|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-371 |
0e+00 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 806.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMN 240
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 241 FLPVKVTAVAIDQVQVELpmPNLQQVWLPVESHNVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQI 320
Cdd:PRK11000 241 FLPVKVTATAIEQVQVEL--PNRQQVWLPVEGRGVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGNETQIHIQI 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 321 PSIRQNLVYRQSDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHQEPGV 371
Cdd:PRK11000 319 PAIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGV 369
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-358 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 572.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMN 240
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 241 FLPVKVTAVAIDQVQVELPMPnlqqvwlpvESHNVQVGANMSLGIRPEHLLPSDIADVILEGEVQVVEQLGNETQIHIQI 320
Cdd:COG3839 241 LLPGTVEGGGVRLGGVRLPLP---------AALAAAAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRL 311
|
330 340 350
....*....|....*....|....*....|....*...
gi 1578826625 321 PSirQNLVYRQSDVVLVEEGATFAIGLPPERCHLFRED 358
Cdd:COG3839 312 GG--QELVARVPGDTRLRPGDTVRLAFDPERLHLFDAE 347
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-366 |
3.55e-175 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 491.28 E-value: 3.55e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAW-GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGM 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKM 239
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 240 NFLPVKVTAvaiDQVQVELPmpnlQQVWLPVE-SHNVQVGANMSLGIRPEHLLPSDiADVILEGEVQVVEQLGNETQIHI 318
Cdd:PRK11650 241 NLLDGRVSA---DGAAFELA----GGIALPLGgGYRQYAGRKLTLGIRPEHIALSS-AEGGVPLTVDTVELLGADNLAHG 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1578826625 319 QIPsiRQNLVYRQSDVVLVEEGATFAIGLPPERCHLFREDGTacRRLH 366
Cdd:PRK11650 313 RWG--GQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADTG--RRIE 356
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-357 |
4.11e-156 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 442.61 E-value: 4.11e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGspKMN 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--EAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 241 FLPVKVTAVAIDQVQVE---LPMPNlqqvwlpveSHNVQVGANMSLGIRPEHLLPSDIADV-ILEGEVQVVEQLGNETQI 316
Cdd:COG3842 241 LLPGTVLGDEGGGVRTGgrtLEVPA---------DAGLAAGGPVTVAIRPEDIRLSPEGPEnGLPGTVEDVVFLGSHVRY 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1578826625 317 HIQIPSIRQNLVYRQSDVVL-VEEGATFAIGLPPERCHLFRE 357
Cdd:COG3842 312 RVRLGDGQELVVRVPNRAALpLEPGDRVGLSWDPEDVVVLPA 353
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
1.24e-136 |
|
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: 387.77 E-value: 1.24e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQS 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-235 |
2.58e-114 |
|
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: 331.89 E-value: 2.58e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQS 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIG 235
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-351 |
6.19e-112 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 330.19 E-value: 6.19e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN-DTPPAERGVGMVF 81
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 162 SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSpkMNF 241
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGC--VNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 242 LPVKVTAVAIDQVQVELPmpnlqqvwlpvESHNVQVGANMsLGIRPEHLLPSDIADV--ILEGEVQVVEQLGNETQIHIQ 319
Cdd:COG1118 240 LRGRVIGGQLEADGLTLP-----------VAEPLPDGPAV-AGVRPHDIEVSREPEGenTFPATVARVSELGPEVRVELK 307
|
330 340 350
....*....|....*....|....*....|....*..
gi 1578826625 320 IPSIRQNLVY-----RQSDVVLVEEGATFAIGLPPER 351
Cdd:COG1118 308 LEDGEGQPLEaevtkEAWAELGLAPGDPVYLRPRPAR 344
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
5.29e-109 |
|
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: 317.92 E-value: 5.29e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQS 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-355 |
6.00e-107 |
|
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: 317.75 E-value: 6.00e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMV 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGspKMN 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG--EVN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 241 FLPVKVTAVAIDQVqvelpmpnlQQVWLPVESHNVQVGANMSLGIRPEH--LLPSDIADVILEGEVQVVEQLGNETQIHI 318
Cdd:TIGR03265 240 WLPGTRGGGSRARV---------GGLTLACAPGLAQPGASVRLAVRPEDirVSPAGNAANLLLARVEDMEFLGAFYRLRL 310
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1578826625 319 QIP-----SIRQNLVYRQSDVVLVEEGATFAIGLPPERCHLF 355
Cdd:TIGR03265 311 RLEglpgqALVADVSASEVERLGIRAGQPIWIELPAERLRAF 352
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-290 |
2.46e-101 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 304.18 E-value: 2.46e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQS 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGspKMNFLP 243
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINIFD 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1578826625 244 VKVTAvAIDQVQVELpmpNLQQVWLPVES-HNVQVGANMSLGIRPEHL 290
Cdd:PRK09452 253 ATVIE-RLDEQRVRA---NVEGRECNIYVnFAVEPGQKLHVLLRPEDL 296
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-355 |
3.34e-101 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 303.46 E-value: 3.34e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 2 ASVQLQNVTKAWGD----VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMND-----TPP 72
Cdd:NF040933 1 VTVRVENVTKIFKKgkkeVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 73 AERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 153 SVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAG 232
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 233 FIGspKMNFLPVKV---TAVAIDQVQVELPMPnlqqvwlPVESHNVQvganmsLGIRPEH--LLPSDIADV-----ILEG 302
Cdd:NF040933 241 LIG--DINLLEGKVeeeGLVDGNDLKIPLPNP-------KLEAGEVI------IGIRPEDidISESDMRLPpgfveVGKG 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 303 EVQVVEQLGNETQIHIQIPSIRQNLVYRQSDVVLvEEGATFAIGLPPERCHLF 355
Cdd:NF040933 306 RVKVSSYAGGVFRVVVSPIDDDSIEIIVNSDRPI-EEGEEVNLYVRPDKIKIF 357
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-288 |
4.59e-92 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 279.68 E-value: 4.59e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQS 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPkmNFLP 243
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIFP 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1578826625 244 VKVTAVAIDQVQVELPMPNLQQVWLPVESHNVqvganmslGIRPE 288
Cdd:PRK11432 245 ATLSGDYVDIYGYRLPRPAAFAFNLPDGECTV--------GVRPE 281
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-236 |
1.17e-90 |
|
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: 272.29 E-value: 1.17e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQ 82
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 SYALYPHLSVAENMSFGLKLAGAK----KEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGS 236
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-215 |
2.10e-87 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 264.64 E-value: 2.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAW----GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPaerG 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA--GRVAQV 215
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-355 |
5.37e-87 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 266.56 E-value: 5.37e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVsKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQS 83
Cdd:NF040840 2 IRIENLSKDWKEFKL-RDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:NF040840 81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNF-- 241
Cdd:NF040840 161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEgv 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 242 --LPVKVTAVAIDQVQVELPmpnlQQVWLPVEshnvqvganmsLGIRPEHLLPS-----DIADVILEGEVQVVEQLGNET 314
Cdd:NF040840 241 aeKGGEGTILDTGNIKIELP----EEKKGKVR-----------IGIRPEDITIStekvkTSARNEFKGKVEEIEDLGPLV 305
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1578826625 315 QIHIQIPSIRQNLVYRQSDVVL-VEEGATFAIGLPPERCHLF 355
Cdd:NF040840 306 KLTLDVGIILVAFITRSSFLDLeINEGKEVYASFKASAVHVF 347
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-235 |
3.39e-85 |
|
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: 3.39e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQS 83
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIG 235
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-328 |
1.96e-83 |
|
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: 256.65 E-value: 1.96e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 35 VGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRV 114
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 115 NQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQ 194
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 195 VEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMnflpVKVTAVAIDQVQV----ELPMPNLQQVWLPV 270
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINV----FEATVIERKSEQVvlagVEGRRCDIYTDVPV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 271 EShnvqvGANMSLGIRPEHL----LPSDIADVILEGEVQVVEQLGNETQIHIQIPSIRQNLV 328
Cdd:TIGR01187 238 EK-----DQPLHVVLRPEKIvieeEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLV 294
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-236 |
3.05e-83 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 255.40 E-value: 3.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGD--VVVsKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMV 80
Cdd:COG1125 3 EFENVTKRYPDgtVAV-DDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQL--AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
Cdd:COG1125 82 IQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGS 236
Cdd:COG1125 162 EPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-235 |
8.61e-83 |
|
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: 251.87 E-value: 8.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVsKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQS 83
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIG 235
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-215 |
2.24e-81 |
|
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: 247.77 E-value: 2.24e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGD----VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAergVGM 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA--GRVAQV 215
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-238 |
1.02e-79 |
|
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: 244.13 E-value: 1.02e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDV-VVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMV 80
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQL--AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPK 238
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADR 240
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-235 |
2.07e-78 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 244.99 E-value: 2.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQ 82
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 SYALYPHLSVAENMSFGLKLAGAKK----EVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVLPRRErpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIG 235
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-239 |
1.19e-76 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 241.28 E-value: 1.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQS 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLKLAGAKKEVINQRVNqvaEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVN---EMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKM 239
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-211 |
7.75e-73 |
|
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: 224.37 E-value: 7.75e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMND----TPPAERGVGM 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYPHLSVAENMSFGlklagakkevinqrvnqvaevlqlahlldrkpkaLSGGQRQRVAIGRTLVAEPSVFLLDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
1.58e-71 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 222.61 E-value: 1.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASV-QLQNVTKAWGD----VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAER 75
Cdd:COG1136 1 MSPLlELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 76 G------VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV 149
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 150 AEPSVFLLDEPLSNLDAALRVQ-MRIeISRLHKRLGRTMIYVTHDQvEAMTLADKIVVLDAGRV 212
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEvLEL-LRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
8-310 |
1.98e-71 |
|
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: 226.91 E-value: 1.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 8 NVTKAWGDVVVskDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDT------PPAERGVGMVF 81
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSargiflPPHRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSYALYPHLSVAENMSFGLKLAGAKKEVInqRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
Cdd:COG4148 84 QEARLFPHLSVRGNLLYGRKRAPRAERRI--SFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 162 SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGfiGSPKMNF 241
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAGSV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 242 LPVKVTAVAIDQVQVELPMPNlQQVWLPveSHNVQVGANMSLGIR----------PEHL-----LPSDIADVILEGEVQV 306
Cdd:COG4148 240 LEATVAAHDPDYGLTRLALGG-GRLWVP--RLDLPPGTRVRVRIRardvslalepPEGSsilniLPGRVVEIEPADGGQV 316
|
....
gi 1578826625 307 VEQL 310
Cdd:COG4148 317 LVRL 320
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-216 |
3.55e-71 |
|
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: 221.40 E-value: 3.55e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIhEGEFVVFVGPSGCGKSTLLRMIAGLETITSGD-------LFIGEKRMNdTPPAERGVGMVFQSYALYPHLSVA 93
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTivlngtvLFDSRKKIN-LPPQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSFGLKlaGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMR 173
Cdd:cd03297 94 ENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1578826625 174 IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-235 |
3.50e-69 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 216.93 E-value: 3.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVvvSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSY 84
Cdd:COG3840 3 RLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 85 ALYPHLSVAENMSFG----LKLAGAKKevinQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:COG3840 81 NLFPHLTVAQNIGLGlrpgLKLTAEQR----AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIG 235
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-234 |
1.68e-68 |
|
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: 216.36 E-value: 1.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 9 VTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE------RGVGMVFQ 82
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 SYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFI 234
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-212 |
2.20e-68 |
|
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: 214.28 E-value: 2.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGD----VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERG--- 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 ---VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMtLADKIVVLDAGRV 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
4.13e-67 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 211.85 E-value: 4.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERG-VGMVFQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 SYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 163 NLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-223 |
1.16e-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: 205.26 E-value: 1.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAW-GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMV 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQsyalYP-----HLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
Cdd:COG1122 81 FQ----NPddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 156 LLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYH 223
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-211 |
2.55e-63 |
|
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: 201.16 E-value: 2.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVS--KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERG--VGMV 80
Cdd:cd03225 1 ELKNLSFSYPDGARPalDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQsyalYP-----HLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
Cdd:cd03225 81 FQ----NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1578826625 156 LLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-227 |
3.57e-63 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 201.76 E-value: 3.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDtPPAE-----RGVG 78
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDinklrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSYALYPHLSVAENMSFGL-KLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 158 DEPLSNLD-----AALRVqMRieisRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAD 227
Cdd:COG1126 161 DEPTSALDpelvgEVLDV-MR----DLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-234 |
1.14e-62 |
|
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: 200.59 E-value: 1.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE-----RGVG 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSYALYPHLSVAENMSFGLK-LAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 158 DEPLSNLD---AALRVQMrieISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPaDRFVAGFI 234
Cdd:COG1127 166 DEPTAGLDpitSAVIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-217 |
3.48e-60 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 193.35 E-value: 3.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAW-GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE-----RGV 77
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 158 DEPLSNLDAALRVQ-MRIeISRLHkRLGRTMIYVTHDQ--VEAMtlADKIVVLDAGRVAQVGK 217
Cdd:COG2884 162 DEPTGNLDPETSWEiMEL-LEEIN-RRGTTVLIATHDLelVDRM--PKRVLELEDGRLVRDEA 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-232 |
5.12e-59 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 192.00 E-value: 5.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVT----KAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMnDTPPAERG 76
Cdd:COG4525 1 MSMLTVRHVSvrypGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 VgmVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
Cdd:COG4525 80 V--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA--GRVAQVgkplelyhYPAD---RFVA 231
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER--------LELDfsrRFLA 229
|
.
