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIY-FGDTCMYSSAKKIKTspherNIGMVFQDfalw 92
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKiDGITISKENLKEIRK-----KIGIIFQN---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 93 PHmNVF------ENVAFGLRATKQT-NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:PRK13632 92 PD-NQFigatveDDIAFGLENKKVPpKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446273968 166 SALDAILREEMrLELMDIVHSIGL-TALYVTHDQTEAMsMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:PRK13632 171 SMLDPKGKREI-KKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-226 |
2.50e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 129.44 E-value: 2.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFG--DTCMYSSAKKIKtspheRNIGMVFQDfalwPH 94
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDglDTSDEENLWDIR-----NKAGMVFQN----PD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 95 MN-----VFENVAFGLRATK-QTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSAL 168
Cdd:PRK13633 96 NQivatiVEEDVAFGPENLGiPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 169 DAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSmSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-225 |
2.88e-35 |
|
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: 127.79 E-value: 2.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 4 KISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMyssakkIKTSPHERN-- 81
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI------TGLPPHRIArl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 -IGMVFQDFALWPHMNVFENVAFGLRATKQtnqlREKVEDAIKRV-----RLQGMEKRYPHELSGGQQQRVAFARAIVTK 155
Cdd:COG0410 79 gIGYVPEGRRIFPSLTVEENLLLGAYARRD----RAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446273968 156 PHFILFDEPLSALDAILREEMrlelMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEI----FEIIRRLnreGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-226 |
3.57e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 129.47 E-value: 3.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 15 TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPHERNIGMVFQdfalWPH 94
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQ----FPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 95 MNVFE-----NVAFGLRATKQTNQLREKVedAIKRVRLQGMEKRY----PHELSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:PRK13643 95 SQLFEetvlkDVAFGPQNFGIPKEKAEKI--AAEKLEMVGLADEFweksPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446273968 166 SALDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:PRK13643 173 AGLDPKARIEM-MQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-225 |
4.58e-35 |
|
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: 127.10 E-value: 4.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKtspheRNI 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVR-----RRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVA-FGLRATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILF 161
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYiHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 162 DEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
5.40e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 128.98 E-value: 5.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGLEKNFGK-----TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKT 75
Cdd:PRK13634 1 MDITFQKVEHRYQYktpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 76 SPHERNIGMVFQdfalWPHMNVFE-----NVAFGlratkQTNqLREKVEDAIKRVR----LQGMEK----RYPHELSGGQ 142
Cdd:PRK13634 81 KPLRKKVGIVFQ----FPEHQLFEetvekDICFG-----PMN-FGVSEEDAKQKARemieLVGLPEellaRSPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 143 QQRVAFARAIVTKPHFILFDEPLSALDAILREEMrlelMDIVHSI----GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQ 218
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEM----MEMFYKLhkekGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
250
....*....|.
gi 446273968 219 KGTPEDIYVKP 229
Cdd:PRK13634 227 QGTPREIFADP 237
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-226 |
6.12e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 127.89 E-value: 6.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGK-----TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKI-KTS 76
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG-------KDVtKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 77 PHER--NIGMVFQDFAL--WPHMNVFENVA--------FGLRATkQTNQLREKVEDAIKRVRLqGMEKRYPHE---LSGG 141
Cdd:COG1101 75 EYKRakYIGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRG-LTKKRRELFRELLATLGL-GLENRLDTKvglLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 142 QQQRVAFARAIVTKPHFILFDEPLSALD---AilreEMRLEL-MDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVL 217
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDpktA----ALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
250
....*....|....*..
gi 446273968 218 --------QKGTPEDIY 226
Cdd:COG1101 229 ldvsgeekKKLTVEDLL 245
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-228 |
6.63e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 128.43 E-value: 6.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 15 TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSphERNIGMVFQD-----F 89
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKL--RESVGMVFQDpdnqlF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 90 AlwphMNVFENVAFG-LRATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSAL 168
Cdd:PRK13636 97 S----ASVYQDVSFGaVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 169 DAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVK 228
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-220 |
6.75e-35 |
|
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: 126.24 E-value: 6.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAK-KIKTSPHERn 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARnRIGYLPEER- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 igmvfqdfALWPHMNVFEN-VAFG-LRATKQTnQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFI 159
Cdd:cd03269 80 --------GLYPKMKVIDQlVYLAqLKGLKKE-EARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446273968 160 LFDEPLSALDAILREEMRLELMDIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-233 |
7.82e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 132.91 E-value: 7.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 8 LEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTT----LLRMIAGleepdKGEIYFGDTCMYSSAKKiKTSPHERNIG 83
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRR-QLLPVRHRIQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 84 MVFQD--FALWPHMNVFENVAFGLRATKQT---NQLREKVEDAIKRVRLQGMEK-RYPHELSGGQQQRVAFARAIVTKPH 157
Cdd:PRK15134 366 VVFQDpnSSLNPRLNVLQIIEEGLRVHQPTlsaAQREQQVIAVMEEVGLDPETRhRYPAEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 158 FILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEF 233
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-239 |
7.92e-35 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 126.71 E-value: 7.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 21 LQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPD----KGEIYFGDTCMYSSAKKiktsphERNIGMVFQD--FALWPH 94
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSIR------GRHIATIMQNprTAFNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 95 MNVFENVAFGLRA-TKQTNQLREKVEDAIKRVRLQGME---KRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDA 170
Cdd:TIGR02770 79 FTMGNHAIETLRSlGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 171 ILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVG 239
Cdd:TIGR02770 159 VNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-226 |
1.33e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.50 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 15 TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GDTCMYSSAKKIKTsphERNIGMVFQD----- 88
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKYDKKSLLEV---RKTVGIVFQNpddql 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 89 FAlwPhmNVFENVAFG-LRATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSA 167
Cdd:PRK13639 92 FA--P--TVEEDVAFGpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 168 LDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:PRK13639 168 LDPMGASQI-MKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
27-226 |
1.62e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 127.17 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 27 QGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYS-SAKKIKtspheRNIGMVFQDfalwPHmNVF------E 99
Cdd:PRK13648 34 KGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdNFEKLR-----KHIGIVFQN----PD-NQFvgsivkY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 100 NVAFGLRA-TKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAilreEMRL 178
Cdd:PRK13648 104 DVAFGLENhAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP----DARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446273968 179 ELMDIVHSI----GLTALYVTHDQTEAMSmSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:PRK13648 180 NLLDLVRKVksehNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-223 |
2.15e-34 |
|
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: 125.81 E-value: 2.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 16 QALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmySSAKKIKTSPHERNIGMVFQDFALWpHM 95
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG----QDIREVTLDSLRRAIGVVPQDTVLF-ND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 96 NVFENVAFG-LRATKqtnqlrEKVEDAIKRVRLQGMEKRYPH-----------ELSGGQQQRVAFARAIVTKPHFILFDE 163
Cdd:cd03253 90 TIGYNIRYGrPDATD------EEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 164 PLSALDAILREEMRLELMDIvhSIGLTALYVTHDQTEAMSmSDQIIVMKQGEVLQKGTPE 223
Cdd:cd03253 164 ATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHE 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-238 |
3.84e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 125.72 E-value: 3.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPD-----KGEIYFGDTCMYSSakkiKTSP 77
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSP----DVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 78 HE--RNIGMVFQDFALWPHMNVFENVAFGLRAT---KQTNQLREKVEDAIKRVRL----QGMEKRYPHELSGGQQQRVAF 148
Cdd:PRK14267 81 IEvrREVGMVFQYPNPFPHLTIYDNVAIGVKLNglvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 149 ARAIVTKPHFILFDEPLSALDAILR---EEMRLELMDivhsiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTakiEELLFELKK-----EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
250
....*....|...
gi 446273968 226 YVKPSHEFVAKFV 238
Cdd:PRK14267 236 FENPEHELTEKYV 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-216 |
5.87e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.15 E-value: 5.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIK-TSPHE-- 79
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-------KPVRiRSPRDai 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 -RNIGMVFQDFALWPHMNVFENVAFGLRATKQ----TNQLREKVEDAIKRVrlqGME---KRYPHELSGGQQQRVAFARA 151
Cdd:COG3845 79 aLGIGMVHQHFMLVPNLTVAENIVLGLEPTKGgrldRKAARARIRELSERY---GLDvdpDAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 152 IVTKPHFILFDEPLSALDAilrEEMRlELMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:COG3845 156 LYRGARILILDEPTAVLTP---QEAD-ELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-226 |
8.59e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.55 E-value: 8.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGL-----EKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSsaKKIKT 75
Cdd:PRK13637 1 MSIKIENLthiymEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD--KKVKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 76 SPHERNIGMVFQdfalWPHMNVFE-----NVAFGLRATKQT-NQLREKVEDAIKRVRL--QGMEKRYPHELSGGQQQRVA 147
Cdd:PRK13637 79 SDIRKKVGLVFQ----YPEYQLFEetiekDIAFGPINLGLSeEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 148 FARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-225 |
2.70e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 124.45 E-value: 2.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEI-YFGDTCMYSSAKKIKTSPHERn 81
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlWDGEPLDPEDRRRIGYLPEER- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 igmvfqdfALWPHMNVFENVAF-----GLRAtkqtNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKP 156
Cdd:COG4152 81 --------GLYPKMKVGEQLVYlarlkGLSK----AEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 157 HFILFDEPLSALDAILREEMRLELMDIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-226 |
1.33e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 120.90 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTC-----MYSSAKKikt 75
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlpMHKRARL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 76 spherniGM--------VFQDfalwphMNVFENVAFGLRATKQT-NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRV 146
Cdd:COG1137 79 -------GIgylpqeasIFRK------LTVEDNILAVLELRKLSkKEREERLEELLEEFGITHLRKSKAYSLSGGERRRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 147 AFARAIVTKPHFILFDEPLSALDAILREEMRlelmDIVHS-----IG-LtalyVT-HDQTEAMSMSDQIIVMKQGEVLQK 219
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVDPIAVADIQ----KIIRHlkergIGvL----ITdHNVRETLGICDRAYIISEGKVLAE 217
|
....*..
gi 446273968 220 GTPEDIY 226
Cdd:COG1137 218 GTPEEIL 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-220 |
2.64e-32 |
|
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: 119.24 E-value: 2.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmySSAKKIKTSPHERNI 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF------DGKSYQKNIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGLRATkqtnQLREK-VEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILF 161
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLL----GIRKKrIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 162 DEPLSALDAILREEMRLELMDIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-224 |
6.12e-32 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 119.84 E-value: 6.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSsakkikTSPHE--R 80
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAA------WSPWElaR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQD----FALwphmNVFENVAFGL----RATKQTNQLrekVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAI 152
Cdd:COG4559 76 RRAVLPQHsslaFPF----TVEEVVALGRaphgSSAAQDRQI---VREALALVGLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 153 V-------TKPHFILFDEPLSALD--------AILRE--EMRLELMDIVHSIGLTALYvthdqteamsmSDQIIVMKQGE 215
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDlahqhavlRLARQlaRRGGGVVAVLHDLNLAAQY-----------ADRILLLHQGR 217
|
....*....
gi 446273968 216 VLQKGTPED 224
Cdd:COG4559 218 LVAQGTPEE 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-223 |
6.22e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 120.12 E-value: 6.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKG-----EIyFGDTCMYSS--AKKIKT 75
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiEL-LGRTVQREGrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 76 SphERNIGMVFQDFALWPHMNVFENVAFGLRATKQ---------TNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRV 146
Cdd:PRK09984 84 S--RANTGYIFQQFNLVNRLSVLENVLIGALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 147 AFARAIVTKPHFILFDEPLSALDAilrEEMRLeLMDIVHSI----GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTP 222
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDP---ESARI-VMDTLRDInqndGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
.
gi 446273968 223 E 223
Cdd:PRK09984 238 Q 238
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-238 |
8.95e-32 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 119.89 E-value: 8.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 16 QALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIY-------FGDTCmYSSAKkiktsphernIGMVFQD 88
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplhFGDYS-YRSQR----------IRMIFQD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 89 --FALWPHMNVFENVAFGLRA-TKQTNQLREK-VEDAIKRVRL-QGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDE 163
Cdd:PRK15112 96 psTSLNPRQRISQILDFPLRLnTDLEPEQREKqIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 164 PLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFV 238
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLI 250
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
15-221 |
1.07e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 118.76 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 15 TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPHERNIGMVFQDFALWPH 94
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 95 MNVFENVAFGLR-ATKQTNQLREKVEDAIKRVrlqGMEKRYPH---ELSGGQQQRVAFARAIVTKPHFILFDEPLSALDA 170
Cdd:PRK11629 102 FTALENVAMPLLiGKKKPAEINSRALEMLAAV---GLEHRANHrpsELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446273968 171 ILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQiIVMKQGEVLQKGT 221
Cdd:PRK11629 179 RNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDGRLTAELS 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-231 |
1.69e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 120.45 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 7 GLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GDTCMYSSAKKIKTSphERNIGMV 85
Cdd:PRK11308 20 GLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLKADPEAQKLL--RQKIQIV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 86 FQDfalwPH--MNVFENVAFGLRATKQTN------QLREKVEDAIKRVRLQGmE--KRYPHELSGGQQQRVAFARAIVTK 155
Cdd:PRK11308 98 FQN----PYgsLNPRKKVGQILEEPLLINtslsaaERREKALAMMAKVGLRP-EhyDRYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 156 PHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSH 231
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRH 248
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
3-225 |
1.93e-31 |
|
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: 118.15 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmyssakKIKTSP-HER- 80
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQ-------DITHLPmHERa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 --NIGMVFQDFALWPHMNVFENVAFGLRATKQT--NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKP 156
Cdd:TIGR04406 75 rlGIGYLPQEASIFRKLTVEENIMAVLEIRKDLdrAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 157 HFILFDEPLSALDAILREEMRlELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:TIGR04406 155 KFILLDEPFAGVDPIAVGDIK-KIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-230 |
2.33e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 118.94 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 15 TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFG--DTCMYSSAKKIKtspheRNIGMVFQDfalw 92
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgiDTGDFSKLQGIR-----KLVGIVFQN---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 93 PHMN-----VFENVAFGLR-ATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLS 166
Cdd:PRK13644 86 PETQfvgrtVEEDLAFGPEnLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 167 ALD-----AILREEMRLelmdivHSIGLTALYVTHDqTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPS 230
Cdd:PRK13644 166 MLDpdsgiAVLERIKKL------HEKGKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-224 |
2.94e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.95 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIK-TSPHE-- 79
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG-------RPLAdWSPAEla 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 RNIGMVFQ----DFALwphmNVFENVAFGL----RATKQTNQLrekVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARA 151
Cdd:PRK13548 76 RRRAVLPQhsslSFPF----TVEEVVAMGRaphgLSRAEDDAL---VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 152 IV------TKPHFILFDEPLSALDaiLREEmrLELMDIVHSI----GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGT 221
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALD--LAHQ--HHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
...
gi 446273968 222 PED 224
Cdd:PRK13548 225 PAE 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-238 |
3.50e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 117.96 E-value: 3.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 12 FGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLR-------MIAGLEEpdKGEIYFGDTCMYssAKKIKTSPHERNIGM 84
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLY--APDVDPVEVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 85 VFQDFALWPHmNVFENVAFGLRATKQTNQLREKVEDAIKRVRL----QGMEKRYPHELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:PRK14243 96 VFQKPNPFPK-SIYDNIAYGARINGYKGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 161 FDEPLSALDAI--LREEmrlELMdivHSIG--LTALYVTHDQTEAMSMSDQIIVM---------KQGEVLQKGTPEDIYV 227
Cdd:PRK14243 175 MDEPCSALDPIstLRIE---ELM---HELKeqYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFN 248
|
250
....*....|.