gi 1578826625 232 G 232
Cdd:COG4525 230 G 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-221 |
1.06e-58 |
|
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: 190.02 E-value: 1.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE-----RGVG 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSYALYPHLSVAENMSFGLKLAGA-KKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 158 DEPLSNLD-AALRVQMRIeISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03261 161 DEPTAGLDpIASGVIDDL-IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-225 |
1.15e-58 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 190.30 E-value: 1.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGV----GM 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYPHLSVAENMSFG-LKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 159 EPLSNLDAALRVqmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK09493 162 EPTSALDPELRH----EVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-212 |
3.10e-58 |
|
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: 188.12 E-value: 3.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPA----ERGVGM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYPHLSVAENMSFGL-KLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 159 EPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03262 161 EPTSALDP----ELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-212 |
2.08e-57 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.79 E-value: 2.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMVFQ 82
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 SYALYPHlSVAENMSFGLKLagAKKEVINQRVNQVAEVLQLAH-LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
Cdd:COG4619 82 EPALWGG-TVRDNLPFPFQL--RERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 162 SNLDAALRVqmRIE--ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:COG4619 159 SALDPENTR--RVEelLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-212 |
2.18e-56 |
|
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: 2.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAW-GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE-----RGV 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSYALYPHLSVAEN--------MSFGLKLAGA-KKEVInQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTL 148
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNvlagrlgrTSTWRSLLGLfPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 149 VAEPSVFLLDEPLSNLD--AALRVqMRIeISRLHKRLGRTMIYVTHdQVE-AMTLADKIVVLDAGRV 212
Cdd:COG3638 162 VQEPKLILADEPVASLDpkTARQV-MDL-LRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDGRV 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-237 |
5.32e-56 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 186.44 E-value: 5.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTK----AWGDVVVSKDINLEIHEGEfvVF--VGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--- 74
Cdd:COG1135 2 IELENLSKtfptKGGPVTALDDVSLTIEKGE--IFgiIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 75 --RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVnqvAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLV 149
Cdd:COG1135 80 arRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRV---AELLELVGLSDKAdayPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 150 AEPSVFLLDEPLSNLDAA-----LRVqmrieISRLHKRLGRTMIYVTHDqveaM----TLADKIVVLDAGRVAQVGKPLE 220
Cdd:COG1135 157 NNPKVLLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLD 227
|
250
....*....|....*..
gi 1578826625 221 LYHYPADRFVAGFIGSP 237
Cdd:COG1135 228 VFANPQSELTRRFLPTV 244
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-227 |
6.80e-56 |
|
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: 190.88 E-value: 6.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTK-----AWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE---- 74
Cdd:COG1123 261 LEVRNLSKrypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 75 -RGVGMVFQ--SYALYPHLSVAENMSFGLKLAG-AKKEVINQRVNQVAEVLQL-AHLLDRKPKALSGGQRQRVAIGRTLV 149
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHD--QVEAMtlADKIVVLDAGRVAQVGKPLELYHYPAD 227
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlaVVRYI--ADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-218 |
8.63e-56 |
|
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: 182.38 E-value: 8.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETI-----TSGDLFIGEK--RMNDTPPAE-- 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKdiYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 75 RGVGMVFQSYALYPhLSVAENMSFGLKLAG-AKKEVINQRvnqVAEVLQLAHLLDR-----KPKALSGGQRQRVAIGRTL 148
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDER---VEEALRKAALWDEvkdrlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 149 VAEPSVFLLDEPLSNLDAALRvqMRIE--ISRLHKRLgrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPIST--AKIEelIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-213 |
2.20e-55 |
|
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: 181.92 E-value: 2.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKA----WGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGV 77
Cdd:COG1124 2 LEVRNLSVSygqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSY--ALYPHLSVAENMSFGLKLAGakkevINQRVNQVAEVLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAE 151
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHG-----LPDREERIAELLEQvglpPSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 152 PSVFLLDEPLSNLDAAlrVQMRI--EISRLHKRLGRTMIYVTHDqVEAMT-LADKIVVLDAGRVA 213
Cdd:COG1124 157 PELLLLDEPTSALDVS--VQAEIlnLLKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIV 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-237 |
3.34e-55 |
|
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: 181.78 E-value: 3.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERG--VGMVF 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELArrIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSYALYPHLSVAENMSFG----LKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:COG1120 82 QEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 158 DEPLSNLDaaLRVQMRI--EISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE---------LYHYPA 226
Cdd:COG1120 162 DEPTSHLD--LAHQLEVleLLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEvltpelleeVYGVEA 239
|
250
....*....|.
gi 1578826625 227 DRFVAGFIGSP 237
Cdd:COG1120 240 RVIEDPVTGRP 250
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
3.83e-55 |
|
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: 180.85 E-value: 3.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGD----VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE----- 74
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 75 RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHdQVEAM-TLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-216 |
1.40e-54 |
|
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: 178.84 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGL 100
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 101 KLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLH 180
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1578826625 181 KRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-226 |
5.82e-54 |
|
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: 181.46 E-value: 5.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGD-------LFIGEKRMnDTPPAERGVGMVFQSYALYPHLSVA 93
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEivlngrtLFDSRKGI-FLPPEKRRIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSFGLKLAGAKKEVINQrvNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMR 173
Cdd:TIGR02142 94 GNLRYGMKRARPSERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 174 IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-221 |
4.60e-53 |
|
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: 175.82 E-value: 4.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFI-GEKRMNDTPPAERGVGMVFQS 83
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDVRKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 164 LDAALRVQMRiEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG4555 163 LDVMARRLLR-EILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
4-217 |
4.41e-52 |
|
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: 172.35 E-value: 4.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTkaWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQS 83
Cdd:TIGR01277 1 LALDKVR--YEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:TIGR01277 79 NNLFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:TIGR01277 159 LDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-209 |
1.04e-51 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 171.13 E-value: 1.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAG-LETI--TSGDLFIGEKRMNDTPPAERGVGM 79
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYPHLSVAENMSFGLKlAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 160 PLSNLDAALRVQMRIEI-SRLHKRlGRTMIYVTHDqVEAMTLADKIVVLDA 209
Cdd:COG4136 160 PFSKLDAALRAQFREFVfEQIRQR-GIPALLVTHD-EEDAPAAGRVLDLGN 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
2.49e-51 |
|
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: 170.38 E-value: 2.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGD--VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPP-AERGVGMV 80
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKaARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 161 LSNLDAALRVQMRIEISRLhkRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
14-212 |
4.65e-51 |
|
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: 169.99 E-value: 4.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 14 GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEK---RMNDTPPAERG--VGMVFQSY--AL 86
Cdd:cd03257 16 GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIRRkeIQMVFQDPmsSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 87 YPHLSVAENMSFGLKLAGA--KKEVINQRVNQVAEVLQL-AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:cd03257 96 NPRMTIGEQIAEPLRIHGKlsKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1578826625 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03257 176 LDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-221 |
5.18e-51 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 170.15 E-value: 5.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 23 NLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFG--- 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 100 -LKLAGAKKEVINQRVNQVAevlqLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISR 178
Cdd:PRK10771 99 gLKLNAAQREKLHAIARQMG----IEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1578826625 179 LHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-216 |
5.49e-51 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 170.58 E-value: 5.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN-DTPPAE------- 74
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfSQKPSEkairllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 75 RGVGMVFQSYALYPHLSVAENMSFG-LKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 154 VFLLDEPLSNLDAALRVQMrIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:COG4161 162 VLLFDEPTAALDPEITAQV-VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-221 |
5.80e-51 |
|
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: 170.44 E-value: 5.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGD-VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE-----RGVG 78
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSYALYPHLSVAEN--------MSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA 150
Cdd:cd03256 82 MIFQQFNLIERLSVLENvlsgrlgrRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 151 EPSVFLLDEPLSNLDAALRVQ-MRIeISRLHKRLGRTMIYVTHdQVE-AMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLH-QVDlAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
8.60e-50 |
|
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: 174.71 E-value: 8.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGL---ETITSGDLFIGEKRMNDTPPAERG- 76
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRGr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 -VGMVFQS--YALYPhLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
Cdd:COG1123 84 rIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-211 |
5.94e-49 |
|
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: 164.34 E-value: 5.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAW-GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEK-----RMNDTPPAERGV 77
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEdvnrlRGRQLPLLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 158 DEPLSNLDAALRVQ-MRIeISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:TIGR02673 162 DEPTGNLDPDLSERiLDL-LKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
7.59e-49 |
|
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: 162.57 E-value: 7.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERG-VGMVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 SYALYPHLSVAENMSfglklagakkevinqrvnqvaevlqlahlldrkpkaLSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
Cdd:cd03230 81 EPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1578826625 163 NLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-212 |
1.49e-48 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 164.47 E-value: 1.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 6 LQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDtppAERGVGMVFQSYA 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE---AREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 86 LYPHLSVAENMSFGLKlaGAKKEvinqrvnQVAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
Cdd:PRK11247 92 LLPWKKVIDNVGLGLK--GQWRD-------AALQALAAVGLADRAnewPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1578826625 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-216 |
1.69e-48 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 164.03 E-value: 1.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN-DTPPAE------- 74
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfSKTPSDkairelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 75 RGVGMVFQSYALYPHLSVAENM-SFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 154 VFLLDEPLSNLDAALRVQMrIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQI-VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-218 |
1.85e-48 |
|
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: 163.76 E-value: 1.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPP---AERGVGMVF 81
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSYALYPHLSVAENM----------SFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
Cdd:cd03219 82 QIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-222 |
2.81e-48 |
|
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: 164.55 E-value: 2.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE-----RGVGMVFQsyalYPH----- 89
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrKKVGLVFQ----FPEhqlfe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 90 LSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQL-AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAL 168
Cdd:TIGR04521 98 ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKG 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 169 RVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:TIGR04521 178 RKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-228 |
1.03e-47 |
|
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: 162.08 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 8 NVTKAWG-DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLF-----IGEKRMNDTPPAERGVGMVF 81
Cdd:TIGR02315 6 NLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILlegtdITKLRGKKLRKLRRRIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSYALYPHLSVAEN--------MSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
Cdd:TIGR02315 86 QHYNLIERLTVLENvlhgrlgyKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADR 228
Cdd:TIGR02315 166 LILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRH 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-214 |
4.16e-47 |
|
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: 159.91 E-value: 4.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGD----VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFI-GEK--RMNDTPPAE-- 74
Cdd:COG4181 9 IELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLaGQDlfALDEDARARlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 75 -RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKkevinQRVNQVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVA 150
Cdd:COG4181 89 aRHVGFVFQSFQLLPTLTALENVMLPLELAGRR-----DARARARALLErvgLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 151 EPSVFLLDEPLSNLDAALRVQMrIE-ISRLHKRLGRTMIYVTHDQveamTLA---DKIVVLDAGRVAQ 214
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQI-IDlLFELNRERGTTLVLVTHDP----ALAarcDRVLRLRAGRLVE 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-211 |
4.43e-47 |
|
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: 159.18 E-value: 4.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 2 ASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERG-VGMV 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHLSVAENMSFGLKLAGAKKEviNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 161 LSNLDAAlRVQMRIEISRLHKRLGRTMIYVTHDQVEAmtLADKIVVLDAGR 211
Cdd:COG4133 159 FTALDAA-GVALLAELIAAHLARGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
7.84e-47 |
|
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: 160.29 E-value: 7.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAW--GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFI-GEKRMND--TPPAERGVG 78
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVdGLDTLDEenLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSyalyPH-----LSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
Cdd:TIGR04520 81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAmTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-228 |
1.14e-46 |
|
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: 158.78 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIgEKRMNDTPPAERGVgmVFQSYALYPHLSVAENMSFG 99
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL-EGKQITEPGPDRMV--VFQNYSLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 100 LK--LAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEIS 177
Cdd:TIGR01184 79 VDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 178 RLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL-YHYPADR 228
Cdd:TIGR01184 159 QIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDR 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-232 |
1.79e-46 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 159.09 E-value: 1.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDtPPAERGVgmVFQSY 84
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 85 ALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 165 DAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVL--DAGRVAQvGKPLELyhypADRFVAG 232