gi 446273968 228 KPSHEFVAKFV 238
Cdd:PRK14243 249 SPQQQATRDYV 259
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-218 |
5.96e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 117.48 E-value: 5.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 12 FGKTQALKPLQIV---MKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPH---ERNIGMV 85
Cdd:PRK10419 19 SGKHQHQTVLNNVslsLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE----PLAKLNRAQRkafRRDIQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 86 FQDF--ALWPHMNVFENVAFGLRatkqtNQLREKVEDAIKRVR--LQGME------KRYPHELSGGQQQRVAFARAIVTK 155
Cdd:PRK10419 95 FQDSisAVNPRKTVREIIREPLR-----HLLSLDKAERLARASemLRAVDlddsvlDKRPPQLSGGQLQRVCLARALAVE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446273968 156 PHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQ 218
Cdd:PRK10419 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-231 |
9.32e-31 |
|
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: 121.33 E-value: 9.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKT----TLLRMIAGLEEPDKGEIYFGDTCMyssakkIKTSPHE------RNI 82
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL------LGLSERElrrirgNRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQD--FALWPHMNVFENVA------FGLRATkqtnQLREKVEDAIKRVRLQGMEKR---YPHELSGGQQQRVAFARA 151
Cdd:COG4172 95 AMIFQEpmTSLNPLHTIGKQIAevlrlhRGLSGA----AARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIAMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 152 IVTKPHFILFDEPLSALDAILREEMrLELM-DIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPS 230
Cdd:COG4172 171 LANEPDLLIADEPTTALDVTVQAQI-LDLLkDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
.
gi 446273968 231 H 231
Cdd:COG4172 250 H 250
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-225 |
4.30e-30 |
|
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: 119.52 E-value: 4.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF-----GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF--GDTCMyssaKKIKT 75
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvGDEWV----DMTKP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 76 SPHERN-----IGMVFQDFALWPHMNVFENV--AFGLRATKQTNQLRekvedAIKRVRLQGMEK--------RYPHELSG 140
Cdd:TIGR03269 356 GPDGRGrakryIGILHQEYDLYPHRTVLDNLteAIGLELPDELARMK-----AVITLKMVGFDEekaeeildKYPDELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 141 GQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
....*
gi 446273968 221 TPEDI 225
Cdd:TIGR03269 511 DPEEI 515
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-220 |
5.56e-30 |
|
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: 113.03 E-value: 5.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGL--EEPDKGEIYFGDTCMYSSAKKiktspheRNIGMVFQDFA 90
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFR-------KIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 91 LWPHMNVFENVAFGlratkqtnqlrekvedaikrVRLQGmekrypheLSGGQQQRVAFARAIVTKPHFILFDEPLSALDA 170
Cdd:cd03213 93 LHPTLTVRETLMFA--------------------AKLRG--------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446273968 171 IlreeMRLELMDIVHSI---GLTALYVTHD-QTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03213 145 S----SALQVMSLLRRLadtGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-230 |
9.29e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.90 E-value: 9.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 14 KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGE--------IYFGDTCMYSSAKKIktspherniGMV 85
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVWDIREKV---------GIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 86 FQDfalwPH-----MNVFENVAFGL--RATKQtNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHF 158
Cdd:PRK13640 90 FQN----PDnqfvgATVGDDVAFGLenRAVPR-PEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446273968 159 ILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAmSMSDQIIVMKQGEVLQKGTPEDIYVKPS 230
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-228 |
1.19e-29 |
|
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: 113.09 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPHERNIGMVFQDFALW 92
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI----DIRDISRKSLRSMIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 93 PHmNVFENVAFGlratKQTNQlREKVEDAIKRVRLQGMEKRYP-----------HELSGGQQQRVAFARAIVTKPHFILF 161
Cdd:cd03254 90 SG-TIMENIRLG----RPNAT-DEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446273968 162 DEPLSALD----AILREEMRlELMDivhsiGLTALYVTHdQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVK 228
Cdd:cd03254 164 DEATSNIDteteKLIQEALE-KLMK-----GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-211 |
1.65e-29 |
|
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: 118.16 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF-GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPHERN 81
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV----PLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVFQDfalwPHM---NVFENVAFGLRATKqtnqlREKVEDAIKRVRLQGMEKRYP-----------HELSGGQQQRVA 147
Cdd:TIGR02857 398 IAWVPQH----PFLfagTIAENIRLARPDAS-----DAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 148 FARAIVTKPHFILFDEPLSALD----AILREEMRlELMDivhsiGLTALYVTHDqTEAMSMSDQIIVM 211
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDaeteAEVLEALR-ALAQ-----GRTVLLVTHR-LALAALADRIVVL 529
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-225 |
3.53e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.41 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYS-SAKKIKtsphe 79
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 RNIGMVFQDFALWPHMNVFENVAFGlRAT------KQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIV 153
Cdd:PRK11231 76 RRLALLPQHHLTPEGITVRELVAYG-RSPwlslwgRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446273968 154 TKPHFILFDEPLSALDaILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:PRK11231 155 QDTPVVLLDEPTTYLD-INHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-226 |
4.15e-29 |
|
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: 111.55 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPHERNIGMVFQDFALWpHMN 96
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGH----DVRDYTLASLRRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 97 VFENVAFGLRatkqtNQLREKVEDAIKRVRLQGMEKRYPH-----------ELSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:cd03251 92 VAENIAYGRP-----GATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 166 SALDaiLREEMRL-----ELMDivhsiGLTALYVTHDQTEAMSmSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:cd03251 167 SALD--TESERLVqaaleRLMK-----NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELL 224
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
16-224 |
9.93e-29 |
|
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: 116.59 E-value: 9.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 16 QALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GdtcmySSAKKIKTSPHERNIGMVFQDFALWPH 94
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYdG-----QDLAGLDVQAVRRQLGVVLQNGRLMSG 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 95 mNVFENVAFGLRATkqtnqlrekVEDAIKRVRLQGME---KRYP---H--------ELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:TIGR03797 542 -SIFENIAGGAPLT---------LDEAWEAARMAGLAediRAMPmgmHtvisegggTLSGGQRQRLLIARALVRKPRILL 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 161 FDEPLSALDAILREemrlelmdIVhSIGLTALYVT-----HDQTEAMSmSDQIIVMKQGEVLQKGTPED 224
Cdd:TIGR03797 612 FDEATSALDNRTQA--------IV-SESLERLKVTriviaHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-238 |
1.01e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 111.29 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEE-------PDKGEIYFGDTCMYSSAKKIKtspheRNIGMVFQDFA 90
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskikVDGKVLYFGKDIFQIDAIKLR-----KEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 91 LWPHMNVFENVAFGLRA--TKQTNQLREKVEDAIKRVRL-QGMEKRY---PHELSGGQQQRVAFARAIVTKPHFILFDEP 164
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKShgIKEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 165 LSALDAILREEMRLELMDIVHSIglTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFV 238
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-229 |
2.17e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 110.51 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPD-----KGEIYFGDTCMYSsaKKIKTSP 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYE--RRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 78 HERNIGMVFQDFALWPhMNVFENVAFGLRAT--KQTNQLREKVEDAIKRVRLQGMEKRYPH----ELSGGQQQRVAFARA 151
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwRPKLEIDDIVESALKDADLWDEIKHKIHksalDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 152 IVTKPHFILFDEPLSALDAIlrEEMRLElmDIVHSIG----LTALYVTHDQTEAMSMSDQIIVMKQ-----GEVLQKGTP 222
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPI--ASMKVE--SLIQSLRlrseLTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLT 240
|
....*..
gi 446273968 223 EDIYVKP 229
Cdd:PRK14258 241 KKIFNSP 247
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
2.25e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 111.33 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGLEKNFGKT-----QALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-------------- 61
Cdd:PRK13651 1 MQIKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 62 -----GDTCMYSSAKKIKTSPH-ERNIGMVFQdFALWphmNVFE-----NVAFGLRATKQTNQlrEKVEDAIKRVRLQGM 130
Cdd:PRK13651 81 ekvleKLVIQKTRFKKIKKIKEiRRRVGVVFQ-FAEY---QLFEqtiekDIIFGPVSMGVSKE--EAKKRAAKYIELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 131 E----KRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSD 206
Cdd:PRK13651 155 DesylQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEI-LEIFDNLNKQGKTIILVTHDLDNVLEWTK 233
|
250
....*....|....*....
gi 446273968 207 QIIVMKQGEVLQKGTPEDI 225
Cdd:PRK13651 234 RTIFFKDGKIIKDGDTYDI 252
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-201 |
3.78e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 109.10 E-value: 3.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPHERNIGMVFQDFALWPHMNV 97
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 98 FENVAfgLRATKQTNQLREKVEDAIKRVRLQGMEKRYPH---ELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILRE 174
Cdd:PRK10584 106 LENVE--LPALLRGESSRQSRNGAKALLEQLGLGKRLDHlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180
....*....|....*....|....*..
gi 446273968 175 EMRLELMDIVHSIGLTALYVTHDQTEA 201
Cdd:PRK10584 184 KIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-225 |
5.65e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 109.31 E-value: 5.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKTSPHER-- 80
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG-------QHIEGLPGHQia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMV--FQDFALWPHMNVFEN--VA----------FGLRATKQTNQL-REKVEDA---IKRVRLQGMEKRYPHELSGGQ 142
Cdd:PRK11300 79 RMGVVrtFQHVRLFREMTVIENllVAqhqqlktglfSGLLKTPAFRRAeSEALDRAatwLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 143 QQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTP 222
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
...
gi 446273968 223 EDI 225
Cdd:PRK11300 239 EEI 241
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-226 |
7.65e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 109.71 E-value: 7.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 16 QALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPH-ERNIGMVFQdfalWPH 94
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRlRKEIGLVFQ----FPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 95 MNVFE-----NVAFG---LRATKQtnQLREKVEDAIKRVRL-QGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:PRK13645 101 YQLFQetiekDIAFGpvnLGENKQ--EAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446273968 166 SALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-224 |
9.66e-28 |
|
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: 108.01 E-value: 9.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 16 QALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmySSAKKIKTSPHERNIGMVFQDFALWPhM 95
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG----VDIRDLNLRWLRSQIGLVSQEPVLFD-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 96 NVFENVAFGLRATKQtnqlrEKVEDAIKRVRL----QGMEKRY-----PH--ELSGGQQQRVAFARAIVTKPHFILFDEP 164
Cdd:cd03249 92 TIAENIRYGKPDATD-----EEVEEAAKKANIhdfiMSLPDGYdtlvgERgsQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 165 LSALDAILREEMRLELMDIvhSIGLTALYVTHDQTeAMSMSDQIIVMKQGEVLQKGTPED 224
Cdd:cd03249 167 TSALDAESEKLVQEALDRA--MKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-209 |
1.11e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.55 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 12 FGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIyfgdtcmyssakkikTSPHERNIGMVFQDFAL 91
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQRSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 92 ---WPhMNVFENVAFGLRATKQ-----TNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDE 163
Cdd:NF040873 67 pdsLP-LTVRDLVAMGRWARRGlwrrlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446273968 164 PLSALDAILREEMRlELMDIVHSIGLTALYVTHDQTEAMSMSDQII 209
Cdd:NF040873 146 PTTGLDAESRERII-ALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-229 |
1.17e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 109.12 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GDTCMYSSAKKIKtspheRNIGMVFQDfal 91
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVR-----KFVGLVFQN--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 92 wPHMNVF-----ENVAFG-LRATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:PRK13652 87 -PDDQIFsptveQDIAFGpINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 166 SALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKP 229
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-233 |
2.54e-27 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 107.61 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGD--------TCMySSAKKIK 74
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMrsgaelelYQL-SEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 75 TSPHErnIGMVFQDFALWPHMNVFE--NVAFGLRATKQTN--QLREKVEDAIKRVRL-QGMEKRYPHELSGGQQQRVAFA 149
Cdd:TIGR02323 83 LMRTE--WGFVHQNPRDGLRMRVSAgaNIGERLMAIGARHygNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 150 RAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKP 229
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
....
gi 446273968 230 SHEF 233
Cdd:TIGR02323 241 QHPY 244
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
3.01e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 110.32 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYS-SAKKIKtsphe 79
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAAS----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 RNIGMVFQDFALWPHMNVFENVAFGL-----RATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVT 154
Cdd:PRK09536 77 RRVASVPQDTSLSFEFDVRQVVEMGRtphrsRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446273968 155 KPHFILFDEPLSALDaILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:PRK09536 157 ATPVLLLDEPTASLD-INHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-225 |
3.26e-27 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 111.88 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 14 KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPHERNIGMVFQDFALWp 93
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGV----DIRQIDPADLRRNIGYVPQDPRLF- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 94 HMNVFENVAFGLRATKQTNQLRekvedAIKRVRLQGMEKRYPH-----------ELSGGQQQRVAFARAIVTKPHFILFD 162
Cdd:TIGR03375 552 YGTLRDNIALGAPYADDEEILR-----AAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLD 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 163 EPLSALDAilREEMRleLMDIVH--SIGLTALYVTHdQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:TIGR03375 627 EPTSAMDN--RSEER--FKDRLKrwLAGKTLVLVTH-RTSLLDLVDRIIVMDNGRIVADGPKDQV 686
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-238 |
3.88e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 106.46 E-value: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 4 KISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKI-KTSPHER-- 80
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDG-------EDItKLPPHERar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 -NIGMVFQDFALWPHMNVFENVAFGLRATKQTNQlreKVEDAIKRV--RLQGMEKRYPHELSGGQQQRVAFARAIVTKPH 157
Cdd:TIGR03410 75 aGIAYVPQGREIFPRLTVEENLLTGLAALPRRSR---KIPDEIYELfpVLKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 158 FILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIyvkpSHEFVAKF 237
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRY 227
|
.