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVE-RLPLNF----ARRFVAG 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
3.65e-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: 155.67 E-value: 3.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERgvgmvfqsy 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 85 alyphlsvAENMSFglklagakkevinqrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
Cdd:cd03214 72 --------ARKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 165 DaaLRVQMRI--EISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03214 129 D--IAHQIELleLLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-211 |
4.12e-46 |
|
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: 154.71 E-value: 4.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMVFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 syalyphlsvaenmsfglklagakkevinqrvnqvaevlqlahlldrkpkaLSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1578826625 163 NLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-212 |
4.18e-46 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 156.61 E-value: 4.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQS 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLKLAGAKKEvinqRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1578826625 164 LDAALRVQMRiEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03268 157 LDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-221 |
2.60e-45 |
|
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: 165.39 E-value: 2.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMVFQSYALYpHLSVAENMS 97
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGTIRENIT 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 98 FGlklagaKKEVINQRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
Cdd:COG2274 571 LG------DPDATDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1578826625 167 ALrvQMRIeISRLHKRL-GRTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG2274 645 ET--EAII-LENLRRLLkGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-220 |
1.10e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 154.09 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigekRMNDTPPAERG--VG 78
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTV-----RLFGKPPRRARrrIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSYALYPH--LSVAENMSFGLK-----LAGAKKEViNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDVVLMGRYgrrglFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 152 PSVFLLDEPLSNLDAALRVQ-MRIeISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQvGKPLE 220
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEAlYEL-LRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEE 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-212 |
1.36e-44 |
|
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: 152.95 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVS-KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMND-----TPPAERGV 77
Cdd:cd03292 1 IEFINVTKTYPNGTAAlDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 158 DEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-223 |
1.87e-44 |
|
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: 161.08 E-value: 1.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 2 ASVQLQNVTKAWGD-VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVG 78
Cdd:COG4988 335 PSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSyalyPHL---SVAENmsfglkLAGAKKEVINQRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAI 144
Cdd:COG4988 415 WVPQN----PYLfagTIREN------LRLGRPDASDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHDQvEAMTLADKIVVLDAGRVAQVGKPLELYH 223
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-207 |
2.82e-44 |
|
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: 151.61 E-value: 2.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 6 LQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKrmnDTPPAERG--------- 76
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQ---ETPPLNSKkaskfrrek 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 157 LDEPLSNLDAALRvQMRIEISRLHKRLGRTMIYVTHDQvEAMTLADKIVVL 207
Cdd:TIGR03608 158 ADEPTGSLDPKNR-DEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
3.14e-44 |
|
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: 152.14 E-value: 3.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFI-GEKRMNDTPPAERGVGMVFQ 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 SYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
7.70e-44 |
|
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: 149.46 E-value: 7.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGD--VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGM 79
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYpHLSVAENMsfglklagakkevinqrvnqvaevlqlahlldrkpkaLSGGQRQRVAIGRTLVAEPSVFLLDE 159
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 160 PLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHDqVEAMTLADKIVVLDAGR 211
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-162 |
1.15e-43 |
|
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: 148.18 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDT--PPAERGVGMVFQSYALYPHLSVAENMS 97
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerKSLRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 98 FGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRK----PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-216 |
3.38e-43 |
|
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: 149.44 E-value: 3.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGD----VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTP-PAERGVG 78
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 159 EPLSNLDaALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03266 162 EPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-221 |
4.96e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 157.25 E-value: 4.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAW-GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGM 79
Cdd:COG1132 339 EIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYpHLSVAENMSFGlklagaKKEVINQRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTL 148
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYG------RPDATDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 149 VAEPSVFLLDEPLSNLDAA--LRVQMRIEisRLHKrlGRTMIYVTH--DQVEAmtlADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG1132 492 LKDPPILILDEATSALDTEteALIQEALE--RLMK--GRTTIVIAHrlSTIRN---ADRILVLDDGRIVEQGTHEEL 561
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
4.68e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 147.59 E-value: 4.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPP--AERG-- 76
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsQQKGli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 ------VGMVFQSYALYPHLSVAENMSFG-LKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV 149
Cdd:PRK11264 81 rqlrqhVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1578826625 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-221 |
7.42e-42 |
|
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: 154.15 E-value: 7.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 2 ASVQLQNVTKAW--GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGV 77
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSyalyPHL---SVAENmsfgLKLagAKKEVINQRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVA 143
Cdd:COG4987 412 AVVPQR----PHLfdtTLREN----LRL--ARPDATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 144 IGRTLVAEPSVFLLDEPLSNLDAALRVQMrieISRLHKRL-GRTMIYVTHDQVeAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALaGRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEEL 556
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-230 |
9.93e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 149.18 E-value: 9.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTK----AWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE----- 74
Cdd:PRK11153 2 IELKNISKvfpqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 75 RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTH--DQVEAmtLADKIVVLDAGRVAQVGKPLELYHYP----ADR 228
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHemDVVKR--ICDRVAVIDAGRLVEQGTVSEVFSHPkhplTRE 239
|
..
gi 1578826625 229 FV 230
Cdd:PRK11153 240 FI 241
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-222 |
1.09e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 144.81 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIG-----EKRMNDTPPAERgVGMVFQ--SYALYPHlSV 92
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvditDKKVKLSDIRKK-VGLVFQypEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 AENMSFGLKLAGAKKEVINQRVNQVAEVLQLAH--LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 171 QMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-233 |
1.17e-40 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 147.87 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE------RGVGMVFQSYALYPHLSVA 93
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMR 173
Cdd:PRK10070 125 DNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 174 IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGF 233
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-234 |
1.37e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 143.64 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 2 ASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLR-------MIAGLEtiTSGDLFIGEKRMND--TPP 72
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDIYDpdVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 73 AE--RGVGMVFQSYALYPHlSVAENMSFGLKLAGAK-KEVINQRVNqvaEVLQLAHL-------LDRKPKALSGGQRQRV 142
Cdd:COG1117 88 VElrRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKsKSELDEIVE---ESLRKAALwdevkdrLKKSALGLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 143 AIGRTLVAEPSVFLLDEPLSNLD--AAlrvqMRIE--ISRLHKRLgrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDpiST----AKIEelILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPT 237
|
250
....*....|....*.
gi 1578826625 219 LELYHYPADRFVAGFI 234
Cdd:COG1117 238 EQIFTNPKDKRTEDYI 253
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
8-228 |
4.35e-40 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 145.02 E-value: 4.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 8 NVTKAWGDVVVskDINLEI-HEGEFVVFvGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDT------PPAERGVGMV 80
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLpAQGITAIF-GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAekgiclPPEKRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHLSVAENMSFGLKlagakkEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:PRK11144 82 FQDARLFPHYKVRGNLRYGMA------KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADR 228
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
7.49e-40 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 141.76 E-value: 7.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMVF 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSYALYPHLSVAENMSFGL------KLAGAKKEVINQRVnqvaEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
Cdd:COG4604 82 QENHINSRLTVRELVAFGRfpyskgRLTAEDREIIDEAI----AYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1578826625 156 LLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-204 |
8.48e-40 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 140.56 E-value: 8.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGD----VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERG--- 76
Cdd:TIGR02211 2 LKCENLGKRYQEgkldTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 ---VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
Cdd:TIGR02211 82 nkkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDqveaMTLADKI 204
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHD----LELAKKL 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-221 |
8.71e-40 |
|
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: 140.65 E-value: 8.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPP---AERGVGMVF 81
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPherARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSYALYPHLSVAENmsfgLKLAG--AKKEVINQRVNQVAEVL-QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
Cdd:cd03224 82 EGRRIFPELTVEEN----LLLGAyaRRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 159 EPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-229 |
1.25e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 141.09 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFI-GEK------RMNDTPPAER- 75
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVgGEEirlkpdRDGELVPADRr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 76 -------GVGMVFQSYALYPHLSVAENMSFG----LKLAgaKKEVINQrvnqvAEVL----QLAHLLDRKPKALSGGQRQ 140
Cdd:COG4598 89 qlqrirtRLGMVFQSFNLWSHMTVLENVIEApvhvLGRP--KAEAIER-----AEALlakvGLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 141 RVAIGRTLVAEPSVFLLDEPLSNLDAALrVQmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPEL-VG---EVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237
|
250
....*....|...
gi 1578826625 218 PLELYHYPA-DRF 229
Cdd:COG4598 238 PAEVFGNPKsERL 250
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-227 |
2.32e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 141.31 E-value: 2.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGE------KRMNDTPPAERGVGMVFQ--SYALYPHlS 91
Cdd:PRK13634 24 YDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitagKKNKKLKPLRKKVGIVFQfpEHQLFEE-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 92 VAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAH-LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
Cdd:PRK13634 103 VEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 171 QMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAD 227
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-216 |
4.30e-39 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 138.18 E-value: 4.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTP-------PAERG 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 vgmvfqsyaLYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
Cdd:cd03269 81 ---------LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 157 LDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTH--DQVEAMtlADKIVVLDAGRVAQVG 216
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHqmELVEEL--CDRVLLLNKGRAVLYG 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-214 |
3.11e-38 |
|
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: 136.12 E-value: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFI-GEKRMNDtppaERGVGMVFQS 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLEKE----RKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YAL---YPhLSVAENMSFGL-----KLAGAKKEVInQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
Cdd:cd03235 77 RSIdrdFP-ISVRDVVLMGLyghkgLFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 156 LLDEPLSNLDAALRVQMRIEISRLHkRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQ 214
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-226 |
3.29e-38 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 139.03 E-value: 3.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 14 GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLE---TITSGDLFIGEKRMNDTPPAE------RGVGMVFQ-S 83
Cdd:COG0444 16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKElrkirgREIQMIFQdP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 Y-ALYPHLSVAENMSFGLKL-AGAKKEVINQRVnqvAEVLQLAHL------LDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
Cdd:COG0444 96 MtSLNPVMTVGDQIAEPLRIhGGLSKAEARERA---IELLERVGLpdperrLDRYPHELSGGMRQRVMIARALALEPKLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 156 LLDEPLSNLDAAlrVQMRI--EISRLHKRLGRTMIYVTHD--QVEAMtlADKIVVLDAGRVAQVGKPLELYHYPA 226
Cdd:COG0444 173 IADEPTTALDVT--IQAQIlnLLKDLQRELGLAILFITHDlgVVAEI--ADRVAVMYAGRIVEEGPVEELFENPR 243
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
3.55e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.81 E-value: 3.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 2 ASVQLQNVTKAWGDVV--VSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN-DTPPAERG-V 77
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkENLKEIRKkI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSyalyPH-----LSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
Cdd:PRK13632 86 GIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 153 SVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAmTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-221 |
4.81e-37 |
|
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: 134.06 E-value: 4.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSG---DLFiGEKR-------------- 66
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF-GERRggedvwelrkrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 67 -----MNDTPPAERGVGMV----FQSYALYPHLSVAENmsfglklagakkevinQRVNQVAEVLQLAHLLDRKPKALSGG 137
Cdd:COG1119 83 vspalQLRFPRDETVLDVVlsgfFDSIGLYREPTDEQR----------------ERARELLELLGLAHLADRPFGTLSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 138 QRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGP 226
|
....
gi 1578826625 218 PLEL 221
Cdd:COG1119 227 KEEV 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-212 |
8.62e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 139.00 E-value: 8.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE---RGVGMV 80
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHLSVAENMSFGLKLAGAKkeVINQR-VNQVAEVLqLAHL-----LDRKPKALSGGQRQRVAIGRTLVAEPSV 154
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGREPRRGG--LIDWRaMRRRAREL-LARLgldidPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 155 FLLDEPLSNLDAAlrvqmriEISRLHKRL------GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:COG1129 162 LILDEPTASLTER-------EVERLFRIIrrlkaqGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
9.19e-37 |
|
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: 130.63 E-value: 9.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE---RGVGMV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQsyalyphlsvaenmsfglklagakkevinqrvnqvaevlqlahlldrkpkaLSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 161 LSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-259 |
1.25e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.47 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTP-------PAER 75
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 76 GvgmvfqsyaLYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
Cdd:COG4152 81 G---------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 156 LLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTH--DQVEAmtLADKIVVLDAGRVAQVGKPLELYH-YPADRFVAG 232
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHqmELVEE--LCDRIVIINKGRKVLSGSVDEIRRqFGRNTLRLE 228
|
250 260
....*....|....*....|....*....