gi 446273968 238 V 238
Cdd:TIGR03410 228 L 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-226 |
5.01e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.49 E-value: 5.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GDTCMYSSAKKIKtspheRNIGMVFQD-FALWPHM 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLR-----RKIGMVFQNpDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 96 NVFENVAFGLRATK-QTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILRE 174
Cdd:PRK13642 98 TVEDDVAFGMENQGiPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446273968 175 EMRLELMDIVHSIGLTALYVTHDQTEAMSmSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:PRK13642 178 EIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
28-238 |
5.70e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 111.10 E-value: 5.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 28 GEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFG----DTCmysSAKKIKtsPHERNIGMVFQD--FALWPHMNVFENV 101
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqriDTL---SPGKLQ--ALRRDIQFIFQDpyASLDPRQTVGDSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 102 AFGLRATK--QTNQLREKVEDAIKRVRLQGMEK-RYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRL 178
Cdd:PRK10261 425 MEPLRVHGllPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIIN 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 179 ELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFV 238
Cdd:PRK10261 505 LLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-226 |
6.37e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.14 E-value: 6.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPHERNIGMVFQdfalWPHMN 96
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 97 VFE-----NVAFGLRATKQTNQLREKVedAIKRVRLQGMEK----RYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSA 167
Cdd:PRK13649 98 LFEetvlkDVAFGPQNFGVSQEEAEAL--AREKLALVGISEslfeKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 168 LDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:PRK13649 176 LDPKGRKEL-MTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-220 |
2.39e-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: 103.82 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 14 KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPHERNIGMVFQDFALWp 93
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT----DIRQLDPADLRRNIGYVPQDVTLF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 94 HMNVFENVAFGLRATKQtnqlrEKVEDAIKRVRLQGMEKRYPH-----------ELSGGQQQRVAFARAIVTKPHFILFD 162
Cdd:cd03245 91 YGTLRDNITLGAPLADD-----ERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446273968 163 EPLSALDaiLREEMRLelmdiVHSI-----GLTALYVTHdQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03245 166 EPTSAMD--MNSEERL-----KERLrqllgDKTLIIITH-RPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-225 |
4.15e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 105.27 E-value: 4.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAkkiktsPHER-N 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA------RHARqR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVFQDFALWPHMNVFENVA-----FGLRATkqtnQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKP 156
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLvfgryFGLSAA----AARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 157 HFILFDEPLSALDAILREEMRLELMDIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-226 |
9.05e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 103.93 E-value: 9.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 6 SGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GDTCMYSSAKKIKTsphERNIGM 84
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqGKPLDYSKRGLLAL---RQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 85 VFQDfalwPHMNVF-----ENVAFGLRATK-QTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHF 158
Cdd:PRK13638 82 VFQD----PEQQIFytdidSDIAFSLRNLGvPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 159 ILFDEPLSALDAILREEMRLELMDIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-225 |
1.01e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 103.05 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 8 LEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKTSP-HER---NIG 83
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD-------EDISLLPlHARarrGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 84 MVFQDFALWPHMNVFENV--AFGLRATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILF 161
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLmaVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 162 DEPLSALDAILREEMRlELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:PRK10895 162 DEPFAGVDPISVIDIK-RIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-211 |
1.66e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.71 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKTSPHER---NIGMVFQDF 89
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEG-------EDISTLKPEIyrqQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 90 ALWPHmNVFENVAFGLRATKQTNQlREKVEDAIKRVRL-QGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSAL 168
Cdd:PRK10247 91 TLFGD-TVYDNLIFPWQIRNQQPD-PAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446273968 169 DailrEEMRLELMDIVHSI----GLTALYVTHDQTEaMSMSDQIIVM 211
Cdd:PRK10247 169 D----ESNKHNVNEIIHRYvreqNIAVLWVTHDKDE-INHADKVITL 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-170 |
3.01e-25 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 100.51 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPHeRNIGMVFQDFALW 92
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT----PLAEQRDEPH-ENILYLGHLPGLK 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 93 PHMNVFENVAFgLRATKQTNQLreKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDA 170
Cdd:TIGR01189 86 PELSALENLHF-WAAIHGGAQR--TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-239 |
4.25e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 102.10 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 31 TTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCM--YSSAKKIKTSPHERNIGMVFQDFALWPhMNVFENVAFGLRAT 108
Cdd:PRK14271 50 TSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggRSIFNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 109 KQT--NQLREKVEDAIKRVRL-QGMEKRY---PHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRlelmD 182
Cdd:PRK14271 129 KLVprKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE----E 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 183 IVHSIG--LTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFVAKFVG 239
Cdd:PRK14271 205 FIRSLAdrLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-225 |
1.22e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.22 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKtspheR 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR-----A 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQDFALWPHMNVFEN-VAFGLRATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFI 159
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENlLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 160 LFDEPLSALDAILR----EEMRLELmdivhSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:PRK13536 195 ILDEPTTGLDPHARhliwERLRSLL-----ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-229 |
1.46e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.67 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 14 KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYS--SAKKIKTSphERNIGMVFQdfal 91
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetGNKNLKKL--RKKVSLVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 92 WPHMNVFEN-----VAFGLRATKQTNQ-LREKVEDAIKRVRL-QGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEP 164
Cdd:PRK13641 93 FPEAQLFENtvlkdVEFGPKNFGFSEDeAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 165 LSALDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKP 229
Cdd:PRK13641 173 AAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-273 |
1.51e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 100.62 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 16 QALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPHERNIGMVFQdfalWPHM 95
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 96 NVFEN-----VAFGlraTKQTNQLREKVEDAIKRVRLQ-GMEK----RYPHELSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:PRK13646 97 QLFEDtvereIIFG---PKNFKMNLDEVKNYAHRLLMDlGFSRdvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 166 SALDAilreEMRLELMDIVHSIGL----TALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI-----YVKPSHEFVAK 236
Cdd:PRK13646 174 AGLDP----QSKRQVMRLLKSLQTdenkTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELfkdkkKLADWHIGLPE 249
|
250 260 270
....*....|....*....|....*....|....*..
gi 446273968 237 FVgKANWLVEGKQMIRPEHVSWTKNEVCEMYTgEIQH 273
Cdd:PRK13646 250 IV-QLQYDFEQKYQTKLKDIALTEEEFVSLYK-EWQH 284
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-257 |
1.90e-24 |
|
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: 103.34 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLE--EPDKGEIYF-----------------GD 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYhvalcekcgyverpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 64 TC-------------MYSSAKKIKTSPHERNIGMVFQDFALWPHMNVFENVAFGLratkqtNQLREKVEDAIKR----VR 126
Cdd:TIGR03269 81 PCpvcggtlepeevdFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEAL------EEIGYEGKEAVGRavdlIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 127 LQGMEKRYPH---ELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHdQTEAMS 203
Cdd:TIGR03269 155 MVQLSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH-WPEVIE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446273968 204 -MSDQIIVMKQGEVLQKGTPEdiyvkpshEFVAKF------VGKANWLVEGKQMIRPEHVS 257
Cdd:TIGR03269 234 dLSDKAIWLENGEIKEEGTPD--------EVVAVFmegvseVEKECEVEVGEPIIKVRNVS 286
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-237 |
1.44e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.34 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPHERNIGMVFQDFALW 92
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 93 PHMNVFENVAF-GLRATKQTNQLREKVEDAIKRVrlqGMEKR---YPHELSGGQQQRVAFARAIVTKPHFILFDEPLSAL 168
Cdd:PRK10535 99 SHLTAAQNVEVpAVYAGLERKQRLLRAQELLQRL---GLEDRveyQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 169 DAILREemrlELMDIVHSI---GLTALYVTHDQTEAmSMSDQIIVMKQGEVLQ----------KGTPEDIYVKPS--HEF 233
Cdd:PRK10535 176 DSHSGE----EVMAILHQLrdrGHTVIIVTHDPQVA-AQAERVIEIRDGEIVRnppaqekvnvAGGTEPVVNTASgwRQF 250
|
....
gi 446273968 234 VAKF 237
Cdd:PRK10535 251 VSGF 254
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
33-229 |
1.69e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.38 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 33 LLGPSGCGKTTLLRMIAGLEEPDKGEIYFGD-----------TCMYSSAKKIKTSPH-ERNIGMVFQdfalWPHMNVFE- 99
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnheLITNPYSKKIKNFKElRRRVSMVFQ----FPEYQLFKd 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 100 ----NVAFGLRATKQT-NQLREKVEDAIKRVRLQ-GMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILR 173
Cdd:PRK13631 133 tiekDIMFGPVALGVKkSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGE 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 174 EEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKP 229
Cdd:PRK13631 213 HEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
28-216 |
2.04e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 94.59 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 28 GEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPHERNIGMVFQDFALWPHmNVFENVafglra 107
Cdd:cd03246 28 GESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA----DISQWDPNELGDHVGYLPQDDELFSG-SIAENI------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 108 tkqtnqlrekvedaikrvrlqgmekrypheLSGGQQQRVAFARAIVTKPHFILFDEPLSALDaILREEMRLELMDIVHSI 187
Cdd:cd03246 97 ------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERALNQAIAALKAA 145
|
170 180
....*....|....*....|....*....
gi 446273968 188 GLTALYVTHdQTEAMSMSDQIIVMKQGEV 216
Cdd:cd03246 146 GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-233 |
2.08e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.92 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 4 KISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-----GDTCMYSSAKKIKTSPH 78
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgQLRDLYALSEAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 ERNIGMVFQDFALWPHMNVFE--NVAFGLRATKQTN--QLREKVEDAIKRVRLQgmEKR---YPHELSGGQQQRVAFARA 151
Cdd:PRK11701 88 RTEWGFVHQHPRDGLRMQVSAggNIGERLMAVGARHygDIRATAGDWLERVEID--AARiddLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 152 IVTKPHFILFDEPLSALD----AILreemrLELM-DIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIY 226
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDvsvqARL-----LDLLrGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240
|
....*..
gi 446273968 227 VKPSHEF 233
Cdd:PRK11701 241 DDPQHPY 247
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-197 |
2.17e-23 |
|
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: 100.51 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPHERNIGMVFQDfalw 92
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV----PVSSLDQDEVRRRVSVCAQD---- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 93 PHM---NVFENVAFGlratkQTNQLREKVEDAIKRVRLQGMEKRYPH-----------ELSGGQQQRVAFARAIVTKPHF 158
Cdd:TIGR02868 418 AHLfdtTVRENLRLA-----RPDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*....
gi 446273968 159 ILFDEPLSALDAILREEMrLELMDIVHSiGLTALYVTHD 197
Cdd:TIGR02868 493 LLLDEPTEHLDAETADEL-LEDLLAALS-GRTVVLITHH 529
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-225 |
2.45e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.78 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIktspHERNIGMVFQDFALWPHMNV 97
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA----FARKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 98 FENVAFG-------LRATKQTNqlREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDA 170
Cdd:PRK10575 103 RELVAIGrypwhgaLGRFGAAD--REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 171 ilreEMRLELMDIVHSI----GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:PRK10575 181 ----AHQVDVLALVHRLsqerGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-277 |
6.89e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.16 E-value: 6.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKT----TLLRMIagleEPDKGEIYFGDTCMYSSAKKI--------KTSPHER 80
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLL----EQAGGLVQCDKMLLRRRSRQVielseqsaAQMRHVR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 --NIGMVFQD--FALWPHMNVFENVAFGLRATKQTNqlREKVEDAIKR----VRL---QGMEKRYPHELSGGQQQRVAFA 149
Cdd:PRK10261 103 gaDMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGAS--REEAMVEAKRmldqVRIpeaQTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 150 RAIVTKPHFILFDEPLSALDAILREEMrLELMDIVHS-IGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVK 228
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQI-LQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446273968 229 PSHEFVAKFVGKANWLVEGKQMIRPEHVSWTKNEVCEMYTGEIQHVTYV 277
Cdd:PRK10261 260 PQHPYTRALLAAVPQLGAMKGLDYPRRFPLISLEHPAKQEPPIEQDTVV 308
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-225 |
7.01e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 95.82 E-value: 7.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 12 FGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GDTCMYSSAKKIKtspheRNIGMVFQDFA 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIQHYASKEVA-----RRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 91 LWPHMNVFENVAFGlRATKQT--NQLREKVEDAIKR-VRLQG---MEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEP 164
Cdd:PRK10253 92 TPGDITVQELVARG-RYPHQPlfTRWRKEDEEAVTKaMQATGithLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446273968 165 LSALDaILREEMRLELM-DIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:PRK10253 171 TTWLD-ISHQIDLLELLsELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-176 |
1.11e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 98.34 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF--GDTCMYSSAKkiktsphernigmvfqdfalwPHM 95
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQR---------------------PYL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 96 ---NVFENVAFGLRATKQTnqlREKVEDAIKRVRLQGM------EKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLS 166
Cdd:COG4178 438 plgTLREALLYPATAEAFS---DAELREALEAVGLGHLaerldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170
....*....|
gi 446273968 167 ALDAILREEM 176
Cdd:COG4178 515 ALDEENEAAL 524
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-170 |
1.43e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.40 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 26 KQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKTSPHERNIGMVFQDFALWPHMNVFENVAFgL 105
Cdd:PRK13539 26 AAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG-------GDIDDPDVAEACHYLGHRNAMKPALTVAENLEF-W 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 106 RATKQTNQLRekVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDA 170
Cdd:PRK13539 98 AAFLGGEELD--IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-237 |
1.96e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.03 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 11 NFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGeiyfgdtcmyssakKIKTSPHERnIGMVFQDFA 90
Cdd:PRK09544 13 SFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG--------------VIKRNGKLR-IGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 91 LWPHMNVfenvafglrATKQTNQLREKVED-----AIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:PRK09544 78 LDTTLPL---------TVNRFLRLRPGTKKedilpALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 166 SALDAilreEMRLELMDIV----HSIGLTALYVTHDQTEAMSMSDQIIVMKQgEVLQKGTPEDIYVKPshEFVAKF 237
Cdd:PRK09544 149 QGVDV----NGQVALYDLIdqlrRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHP--EFISMF 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-170 |
2.44e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 92.56 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 21 LQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKTSPHErnigmvFQDFALW-------- 92
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG-------EPIRRQRDE------YHQDLLYlghqpgik 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 93 PHMNVFENVAFGLRATKQTNqlREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDA 170
Cdd:PRK13538 87 TELTALENLRFYQRLHGPGD--DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-199 |
3.31e-22 |
|
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: 91.45 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmyssakkiktsPHERNIGMVFQDfalwPHMNv 97
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------------PEGEDLLFLPQR----PYLP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 98 fenvafglRATkqtnqLREKVedaikrvrlqgmekRYP--HELSGGQQQRVAFARAIVTKPHFILFDEPLSALDailrEE 175
Cdd:cd03223 77 --------LGT-----LREQL--------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EE 125
|
170 180
....*....|....*....|....