gi 1578826625 233 FIGSPKM--NFLPVKVTAVAIDQVQVELP 259
Cdd:COG4152 229 ADGDAGWlrALPGVTVVEEDGDGAELKLE 257
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-212 |
2.82e-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: 2.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKrmnDTPPAER--GVGMVFQS--YALYPHlSVAEN 95
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERrkSIGYVMQDvdYQLFTD-SVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 96 MSFGLKLAGAKkeviNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlrvQMRiE 175
Cdd:cd03226 93 LLLGLKELDAG----NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK---NME-R 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1578826625 176 ISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03226 165 VGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-221 |
5.00e-36 |
|
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: 130.87 E-value: 5.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPP---AERGVGMVF 81
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhriARLGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSYALYPHLSVAENMSFGLKLAGAKKEvINQRVNQVAEVL-QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:COG0410 85 EGRRIFPSLTVEENLLLGAYARRDRAE-VRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 161 LSNLdAALRVQ--MRIeISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG0410 164 SLGL-APLIVEeiFEI-IRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-226 |
5.79e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 133.32 E-value: 5.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE-----RGVGMVFQ-SYA-LYPHLSVA 93
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQdPYAsLNPRMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSFGLKLAGAKKEviNQRVNQVAEVLQLAHL----LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
Cdd:COG4608 116 DIIAEPLRIHGLASK--AERRERVAELLELVGLrpehADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQ 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 170 VQ----MRieisRLHKRLGRTMIYVTHD--QVEAMtlADKIVVLDAGRVAQVGKPLELYHYPA 226
Cdd:COG4608 194 AQvlnlLE----DLQDELGLTYLFISHDlsVVRHI--SDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-216 |
7.73e-36 |
|
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: 129.62 E-value: 7.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVfVGPSGCGKSTLLRMIAGLETITSGDLFI-GEKRMNDTPPAERGVGMVFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGL-LGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 SYALYPHLSVAENmsfgLKLAGAKKEVINQRVN-QVAEVLQLAHLLDR---KPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
Cdd:cd03264 80 EFGVYPNFTVREF----LDYIAWLKGIPSKEVKaRVDEVLELVNLGDRakkKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 159 EPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTH--DQVEAMtlADKIVVLDAGRVAQVG 216
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGE--DRIVILSTHivEDVESL--CNQVAVLNKGKLVFEG 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-216 |
1.10e-35 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 128.82 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGL--ETITSGDLFI-GEKRMNDTPPAErgVGMVFQSYALYPHLSVAENM 96
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLInGRPLDKRSFRKI--IGYVPQDDILHPTLTVRETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 97 SFGLKLAGakkevinqrvnqvaevlqlahlldrkpkaLSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEI 176
Cdd:cd03213 104 MFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1578826625 177 SRLHKrLGRTMIYVTHD-QVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03213 155 RRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-218 |
1.31e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 135.92 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE---RGVGMV 80
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHLSVAENMSFGL---KLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:COG3845 86 HQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1578826625 158 DEPLSNL-----DAALRVqMRieisRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:COG3845 166 DEPTAVLtpqeaDELFEI-LR----RL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDT 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-212 |
2.19e-35 |
|
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: 128.86 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAWGD--VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVG 78
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSyalyPHL---SVAENMSFGLKLAGakkeviNQRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAI 144
Cdd:cd03245 82 YVPQD----VTLfygTLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 145 GRTLVAEPSVFLLDEPLSNLDaaLRVQMRIeISRLHKRL-GRTMIYVTHDQVeAMTLADKIVVLDAGRV 212
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMD--MNSEERL-KERLRQLLgDKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-222 |
2.41e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.52 E-value: 2.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMVFQSyalyPH-----LSV 92
Cdd:PRK13635 24 KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGMVFQN----PDnqfvgATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 AENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQM 172
Cdd:PRK13635 100 QDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1578826625 173 RIEISRLHKRLGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13635 180 LETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-222 |
3.98e-34 |
|
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: 125.73 E-value: 3.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 6 LQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAER---GVGMVFQ 82
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 SYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
Cdd:cd03218 83 EASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 163 NLDaALRVQmriEISRLHKRLGRTMIYV---THDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:cd03218 163 GVD-PIAVQ---DIQKIIKILKDRGIGVlitDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-228 |
1.44e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 125.57 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 18 VSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigekRMNDTPPAE----------RGVGMVFQSY--A 85
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV-----SWRGEPLAKlnraqrkafrRDIQMVFQDSisA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 86 LYPHLSV----AENMSFGLKLAGAKKEVinqRVNQVAEVLQLA-HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:PRK10419 102 VNPRKTVreiiREPLRHLLSLDKAERLA---RASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV---AQVGKPLELYHyPADR 228
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvetQPVGDKLTFSS-PAGR 248
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-221 |
1.95e-33 |
|
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: 123.87 E-value: 1.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 18 VSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMVFQSYALYPHlSVAEN 95
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 96 MSFGLKLagAKKEVinqrVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
Cdd:cd03254 97 IRLGRPN--ATDEE----VIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 165 D--AALRVQMRIEisRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03254 171 DteTEKLIQEALE--KLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-216 |
5.32e-33 |
|
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: 123.02 E-value: 5.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAER---GVGMVF 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQlaHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVLK--EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 162 SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASG 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-235 |
6.31e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 123.41 E-value: 6.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRM-------NDTPPA 73
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLfgrniysPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 74 E--RGVGMVFQSYALYPHLSVAENMSFGLKLAG--AKKEVINQRV----NQVAEVLQLAHLLDRKPKALSGGQRQRVAIG 145
Cdd:PRK14267 82 EvrREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVewalKKAALWDEVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 146 RTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLgrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
250
....*....|....
gi 1578826625 226 ----ADRFVAGFIG 235
Cdd:PRK14267 240 ehelTEKYVTGALG 253
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-229 |
7.71e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 122.83 E-value: 7.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPP---AERGV 77
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhkrARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 158 DEPLSNLD--AALRVQmRIeISRLHKR-LGrtmIYVT-HDQVEAMTLADKIVVLDAGRVAQVGKPLELY-------HYPA 226
Cdd:COG1137 161 DEPFAGVDpiAVADIQ-KI-IRHLKERgIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILnnplvrkVYLG 235
|
...
gi 1578826625 227 DRF 229
Cdd:COG1137 236 EDF 238
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-232 |
2.27e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 121.94 E-value: 2.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGL-----ETITSGDLFIGEKRMNDTPPAE- 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 75 -RGVGMVFQSYALYPHLSVAENMSFGLKL---AGAKKEvINQRVNQVAEVLQL----AHLLDRKPKALSGGQRQRVAIGR 146
Cdd:PRK14247 81 rRRVQMVFQIPNPIPNLSIFENVALGLKLnrlVKSKKE-LQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 147 TLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLgrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP- 225
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPr 237
|
250
....*....|
gi 1578826625 226 ---ADRFVAG 232
Cdd:PRK14247 238 helTEKYVTG 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-193 |
2.66e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 121.08 E-value: 2.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 18 VSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGD-LFIGE--KRMNDTPPAE---RGVGMVFQSYALYPHLS 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvIFNGQpmSKLSSAAKAElrnQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 92 VAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180
....*....|....*....|..
gi 1578826625 172 MRIEISRLHKRLGRTMIYVTHD 193
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTHD 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-225 |
4.46e-32 |
|
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: 126.34 E-value: 4.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 11 KAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETiTSGDLFIGEKRMNDTPPAE-----RGVGMVFQS-Y 84
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 85 A-LYPHLSVAENMSFGLKL--AGAKKEvinQRVNQVAEVLQLAHL----LDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:COG4172 373 GsLSPRMTVGQIIAEGLRVhgPGLSAA---ERRARVAEALEEVGLdpaaRHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 158 DEPLSNLDAALRVQMrIEI-SRLHKRLGRTMIYVTHDQ--VEAMtlADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:COG4172 450 DEPTSALDVSVQAQI-LDLlRDLQREHGLAYLFISHDLavVRAL--AHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-221 |
5.11e-32 |
|
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: 120.41 E-value: 5.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGD-VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDT--PPAERGVGMV 80
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYpHLSVAENMSFGlKLAGAKKEVINqrvnqVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLV 149
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYG-RPDATDEEVIE-----AAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-220 |
5.69e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 120.89 E-value: 5.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGvgmvfQ 82
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 SYALYP--HL-----SVAENMSFG----LKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
Cdd:PRK11231 77 RLALLPqhHLtpegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 152 PSVFLLDEPLSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
Cdd:PRK11231 157 TPVVLLDEPTTYLD----INHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
6.05e-32 |
|
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: 126.07 E-value: 6.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAW-----GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLF--IGEK--RMNDTPPAE 74
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEwvDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 75 RG-----VGMVFQSYALYPHLSVAENM--SFGLKLA---GAKKEVINQRVNQVAEVlQLAHLLDRKPKALSGGQRQRVAI 144
Cdd:TIGR03269 360 RGrakryIGILHQEYDLYPHRTVLDNLteAIGLELPdelARMKAVITLKMVGFDEE-KAEEILDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-216 |
2.45e-31 |
|
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: 118.40 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 14 GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigEKRMNDTPPAERGVGMVfqsyalyPHLSVA 93
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV---TVRGRVSSLLGLGGGFN-------PELTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMR 173
Cdd:cd03220 103 ENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1578826625 174 IEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03220 183 RRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-212 |
2.59e-31 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 118.59 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 15 DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigekRMNDTPPAERG------VGMVF-QSYALY 87
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-----RVAGLVPWKRRkkflrrIGVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 88 PHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1578826625 168 LRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-224 |
5.99e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 117.88 E-value: 5.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 14 GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIgekRMNDTPPAERGVGMVfqsyalyPHLSVA 93
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV---NGRVSALLELGAGFH-------PELTGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR--VQ 171
Cdd:COG1134 107 ENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQkkCL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 172 MRIEisRLHKRlGRTMIYVTHD--QVEamTLADKIVVLDAGRVAQVGKP---LELYHY 224
Cdd:COG1134 187 ARIR--ELRES-GRTVIFVSHSmgAVR--RLCDRAIWLEKGRLVMDGDPeevIAAYEA 239
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-203 |
6.07e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 118.35 E-value: 6.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLR-------MIAGLETitSGDLFIGEKRMNDT--PPAE 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLYAPdvDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 75 --RGVGMVFQSYALYPHlSVAENMSFGLKLAGAK---KEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV 149
Cdd:PRK14243 89 vrRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKgdmDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 150 AEPSVFLLDEPLSNLD--AALRVQmrieisRLHKRLGR--TMIYVTHDQVEAMTLADK 203
Cdd:PRK14243 168 VQPEVILMDEPCSALDpiSTLRIE------ELMHELKEqyTIIIVTHNMQQAARVSDM 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-212 |
7.75e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 122.87 E-value: 7.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 6 LQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIgekrmndtPPAERgVGMVFQSYA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGLR-IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 86 LYPHLSVAENMSFGLK-LAGAKKEV-------------------------------INQRVNQVAEVLQLAH-LLDRKPK 132
Cdd:COG0488 72 LDDDLTVLDTVLDGDAeLRALEAELeeleaklaepdedlerlaelqeefealggweAEARAEEILSGLGFPEeDLDRPVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 133 ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqmrIE-ISRLHKRLGR---TMIYVTHD-----QVeamtlADK 203
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--------LEsIEWLEEFLKNypgTVLVVSHDryfldRV-----ATR 218
|
....*....
gi 1578826625 204 IVVLDAGRV 212
Cdd:COG0488 219 ILELDRGKL 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-222 |
1.50e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 117.53 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFI-GEKRMNDTP-PAERGVGMVFQSyalyPH-----LSV 92
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVwDIRHKIGMVFQN----PDnqfvgATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 AENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQM 172
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1578826625 173 RIEISRLHKRLGRTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13650 180 IKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELF 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-212 |
2.35e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 116.72 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWG-----DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERG-- 76
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 VGMVFQSYAL--YPHLSVAENMS--------FGLKLAGAKKEvINQRVNQVAEV-LQLAHLLDRKPKALSGGQRQRVAIG 145
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLTKKR-RELFRELLATLgLGLENRLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 146 RTLVAEPSVFLLDEPLSNLD--AALRVqmrIEIS-RLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDpkTAALV---LELTeKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-228 |
2.73e-30 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 116.83 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 18 VSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE-----RGVGMVFQ-SY-ALYPHL 90
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQdSPsAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 91 SVAENMSFGLKLAGAKKEviNQRVNQVAEVLQLAHL----LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
Cdd:TIGR02769 106 TVRQIIGEPLRHLTSLDE--SEQKARIAELLDMVGLrsedADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 167 ALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL--YHYPADR 228
Cdd:TIGR02769 184 VLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLlsFKHPAGR 247
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
2.80e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 117.60 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 2 ASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFI-GEKRMNDTPPAERGVGMV 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 161 LSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-234 |
2.82e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 116.41 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLE------TITSGDLFIGEK---RMNDTPPAERGVGMVFQSYALYPhL 90
Cdd:PRK14239 22 NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpevTITGSIVYNGHNiysPRTDTVDLRKEIGMVFQQPNPFP-M 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 91 SVAENMSFGLKLAGAK-KEVINQRV----------NQVAEVLQLAHLldrkpkALSGGQRQRVAIGRTLVAEPSVFLLDE 159
Cdd:PRK14239 101 SIYENVVYGLRLKGIKdKQVLDEAVekslkgasiwDEVKDRLHDSAL------GLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 160 PLSNLDAAlrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFI 234
Cdd:PRK14239 175 PTSALDPI--SAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-222 |
3.09e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 116.73 E-value: 3.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 17 VVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGE---KRMNDTPPAERGVGMVFQSyalyPHLS-- 91
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PDNQiv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 92 ---VAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAL 168
Cdd:PRK13633 100 atiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 169 RVQMRIEISRLHKRLGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-222 |
8.48e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 115.23 E-value: 8.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMVFQSyalyPH-----LSV 92
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQN----PDnqfvgSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 AENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQM 172
Cdd:PRK13648 102 KYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1578826625 173 RIEISRLHKRLGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13648 182 LDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-222 |
1.09e-29 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 114.17 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 15 DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMVFQSYALYPhLSV 92
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 AENMSFGLKlaGAKKEVInQRVNQVAE----VLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
Cdd:cd03249 94 AENIRYGKP--DATDEEV-EEAAKKANihdfIMSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 165 DAA--LRVQMRIEisRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:cd03249 171 DAEseKLVQEALD--RAMK--GRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-220 |
1.31e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 114.44 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE----RGVgmVFQSYALYPHLSVAEN 95
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElarrRAV--LPQHSSLAFPFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 96 MSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV-------AEPSVFLLDEPLSNLDaaL 168
Cdd:COG4559 96 VALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD--L 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 169 RVQMRI-EISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
Cdd:COG4559 174 AHQHAVlRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-212 |
1.85e-29 |
|
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: 119.59 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMVFQSYALYpHLSVAENMS 97
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTLRDNIA 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 98 FGLKLAGakkeviNQRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
Cdd:TIGR03375 561 LGAPYAD------DEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEPTSAMDN 634
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1578826625 167 alRVQMRIeISRLHKRL-GRTMIYVTHdQVEAMTLADKIVVLDAGRV 212
Cdd:TIGR03375 635 --RSEERF-KDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-192 |
1.88e-29 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 112.66 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 8 NVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERGVgmvfqsY--- 84
Cdd:PRK13539 7 DLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH------Ylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 85 --ALYPHLSVAENMSFGLKLAGAKkeviNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
Cdd:PRK13539 81 rnAMKPALTVAENLEFWAAFLGGE----ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|
gi 1578826625 163 NLDAAlRVQMRIEISRLHKRLGRTMIYVTH 192
Cdd:PRK13539 157 ALDAA-AVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-216 |
1.91e-29 |
|
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: 113.13 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 9 VTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGL---ETITSGDLFIGEKRMNdtpPAE--RGVGMVFQS 83
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRK---PDQfqKCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLKLAG---AKKEVINQRVNQVAEV-LQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
Cdd:cd03234 90 DILLPGLTVRETLTYTAILRLprkSSDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 160 PLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHD-QVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-222 |
2.39e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.51 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 18 VSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGL--------ETITSGDLFIGEKRMNDTppAERgVGMVFQSY-ALYP 88
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWDI--REK-VGIVFQNPdNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 89 HLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAL 168
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 169 RVQMRIEISRLHKRLGRTMIYVTHDQVEAmTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIF 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-225 |
6.81e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 114.42 E-value: 6.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGD-LFIGE--KRMNDTP--PAERGVGMVFQS--YALYPHLSV 92
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEvAWLGKdlLGMKDDEwrAVRSDIQMIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 AENMSFGLKLAGAK--KEVINQRV-NQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
Cdd:PRK15079 118 GEIIAEPLRTYHPKlsRQEVKDRVkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1578826625 170 VQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK15079 198 AQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-212 |
9.64e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 111.51 E-value: 9.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAW-GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLF-----IGEKRMNDTPPAERGV 77
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWfsghdITRLKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVnqvAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAEPSV 154
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRV---SAALDKVGLLDKAknfPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 155 FLLDEPLSNLDAALRVqmriEISRLHK---RLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:PRK10908 159 LLADEPTGNLDDALSE----GILRLFEefnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-218 |
9.88e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 112.17 E-value: 9.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 2 ASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGM 79
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYPHLSVAENMSFGL-KLAGAKKEVinQRVnqVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLV------ 149
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRaPHGLSRAED--DAL--VAAALAqvdLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 150 AEPSVFLLDEPLSNLDaaLRVQ---MRIeISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:PRK13548 157 GPPRWLLLDEPTSALD--LAHQhhvLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-207 |
1.25e-28 |
|
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: 116.62 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAWGDV-VVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGM 79
Cdd:TIGR02857 321 SLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYPHlSVAENMSFGLKlaGAKKEVINQRVNQV--AEVLQ-----LAHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARP--DASDAEIREALERAglDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 153 SVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHDqVEAMTLADKIVVL 207
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-222 |
1.33e-28 |
|
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: 111.17 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGD--VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGM 79
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYpHLSVAENMSFGLKlaGAKKEvinqrvnQVAEVLQLAHLLD---RKPKA-----------LSGGQRQRVAIG 145
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGRP--GATRE-------EVEEAARAANAHEfimELPEGydtvigergvkLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 146 RTLVAEPSVFLLDEPLSNLDaaLRVQMRIE--ISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:cd03251 151 RALLKDPPILILDEATSALD--TESERLVQaaLERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-238 |
1.71e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.52 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGE------KRMNDTPPAERGVGMVFQ--SYALYPHlSV 92
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstSKQKEIKPVRKKVGVVFQfpESQLFEE-TV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 AENMSFGLKLAGAKKEVINQRVNQVAEVLQLA-HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
Cdd:PRK13643 103 LKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 172 MRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHyPADRFVAGFIGSPK 238
Cdd:PRK13643 183 MMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ-EVDFLKAHELGVPK 247
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-222 |
1.88e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 112.15 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN------DTPPAERGVGMVFQsyalYPHL---- 90
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPESqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 91 -SVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAH-LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAL 168
Cdd:PRK13649 101 eTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 169 RVQMRIEISRLHkRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13649 181 RKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-211 |
2.07e-28 |
|
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: 109.87 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVS-----KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGekrmndtppaeRGVG 78
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsftlKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP-----------GSIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSyalyPHL---SVAENMSFGlklagakKEVINQRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAI 144
Cdd:cd03250 70 YVSQE----PWIqngTIRENILFG-------KPFDEERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 145 GRTLVAEPSVFLLDEPLSNLDAalRVQMRIeISRL---HKRLGRTMIYVTHdQVEAMTLADKIVVLDAGR 211
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDA--HVGRHI-FENCilgLLLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
17-221 |
2.94e-28 |
|
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: 116.38 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 17 VVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPA--ERGVGMVFQSYALYPHlSVAE 94
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIRD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 95 NMSFG------------LKLAGAKKEVINQRVNQVAEVlqlahllDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
Cdd:TIGR01846 550 NIALCnpgapfehvihaAKLAGAHDFISELPQGYNTEV-------GEKGANLSGGQRQRIAIARALVGNPRILIFDEATS 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 163 NLD----AALRVQMRiEISRlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR01846 623 ALDyeseALIMRNMR-EICR-----GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
5.27e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 110.66 E-value: 5.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAW-GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFI-GEK-RMNDTPPAERGV 77
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPiTKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQS---YALYPhlSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
Cdd:PRK13652 81 GLVFQNpddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-212 |
5.83e-28 |
|
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: 107.69 E-value: 5.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDV--VVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERG--VGMV 80
Cdd:cd03246 2 EVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHlSVAENMsfglklagakkevinqrvnqvaevlqlahlldrkpkaLSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:cd03246 82 PQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 161 LSNLDAALRVQMRIEISRLHKRlGRTMIYVTHdQVEAMTLADKIVVLDAGRV 212
Cdd:cd03246 124 NSHLDVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-207 |
6.44e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 108.09 E-value: 6.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 12 AWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigekrmndTPPAERGVGMVFQSYAL---YP 88
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------RRAGGARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 89 hLSVAENMSFGL--KLAGAKKEVINQR--VNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
Cdd:NF040873 72 -LTVRDLVAMGRwaRRGLWRRLTRDDRaaVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1578826625 165 DAALRVQMRIEISRLHKRlGRTMIYVTHDqVEAMTLADKIVVL 207
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHD-LELVRRADPCVLL 191
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-222 |
6.47e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 110.71 E-value: 6.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPA----ERGVGMVFQS--YALYPhLSVA 93
Cdd:PRK13636 23 KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklRESVGMVFQDpdNQLFS-ASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMR 173
Cdd:PRK13636 102 QDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1578826625 174 IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13636 182 KLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-212 |
7.90e-28 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 114.82 E-value: 7.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 2 ASVQLQNVTKAW----GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRM----NDTPPA 73
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 74 ER--GVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
Cdd:PRK10535 83 LRreHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHD-QVEAMtlADKIVVLDAGRV 212
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDpQVAAQ--AERVIEIRDGEI 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-207 |
1.75e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.88 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMVFQ 82
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 SYALYPHlSVAENMSFglklagaKKEVINQRVNQVAEVLQLA------HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
Cdd:PRK10247 89 TPTLFGD-TVYDNLIF-------PWQIRNQQPDPAIFLDDLErfalpdTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEaMTLADKIVVL 207
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-221 |
2.39e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 108.92 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 7 QNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMVFQSY 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 85 ALYPHLSVAENMSFGL----KLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:PRK10253 91 TTPGDITVQELVARGRyphqPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-218 |
2.52e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 108.92 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVS-KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMND---TPPAERGVGM 79
Cdd:PRK13644 2 IRLENVSYSYPDGTPAlENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfskLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQS-YALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 159 EPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEP 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-216 |
3.03e-27 |
|
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: 112.92 E-value: 3.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 2 ASVQLQNVTKA--WGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERG--V 77
Cdd:COG4618 329 GRLSVENLTVVppGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSYALYPHlSVAENMS-FG----------LKLAGAKkEVInqrvnqvaevLQLAH----LLDRKPKALSGGQRQRV 142
Cdd:COG4618 409 GYLPQDVELFDG-TIAENIArFGdadpekvvaaAKLAGVH-EMI----------LRLPDgydtRIGEGGARLSGGQRQRI 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 143 AIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQvEAMTLADKIVVLDAGRVAQVG 216
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFG 548
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-222 |
5.86e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 108.17 E-value: 5.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 23 NLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGE-------KRMNDTPPAERGVGMVFQ--SYALYPHlSVA 93
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVFQfpEYQLFQE-TIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSFGLKLAGAKKEVINQRVNQVAEVLQLAH-LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQM 172
Cdd:PRK13645 110 KDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDF 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1578826625 173 RIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13645 190 INLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-225 |
9.97e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 108.51 E-value: 9.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE-----RGVGMVFQS-YA-LYPHLSV- 92
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNPRKKVg 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 ---AENMSFGLKLAGAkkevinQRVNQVAEVLQLAHL----LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
Cdd:PRK11308 113 qilEEPLLINTSLSAA------ERREKALAMMAKVGLrpehYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 166 AALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK11308 187 VSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-225 |
1.05e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 106.59 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLqNVT---KAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFI------------GEK 65
Cdd:PRK10619 1 MSENKL-NVIdlhKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtinlvrdkdGQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 66 RMNDTPPAE---RGVGMVFQSYALYPHLSVAEN-MSFGLKLAGAKKEVINQR-VNQVAEVLQLAHLLDRKPKALSGGQRQ 140
Cdd:PRK10619 80 KVADKNQLRllrTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERaVKYLAKVGIDERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 141 RVAIGRTLVAEPSVFLLDEPLSNLDAALRVqmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVG----EVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
....*...