gi 446273968 176 MRLELMDIVHSIGLTALYVTHDQT 199
Cdd:cd03223 126 SEDRLYQLLKELGITVISVGHRPS 149
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-225 |
3.56e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 97.12 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 2 DIKISGLEKNFG-KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPHER 80
Cdd:TIGR01193 473 DIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF----SLKDIDRHTLRQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQDfalwPHM---NVFENVAFGLRATKQTNQLREKVEDAIKRVRLQGMEKRYPHEL-------SGGQQQRVAFAR 150
Cdd:TIGR01193 549 FINYLPQE----PYIfsgSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELseegssiSGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 151 AIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSiglTALYVTHDQTEAmSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-225 |
9.50e-22 |
|
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: 92.16 E-value: 9.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKkiktSPHERNIGMVFQDFALWpHMN 96
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP----AWLRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 97 VFENVAFGLRATKqtnqlREKVEDAikrVRLQG-----MEKRYPHE---------LSGGQQQRVAFARAIVTKPHFILFD 162
Cdd:cd03252 92 IRDNIALADPGMS-----MERVIEA---AKLAGahdfiSELPEGYDtivgeqgagLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 163 EPLSALDAilreEMRLELMDIVHSI--GLTALYVTHDQTEAMSmSDQIIVMKQGEVLQKGTPEDI 225
Cdd:cd03252 164 EATSALDY----ESEHAIMRNMHDIcaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
13-233 |
9.96e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 93.64 E-value: 9.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDkGEIyfGDTCMYSSAKKIKTSPHERN------IGMVF 86
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRI--GGSATFNGREILNLPEKELNklraeqISMIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 87 QD--FALWPHMNVFENVAFGLRATKQTNQlREKVEDAIKR---VRLQGMEKR---YPHELSGGQQQRVAFARAIVTKPHF 158
Cdd:PRK09473 104 QDpmTSLNPYMRVGEQLMEVLMLHKGMSK-AEAFEESVRMldaVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 159 ILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEF 233
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
28-221 |
1.15e-21 |
|
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: 95.66 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 28 GEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmyssakKIKTSPHE---RNIGMVFQDFALWphmN--VFENVA 102
Cdd:COG5265 384 GKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ-------DIRDVTQAslrAAIGIVPQDTVLF---NdtIAYNIA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 103 FG-LRATkqtnqlREKVEDAIKRVRLQGMEKRYPH-----------ELSGGQQQRVAFARAIVTKPHFILFDEPLSALD- 169
Cdd:COG5265 454 YGrPDAS------EEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDs 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446273968 170 ----AILReemrlELMDIvhSIGLTALYVTH------DqteamsmSDQIIVMKQGEVLQKGT 221
Cdd:COG5265 528 rterAIQA-----ALREV--ARGRTTLVIAHrlstivD-------ADEILVLEAGRIVERGT 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-229 |
2.79e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.40 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 16 QALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmysSAKKIKTSPH---ERNIGMVFQDFALW 92
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-------DGVPLVQYDHhylHRQVALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 93 PHmNVFENVAFGLRATKQtNQLREKVEDAIKRVRLQGMEKRYPHE-------LSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:TIGR00958 568 SG-SVRENIAYGLTDTPD-EEIMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 166 SALDAilreEMRLELMDIVHSIGLTALYVTHdQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKP 229
Cdd:TIGR00958 646 SALDA----ECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-221 |
2.81e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.71 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFG--DTCMYSSAKKIKTSpher 80
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkDITDWQTAKIMREA---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 nIGMVFQDFALWPHMNVFENVAF-GLRATKQTNQLRekvedaIKRV-----RLQGMEKRYPHELSGGQQQRVAFARAIVT 154
Cdd:PRK11614 82 -VAIVPEGRRVFSRMTVEENLAMgGFFAERDQFQER------IKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 155 KPHFILFDEPLSALDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGT 221
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQI-FDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-170 |
3.19e-21 |
|
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: 89.47 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 27 QGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIktsphERNIGMVFQDFALWPHMNVFENVAFgLR 106
Cdd:cd03231 25 AGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-----ARGLLYLGHAPGIKTTLSVLENLRF-WH 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 107 ATKQTNQlrekVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDA 170
Cdd:cd03231 99 ADHSDEQ----VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
28-225 |
3.43e-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: 94.04 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 28 GEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSakkiktSPHE--RNIGMVFQDFALWPHmNVFENVA-FG 104
Cdd:COG4618 358 GEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW------DREElgRHIGYLPQDVELFDG-TIAENIArFG 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 105 lRATkqtnqlREKVEDAIKRVRLQGMEKRYP-----------HELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILr 173
Cdd:COG4618 431 -DAD------PEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEG- 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446273968 174 EEMRLELMDIVHSIGLTALYVTHDQTeAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG4618 503 EAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-216 |
3.45e-21 |
|
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: 90.22 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 15 TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmysSAKKIKTSPHE---RNIGMVFQDFAL 91
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL-------DGKPISQYEHKylhSKVSLVGQEPVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 92 WPHmNVFENVAFGLrATKQTNQLREKVEDAIKRVRLQGMEKRYPHE-------LSGGQQQRVAFARAIVTKPHFILFDEP 164
Cdd:cd03248 100 FAR-SLQDNIAYGL-QSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446273968 165 LSALDAILREEMRLELMDIVHSigLTALYVTHdQTEAMSMSDQIIVMKQGEV 216
Cdd:cd03248 178 TSALDAESEQQVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-220 |
1.51e-20 |
|
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: 86.98 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 15 TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIktsphERNIGMVFQDfalwPH 94
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL-----SSLISVLNQR----PY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 95 M---NVFENVafGLRatkqtnqlrekvedaikrvrlqgmekrypheLSGGQQQRVAFARAIVTKPHFILFDEPLSALDAI 171
Cdd:cd03247 86 LfdtTLRNNL--GRR-------------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446273968 172 LREEMrLELMdIVHSIGLTALYVTHDQTeAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03247 133 TERQL-LSLI-FEVLKDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-215 |
1.58e-20 |
|
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: 87.91 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSakkikTSPhernigmvfqdfalWpHMN 96
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVS-----QEP--------------W-IQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 97 --VFENVAFGlratKQTNQlrEKVEDAIKRVRLQGMEKRYPH-------E----LSGGQQQRVAFARAIVTKPHFILFDE 163
Cdd:cd03250 80 gtIRENILFG----KPFDE--ERYEKVIKACALEPDLEILPDgdlteigEkginLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 164 PLSALDA-----ILREEMRLELMDivhsiGLTALYVTHdQTEAMSMSDQIIVMKQGE 215
Cdd:cd03250 154 PLSAVDAhvgrhIFENCILGLLLN-----NKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
13-225 |
1.71e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 92.03 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgDTCMYSSAKKIKTSPHernIGMVFQDFALW 92
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL-DGADLKQWDRETFGKH---IGYLPQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 93 PHmNVFENVA-FGLRATKqtnqlrEKVEDAIKRVRLQGMEKRYPH-----------ELSGGQQQRVAFARAIVTKPHFIL 160
Cdd:TIGR01842 405 PG-TVAENIArFGENADP------EKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 161 FDEPLSALDailrEEMRLELMDIVHSI---GLTALYVTHdQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:TIGR01842 478 LDEPNSNLD----EEGEQALANAIKALkarGITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-220 |
1.74e-20 |
|
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: 88.54 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKiktspHERNIGMVF-QDFALWPHM 95
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK-----FLRRIGVVFgQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 96 NVFENVAFgLRATKQTN--QLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILR 173
Cdd:cd03267 111 PVIDSFYL-LAAIYDLPpaRFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446273968 174 EEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-240 |
1.94e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.77 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTsphERNI 82
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA---QLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGLRATKQT--------NQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVT 154
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGRHLTKKVcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 155 KPHFILFDEPLSALDAILREEMRLeLMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKpshEFV 234
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFL-IMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND---DIV 238
|
....*.
gi 446273968 235 AKFVGK 240
Cdd:PRK09700 239 RLMVGR 244
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-216 |
2.21e-20 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 86.72 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKT-SPHER-NIGMVF-----QDF 89
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG-------KPVTRrSPRDAiRAGIAYvpedrKRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 90 ALWPHMNVFENVAFGLRatkqtnqlrekvedaikrvrlqgmekrypheLSGGQQQRVAFARAIVTKPHFILFDEPLSALD 169
Cdd:cd03215 88 GLVLDLSVAENIALSSL-------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 170 --------AILReEMRLElmdivhsiGLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:cd03215 137 vgakaeiyRLIR-ELADA--------GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-225 |
2.47e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.21 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 2 DIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIyfgdtcmyssakKIK---TSPH 78
Cdd:COG1134 26 ELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV------------EVNgrvSALL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 ErnIGMVFQdfalwPHMNVFENVAFGLRA----TKQTNQLREKV------EDAIKR-VrlqgmeKRYphelSGGQQQRVA 147
Cdd:COG1134 94 E--LGAGFH-----PELTGRENIYLNGRLlglsRKEIDEKFDEIvefaelGDFIDQpV------KTY----SSGMRARLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 148 FARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG1134 157 FAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-197 |
3.74e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 5 ISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIyfgdtcmySSAKKIKtsphernIGM 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLR-------IGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 85 VFQDFALWPHMNVFENVAFGLRATKQTNQLREKVEDAIK--------------------------RVR--LQGME-KRYP 135
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLDGDAELRALEAELEELEAKLAepdedlerlaelqeefealggweaeaRAEeiLSGLGfPEED 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 136 H-----ELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAilreEMRLELMDIVHSIGLTALYVTHD 197
Cdd:COG0488 146 LdrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEFLKNYPGTVLVVSHD 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-216 |
4.35e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 4.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCmyssakkiktspherNI 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV---------------KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFA-LWPHMNVFENVAFGLRATKQTnQLREKV-------EDAIKRVRlqgmekryphELSGGQQQRVAFARAIVT 154
Cdd:COG0488 381 GYFDQHQEeLDPDKTVLDELRDGAPGGTEQ-EVRGYLgrflfsgDDAFKPVG----------VLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 155 KPHFILFDEPLSALDAilreEMRLELMDivhsiGL-----TALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:COG0488 450 PPNVLLLDEPTNHLDI----ETLEALEE-----ALddfpgTVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-221 |
5.27e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.67 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 15 TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEePDKGEIyfgdtcmyssakKI-----KTSPHE---RNIGMVF 86
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSL------------KIngielRELDPEswrKHLSWVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 87 QDFALwPHMNVFENVAFGlratkQTNQLREKVEDAIKRVRLQGMEKRYPH-----------ELSGGQQQRVAFARAIVTK 155
Cdd:PRK11174 430 QNPQL-PHGTLRDNVLLG-----NPDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQP 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 156 PHFILFDEPLSALDAILREEMRLELMDIvhSIGLTALYVTH--DQTEAMsmsDQIIVMKQGEVLQKGT 221
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHqlEDLAQW---DQIWVMQDGQIVQQGD 566
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-225 |
5.74e-20 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 90.57 E-value: 5.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIyfgdtcMYSSAKKIKTSPH--ERNIGMVFQDFALWPHm 95
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQV------LVDGVDLAIADPAwlRRQMGVVLQENVLFSR- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 96 NVFENVAFGLRATKqtnqlrekVEDAIKRVRLQGMEK---RYPH-----------ELSGGQQQRVAFARAIVTKPHFILF 161
Cdd:TIGR01846 546 SIRDNIALCNPGAP--------FEHVIHAAKLAGAHDfisELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIF 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 162 DEPLSALDAilreEMRLELMDIVHSI--GLTALYVTHdQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:TIGR01846 618 DEATSALDY----ESEALIMRNMREIcrGRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
10-220 |
6.34e-20 |
|
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: 86.56 E-value: 6.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 10 KNFGKT-QALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDK---GEIYFGdtcmySSAKKIKTSPheRNIGMV 85
Cdd:cd03234 14 KNWNKYaRILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFN-----GQPRKPDQFQ--KCVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 86 FQDFALWPHMNVFENVAF----GLRATKQTNQLREKVED------AIKRVRLQGMEKrypheLSGGQQQRVAFARAIVTK 155
Cdd:cd03234 87 RQDDILLPGLTVRETLTYtailRLPRKSSDAIRKKRVEDvllrdlALTRIGGNLVKG-----ISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 156 PHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-223 |
1.04e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 89.72 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 24 VMKQGEFTTLLGPSGCGKTTLLRMIAGLEEpdKGEIYFGDTCMysSAKKIKTSPHERNIGMVFQDFALWPHMNVFENVAF 103
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRSP--KGVKGSGSVLL--NGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 104 G--LRATKQT--NQLREKVEDAIKRVRLQ-------GMEKRYpHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAIL 172
Cdd:TIGR00955 123 QahLRMPRRVtkKEKRERVDEVLQALGLRkcantriGVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFM 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446273968 173 REEMRLELMDIVHSiGLTALYVTHDQT-EAMSMSDQIIVMKQGEVLQKGTPE 223
Cdd:TIGR00955 202 AYSVVQVLKGLAQK-GKTIICTIHQPSsELFELFDKIILMAEGRVAYLGSPD 252
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
38-216 |
3.38e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.77 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 38 GCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIK-TSPHE--RN-IGMVFQD---FALWPHMNVFENVA-------- 102
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDG-------KPVRiRSPRDaiRAgIAYVPEDrkgEGLVLDLSIRENITlasldrls 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 103 -FGLRatkQTNQLREKVEDAIKRVRLqgmekRYPH------ELSGGQQQRVAFARAIVTKPHFILFDEPLSALD--Ailr 173
Cdd:COG1129 361 rGGLL---DRRRERALAEEYIKRLRI-----KTPSpeqpvgNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgA--- 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446273968 174 eemRLELMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:COG1129 430 ---KAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-215 |
5.26e-19 |
|
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: 87.57 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPD--KGEIYFGDTCMysSAKKIKTSpHER 80
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPL--KASNIRDT-ERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQDFALWPHMNVFENVAFGLRAT-----KQTNQLREKVEDAIKRVRLQGMEKRYP-HELSGGQQQRVAFARAIVT 154
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIFLGNEITlpggrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 155 KPHFILFDEPLSALDailREEMRLeLMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGE 215
Cdd:TIGR02633 159 QARLLILDEPSSSLT---EKETEI-LLDIIRDLkahGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-225 |
7.95e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.12 E-value: 7.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEePDKGEIYFGDTCMySSAkkiktSPHE--RNIGMVFQDFALWPHM 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPL-SDW-----SAAElaRHRAYLSQQQSPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 96 NVFENVAFGLRATKQTnqlrEKVEDAIKRV--RLQGMEK--RYPHELSGGQQQRVAFARAIV-----TKPH--FILFDEP 164
Cdd:COG4138 85 PVFQYLALHQPAGASS----EAVEQLLAQLaeALGLEDKlsRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 165 L--------SALDAILREemrlelmdiVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG4138 161 MnsldvaqqAALDRLLRE---------LCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-216 |
8.39e-19 |
|
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: 83.35 E-value: 8.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 1 MDIKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIyfgdtcmySSAKKIkTSPHER 80
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV--------TVRGRV-SSLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVfqdfalwPHMNVFENVAFGLRATKQTNQLREKVEDAI-----------KRVRlqgmekryphELSGGQQQRVAFA 149
Cdd:cd03220 92 GGGFN-------PELTGRENIYLNGRLLGLSRKEIDEKIDEIiefselgdfidLPVK----------TYSSGMKARLAFA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 150 RAIVTKPHFILFDEPLSALDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAAFQEKC-QRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
27-233 |
9.35e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 85.18 E-value: 9.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 27 QGEFTTLLGPSGCGKTTLLRMIAGL-EEPDKgeiYFGDTCMYSSAKKIKTSPHER------NIGMVFQD--FALWPHMNV 97
Cdd:PRK11022 32 QGEVVGIVGESGSGKSVSSLAIMGLiDYPGR---VMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPCYTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 98 FENVAFGLRaTKQTNQLREKVEDAIKRVRLQGM---EKR---YPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAI 171
Cdd:PRK11022 109 GFQIMEAIK-VHQGGNKKTRRQRAIDLLNQVGIpdpASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVT 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446273968 172 LREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEF 233
Cdd:PRK11022 188 IQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPY 249
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
18-225 |
1.53e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 83.44 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLeEPDKGEIYFGDTCM--YSSAKKiktsPHERniGMVFQDFALWPHM 95
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLeaWSAAEL----ARHR--AYLSQQQTPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 96 NVFENVAFGLRATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAI-----VTKPH--FILFDEPLS-- 166
Cdd:PRK03695 85 PVFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNsl 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 167 ------ALDAILREEMRLelmdivhsiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:PRK03695 165 dvaqqaALDRLLSELCQQ---------GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
28-233 |
5.15e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 28 GEFTTLLGPSGCGKT-TLLRMIAGLEEPD----KGEIYF-GDTCMYSSAKKIKtspHER--NIGMVFQD--FALWPHMNV 97
Cdd:PRK15134 35 GETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFhGESLLHASEQTLR---GVRgnKIAMIFQEpmVSLNPLHTL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 98 FENVA--FGLRATKQTNQLREKVEDAIKRVRLQGMEKR---YPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAIL 172
Cdd:PRK15134 112 EKQLYevLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSV 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446273968 173 REEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEF 233
Cdd:PRK15134 192 QAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPY 252
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-215 |
1.60e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.05 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 7 GLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEePD---KGEIYF-GDTCmysSAKKIKTSpHERNI 82
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFeGEEL---QASNIRDT-ERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFG---------------LRATKQTNQLREKVEDAIKrVRlqgmekryphELSGGQQQRVA 147
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGneitpggimdydamyLRAQKLLAQLKLDINPATP-VG----------NLGLGQQQLVE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446273968 148 FARAIVTKPHFILFDEPLSALDAilrEEMRLeLMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGE 215
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASLTE---SETAV-LLDIIRDLkahGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-225 |
2.29e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcMYSSAKKIKTspHERNI 82
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN-PCARLTPAKA--HQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPHMNVFENVAFGLRATKQTnqlREKVEDAIKRVRLQgmekRYPHELSG----GQQQRVAFARAIVTKPHF 158
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENILFGLPKRQAS---MQKMKQLLAALGCQ----LDLDSSAGslevADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446273968 159 ILFDEPLSALDAIlrEEMRL-----ELMDIVHSIgltaLYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:PRK15439 162 LILDEPTASLTPA--ETERLfsrirELLAQGVGI----VFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-222 |
3.10e-17 |
|
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: 82.75 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSphernIGMVFQDFALWPHMN 96
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQS-----LGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 97 VFENVAFGLRAT-KQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREE 175
Cdd:TIGR01257 1020 VAEHILFYAQLKgRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446273968 176 MRLELMDivHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTP 222
Cdd:TIGR01257 1100 IWDLLLK--YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-214 |
3.13e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 7 GLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCM-YSSAkkikTSPHERNIGMV 85
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrFAST----TAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 86 FQDFALWPHMNVFENVAFGlratkqtnQLREK-----VEDAIKRVRLQ----GMEKRyPH----ELSGGQQQRVAFARAI 152
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLG--------QLPHKggivnRRLLNYEAREQlehlGVDID-PDtplkYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 153 VTKPHFILFDEPLSALDAilREEMRleLMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQG 214
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSA--REIEQ--LFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-215 |
3.93e-17 |
|
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: 76.72 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIyfgdtcmyssakkikTSPHERNI 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------TWGSTVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQdfalwphmnvfenvafglratkqtnqlrekvedaikrvrlqgmekrypheLSGGQQQRVAFARAIVTKPHFILFD 162
Cdd:cd03221 66 GYFEQ--------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446273968 163 EPLSALDailrEEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGE 215
Cdd:cd03221 96 EPTNHLD----LESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-216 |
4.76e-17 |
|
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: 78.07 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 9 EKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPD---KGEIYFGDTcmysSAKKIKtSPHERNIGMV 85
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGI----PYKEFA-EKYPGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 86 FQDFALWPHMNVFENVAFGLRAtkQTNQLrekvedaikrVRlqgmekryphELSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:cd03233 89 SEEDVHFPTLTVRETLDFALRC--KGNEF----------VR----------GISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446273968 166 SALDAILREEMRLELMDIVHSIGLTALyVTHDQT--EAMSMSDQIIVMKQGEV 216
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVLKTTTF-VSLYQAsdEIYDLFDKVLVLYEGRQ 198
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-214 |
8.68e-17 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 77.86 E-value: 8.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNF------GKT-QALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmYSSAKKI-- 73
Cdd:COG4778 5 LEVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV-----RHDGGWVdl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 74 -KTSPHE------RNIGMVFQdF--------ALwphmnvfENVAFGLRAT-KQTNQLREKVEDAIKRVRLQgmEKR---Y 134
Cdd:COG4778 80 aQASPREilalrrRTIGYVSQ-FlrviprvsAL-------DVVAEPLLERgVDREEARARARELLARLNLP--ERLwdlP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 135 PHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILRE---EMRLELMDivhsIGLTALYVTHDqTEAMS-MSDQIIV 210
Cdd:COG4778 150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAvvvELIEEAKA----RGTAIIGIFHD-EEVREaVADRVVD 224
|
....