gi 1578826625 218 PLELYHYP 225
Cdd:PRK10619 236 PEQLFGNP 243
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-221 |
1.13e-26 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 105.70 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 24 LEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKrmnDTPPAERGVGMVFQSYAL---YPhLSVAEN-MSFG 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFP-ISVAHTvMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 100 LKLAG--AKKEVINQR-VNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD---AALRVQMR 173
Cdd:TIGR03771 77 TGHIGwlRRPCVADFAaVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDmptQELLTELF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1578826625 174 IEISrlhkRLGRTMIYVTHDQVEAMTLADKIVVLDaGRVAQVGKPLEL 221
Cdd:TIGR03771 157 IELA----GAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQL 199
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-218 |
1.53e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 106.74 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE-RG-VGMVFQSyalyPH-----LSV 92
Cdd:PRK13647 22 KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSkVGLVFQD----PDdqvfsSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 AENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQM 172
Cdd:PRK13647 98 WDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1578826625 173 RIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:PRK13647 178 MEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-221 |
2.24e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 105.36 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTP---PAERGV 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSYALYPHLSVAENMSFGLKL-AGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 157 LDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-222 |
3.36e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.07 E-value: 3.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE------RGVGMVFQsyalYPHL---- 90
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklrKKVSLVFQ----FPEAqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 91 -SVAENMSFGLKLAGA-KKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAL 168
Cdd:PRK13641 101 nTVLKDVEFGPKNFGFsEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 169 RVQMrIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13641 181 RKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-212 |
3.45e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 106.71 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigekRMNDTPPAE------RGVGMVF-QSYALYPHLSV 92
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV-----RVLGYVPFKrrkefaRRIGVVFgQRSQLWWDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 AEnmSFGL--KLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
Cdd:COG4586 114 ID--SFRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1578826625 171 QMRIEISRLHKRLGRTMIYVTHD--QVEAmtLADKIVVLDAGRV 212
Cdd:COG4586 192 AIREFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHGRI 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-212 |
4.79e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.00 E-value: 4.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKrmndtppaergvgmVFQS 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET--------------VKIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 Y------ALYPHLSVAENMSfglklaGAKKEVINQRVNQVaevlqLAHLL------DRKPKALSGGQRQRVAIGRTLVAE 151
Cdd:COG0488 382 YfdqhqeELDPDKTVLDELR------DGAPGGTEQEVRGY-----LGRFLfsgddaFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 152 PSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGRTMIYVTHDQ--VEamTLADKIVVLDAGRV 212
Cdd:COG0488 451 PNVLLLDEPTNHLD----IETLEALEEALDDFPGTVLLVSHDRyfLD--RVATRILEFEDGGV 507
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
6.82e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 104.73 E-value: 6.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSG-------DLF---IGEKRMNdT 70
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEvrvegrvEFFnqnIYERRVN-L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 71 PPAERGVGMVFQSYALYPhLSVAENMSFGLKLAGAKKEV----INQRVNQVAEVL-QLAHLLDRKPKALSGGQRQRVAIG 145
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLeiddIVESALKDADLWdEIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 146 RTLVAEPSVFLLDEPLSNLD--AALRVQMRIEISRLHKRLgrTMIYVTHDQVEAMTLADKIVVLDA-----GRVAQVGKP 218
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDpiASMKVESLIQSLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLT 240
|
....*....
gi 1578826625 219 LELYHYPAD 227
Cdd:PRK14258 241 KKIFNSPHD 249
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-288 |
7.73e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 107.23 E-value: 7.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVG 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSYAL--------------YPHLSVAENMSfglklaGAKKEVINQRVNQVaEVLQLAhllDRKPKALSGGQRQRVAI 144
Cdd:PRK09536 81 SVPQDTSLsfefdvrqvvemgrTPHRSRFDTWT------ETDRAAVERAMERT-GVAQFA---DRPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMrIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhY 224
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRT-LELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV--L 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 225 PADRFVAGF-----------IGSPKMNFLPVKVTAVAIDQVQVELpmPNLQQVWLPVESHNVQVGANMSLGIRPE 288
Cdd:PRK09536 228 TADTLRAAFdartavgtdpaTGAPTVTPLPDPDRTEAAADTRVHV--VGGGQPAARAVSRLVAAGASVSVGPVPE 300
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-221 |
7.99e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 106.07 E-value: 7.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDL-FIGEKRMNDTPPAERGVGM 79
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 160 PLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
8.85e-26 |
|
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: 108.35 E-value: 8.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETI--TSGDL-----------------FIGE 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 65 K----------------RMNDTPPAE--RGVGMVFQ-SYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAH 125
Cdd:TIGR03269 81 PcpvcggtlepeevdfwNLSDKLRRRirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 126 LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIV 205
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*.
gi 1578826625 206 VLDAGRVAQVGKPLEL 221
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV 256
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-193 |
1.89e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 102.55 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 22 INLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLF-IGE--KRMNDTPPAE---RGVGMVFQSYALYPHLSVAEN 95
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlVGQplHQMDEEARAKlraKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 96 MSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIE 175
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170
....*....|....*...
gi 1578826625 176 ISRLHKRLGRTMIYVTHD 193
Cdd:PRK10584 189 LFSLNREHGTTLILVTHD 206
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-221 |
2.09e-25 |
|
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: 102.56 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 17 VVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPA--ERGVGMVFQSYALYpHLSVAE 94
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 95 NMSFG------------LKLAGAKKEVINQRvnqvaevLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
Cdd:cd03252 95 NIALAdpgmsmervieaAKLAGAHDFISELP-------EGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 163 NLDAAlrvQMRIEISRLHKRL-GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03252 168 ALDYE---SEHAIMRNMHDICaGRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-217 |
2.18e-25 |
|
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: 107.43 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERG--VGMVFQSYALYPHlSVAENMS 97
Cdd:TIGR01842 335 RGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIGYLPQDVELFPG-TVAENIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 98 -FGlKLAGAKKEVINQRVNQVAEVLQlahlldRKPK-----------ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
Cdd:TIGR01842 414 rFG-ENADPEKIIEAAKLAGVHELIL------RLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 166 AALRVQMRIEISRLHKRlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:TIGR01842 487 EEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGE 536
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-234 |
2.72e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.82 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 15 DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN--------DTPPAERGVGMVFQSYAL 86
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqiDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 87 YPHLSVAENMSFGLKLAGAK-----KEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKekreiKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 162 SNLDAALRVQMRIEISRLHKRLgrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFI 234
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
15-227 |
3.23e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 103.25 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 15 DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN--DTPPAERGVGMVFQSY-ALYPHLS 91
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 92 VAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
Cdd:PRK13642 99 VEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1578826625 172 MRIEISRLHKRLGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLELYHYPAD 227
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-212 |
3.48e-25 |
|
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: 101.78 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAW---GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN--DTPPAERGVG 78
Cdd:cd03248 12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSYALYPHlSVAENMSFGLklAGAKKEVIN---QRVNQVAEVLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAE 151
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYGL--QSCSFECVKeaaQKAHAHSFISELASGYDtevgEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHKRlgRTMIYVTHdQVEAMTLADKIVVLDAGRV 212
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-222 |
4.02e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.78 E-value: 4.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 15 DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAERG------------------ 76
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELitnpyskkiknfkelrrr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 VGMVFQ--SYALYPHlSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAH-LLDRKPKALSGGQRQRVAIGRTLVAEPS 153
Cdd:PRK13631 118 VSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 154 VFLLDEPLSNLDAALRVQMrIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-221 |
4.09e-25 |
|
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: 106.96 E-value: 4.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAWGD--VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN--DTPPAERGVG 78
Cdd:TIGR03797 451 AIEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSYALYPHlSVAENMSFGLKLAgakkevinqrVNQVAEVLQLAHL---LDRKP-----------KALSGGQRQRVAI 144
Cdd:TIGR03797 531 VVLQNGRLMSG-SIFENIAGGAPLT----------LDEAWEAARMAGLaedIRAMPmgmhtviseggGTLSGGQRQRLLI 599
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 145 GRTLVAEPSVFLLDEPLSNLDAalRVQmRIEISRLhKRLGRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALDN--RTQ-AIVSESL-ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDEL 671
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-226 |
1.10e-24 |
|
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: 100.52 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGL----ETITSGDLFIGEKRMNDTPPAERGVGMVFQS--YALYPHLSVAE 94
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 95 NMSFGLKLAGAKKEVINQRVNQVAEVLQLAH---LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
Cdd:TIGR02770 84 HAIETLRSLGKLSKQARALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 172 MRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPK 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-221 |
1.13e-24 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 106.25 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 22 INLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAER-GVGMVFQSYALYPHLSVAENMSFGL 100
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRqSLGMCPQHNILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 101 KLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRvqMRIEISRLH 180
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR--RSIWDLLLK 1106
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1578826625 181 KRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL 1147
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-222 |
1.29e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.57 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAW---GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN--DTPPAERGVG 78
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqyDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSYALYPHlSVAENMSFGLKLAgAKKEVINQRVNQVAE--VLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEP 152
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGLTDT-PDEEIMAAAKAANAHdfIMEFPNGYDtevgEKGSQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 153 SVFLLDEPLSNLDAalRVQMRIEISRlhKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:TIGR00958 637 RVLILDEATSALDA--ECEQLLQESR--SRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLM 701
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-217 |
1.46e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 104.75 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPA---ERGVGMV 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkahQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHLSVAENMSFGLklagAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 161 LSNLDAAlrvqmriEISRLHKRL------GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:PRK15439 168 TASLTPA-------ETERLFSRIrellaqGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-222 |
1.94e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.92 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 15 DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN----DTPPAERGVGMVFQS-----YA 85
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkkSLLEVRKTVGIVFQNpddqlFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 86 lyPhlSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
Cdd:PRK13639 94 --P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 166 AalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13639 170 P----MGASQIMKLLYDLnkeGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-222 |
2.94e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 100.62 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGE-KRMNDTP-----PAERGVGMVFQsyalYPHL--- 90
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKdkyirPVRKRIGMVFQ----FPESqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 91 --SVAENMSFGLKLAGAKKEVINQRVNQVaeVLQLA---HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
Cdd:PRK13646 100 edTVEREIIFGPKNFKMNLDEVKNYAHRL--LMDLGfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 166 AALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-234 |
3.13e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 100.22 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGD-LFIGEkrmnDTPPAERG------ 76
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEiLFDGE----NIPAMSRSrlytvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 --VGMVFQSYALYPHLSVAENMSFGLK-LAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
Cdd:PRK11831 84 krMSMLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 154 VFLLDEPLSNLDA-ALRVQMRIeISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPaDRFVAG 232
Cdd:PRK11831 164 LIMFDEPFVGQDPiTMGVLVKL-ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQ 241
|
..
gi 1578826625 233 FI 234
Cdd:PRK11831 242 FL 243
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-220 |
4.54e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.55 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDL-FIGEKRMNDTPPAE------------------------ 74
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKNKKKTKEkekvleklviqktrfkkikkikei 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 75 -RGVGMVFQ--SYALYPHlSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQL-AHLLDRKPKALSGGQRQRVAIGRTLVA 150
Cdd:PRK13651 104 rRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-192 |
7.37e-24 |
|
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: 97.43 E-value: 7.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 6 LQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPaERGVGMVFQSY- 84
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 85 -ALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAevlqLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:TIGR01189 82 pGLKPELSALENLHFWAAIHGGAQRTIEDALAAVG----LTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*....
gi 1578826625 164 LDAAlRVQMRIEISRLHKRLGRTMIYVTH 192
Cdd:TIGR01189 158 LDKA-GVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-223 |
9.55e-24 |
|
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: 97.21 E-value: 9.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLE--TITSGDLFIGEKRMNDTPPAER---GVGM 79
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYPHLSVAENMSFglklagakkevinqrVNqvaevlqlahlldrkpKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
Cdd:cd03217 82 AFQYPPEIPGVKNADFLRY---------------VN----------------EGFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 160 PLSNLDA-ALRVQMRIeISRLHKRlGRTMIYVTH-----DQVEamtlADKIVVLDAGRVAQVGkPLELYH 223
Cdd:cd03217 131 PDSGLDIdALRLVAEV-INKLREE-GKSVLIITHyqrllDYIK----PDRVHVLYDGRIVKSG-DKELAL 193
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-212 |
9.80e-24 |
|
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: 96.73 E-value: 9.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAER---GVGMV---FQSYALYPHLSVA 93
Cdd:cd03215 17 RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYVpedRKREGLVLDLSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSfglklagakkevinqrvnqvaevlqLAHLLdrkpkalSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMR 173
Cdd:cd03215 97 ENIA-------------------------LSSLL-------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIY 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 1578826625 174 IEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03215 145 RLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-192 |
1.04e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.58 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 2 ASVQLQNVT--KAWGDVVVsKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigekrmnDTPPAERgvgM 79
Cdd:COG4178 361 GALALEDLTlrTPDGRPLL-EDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR---V 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VF---QSY--------AL-YPHLsvAENMSfglklagakkeviNQRVNQVAEVLQLAHLLDR------KPKALSGGQRQR 141
Cdd:COG4178 429 LFlpqRPYlplgtlreALlYPAT--AEAFS-------------DAELREALEAVGLGHLAERldeeadWDQVLSLGEQQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 142 VAIGRTLVAEPSVFLLDEPLSNLDAALRVQMrieISRLHKRL-GRTMIYVTH 192
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-211 |
1.10e-23 |
|
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: 97.89 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 16 VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFI----GEKRMNDTPPAE------RGVGMVFQSYA 85
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPREilalrrRTIGYVSQFLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 86 LYPHLS----VAEnmsfGLKLAGAKKEVINQRvnqvAEVLqLAHL-LDRK-----PKALSGGQRQRVAIGRTLVAEPSVF 155
Cdd:COG4778 104 VIPRVSaldvVAE----PLLERGVDREEARAR----AREL-LARLnLPERlwdlpPATFSGGEQQRVNIARGFIADPPLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 156 LLDEPLSNLDAALRvQMRIEISRLHKRLGRTMIYVTHDQvEAM-TLADKIVVLDAGR 211
Cdd:COG4778 175 LLDEPTASLDAANR-AVVVELIEEAKARGTAIIGIFHDE-EVReAVADRVVDVTPFS 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-211 |
1.11e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.91 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRM---NDTPPAERGV 77
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSYALYPHLSVAENMSFGlKLAgAKKEVINQRVNQVAEVLQLAHL-LDRKP----KALSGGQRQRVAIGRTLVAEP 152
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLG-QLP-HKGGIVNRRLLNYEAREQLEHLgVDIDPdtplKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 153 SVFLLDEPLSNLDA-ALRVQMRIeISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:PRK11288 160 RVIAFDEPTSSLSArEIEQLFRV-IRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-211 |
2.08e-23 |
|
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: 94.44 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigekrmndtppaergvgmvfqs 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 yalyphlsvaenmsfglklagakkevinqRVNQVAEVLQLAHlldrkpkaLSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:cd03221 58 -----------------------------TWGSTVKIGYFEQ--------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1578826625 164 LDaalrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:cd03221 101 LD----LESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-212 |
2.31e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 97.26 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE---RGV 77
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSYALYPHLSVAENMSFGLKLagAKKEVINQRVNQVAEVlqLAHLLDRKPK---ALSGGQRQRVAIGRTLVAEPSV 154
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFF--AERDQFQERIKWVYEL--FPRLHERRIQragTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 155 FLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-193 |
3.46e-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: 100.90 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 2 ASVQLQNVTKAW-GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIgekrmNDTPPAERGVGMV 80
Cdd:TIGR02868 333 PTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTL-----DGVPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALY---PHL---SVAENMSFGlklagaKKEVINQRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVA 143
Cdd:TIGR02868 408 RRRVSVCaqdAHLfdtTVRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 144 IGRTLVAEPSVFLLDEPLSNLDAALRVQMrieISRLHKRL-GRTMIYVTHD 193
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADEL---LEDLLAALsGRTVVLITHH 529
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-221 |
4.05e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 96.67 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLE--TITSGDLFIGEKRMNDTPPAER---GVGMVFQsyalYPhlsvAE 94
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFLAFQ----YP----VE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 95 -----NMSFgLKLA-GAKKEV------INQRVNQVAEVLQLAH-LLDRkpkAL----SGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:COG0396 89 ipgvsVSNF-LRTAlNARRGEelsareFLKLLKEKMKELGLDEdFLDR---YVnegfSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 158 DEPLSNLDA-ALRVqMRIEISRLHKRlGRTMIYVTH-----DQVEamtlADKIVVLDAGRVAQVGKPlEL 221
Cdd:COG0396 165 DETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHyqrilDYIK----PDFVHVLVDGRIVKSGGK-EL 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-221 |
4.72e-23 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 100.56 E-value: 4.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWG--DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGM 79
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYPHlSVAENMSFGlklagAKKEVINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTL 148
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG-----RTEQADRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-221 |
6.33e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.58 E-value: 6.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 7 QNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGD--LF---IGEKRMNdtppAERGVGMVF 81
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawLFgqpVDAGDIA----TRRRVGYMS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQR----VAIgrtlVAEPSVFLL 157
Cdd:NF033858 346 QAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRlslaVAV----IHKPELLIL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 158 DEPLSNLDAALR---VQMRIEISRlhkRLGRTmIYV-THDQVEAMtLADKIVVLDAGRVAQVGKPLEL 221
Cdd:NF033858 422 DEPTSGVDPVARdmfWRLLIELSR---EDGVT-IFIsTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
4-222 |
1.05e-22 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 99.63 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWG--DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGM 79
Cdd:TIGR03796 478 VELRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVlaNSVAM 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYPHlSVAENMS--------FGLKLA---GAKKEVINQRVNQV-AEVLQLAhlldrkpKALSGGQRQRVAIGRT 147
Cdd:TIGR03796 558 VDQDIFLFEG-TVRDNLTlwdptipdADLVRAckdAAIHDVITSRPGGYdAELAEGG-------ANLSGGQRQRLEIARA 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 148 LVAEPSVFLLDEPLSNLDAAlrVQMRIeISRLHKRlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:TIGR03796 630 LVRNPSILILDEATSALDPE--TEKII-DDNLRRR-GCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELW 699
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-221 |
1.15e-22 |
|
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: 99.51 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMVFQSYALYpHLSVAENMS 97
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAYNIA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 98 FGLklAGAKKEvinqrvnQVAEVLQLAHLLD---RKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:COG5265 454 YGR--PDASEE-------EVEAAARAAQIHDfieSLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 164 LD--------AALRvqmriEISRlhkrlGRTMIYVTH------DqveamtlADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG5265 525 LDsrteraiqAALR-----EVAR-----GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAEL 579
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-237 |
1.49e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 95.63 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN--DTPPAERGVGMVFQ--SYALYPHLSVAEN 95
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQdpSTSLNPRQRISQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 96 MSFGLKL-----AGAKKEVINQRVNQVAEVLQLAHLLdrkPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
Cdd:PRK15112 110 LDFPLRLntdlePEQREKQIIETLRQVGLLPDHASYY---PHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 171 QMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP----ADRFVAGFIGSP 237
Cdd:PRK15112 187 QLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPlhelTKRLIAGHFGEA 257
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-213 |
1.52e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE---RGVGMV---FQSYALYPHLSVA 93
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVpedRKGEGLVLDLSIR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSFGLKLAGAKKEVINQRvNQVAEVLQLAHLLDRKP-------KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
Cdd:COG1129 349 ENITLASLDRLSRGGLLDRR-RERALAEEYIKRLRIKTpspeqpvGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1578826625 167 ALRVqmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
Cdd:COG1129 428 GAKA----EIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-212 |
1.92e-22 |
|
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: 98.60 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 14 GDVVVSKDINLEIHEGEFVVFVGPSGCGKS----TLLRMIAGLETITSGDLFIGEKRMNDTPPAE----RG--VGMVFQ- 82
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrriRGnrIAMIFQe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 -SYALYPHLSVAENMSFGLKL-AGAKKEVINQRVnqvAEVLQLAHL------LDRKPKALSGGQRQRVAIGRTLVAEPSV 154
Cdd:COG4172 101 pMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARA---LELLERVGIpdperrLDAYPHQLSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQ--VEAMtlADKIVVLDAGRV 212
Cdd:COG4172 178 LIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLgvVRRF--ADRVAVMRQGEI 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-210 |
2.38e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 98.32 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPP---AERGVGMV 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSYALYPHLSVAENMSFGlKLAGAKKEVIN----QRVNQVAEVL----QLAHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
Cdd:PRK09700 86 YQELSVIDELTVLENLYIG-RHLTKKVCGVNiidwREMRVRAAMMllrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 153 SVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-218 |
2.48e-22 |
|
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: 94.40 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 25 EIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPaergvgmvfQSYALYPhLSVAENMSFGLKLAG 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQ---------YIKADYE-GTVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 105 AKkeviNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLG 184
Cdd:cd03237 91 TH----PYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD----VEQRLMASKVIRRFA 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1578826625 185 ----RTMIYVTHDQVEAMTLADKIVVLDagrvaqvGKP 218
Cdd:cd03237 163 enneKTAFVVEHDIIMIDYLADRLIVFE-------GEP 193
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-216 |
2.75e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.61 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigEKRMNDTPP--------AERG 76
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV---HYRMRDGQLrdlyalseAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 V------GMVFQSYA--LYPHLSVAENMSFGLKLAGAKK--EVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGR 146
Cdd:PRK11701 85 RllrtewGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHygDIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 147 TLVAEPSVFLLDEPLSNLDAAlrVQMRI--EISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVS--VQARLldLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-229 |
2.83e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 94.69 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 22 INLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETitsGDLFIG------------EKRM-NDTPPAERGVGMVFQSYALYP 88
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT---GDKSAGshiellgrtvqrEGRLaRDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 89 HLSVAENMSFGlKLAGAK---------KEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
Cdd:PRK09984 100 RLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 160 PLSNLDA-ALRVQMRIeISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPlelYHYPADRF 229
Cdd:PRK09984 179 PIASLDPeSARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS---QQFDNERF 245
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-238 |
4.87e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.39 E-value: 4.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVqlqNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSG-----DLFIGEKRM---NDTPP 72
Cdd:PRK14271 22 MAAV---NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 73 AERGVGMVFQSYALYPhLSVAENMSFGL---KLAGAK--KEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRT 147
Cdd:PRK14271 99 FRRRVGMLFQRPNPFP-MSIMDNVLAGVrahKLVPRKefRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 148 LVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLgrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP-- 225
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPkh 255
|
250
....*....|....*
gi 1578826625 226 --ADRFVAGFIGSPK 238
Cdd:PRK14271 256 aeTARYVAGLSGDVK 270
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-229 |
4.91e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.47 E-value: 4.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 17 VVSKDINLEIHEGEFVVFVGPSGCGKST----LLRMIAGLETITSGDLFIGEKRMNDTPPAERGVGMVFQ--SYALYPHL 90
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQdpNSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 91 SVAENMSFGLK-----LAGAKKEvinQRVNQVAEVLQL-AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
Cdd:PRK15134 380 NVLQIIEEGLRvhqptLSAAQRE---QQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 165 DAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRF 229
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-220 |
1.93e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.21 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 22 INLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETiTSGDLFIGEKRMNDTPPAE----RGV---------GM-VFQSYALY 87
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElarhRAYlsqqqsppfAMpVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 88 PHlsvaenmsfglklAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV-------AEPSVFLLDEP 160
Cdd:COG4138 94 QP-------------AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 161 LSNLDAALRVQMRIEISRLHkRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-216 |
3.42e-21 |
|
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: 91.43 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFI-----GEKRMNDTPPAERGV- 77
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERRRl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 -----GMVFQSYA--LYPHLSVAENMSFGLKLAGAKK--EVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTL 148
Cdd:TIGR02323 84 mrtewGFVHQNPRdgLRMRVSAGANIGERLMAIGARHygNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-222 |
3.78e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.99 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 13 WGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTppaERG-------VGMVFQSya 85
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYS---KRGllalrqqVATVFQD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 86 lyP-----HLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:PRK13638 86 --PeqqifYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 161 LSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-215 |
4.11e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.47 E-value: 4.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAwgDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE---RGVGMVF 81
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSY---ALYPHLSVAENMSFG--LKLAGAK------KEVINQRVNQVA-EVLQL-AHLLDRKPKALSGGQRQRVAIGRTL 148
Cdd:PRK09700 345 ESRrdnGFFPNFSIAQNMAISrsLKDGGYKgamglfHEVDEQRTAENQrELLALkCHSVNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 149 VAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
Cdd:PRK09700 425 CCCPEVIIFDEPTRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-221 |
6.04e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 94.10 E-value: 6.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 25 EIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKrmndtppaergvgmvfQSYAlyP-HLSVAENMSFGLKLA 103
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK----------------ISYK--PqYIKPDYDGTVEDLLR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 104 GAKKEVINQRVN-QVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKR 182
Cdd:PRK13409 423 SITDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VEQRLAVAKAIRR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1578826625 183 L----GRTMIYVTHDQVEAMTLADKIVVLD--AGRVAQVGKPLEL 221
Cdd:PRK13409 499 IaeerEATALVVDHDIYMIDYISDRLMVFEgePGKHGHASGPMDM 543
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-227 |
7.25e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.96 E-value: 7.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETitsGDLFIGEKRMNDTPPAERG-----VGMVFQSYALYPHLSVAE 94