gi 446273968 211 MKQG 214
Cdd:COG4778 225 VTPF 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-221 |
1.19e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.39 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPHERNIGMVFQDfALW 92
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT----DIRTVTRASLRRNIAVVFQD-AGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 93 PHMNVFENVAFGlratkQTNQLREKVEDAIKRVRLQGMEKRYPH-----------ELSGGQQQRVAFARAIVTKPHFILF 161
Cdd:PRK13657 421 FNRSIEDNIRVG-----RPDATDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 162 DEPLSALDAILREEMRLELMDIVHsiGLTALYVTHdQTEAMSMSDQIIVMKQGEVLQKGT 221
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGS 552
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
13-231 |
3.77e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 78.02 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDkgEIYFGDTCMYSSAKKIKTSPHER------NIGMVF 86
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN--WHVTADRFRWNGIDLLKLSPRERrkiigrEIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 87 QD--FALWPHMNVFENVAFGLRATKQT----NQLREKVEDAIK---RVRLQGME---KRYPHELSGGQQQRVAFARAIVT 154
Cdd:COG4170 96 QEpsSCLDPSAKIGDQLIEAIPSWTFKgkwwQRFKWRKKRAIEllhRVGIKDHKdimNSYPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 155 KPHFILFDEPLSALDA-----ILReemRLELMDIVHsiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKP 229
Cdd:COG4170 176 QPRLLIADEPTNAMESttqaqIFR---LLARLNQLQ--GTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
..
gi 446273968 230 SH 231
Cdd:COG4170 251 HH 252
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
132-232 |
5.30e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.28 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 132 KRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVM 211
Cdd:PRK10418 135 KLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVM 214
|
90 100
....*....|....*....|.
gi 446273968 212 KQGEVLQKGTPEDIYVKPSHE 232
Cdd:PRK10418 215 SHGRIVEQGDVETLFNAPKHA 235
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-221 |
3.31e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.02 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 16 QALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKTSPHE---RNIGMVFQDfalw 92
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG-------QPIADYSEAalrQAISVVSQR---- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 93 PHmnVF-----ENVAFglrATKQTNQlrEKVEDAIKRVrlqGMEK----------------RyphELSGGQQQRVAFARA 151
Cdd:PRK11160 423 VH--LFsatlrDNLLL---AAPNASD--EALIEVLQQV---GLEKlleddkglnawlgeggR---QLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446273968 152 IVTKPHFILFDEPLSALDAIL-REEMRLeLMDivHSIGLTALYVTHDQTEAMSMsDQIIVMKQGEVLQKGT 221
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETeRQILEL-LAE--HAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-220 |
4.26e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.07 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 28 GEFTTLLGPSGCGKTTLLRMIAGLEEPDKgeiyFGDTCMYSSAKKikTSPHERNIGMVFQDFALWPHMNVFENVAFG--L 105
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKP--TKQILKRTGFVTQDDILYPHLTVRETLVFCslL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 106 RATKQ-TNQLREKV-EDAIKRVRLQGMEK-----RYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRL 178
Cdd:PLN03211 168 RLPKSlTKQEKILVaESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446273968 179 ELMDIVHSiGLTALYVTHD-QTEAMSMSDQIIVMKQGEVLQKG 220
Cdd:PLN03211 248 TLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-231 |
5.73e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.71 E-value: 5.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAG-LEEP--DKGEIYFGDTCMYSS----------AKKIKTSPHERNIGM 84
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaPRGARVTGDVTLNGEplaaidaprlARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 85 VF--QDFAL---WPHMNvfenvafglRATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAI------- 152
Cdd:PRK13547 97 AFsaREIVLlgrYPHAR---------RAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 153 --VTKPHFILFDEPLSALDaiLREEMRLelMDIVHSIG----LTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIy 226
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALD--LAHQHRL--LDTVRRLArdwnLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV- 242
|
....*
gi 446273968 227 VKPSH 231
Cdd:PRK13547 243 LTPAH 247
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-214 |
5.75e-15 |
|
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: 72.75 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKKIKTSPHERNIGMVFQDFALWpHMNV 97
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 98 FENVAFGLRATKQtnqlreKVEDAIKRVRLQGMEKRYPH-----------ELSGGQQQRVAFARAIVTKPHFILFDEPLS 166
Cdd:cd03290 96 EENITFGSPFNKQ------RYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446273968 167 ALDAILREEMRLE-LMDIVHSIGLTALYVTHdQTEAMSMSDQIIVMKQG 214
Cdd:cd03290 170 ALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-197 |
1.00e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.59 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCmyssakkiktspherNI 82
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQ--DfALWPHMNVFENVAFG---LRATKQTNQLRE-------KVEDAIKRVRlqgmekryphELSGGQQQRVAFAR 150
Cdd:TIGR03719 388 AYVDQsrD-ALDPNKTVWEEISGGldiIKLGKREIPSRAyvgrfnfKGSDQQKKVG----------QLSGGERNRVHLAK 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446273968 151 AIVTKPHFILFDEPLSALDAilrEEMR-LElmDIVHSIGLTALYVTHD 197
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDV---ETLRaLE--EALLNFAGCAVVISHD 499
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-215 |
3.10e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEI-YFGDTCMYSSAKkiktSPHERN 81
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlYLGKEVTFNGPK----SSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVFQDFALWPHMNVFENVAFGLRATK-----QTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKP 156
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGREFVNrfgriDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 157 HFILFDEPLSAL-----DAILR--EEMRLELMDIVhsigltalYVTHDQTEAMSMSDQIIVMKQGE 215
Cdd:PRK10762 161 KVIIMDEPTDALtdtetESLFRviRELKSQGRGIV--------YISHRLKEIFEICDDVTVFRDGQ 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-198 |
3.54e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 7 GLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEE--PDKGEIyfgdtcmyssakkiktsphernigm 84
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCV------------------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 85 VFQDFALWPHMNVFENVAfglratkqtnqLREKVEDAIKRVRLQGME-----KRYPHELSGGQQQRVAFARAIVTKPHFI 159
Cdd:COG2401 90 DVPDNQFGREASLIDAIG-----------RKGDFKDAVELLNAVGLSdavlwLRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 446273968 160 LFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQ 198
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-210 |
4.28e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 70.90 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 26 KQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEI-YFGDTCMYSSAK-KIKTSPHERNIGM-VFQDFALWPHMNVfenva 102
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIeIELDTVSYKPQYiKADYEGTVRDLLSsITKDFYTHPYFKT----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 103 fglratkqtnqlrekveDAIKRVRLQGMEKRYPHELSGGQQQRVAFArAIVTKPHFI-LFDEPLSALDAilreEMRLELM 181
Cdd:cd03237 98 -----------------EIAKPLQIEQILDREVPELSGGELQRVAIA-ACLSKDADIyLLDEPSAYLDV----EQRLMAS 155
|
170 180 190
....*....|....*....|....*....|...
gi 446273968 182 DIVHSIGL----TALYVTHDQTEAMSMSDQIIV 210
Cdd:cd03237 156 KVIRRFAEnnekTAFVVEHDIIMIDYLADRLIV 188
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
17-218 |
4.61e-14 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 72.68 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKkiktSPHERNIGMVFQDFALWphmN 96
Cdd:TIGR01194 357 ALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSR----DDYRDLFSAIFADFHLF---D 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 97 VFENVAFGLRA-TKQTNQLREKVEDAIKrVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREE 175
Cdd:TIGR01194 430 DLIGPDEGEHAsLDNAQQYLQRLEIADK-VKIEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKRF 508
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446273968 176 MRLELMDIVHSIGLTALYVTHDQtEAMSMSDQIIVMKQGEVLQ 218
Cdd:TIGR01194 509 FYEELLPDLKRQGKTIIIISHDD-QYFELADQIIKLAAGCIVK 550
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-226 |
9.15e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.30 E-value: 9.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKK--IKTSPHERNIGMVF----QDFA 90
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKnlVAYVPQSEEVDWSFpvlvEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 91 LwphMNVFENVAFGLRATKQTnqlREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDa 170
Cdd:PRK15056 102 M---MGRYGHMGWLRRAKKRD---RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 171 iLREEMRL-ELMDIVHSIGLTALYVTHDQTEAMSMSDqIIVMKQGEVLQKGTPEDIY 226
Cdd:PRK15056 175 -VKTEARIiSLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTF 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-216 |
1.78e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 4 KISGLE-KNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMyssakkIKTSPHE-RN 81
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI------TGLSPRErRR 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVF-----QDFALWPHMNVFENVAFGLRATKQ--------TNQLREKVEDAIKR--VRLQGmekryPHE----LSGGQ 142
Cdd:COG3845 333 LGVAYipedrLGRGLVPDMSVAENLILGRYRRPPfsrggfldRKAIRAFAEELIEEfdVRTPG-----PDTparsLSGGN 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 143 QQRVAFARAIVTKPHFILFDEPLSALD--AIlrEEMRLELMDIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDvgAI--EFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-169 |
1.88e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.34 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmysSAKKIKTSPHERNIGMVFQDFALWPHMNV 97
Cdd:PRK13543 27 FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-------DGKTATRGDRSRFMAYLGHLPGLKADLST 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 98 FENVAF--GL--RATKQTNQlrekveDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALD 169
Cdd:PRK13543 100 LENLHFlcGLhgRRAKQMPG------SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-224 |
5.12e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.19 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYfgdtcmyssakkiktspHERNIGMVFQDfalwphmnv 97
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------------AERSIAYVPQQ--------- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 98 fenvAFGLRATKQTNQL------REKVEDAIKRVRLQ--------GMEKRYPHE---LSGGQQQRVAFARAIVTKPHFIL 160
Cdd:PTZ00243 730 ----AWIMNATVRGNILffdeedAARLADAVRVSQLEadlaqlggGLETEIGEKgvnLSGGQKARVSLARAVYANRDVYL 805
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446273968 161 FDEPLSALDAILREEMRLELMdIVHSIGLTALYVTHdQTEAMSMSDQIIVMKQGEVLQKGTPED 224
Cdd:PTZ00243 806 LDDPLSALDAHVGERVVEECF-LGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSAD 867
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-229 |
6.17e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.36 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYssakKIKTSPHERNIGMVFQDFALWPHmN 96
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT----KLQLDSWRSRLAVVSQTPFLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 97 VFENVAFGL-RATKQtnQLRE-----KVEDAIKRVRlQGMEKRYPHE---LSGGQQQRVAFARAIVTKPHFILFDEPLSA 167
Cdd:PRK10789 405 VANNIALGRpDATQQ--EIEHvarlaSVHDDILRLP-QGYDTEVGERgvmLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 168 LDAilREEMRlelmdIVHSI-----GLTALYVTHdQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKP 229
Cdd:PRK10789 482 VDG--RTEHQ-----ILHNLrqwgeGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-223 |
1.02e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 66.63 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 4 KISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLE--EPDKGEIYFGD---TCMyssakkiktSPH 78
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGediLEL---------SPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 ER---NIGMVFQDFALWPHMNVFEnvaFgLRATKQTN--------QLREKVEDAIKRVRL-QGMEKRYPHE-LSGGQQQR 145
Cdd:COG0396 73 ERaraGIFLAFQYPVEIPGVSVSN---F-LRTALNARrgeelsarEFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 146 VAFARAIVTKPHFILFDEPLSALDA----ILRE---EMRLElmdivhsiGLTALYVTH-----DQTEAmsmsDQIIVMKQ 213
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDIdalrIVAEgvnKLRSP--------DRGILIITHyqrilDYIKP----DFVHVLVD 216
|
250
....*....|
gi 446273968 214 GEVLQKGTPE 223
Cdd:COG0396 217 GRIVKSGGKE 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
13-233 |
1.25e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.52 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEpDKGEIYfGDTCMYSSAKKIKTSPHER------NIGMVF 86
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVT-ADRMRFDDIDLLRLSPRERrklvghNVSMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 87 QD--FALWPHMNVFENV-------AFGLRATKQTNQLREKVEDAIKRVRLQ---GMEKRYPHELSGGQQQRVAFARAIVT 154
Cdd:PRK15093 96 QEpqSCLDPSERVGRQLmqnipgwTYKGRWWQRFGWRKRRAIELLHRVGIKdhkDAMRSFPYELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 155 KPHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEF 233
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPY 254
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-197 |
1.50e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 68.04 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 33 LLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmyssAKKIKtsphernIGMVFQDFALWPHMNVFENVAFGLRATKQT- 111
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARP--------QPGIK-------VGYLPQEPQLDPTKTVRENVEEGVAEIKDAl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 112 -----------------NQLRE---KVEDAIKRVRLQGMEK---------RYP------HELSGGQQQRVAFARAIVTKP 156
Cdd:TIGR03719 101 drfneisakyaepdadfDKLAAeqaELQEIIDAADAWDLDSqleiamdalRCPpwdadvTKLSGGERRRVALCRLLLSKP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446273968 157 HFILFDEPLSALDAilreEMRLELMDIVHSIGLTALYVTHD 197
Cdd:TIGR03719 181 DMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHD 217
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-169 |
1.71e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.36 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 25 MKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmYSSAKKIKTSPHERNIGMVFQDFALWPHMNVFENVAFG 104
Cdd:PRK13540 24 LPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILF-----ERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYD 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 105 LRATKQTNQLREKVedaikRVRLQGMEKRYP-HELSGGQQQRVAFARAIVTKPHFILFDEPLSALD 169
Cdd:PRK13540 99 IHFSPGAVGITELC-----RLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
17-215 |
2.11e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.69 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcMYSSAKKIktSPHERNIGMVFQDFALWPHM- 95
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG--KPVTAEQP--EDYRKLFSAVFTDFHLFDQLl 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 96 --NVFENVAFGLRATKQTNQLREKVEDAIKRVRLQgmekryphELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILR 173
Cdd:PRK10522 414 gpEGKPANPALVEKWLERLKMAHKLELEDGRISNL--------KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446273968 174 EEMRLELMDIVHSIGLTALYVTHDQtEAMSMSDQIIVMKQGE 215
Cdd:PRK10522 486 REFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQ 526
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-222 |
2.81e-12 |
|
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: 65.21 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTT----LLRMIagleEPDKGEIYFGDtcmyssaKKIKTSPHE---RNIGMVFQDf 89
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDG-------VDISKIGLHdlrSRISIIPQD- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 90 alwPHM---NVFENVAFGLRATKqtnqlrEKVEDAIKRVRL----QGMEKRYPHE-------LSGGQQQRVAFARAIVTK 155
Cdd:cd03244 87 ---PVLfsgTIRSNLDPFGEYSD------EELWQALERVGLkefvESLPGGLDTVveeggenLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 156 PHFILFDEPLSALD--------AILREEMRlelmdivhsiGLTALYVTHdQTEAMSMSDQIIVMKQGEVLQKGTP 222
Cdd:cd03244 158 SKILVLDEATASVDpetdaliqKTIREAFK----------DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-225 |
3.26e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.46 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 26 KQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIY-FG---DtcmyssAKKIKTsphERNIGMVFQDFALWPHMNVFENV 101
Cdd:NF033858 290 RRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlFGqpvD------AGDIAT---RRRVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 102 A-----FGLRAtkqtNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEM 176
Cdd:NF033858 361 ElharlFHLPA----AEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMF 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446273968 177 -RLeLMDIVHSIGLTALYVTHDQTEAMSmSDQIIVMKQGEVLQKGTPEDI 225
Cdd:NF033858 437 wRL-LIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
21-169 |
3.45e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 64.51 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 21 LQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYSSAKkiktsPHERNIGmvfQDFALWPHMNVFEN 100
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK-----PYCTYIG---HNLGLKLEMTVFEN 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 101 VAFGLRATKQTnqlrEKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALD 169
Cdd:PRK13541 91 LKFWSEIYNSA----ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-215 |
4.71e-12 |
|
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: 62.78 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 27 QGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmyssakkiktsphernigmvfqdfalwphmnvfenvafglr 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 107 atkqtnqlrEKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDA-----ILREEMRLELM 181
Cdd:smart00382 39 ---------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRLLL 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 446273968 182 DIVHSIGLTALYVTHDQTEAMSM-----SDQIIVMKQGE 215
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPAllrrrFDRRIVLLLIL 148
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-216 |
5.68e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 25 MKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmysSAKKIKT-SPHE--RNiGMVF--QDF---ALWPHMN 96
Cdd:PRK10762 275 LRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTL-------DGHEVVTrSPQDglAN-GIVYisEDRkrdGLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 97 VFENVAF-GLRA-TKQTNQLREK-----VEDAIK--RVRLQGMEKRYpHELSGGQQQRVAFARAIVTKPHFILFDEPLSA 167
Cdd:PRK10762 347 VKENMSLtALRYfSRAGGSLKHAdeqqaVSDFIRlfNIKTPSMEQAI-GLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446273968 168 LDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:PRK10762 426 VDVGAKKEI-YQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-211 |
6.27e-12 |
|
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: 64.70 E-value: 6.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 24 VMKQGEFTTLLGPSGCGKTTLLRMIAGL---------EEPDKGEI--YFGDTCMYSSAKKIKtsphERNIGMVF--QDFA 90
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKlkpnlgkfdDPPDWDEIldEFRGSELQNYFTKLL----EGDVKVIVkpQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 91 LWPhmNVFE-NVAFGLRATKQTNQLrekvEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALD 169
Cdd:cd03236 98 LIP--KAVKgKVGELLKKKDERGKL----DELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446273968 170 AilreEMRLELMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVM 211
Cdd:cd03236 172 I----KQRLNAARLIRELaedDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-210 |
8.71e-12 |
|
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: 65.96 E-value: 8.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 25 MKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIyfgdtcmySSAKKIKTSPHErnigmVFQDFalwpHMNVFENVAFG 104
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLKISYKPQY-----ISPDY----DGTVEEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 105 LRATKQTNQLREKVedaIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAilreEMRLELMDIV 184
Cdd:COG1245 426 NTDDFGSSYYKTEI---IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV----EQRLAVAKAI 498
|
170 180 190
....*....|....*....|....*....|....
gi 446273968 185 HSI----GLTALYVTHDqteaMSM----SDQIIV 210
Cdd:COG1245 499 RRFaenrGKTAMVVDHD----IYLidyiSDRLMV 528
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-221 |
9.49e-12 |
|
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: 66.12 E-value: 9.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRmiAGLEEPDKGEiyfGDTCMYSSAKKIktsPHERNIgmvfQDFALWphmnv 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLS--ALLAEMDKVE---GHVHMKGSVAYV---PQQAWI----QNDSLR----- 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 98 fENVAFG-------LRATKQTNQLREKVEDAIKRVRLQGMEKRYphELSGGQQQRVAFARAIVTKPHFILFDEPLSALDA 170
Cdd:TIGR00957 717 -ENILFGkalnekyYQQVLEACALLPDLEILPSGDRTEIGEKGV--NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 171 ILREEMrleLMDIVHSIGL----TALYVTHDQTeAMSMSDQIIVMKQGEVLQKGT 221
Cdd:TIGR00957 794 HVGKHI---FEHVIGPEGVlknkTRILVTHGIS-YLPQVDVIIVMSGGKISEMGS 844
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-210 |
1.09e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 26 KQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMYssakK---IKTSPHERnigmvfqdfalwphmnvfenVA 102
Cdd:PRK13409 363 YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISY----KpqyIKPDYDGT--------------------VE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 103 FGLRATKQ---TNQLREKVedaIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAilreEMRLE 179
Cdd:PRK13409 419 DLLRSITDdlgSSYYKSEI---IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV----EQRLA 491
|
170 180 190
....*....|....*....|....*....|....*
gi 446273968 180 LMDIVHSI----GLTALYVTHDQTEAMSMSDQIIV 210
Cdd:PRK13409 492 VAKAIRRIaeerEATALVVDHDIYMIDYISDRLMV 526
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-223 |
2.62e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.77 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLE--EPDKGEIYFGDtcmyssaKKIKT-SPHE 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKG-------EDITDlPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 R---NIGMVFQDFALWPhmnvfenvafGLratkqtnqlreKVEDAIkrvrlqgmekRYPHE-LSGGQQQRVAFARAIVTK 155
Cdd:cd03217 74 RarlGIFLAFQYPPEIP----------GV-----------KNADFL----------RYVNEgFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 156 PHFILFDEPLSALDAilrEEMRL--ELMDIVHSIGLTALYVTH-----DQTEAmsmsDQIIVMKQGEVLQKGTPE 223
Cdd:cd03217 123 PDLAILDEPDSGLDI---DALRLvaEVINKLREEGKSVLIITHyqrllDYIKP----DRVHVLYDGRIVKSGDKE 190
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-225 |
3.03e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.18 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 26 KQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcMYSSAKKIKtspHERNIGMVF-QDFALWPHMNVFENvaFG 104
Cdd:COG4586 46 EPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVPFKRRKE---FARRIGVVFgQRSQLWWDLPAIDS--FR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 105 L----------RATKQTNQLRE--KVEDAIKR-VRlqgmekryphELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAI 171
Cdd:COG4586 119 LlkaiyripdaEYKKRLDELVEllDLGELLDTpVR----------QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVV 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446273968 172 LREEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDI 225
Cdd:COG4586 189 SKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL 242
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-170 |
3.99e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 2 DIKISGleknfGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAglEEPDKGEIYFGDtcMYSSAKKIKTSpHERN 81
Cdd:TIGR00956 768 EVKIKK-----EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGD--RLVNGRPLDSS-FQRS 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 82 IGMVFQDFALWPHMNVFENVAFG--LRATKQTNqLREKVEDAIKRVRLQGMEKrY-------PHE-LSGGQQQRVAFARA 151
Cdd:TIGR00956 838 IGYVQQQDLHLPTSTVRESLRFSayLRQPKSVS-KSEKMEYVEEVIKLLEMES-YadavvgvPGEgLNVEQRKRLTIGVE 915
|
170 180
....*....|....*....|
gi 446273968 152 IVTKPHFILF-DEPLSALDA 170
Cdd:TIGR00956 916 LVAKPKLLLFlDEPTSGLDS 935
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-211 |
4.69e-11 |
|
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: 63.65 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 26 KQGEFTTLLGPSGCGKTTLLRMIAGL---------EEPDKGEI--YFGDTCMYS-----SAKKIKTSpHE----RNIGMV 85
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGElkpnlgdydEEPSWDEVlkRFRGTELQDyfkklANGEIKVA-HKpqyvDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 86 FQDfalwphmNVFEnvafglrATKQTNQlREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:COG1245 176 FKG-------TVRE-------LLEKVDE-RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446273968 166 SALDaiLREEMRL-----ELMDIVHSIgltaLYVTHDQTEAMSMSDQIIVM 211
Cdd:COG1245 241 SYLD--IYQRLNVarlirELAEEGKYV----LVVEHDLAILDYLADYVHIL 285
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-169 |
5.90e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 19 KPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmySSAKKIKTSPHERNIGMVFQDFALWPHmNVF 98
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS---HNLKDINLKWWRSKIGVVSQDPLLFSN-SIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 99 ENVAFGLRATKQ----TNQLRE------------------------------------------------KVEDAIKRVR 126
Cdd:PTZ00265 478 NNIKYSLYSLKDlealSNYYNEdgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVL 557
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446273968 127 LQGMEKRYP-----------HELSGGQQQRVAFARAIVTKPHFILFDEPLSALD 169
Cdd:PTZ00265 558 IHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-228 |
5.92e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.83 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCG--KTTLLRMIAGleePDKGE--IYFGDTCMYSSAKKIKTSPH 78
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRrpWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 ERNIGMVFQDFAlwPHMNVFenvAFGLRATKQTNQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHF 158
Cdd:NF000106 91 RPVR*GRRESFS--GRENLY---MIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 159 ILFDEPLSALDAILREEMRLELMDIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVK 228
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
80-225 |
6.17e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 6.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 RNI-GMVFQDFALWpHMNVFENVAFGlratkQTNQLREKVEDAIKRVRLQGMEKRYPHE-----------LSGGQQQRVA 147
Cdd:PTZ00265 1295 RNLfSIVSQEPMLF-NMSIYENIKFG-----KEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIA 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 148 FARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSIGLTALYVTHdQTEAMSMSDQIIVM----KQGEVLQ-KGTP 222
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFnnpdRTGSFVQaHGTH 1447
|
...
gi 446273968 223 EDI 225
Cdd:PTZ00265 1448 EEL 1450
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
138-225 |
6.47e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.60 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 138 LSGGQQQRVAFARAIVTKPHFILFDEPLSALDA---------ILREEMRlelmdivhsiGLTALYVThDQTEAMSMSDQI 208
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhvgrqvfdkCIKDELR----------GKTRVLVT-NQLHFLSQVDRI 809
|
90
....*....|....*..
gi 446273968 209 IVMKQGEVLQKGTPEDI 225
Cdd:PLN03130 810 ILVHEGMIKEEGTYEEL 826
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-224 |
7.49e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.99 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 5 ISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCmyssakkiktspherNIGM 84
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA---------------NIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 85 VFQD----FAlwPHMNVFENVAfGLRATKQTNQLREKV--------EDAIKRVRLqgmekrypheLSGGQQQRVAFARAI 152
Cdd:PRK15064 387 YAQDhaydFE--NDLTLFDWMS-QWRQEGDDEQAVRGTlgrllfsqDDIKKSVKV----------LSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 153 VTKPHFILFDEPLSALD--AILREEMRLELMDivhsiGlTALYVTHDQTEAMSMSDQIIVMKQGEVLQ-KGTPED 224
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDmeSIESLNMALEKYE-----G-TLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEE 522
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-211 |
1.15e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 23 IVMKQGEFTTLLGPSGCGKTTLLRMIAGL---------EEPDKGEI--YFGDTCMYS-----SAKKIKTSpheRNIGMVf 86
Cdd:PRK13409 94 PIPKEGKVTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSWDEVlkRFRGTELQNyfkklYNGEIKVV---HKPQYV- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 87 qDFAlwPhmNVFE-NVAFGLRATKQtnqlREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:PRK13409 170 -DLI--P--KVFKgKVRELLKKVDE----RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446273968 166 SALDaiLREemRLELMDIVHSI--GLTALYVTHDQTEAMSMSDQIIVM 211
Cdd:PRK13409 241 SYLD--IRQ--RLNVARLIRELaeGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-215 |
1.34e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 5 ISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF-GDTCMYSSAKKiktsPHERNIG 83
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqGKEIDFKSSKE----ALENGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 84 MVFQDFALWPHMNVFENVAFGLRATKQTNQLREKVEDAIKRVRLQGMEKRYPHE----LSGGQQQRVAFARAIVTKPHFI 159
Cdd:PRK10982 77 MVHQELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 160 LFDEPLSALDailrEEMRLELMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGE 215
Cdd:PRK10982 157 IMDEPTSSLT----EKEVNHLFTIIRKLkerGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
30-221 |
1.54e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.04 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 30 FTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDtcmyssaKKIKTSPHE---RNIGMVFQDFALWPHmNVFENVAFGLR 106
Cdd:PRK10790 369 FVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG-------RPLSSLSHSvlrQGVAMVQQDPVVLAD-TFLANVTLGRD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 107 ATKqtnqlrEKVEDAIKRVRLQGMEKRYP-----------HELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREE 175
Cdd:PRK10790 441 ISE------EQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446273968 176 MRLELMDIVHSiglTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGT 221
Cdd:PRK10790 515 IQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-222 |
1.89e-10 |
|
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: 59.73 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 2 DIKISGLEKNFGK--TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPHE 79
Cdd:cd03369 6 EIEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI----DISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 RNIGMVFQDFALwphmnvfenvafgLRATKQTN------QLREKVEDAIkRVRLQGMEkrypheLSGGQQQRVAFARAIV 153
Cdd:cd03369 82 SSLTIIPQDPTL-------------FSGTIRSNldpfdeYSDEEIYGAL-RVSEGGLN------LSQGQRQLLCLARALL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 154 TKPHFILFDEPLSAL----DAILREEMRLELMD-----IVHSIGLTALYvthdqteamsmsDQIIVMKQGEVLQKGTP 222
Cdd:cd03369 142 KRPRVLVLDEATASIdyatDALIQKTIREEFTNstiltIAHRLRTIIDY------------DKILVMDAGEVKEYDHP 207
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-239 |
5.38e-10 |
|
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: 59.49 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGeiyfgdtcmyssakKIKtspHERNIGMVFQDFALWPHmNV 97
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG--------------KIK---HSGRISFSSQFSWIMPG-TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 98 FENVAFGLratkQTNQLREKveDAIKRVRLQGMEKRYPHE-----------LSGGQQQRVAFARAIVTKPHFILFDEPLS 166
Cdd:cd03291 115 KENIIFGV----SYDEYRYK--SVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 167 ALDAILREEM----RLELMdivhsIGLTALYVThDQTEAMSMSDQIIVMKQGEVLQKGT-PEDIYVKPshEFVAKFVG 239
Cdd:cd03291 189 YLDVFTEKEIfescVCKLM-----ANKTRILVT-SKMEHLKKADKILILHEGSSYFYGTfSELQSLRP--DFSSKLMG 258
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-216 |
6.28e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.26 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 33 LLGPSGCGKTTLLRMIAGLEEPDKGEIYfgdtcmySSAK-KIKTSPHERNIGMVFQDFALWPHMNVFENV---------- 101
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVF-------RSAKvRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVpeqklrahlg 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 102 AFGLRATkqtnqlrekvedaikrVRLQGMekrypHELSGGQQQRVAFARAIVTKPHFILFDEPLSALDailreemrlelM 181
Cdd:PLN03073 613 SFGVTGN----------------LALQPM-----YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD-----------L 660
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446273968 182 DIVHSI--GLT-----ALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:PLN03073 661 DAVEALiqGLVlfqggVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-218 |
8.49e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 8.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 25 MKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmysSAKKIK-TSPHER-NIGMVF-----QDFALWPHMNV 97
Cdd:PRK09700 286 VCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL-------NGKDISpRSPLDAvKKGMAYitesrRDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 98 FENVA-------------FGLRATKQTNQLREKVEDAIKrVRLQGMEKRYpHELSGGQQQRVAFARAIVTKPHFILFDEP 164
Cdd:PRK09700 359 AQNMAisrslkdggykgaMGLFHEVDEQRTAENQRELLA-LKCHSVNQNI-TELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446273968 165 LSALDAILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQ 218
Cdd:PRK09700 437 TRGIDVGAKAEI-YKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-172 |
1.21e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 35 GPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmyssakkIKtsphernIGMVFQ--DfALWPHMNVFENVAFGLRATKQTN 112
Cdd:PRK11819 357 GPNGAGKSTLFKMITGQEQPDSGTIKIGET--------VK-------LAYVDQsrD-ALDPNKTVWEEISGGLDIIKVGN 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 113 qlRE------------KVEDAIKRVrlqGMekrypheLSGGQQQRVAFARAIVTKPHFILFDEP--------LSAL-DAI 171
Cdd:PRK11819 421 --REipsrayvgrfnfKGGDQQKKV---GV-------LSGGERNRLHLAKTLKQGGNVLLLDEPtndldvetLRALeEAL 488
|
.
gi 446273968 172 L 172
Cdd:PRK11819 489 L 489
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-216 |
1.21e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.07 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 25 MKQGEFTTLLGPSGCGKTTLLRMIAGLEEPD-KGEIYFGD------TCMYSSAKKIKTSPHERNI-GMVfqdfalwPHMN 96
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpvdirNPAQAIRAGIAMVPEDRKRhGIV-------PILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 97 VFENVAFG-LRATKQTNQLREKVE-----DAIKRVRLQGMEKRYP-HELSGGQQQRVAFARAIVTKPHFILFDEPLSALD 169
Cdd:TIGR02633 356 VGKNITLSvLKSFCFKMRIDAAAElqiigSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446273968 170 AILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:TIGR02633 436 VGAKYEI-YKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-216 |
1.72e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 20 PLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGdtcmySSAKKIKTSPHERNIGMVF------QDfALWP 93
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLD-----GKPIDIRSPRDAIRAGIMLcpedrkAE-GIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 94 HMNVFENVAFGLRATKQTNQ--LREKVEDAIKRVRLQGMEKRYPH------ELSGGQQQRVAFARAIVTKPHFILFDEPL 165
Cdd:PRK11288 345 VHSVADNINISARRHHLRAGclINNRWEAENADRFIRSLNIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446273968 166 SALDAILREEmrleLMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:PRK11288 425 RGIDVGAKHE----IYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-228 |
2.07e-09 |
|
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: 58.87 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQ--ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGleepdkgeiyfgDTCMYSSAKKIKTSPHER 80
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG------------DTTVTSGDATVAGKSILT 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQDFALWPHMNVFENVAFGLRATKQTNQLR-------EKVED-AIKRVRLQGMEKRYPHELSGGQQQRVAFARAI 152
Cdd:TIGR01257 2006 NISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRgvpaeeiEKVANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 153 VTKPHFILFDEPLSALDAILREEMRLELMDIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVK 228
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-249 |
2.12e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 14 KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIA----GLEEPDKGEI-------------YFGDTcMYSS------- 69
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVItydgitpeeikkhYRGDV-VYNAetdvhfp 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 70 ----------AKKIKTsPHERNIGMVFQDFAlwPHMNVFENVAFGLRATKQTnqlreKVEDAIKRvrlqgmekryphELS 139
Cdd:TIGR00956 152 hltvgetldfAARCKT-PQNRPDGVSREEYA--KHIADVYMATYGLSHTRNT-----KVGNDFVR------------GVS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 140 GGQQQRVAFARAIVTKPHFILFDEPLSALDA--------ILReemrlELMDIVHSIGLTALYvtHDQTEAMSMSDQIIVM 211
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLDSatalefirALK-----TSANILDTTPLVAIY--QCSQDAYELFDKVIVL 284
|
250 260 270
....*....|....*....|....*....|....*...
gi 446273968 212 KQGEVlqkgtpedIYVKPSHEfVAKFVGKANWLVEGKQ 249
Cdd:TIGR00956 285 YEGYQ--------IYFGPADK-AKQYFEKMGFKCPDRQ 313
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-228 |
4.34e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 57.72 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 15 TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgDTCmysSAKKIKTSPHERNIGMVFQDFALWpH 94
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-DGH---DLRDYTLASLRNQVALVSQNVHLF-N 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 95 MNVFENVAFGlrATKQTNqlREKVEDAIKRVRLQGMEKRYPH-----------ELSGGQQQRVAFARAIVTKPHFILFDE 163
Cdd:PRK11176 431 DTIANNIAYA--RTEQYS--REQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446273968 164 PLSALD-----AILR--EEMRLElmdivhsigLTALYVTHdQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVK 228
Cdd:PRK11176 507 ATSALDteserAIQAalDELQKN---------RTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-170 |
4.68e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 33 LLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmyssAKKIKtsphernIGMVFQDFALWPHMNVFENVAFGLRATKQ-- 110
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARP--------APGIK-------VGYLPQEPQLDPEKTVRENVEEGVAEVKAal 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 111 ----------------TNQLRE---KVEDAIKRVRL--------QGMEK-RYPH------ELSGGQQQRVAFARAIVTKP 156
Cdd:PRK11819 103 drfneiyaayaepdadFDALAAeqgELQEIIDAADAwdldsqleIAMDAlRCPPwdakvtKLSGGERRRVALCRLLLEKP 182
|
170
....*....|....
gi 446273968 157 HFILFDEPLSALDA 170
Cdd:PRK11819 183 DMLLLDEPTNHLDA 196
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-221 |
4.89e-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: 57.61 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 15 TQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGeiyfgdtcmyssakKIKtspHERNIGMVFQDFALWPH 94
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG--------------KIK---HSGRISFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 95 mNVFENVAFGL-------RATKQTNQLREKVEDAIKRVRLQGMEKRYphELSGGQQQRVAFARAIVTKPHFILFDEPLSA 167
Cdd:TIGR01271 502 -TIKDNIIFGLsydeyryTSVIKACQLEEDIALFPEKDKTVLGEGGI--TLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 168 LDAILREEM----RLELMdivhsIGLTALYVThDQTEAMSMSDQIIVMKQGEVLQKGT 221
Cdd:TIGR01271 579 LDVVTEKEIfescLCKLM-----SNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGT 630
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-214 |
6.52e-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: 54.94 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 13 GKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPD--KGEIYFgdtcmysSAKKIKTSpHERNIGMVFQDFA 90
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILI-------NGRPLDKN-FQRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 91 LWPHMNVFENVAFG--LRAtkqtnqlrekvedaikrvrlqgmekrypheLSGGQQQRVAFARAIVTKPHFILFDEPLSAL 168
Cdd:cd03232 90 HSPNLTVREALRFSalLRG------------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446273968 169 DAilreEMRLELMDIVHSI---GLTALYVTHDQTEA-MSMSDQIIVMKQG 214
Cdd:cd03232 140 DS----QAAYNIVRFLKKLadsGQAILCTIHQPSASiFEKFDRLLLLKRG 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-249 |
1.18e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgdtcmyssAKKIKTSPHE--- 79
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY--------EQDLIVARLQqdp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 -RNI-GMVFqDFalwphmnVFENVAFGLRATKQTNQLREKVED-----AIKRV-RLQG---------MEKRY-------- 134
Cdd:PRK11147 76 pRNVeGTVY-DF-------VAEGIEEQAEYLKRYHDISHLVETdpsekNLNELaKLQEqldhhnlwqLENRInevlaqlg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 135 --PH----ELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSIgltaLYVTHDQTEAMSMSDQI 208
Cdd:PRK11147 148 ldPDaalsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSI----IFISHDRSFIRNMATRI 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446273968 209 IVMKQGEVLQKGTPEDIYVkpshefvakfVGKANWL-VEGKQ 249
Cdd:PRK11147 224 VDLDRGKLVSYPGNYDQYL----------LEKEEALrVEELQ 255
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-214 |
1.56e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 7 GLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGL------EepdkGEIYF-GDTCMYssaKKIKTSpHE 79
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyE----GEILFdGEVCRF---KDIRDS-EA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 80 RNIGMVFQDFALWPHMNVFENVAFG-LRATK---QTNQLREKVEDAIKRVRLqgmeKRYPHELSG----GQQQRVAFARA 151
Cdd:NF040905 78 LGIVIIHQELALIPYLSIAENIFLGnERAKRgviDWNETNRRARELLAKVGL----DESPDTLVTdigvGKQQLVEIAKA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446273968 152 IVTKPHFILFDEPLSAL---DAilreEMRLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQG 214
Cdd:NF040905 154 LSKDVKLLILDEPTAALneeDS----AALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
138-226 |
1.79e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 138 LSGGQQQRVAFARAIVTKPHFILFDEPLSALDA---------ILREEMRlelmdivhsiGLTALYVThDQTEAMSMSDQI 208
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhvahqvfdsCMKDELK----------GKTRVLVT-NQLHFLPLMDRI 809
|
90
....*....|....*...
gi 446273968 209 IVMKQGEVLQKGTPEDIY 226
Cdd:PLN03232 810 ILVSEGMIKEEGTFAELS 827
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-210 |
1.91e-08 |
|
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: 53.34 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 24 VMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYfgdtcmyssakkiktsphernigmvfqdfalWPHMNVfenvaf 103
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE-------------------------------WDGITP------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 104 glratkqtnqlrekvedAIKRVRLqgmekryphELSGGQQQRVAFARAIVTKPHFILFDEPLSALDAilreEMRLELMDI 183
Cdd:cd03222 64 -----------------VYKPQYI---------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI----EQRLNAARA 113
|
170 180 190
....*....|....*....|....*....|.
gi 446273968 184 VHSIGL----TALYVTHDQTEAMSMSDQIIV 210
Cdd:cd03222 114 IRRLSEegkkTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-227 |
2.84e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.06 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 28 GEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFG--DTCMYSSAKKIKTS----PHERNIGMVFQDFAL-WphmnvfeN 100
Cdd:PRK15439 289 GEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNgkEINALSTAQRLARGlvylPEDRQSSGLYLDAPLaW-------N 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 101 VAfGLRATKQTNQLREKVEDAI-KRVRlQGMEKRYPHE------LSGGQQQRVAFARAIVTKPHFILFDEPLSALDAilr 173
Cdd:PRK15439 362 VC-ALTHNRRGFWIKPARENAVlERYR-RALNIKFNHAeqaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV--- 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446273968 174 eEMRLELMDIVHSI---GLTALYVTHDQTEAMSMSDQIIVMKQGEVLQKGTPEDIYV 227
Cdd:PRK15439 437 -SARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINV 492
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-185 |
3.74e-08 |
|
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: 54.75 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 21 LQIVMKQGEFTTLLGPSGCGKTTLLRMIAGL--------EEPDKGEIYFgdtcmyssakkIKTSPHERNigMVFQDFALW 92
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY-----------VPQRPYMTL--GTLRDQIIY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 93 PhMNVFENVAFGLRATKQTNQLRE-KVEDAIKR-VRLQGMEKrYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSAL-- 168
Cdd:TIGR00954 538 P-DSSEDMKRRGLSDKDLEQILDNvQLTHILEReGGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVsv 615
|
170 180
....*....|....*....|..
gi 446273968 169 ---DAILR--EEMRLELMDIVH 185
Cdd:TIGR00954 616 dveGYMYRlcREFGITLFSVSH 637
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
17-216 |
6.69e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 53.65 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 17 ALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTCMyssakkiktSPHER-----NIGMVFQDFAL 91
Cdd:COG4615 347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---------TADNReayrqLFSAVFSDFHL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 92 wphmnvFENVaFGLratkQTNQLREKVEDAIKRVRLQgmekrypH------------ELSGGQQQRVAFARAIVTKPHFI 159
Cdd:COG4615 418 ------FDRL-LGL----DGEADPARARELLERLELD-------HkvsvedgrfsttDLSQGQRKRLALLVALLEDRPIL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 160 LFDEPLSALDAILRE--------EMRlelmdivhSIGLTALYVTHDQTeAMSMSDQIIVMKQGEV 216
Cdd:COG4615 480 VFDEWAADQDPEFRRvfytellpELK--------ARGKTVIAISHDDR-YFDLADRVLKMDYGKL 535
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-170 |
3.11e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 14 KTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEepdKGEIYFGDTCMYSSAKKIKTspHERNIGMVFQDFALWP 93
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK---TGGYIEGDIRISGFPKKQET--FARISGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 94 HMNVFENVAFG--LRATKQ---------TNQLREKVE-----DAIkrVRLQGMEKrypheLSGGQQQRVAFARAIVTKPH 157
Cdd:PLN03140 967 QVTVRESLIYSafLRLPKEvskeekmmfVDEVMELVEldnlkDAI--VGLPGVTG-----LSTEQRKRLTIAVELVANPS 1039
|
170
....*....|...
gi 446273968 158 FILFDEPLSALDA 170
Cdd:PLN03140 1040 IIFMDEPTSGLDA 1052
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-216 |
5.71e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 25 MKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDK-GEIYFgdtcmysSAKKIKT-SPHE---RNIGMVFQD---FALWPHMN 96
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFI-------DGKPVKIrNPQQaiaQGIAMVPEDrkrDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 97 VFENVAFG-LRATKQTNQLREKVEDAIKRVRLQGMEKRYPH------ELSGGQQQRVAFARAIVTKPHFILFDEPLSALD 169
Cdd:PRK13549 358 VGKNITLAaLDRFTGGSRIDDAAELKTILESIQRLKVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446273968 170 AILREEMrLELMDIVHSIGLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:PRK13549 438 VGAKYEI-YKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-201 |
8.64e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 8.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 28 GEFTTLLGPSGCGKTTLLRMIAGleepDKGEIYFGDTCMYSSAK-------KIKtspheRNIGMVFQDFalwpHM----- 95
Cdd:PRK10938 286 GEHWQIVGPNGAGKSTLLSLITG----DHPQGYSNDLTLFGRRRgsgetiwDIK-----KHIGYVSSSL----HLdyrvs 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 96 ----NV-----FENVafGL-RATkqTNQLREKVEDAIKRVRLQGMEKRYP-HELSGGQQQRVAFARAIVTKPHFILFDEP 164
Cdd:PRK10938 353 tsvrNVilsgfFDSI--GIyQAV--SDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEP 428
|
170 180 190
....*....|....*....|....*....|....*...
gi 446273968 165 LSALDAILREEMRlELMDIVHSIGLTAL-YVTHDQTEA 201
Cdd:PRK10938 429 LQGLDPLNRQLVR-RFVDVLISEGETQLlFVSHHAEDA 465
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
33-216 |
1.13e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 33 LLGPSGCGKTTLLRMIAGLEEPDKGEIyfgdtcmySSAKKIKT---SPHErnIGMVFQDFALWPHMnvfenVAFGLRATK 109
Cdd:PRK10636 343 LLGRNGAGKSTLIKLLAGELAPVSGEI--------GLAKGIKLgyfAQHQ--LEFLRADESPLQHL-----ARLAPQELE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 110 QtnQLRE----------KVEDAIKRvrlqgmekrypheLSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLE 179
Cdd:PRK10636 408 Q--KLRDylggfgfqgdKVTEETRR-------------FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
|
170 180 190
....*....|....*....|....*....|....*..
gi 446273968 180 LMDIVHSIgltaLYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:PRK10636 473 LIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-197 |
1.59e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 8 LEKNFGKTqalkplqiVMKqGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGdtcmyssaKKIKTSphernigmVFQ 87
Cdd:PRK11147 334 LVKDFSAQ--------VQR-GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG--------TKLEVA--------YFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 88 DF--ALWPHMNVFENVAFGlratKQTnqlrekVE-DAIKR---VRLQG-----MEKRYP-HELSGGQQQRVAFARaIVTK 155
Cdd:PRK11147 389 QHraELDPEKTVMDNLAEG----KQE------VMvNGRPRhvlGYLQDflfhpKRAMTPvKALSGGERNRLLLAR-LFLK 457
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446273968 156 P-HFILFDEPLSALDAilrEEMRLeLMDIVHSIGLTALYVTHD 197
Cdd:PRK11147 458 PsNLLILDEPTNDLDV---ETLEL-LEELLDSYQGTVLLVSHD 496
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-233 |
8.39e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFgDTCmysSAKKIKTSPHERNIGMVFQDFALWPHmnv 97
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMI-DDC---DVAKFGLTDLRRVLSIIPQSPVLFSG--- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 98 feNVAFGLRATKQTNQlrEKVEDAIKRVRLQGMEKRYPHEL-----------SGGQQQRVAFARAIVTKPHFILFDEPLS 166
Cdd:PLN03232 1325 --TVRFNIDPFSEHND--ADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446273968 167 ALDA--------ILREEMRlelmdivhsiGLTALYVTHdQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEF 233
Cdd:PLN03232 1401 SVDVrtdsliqrTIREEFK----------SCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-225 |
1.46e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYF--GDtcMYSSAKKIKTSPH-- 78
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlgGD--MADARHRRAVCPRia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 ------ERNigmvfqdfaLWPHMNVFENVAF-----GLRATkqtnQLREKVEDAIKRVRLQGMEKRYPHELSGGQQQRVA 147
Cdd:NF033858 80 ympqglGKN---------LYPTLSVFENLDFfgrlfGQDAA----ERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 148 FARAIVTKPHFILFDEPLSALDAILR-------EEMRLElmdivhSIGLTALYVTHDQTEAMSMsDQIIVMKQGEVLQKG 220
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVDPLSRrqfweliDRIRAE------RPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATG 219
|
....*
gi 446273968 221 TPEDI 225
Cdd:NF033858 220 TPAEL 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-219 |
1.57e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.83 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDkGEIY-----------------FG----DTCMYSSAKKIKTS 76
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQidgvswnsvtlqtwrkaFGvipqKVFIFSGTFRKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 77 PHERnigmvFQDFALWphmNVFENVafGLRAtkqtnqLREKVEDAIKRVRLQGmekryPHELSGGQQQRVAFARAIVTKP 156
Cdd:TIGR01271 1314 PYEQ-----WSDEEIW---KVAEEV--GLKS------VIEQFPDKLDFVLVDG-----GYVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 157 HFILFDEPLSALDAILREEMRLELMdivHSIGLTALYVTHDQTEAMSMSDQIIV-----MKQGEVLQK 219
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLK---QSFSNCTVILSEHRVEALLECQQFLViegssVKQYDSIQK 1437
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-223 |
2.16e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNFGKTQALKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGleEPD----KGEIYFGDTCMyssakkIKTSPH 78
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESI------LDLEPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 79 ERNIGMVFQDFALWPHMNVFENVAFgLRATKQTNQ-LREKVE-DAI-------KRVRLQGMEKRYPHE-----LSGGQQQ 144
Cdd:CHL00131 80 ERAHLGIFLAFQYPIEIPGVSNADF-LRLAYNSKRkFQGLPElDPLefleiinEKLKLVGMDPSFLSRnvnegFSGGEKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 145 RVAFARAIVTKPHFILFDEPLSALD----AILREEMRLeLMDIVHSIgltaLYVTHDQteamSMSDQII-----VMKQGE 215
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDidalKIIAEGINK-LMTSENSI----ILITHYQ----RLLDYIKpdyvhVMQNGK 229
|
....*...
gi 446273968 216 VLQKGTPE 223
Cdd:CHL00131 230 IIKTGDAE 237
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-225 |
3.15e-05 |
|
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: 45.71 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLEEPDKGEIYFGDTcmysSAKKIKTSPHERNIGMVFQDFALWP---H 94
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGL----NIAKIGLHDLRFKITIIPQDPVLFSgslR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 95 MNvfenvafgLRATKQTNQlrEKVEDAIKRVRLQGMEKRYP----HE-------LSGGQQQRVAFARAIVTKPHFILFDE 163
Cdd:TIGR00957 1378 MN--------LDPFSQYSD--EEVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446273968 164 PLSALDailreemrLELMDIVHSI------GLTALYVTHDQTEAMSMSdQIIVMKQGEVLQKGTPEDI 225
Cdd:TIGR00957 1448 ATAAVD--------LETDNLIQSTirtqfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-238 |
1.46e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 138 LSGGQQQRVAFAR---AIVTKPHFILfDEPlsaldAI-LREEMRLELMDIVHSI---GLTALYVTHDQtEAMSMSDQIIV 210
Cdd:PRK00635 477 LSGGEQERTALAKhlgAELIGITYIL-DEP-----SIgLHPQDTHKLINVIKKLrdqGNTVLLVEHDE-QMISLADRIID 549
|
90 100 110
....*....|....*....|....*....|....
gi 446273968 211 MKQ------GEVLQKGTPEDiYVKPSHEFVAKFV 238
Cdd:PRK00635 550 IGPgagifgGEVLFNGSPRE-FLAKSDSLTAKYL 582
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
83-230 |
2.12e-04 |
|
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: 43.08 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 83 GMVFQDFALWPhmnVFENVAF--GLRATKQTNQLREKVEDAIKRvRLQ-----GME----KRYPHELSGGQQQRVAFARA 151
Cdd:TIGR00630 427 GKSIADVSELS---IREAHEFfnQLTLTPEEKKIAEEVLKEIRE-RLGflidvGLDylslSRAAGTLSGGEAQRIRLATQ 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 152 I---VTKPHFILfDEPLSALDAilREEMRL-ELMDIVHSIGLTALYVTHDQtEAMSMSDQIIVM------KQGEVLQKGT 221
Cdd:TIGR00630 503 IgsgLTGVLYVL-DEPSIGLHQ--RDNRRLiNTLKRLRDLGNTLIVVEHDE-DTIRAADYVIDIgpgageHGGEVVASGT 578
|
....*....
gi 446273968 222 PEDIYVKPS 230
Cdd:TIGR00630 579 PEEILANPD 587
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
139-233 |
3.07e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 139 SGGQQQRVAFARAIVTK-PHFILFDEPLSALDAILREEMRLELMD---------IVHSIGLTALYvthdqteamsmsDQI 208
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSafsaytvitIAHRLHTVAQY------------DKI 1514
|
90 100
....*....|....*....|....*
gi 446273968 209 IVMKQGEVLQKGTPEDIYVKPSHEF 233
Cdd:PTZ00243 1515 IVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
138-216 |
3.75e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 3.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446273968 138 LSGGQQQRVAFARAIVTKPHFILFDEPLSALDAILREEMRLELMDIVHSiGLTALYVTHDQTEAMSMSDQIIVMKQGEV 216
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
31-197 |
5.75e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 31 TTLLGPSGCGKTTLLRMIA-GLEEPDKGEIYFGDTCMYSSAKKIKtsphernIGMVFQ-------------DFALWPHMN 96
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLINVGSEEAS-------VELEFEhggkryrierrqgEFAEFLEAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 97 ------VFENVaFGL----RATKQTNQLREKVEDAIKRV-RLQGMEKRY---------PHELSGGQQQRVAFARAIVtkp 156
Cdd:COG0419 99 pserkeALKRL-LGLeiyeELKERLKELEEALESALEELaELQKLKQEIlaqlsgldpIETLSGGERLRLALADLLS--- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446273968 157 hfILFDepLSALDailrEEMRLELMDIVHSIGLtalyVTHD 197
Cdd:COG0419 175 --LILD--FGSLD----EERLERLLDALEELAI----ITHV 203
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-242 |
5.95e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 33 LLGPSGCGKTTLLRMIAGLEEPDKGEIYFgDTCMYSsakKIKTSPHERNIGMVFQDFALWPHmnvfeNVAFGLRATKQTN 112
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILI-DGCDIS---KFGLMDLRKVLGIIPQAPVLFSG-----TVRFNLDPFNEHN 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 113 --QLREKVE-----DAIKRVRLqGMEKRYPH---ELSGGQQQRVAFARAIVTKPHFILFDEPLSALDA--------ILRE 174
Cdd:PLN03130 1341 daDLWESLErahlkDVIRRNSL-GLDAEVSEageNFSVGQRQLLSLARALLRRSKILVLDEATAAVDVrtdaliqkTIRE 1419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446273968 175 EMRlelmdivhsiGLTALYVTHdQTEAMSMSDQIIVMKQGEVLQKGTPEDIYVKPSHEFvAKFV---GKAN 242
Cdd:PLN03130 1420 EFK----------SCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF-SKMVqstGAAN 1478
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-225 |
7.95e-04 |
|
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: 41.15 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 138 LSGGQQQRVAFARAI---VTKPHFILFDEPLSALDAilrEEMRlELMDIVHSI---GLTALYVTHDqTEAMSMSDQIIVM 211
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHF---DDIK-KLLEVLQRLvdkGNTVVVIEHN-LDVIKTADYIIDL 904
|
90 100
....*....|....*....|
gi 446273968 212 ------KQGEVLQKGTPEDI 225
Cdd:TIGR00630 905 gpeggdGGGTVVASGTPEEV 924
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
130-169 |
9.70e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 9.70e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446273968 130 MEKRYPHELSGGQQQRVAFARAIVTKPHFILFDEPLSALD 169
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
3-214 |
1.44e-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: 38.84 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 3 IKISGLEKNfgktqALKPLQIVMKQGEFTTLLGPSGCGKTTLLRmiagleepdkgeiyfgdTCMYSSAKK--IKTSPHER 80
Cdd:cd03238 1 LTVSGANVH-----NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------------EGLYASGKArlISFLPKFS 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 81 NIGMVFQDfalwphmnvfenvafglratkqtnQLREKVEDAIKRVRL-QGMEKrypheLSGGQQQRVAFARAIVTKPHFI 159
Cdd:cd03238 59 RNKLIFID------------------------QLQFLIDVGLGYLTLgQKLST-----LSGGELQRVKLASELFSEPPGT 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 160 LF--DEPLSALDailrEEMRLELMDIVHSI---GLTALYVTHDQTeAMSMSDQIIVMKQG 214
Cdd:cd03238 110 LFilDEPSTGLH----QQDINQLLEVIKGLidlGNTVILIEHNLD-VLSSADWIIDFGPG 164
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
18-169 |
1.60e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 18 LKPLQIVMKQGEFTTLLGPSGCGKTTLLRMIAGLE--EPDKGEIYFgdtcmySSAKKIKTSPHER---NIGMVFQDFALW 92
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEF------KGKDLLELSPEDRageGIFMAFQYPVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 93 PHMN--VFENVAF-GLRATKQTNQL-REKVEDAIK-RVRLQGMekryPHEL---------SGGQQQRVAFARAIVTKPHF 158
Cdd:PRK09580 91 PGVSnqFFLQTALnAVRSYRGQEPLdRFDFQDLMEeKIALLKM----PEDLltrsvnvgfSGGEKKRNDILQMAVLEPEL 166
|
170
....*....|.
gi 446273968 159 ILFDEPLSALD 169
Cdd:PRK09580 167 CILDESDSGLD 177
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
138-220 |
2.00e-03 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.16 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 138 LSGGQQQRVAFARAIVTKPHFIL--FDEPLSALDAilREEMRL-ELMDIVHSIGLTALYVTHDQtEAMSMSDQIIVM--- 211
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHP--RDNDRLiETLKRLRDLGNTVLVVEHDE-DTIRAADHVIDIgpg 214
|
90
....*....|..
gi 446273968 212 ---KQGEVLQKG 220
Cdd:cd03270 215 agvHGGEIVAQG 226
|
|
| SpoIIIAA |
COG3854 |
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ... |
31-49 |
2.73e-03 |
|
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443063 Cd Length: 309 Bit Score: 38.98 E-value: 2.73e-03
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
136-212 |
3.03e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 37.72 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 136 HELSGGQQQRVA----FARAIVTKPHFILFDEPLSALDaiLREEMRLELMDIVHSI-GLTALYVTHDQtEAMSMSDQIIV 210
Cdd:cd03227 76 LQLSGGEKELSAlaliLALASLKPRPLYILDEIDRGLD--PRDGQALAEAILEHLVkGAQVIVITHLP-ELAELADKLIH 152
|
..
gi 446273968 211 MK 212
Cdd:cd03227 153 IK 154
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
19-50 |
5.79e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 38.14 E-value: 5.79e-03
10 20 30
....*....|....*....|....*....|....
gi 446273968 19 KPLQIVMKQGEFTTLL--GPSGCGKTTLLRMIAG 50
Cdd:PRK13342 25 KPLRRMIEAGRLSSMIlwGPPGTGKTTLARIIAG 58
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
120-233 |
6.33e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 37.58 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446273968 120 DAIKRVRLQGMEKRYPHEL-----------SGGQQQRVAFARAIVTKPHFILFDEPLSALDailreeMRLElmDIVHSIG 188
Cdd:cd03288 128 EALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASID------MATE--NILQKVV 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446273968 189 LTA------LYVTHDQTEAMSmSDQIIVMKQGEVLQKGTPEDIYVKPSHEF 233
Cdd:cd03288 200 MTAfadrtvVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
12-49 |
7.28e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 36.36 E-value: 7.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446273968 12 FGKTQALKPLQIVMKQGEFTTLL--GPSGCGKTTLLRMIA 49
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLlyGPPGTGKTTLARAIA 40
|
|
|