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSP---KGVKGSGSVLLNGMPIDAKemraiSAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 95 NMSFG--LKL-AGAKKEVINQRVNQVAEVLQL---AHLLDRKP---KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
Cdd:TIGR00955 119 HLMFQahLRMpRRVTKKEKRERVDEVLQALGLrkcANTRIGVPgrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 166 AAlrvqMRIEISRLHKRL---GRTMIYVTHD-QVEAMTLADKIVVLDAGRVAQVGKPLEL-------------YHYPAD 227
Cdd:TIGR00955 199 SF----MAYSVVQVLKGLaqkGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAvpffsdlghpcpeNYNPAD 273
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-221 |
7.40e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.14 E-value: 7.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 22 INLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITsGDLFIGEKRMNDTPPAE--RGVGMVFQSYALyPHLSVAENMSFG 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 100 LKLAGakKEVINQRVNQ--VAE-VLQLAHLLDRKPK----ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA------ 166
Cdd:PRK11174 447 NPDAS--DEQLQQALENawVSEfLPLLPQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAhseqlv 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 167 --ALRVQMRieisrlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK11174 525 mqALNAASR----------RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-221 |
2.15e-20 |
|
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: 92.88 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAWG--DVVVSkDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVG 78
Cdd:TIGR01193 473 DIVINDVSYSYGygSNILS-DISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSYALYPHlSVAENMsfglkLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRT 147
Cdd:TIGR01193 552 YLPQEPYIFSG-SILENL-----LLGAKENVSQDEIWAACEIAEIKDDIENMPLGyqtelseegssISGGQKQRIALARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 148 LVAEPSVFLLDEPLSNLDAALrvQMRIeISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTIT--EKKI-VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-208 |
3.50e-20 |
|
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: 91.77 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 25 EIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKrmndtppaergvgmvfQSY------ALYPhLSVAENMSf 98
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK----------------ISYkpqyisPDYD-GTVEEFLR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 99 glklagakkEVINQRV------NQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQM 172
Cdd:COG1245 424 ---------SANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VEQ 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1578826625 173 RIEISRLHKRL----GRTMIYVTHD-QVEAMtLADKIVVLD 208
Cdd:COG1245 491 RLAVAKAIRRFaenrGKTAMVVDHDiYLIDY-ISDRLMVFE 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-212 |
1.78e-19 |
|
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: 84.67 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWG--DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIgekrmNDTPPAERGVgmvf 81
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL-----DGVPVSDLEK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 qsyalyphlSVAENMSfglklagakkeVINQRVNqvaevLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
Cdd:cd03247 72 ---------ALSSLIS-----------VLNQRPY-----LFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 162 SNLDAALRVQMrieISRLHKRL-GRTMIYVTHdQVEAMTLADKIVVLDAGRV 212
Cdd:cd03247 127 VGLDPITERQL---LSLIFEVLkDKTLIWITH-HLTGIEHMDKILFLENGKI 174
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-208 |
3.45e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.94 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigeKRmndtPPAERgVGMVFQS 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KR----NGKLR-IGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLKlAGAKKEVINQRVNQVaevlQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:PRK09544 76 LYLDTTLPLTVNRFLRLR-PGTKKEDILPALKRV----QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1578826625 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLD 208
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-215 |
3.78e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.01 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 18 VSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGletitsgdlfigekRMNDTPPAERGVGMVFQsyaLYPHLSVAENMS 97
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------------ALKGTPVAGCVDVPDNQ---FGREASLIDAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 98 fglklagakkevINQRVNQVAEVLQLAHLLD-----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQM 172
Cdd:COG2401 108 ------------RKGDFKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1578826625 173 RIEISRLHKRLGRTMIYVT-HDQVEAMTLADKIVVLDAGRVAQV 215
Cdd:COG2401 176 ARNLQKLARRAGITLVVAThHYDVIDDLQPDLLIFVGYGGVPEE 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-240 |
3.99e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 87.09 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 14 GDVVVSKDINLEIHEGEFVVFVGPSGCGKS----TLLRMIAGLETITSGDLFIG-------EKRMNDTPpAERgVGMVFQ 82
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIGGSATFNGreilnlpEKELNKLR-AEQ-ISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 S--YALYPHLSVAENMSFGLKL--AGAKKEVINQRVNqvaevlqlahLLD-------RK-----PKALSGGQRQRVAIGR 146
Cdd:PRK09473 105 DpmTSLNPYMRVGEQLMEVLMLhkGMSKAEAFEESVR----------MLDavkmpeaRKrmkmyPHEFSGGMRQRVMIAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 147 TLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
250
....*....|....*
gi 1578826625 227 DRFVAGFIGS-PKMN 240
Cdd:PRK09473 255 HPYSIGLLNAvPRLD 269
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-209 |
4.98e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.09 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAergvgmvFQSYALY--------PHLSV 92
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDLLYlghqpgikTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 AENMSFGLKLAGakkeviNQRVNQVAEVLQLAHLLDRK--P-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA-- 167
Cdd:PRK13538 92 LENLRFYQRLHG------PGDDEALWEALAQVGLAGFEdvPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQgv 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1578826625 168 LRVQMRIEisrLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA 209
Cdd:PRK13538 166 ARLEALLA---QHAEQGGMVILTTHQDLPVASDKVRKLRLGQ 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-217 |
8.87e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 88.01 E-value: 8.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 29 GEFVVFVGPSGCGKSTLLRMIAGLetiTSGDLFIGEKRMNDTPPAE---RGVGMVFQSYALYPHLSVAENMSFgLKLAGA 105
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGR---IQGNNFTGTILANNRKPTKqilKRTGFVTQDDILYPHLTVRETLVF-CSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 106 KKEVINQRVNQVAEVLqLAHLLDRK----------PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIE 175
Cdd:PLN03211 170 PKSLTKQEKILVAESV-ISELGLTKcentiignsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1578826625 176 ISRLHKRlGRTMIYVTHD-QVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:PLN03211 249 LGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-220 |
1.27e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.21 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 22 INLEIHEGEFVVFVGPSGCGKSTLLRMIAGLeTITSGDLFIGEKRMNDTPPAE----RG---------VGM-VFQSYALY 87
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMpVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 88 PHlsvaenmsfglklAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRV-------AIGRTLVAEPSVFLLDEP 160
Cdd:PRK03695 94 QP-------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 161 LSNLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-211 |
2.21e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.14 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITS--GDLFI-GE----KRMNDTppAERGV 77
Cdd:PRK13549 7 EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFeGEelqaSNIRDT--ERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSYALYPHLSVAENMSFGLKLagAKKEVIN-----QRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNEI--TPGGIMDydamyLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 153 SVFLLDEPLSNLDAAlRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:PRK13549 163 RLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-217 |
2.36e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 86.31 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAW-GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigekRMNDTPPAE------- 74
Cdd:PRK10790 340 RIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI-----RLDGRPLSSlshsvlr 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 75 RGVGMVFQSYALYPHlSVAENMSFGlklagakKEVINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVA 143
Cdd:PRK10790 415 QGVAMVQQDPVVLAD-TFLANVTLG-------RDISEEQVWQALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1578826625 144 IGRTLVAEPSVFLLDEPLSNLDAALR--VQMRIEISRLHKrlgrTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEqaIQQALAAVREHT----TLVVIAH-RLSTIVEADTILVLHRGQAVEQGT 557
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-216 |
3.61e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 86.37 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 17 VVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFigekrmndtppAERGVGMVFQSyALYPHLSVAENM 96
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 97 SF-----GLKLAGAkkevinQRVNQV-AEVLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
Cdd:PTZ00243 742 LFfdeedAARLADA------VRVSQLeADLAQLGGGLEteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 167 AL--RVQMRIEISRLHkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:PTZ00243 816 HVgeRVVEECFLGALA---GKTRVLATH-QVHVVPRADYVVALGDGRVEFSG 863
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-218 |
5.81e-18 |
|
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: 81.77 E-value: 5.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 18 VSKDINLEIHEGEFVVFVGPSGCGKST----LLRMIagleTITSGDLFIGEKRMNDTPPAE--RGVGMVFQSyalyPHL- 90
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQD----PVLf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 91 --SVAENM-SFG----------LKLAGAKKEVINQrvnqvaeVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:cd03244 91 sgTIRSNLdPFGeysdeelwqaLERVGLKEFVESL-------PGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 158 DEPLSNLDAALRVQMRIEISrlHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:cd03244 164 DEATASVDPETDALIQKTIR--EAFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-211 |
5.93e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 84.88 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGD---LFIGE----KRMNDTppAERG 76
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDgeiYWSGSplkaSNIRDT--ERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 VGMVFQSYALYPHLSVAENMSFG--LKLAGAKKE--VINQRVNQVAEVLQLAHLLDRKPKA-LSGGQRQRVAIGRTLVAE 151
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGneITLPGGRMAynAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 152 PSVFLLDEPLSNLDAAlRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:TIGR02633 160 ARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-225 |
6.54e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.35 E-value: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 22 INLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPP---AERGVGMVFQSYALYPHLSVAEN--- 95
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqiARMGVVRTFQHVRLFREMTVIENllv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 96 -----MSFGLkLAG---------AKKEVInQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
Cdd:PRK11300 104 aqhqqLKTGL-FSGllktpafrrAESEAL-DRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 162 SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK11300 182 AGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-221 |
7.28e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.88 E-value: 7.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 2 ASVQLQNVTKAWGD--VVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGV 77
Cdd:PRK11160 337 VSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSYALYPHlSVAENmsfgLKLAGAKKevinqRVNQVAEVLQ---LAHLLDRKP----------KALSGGQRQRVAI 144
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDN----LLLAAPNA-----SDEALIEVLQqvgLEKLLEDDKglnawlgeggRQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMrIEISRLHKRlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQI-LELLAEHAQ-NKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-192 |
9.79e-18 |
|
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: 80.61 E-value: 9.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 8 NVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigekRMNDTPPAE------RGVGMVF 81
Cdd:cd03231 5 ELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-----LLNGGPLDFqrdsiaRGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSYALYPHLSVAENMSFGLKLAGakKEVINQRVNQVAevlqLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
Cdd:cd03231 80 HAPGIKTTLSVLENLRFWHADHS--DEQVEEALARVG----LNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|.
gi 1578826625 162 SNLDAAlRVQMRIEISRLHKRLGRTMIYVTH 192
Cdd:cd03231 154 TALDKA-GVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-260 |
1.09e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.37 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 17 VVSkDINLEIHEGEFVVFVGPSGCGKS-TLLRMIAGLET----ITSGD-LFIGEKRMNDTPPAERGV-----GMVFQS-- 83
Cdd:PRK15134 24 VVN-DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDiRFHGESLLHASEQTLRGVrgnkiAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSV----AENMSF--GLKLAGAKKEVIN--QRVNqvaeVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
Cdd:PRK15134 103 VSLNPLHTLekqlYEVLSLhrGMRREAARGEILNclDRVG----IRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 156 LLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIG 235
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLN 258
|
250 260
....*....|....*....|....*....
gi 1578826625 236 S-PKMNFLPVKVTAVA---IDQVQVELPM 260
Cdd:PRK15134 259 SePSGDPVPLPEPASPlldVEQLQVAFPI 287
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-211 |
1.32e-17 |
|
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: 84.22 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAW-GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETItsgdlFIGEKRmndtPPAERGVGMVFQS 83
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD-----FNGEAR----PQPGIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 YALYPHLSVAENMSFGLklaGAKKEVINqRVNQV--------AEVLQL---------------AHLLDRK---------- 130
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGV---AEIKDALD-RFNEIsakyaepdADFDKLaaeqaelqeiidaadAWDLDSQleiamdalrc 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 131 P------KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlrvqmriEISRLHKRLGR---TMIYVTHDQVEAMTLA 201
Cdd:TIGR03719 153 PpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-------SVAWLERHLQEypgTVVAVTHDRYFLDNVA 225
|
250
....*....|
gi 1578826625 202 DKIVVLDAGR 211
Cdd:TIGR03719 226 GWILELDRGR 235
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
4-210 |
1.44e-17 |
|
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: 80.45 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWG-DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLF-----IGEKRMNDTPPAERG- 76
Cdd:cd03290 1 VQVTNGYFSWGsGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknESEPSFEATRSRNRYs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 VGMVFQSYALYpHLSVAENMSFGLKLAgakkeviNQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIG 145
Cdd:cd03290 81 VAYAAQKPWLL-NATVEENITFGSPFN-------KQRYKAVTDACSLQPDIDLLPFGdqteigerginLSGGQRQRICVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1578826625 146 RTLVAEPSVFLLDEPLSNLDAALRVQ-MRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAG 210
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-221 |
1.69e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.86 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPA--ERGVGMVFQSYALYpHLSVAENMSF 98
Cdd:PRK13657 353 DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVVFQDAGLF-NRSIEDNIRV 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 99 GlklagaKKEVINQRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
Cdd:PRK13657 432 G------RPDATDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 168 LRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK13657 506 TEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDEL 556
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
14-224 |
1.81e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 80.84 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 14 GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLE--TITSGDLFIGEKRMNDTPPAER---GVGMVFQsyalYP 88
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERahlGIFLAFQ----YP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 89 -HLSVAENMSFgLKLAGAKK---------------EVINQRVNQVAevLQlAHLLDRK-PKALSGGQRQRVAIGRTLVAE 151
Cdd:CHL00131 94 iEIPGVSNADF-LRLAYNSKrkfqglpeldpleflEIINEKLKLVG--MD-PSFLSRNvNEGFSGGEKKRNEILQMALLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 152 PSVFLLDEPLSNLDA-ALRVqMRIEISRLhKRLGRTMIYVTHDQveamTLADKIV-----VLDAGRVAQVG-----KPLE 220
Cdd:CHL00131 170 SELAILDETDSGLDIdALKI-IAEGINKL-MTSENSIILITHYQ----RLLDYIKpdyvhVMQNGKIIKTGdaelaKELE 243
|
....
gi 1578826625 221 LYHY 224
Cdd:CHL00131 244 KKGY 247
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-212 |
2.61e-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: 79.23 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGletITSGDLFI-GEKRMNDTPPAErgVGMVFQSYALY--------PHL 90
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVeGDIHYNGIPYKE--FAEKYPGEIIYvseedvhfPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 91 SVAENMSFGLKLAGakkeviNQRVnqvaevlqlahlldrkpKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
Cdd:cd03233 99 TVRETLDFALRCKG------NEFV-----------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1578826625 171 QMRIEISRLHKRLGRT-MIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03233 156 EILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-165 |
3.47e-17 |
|
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: 82.68 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMndtppaergVGMVFQS 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK---------LAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 Y-ALYPHLSVAENMSFGLKLAGAKKEVINQR----------VNQvaevlqlahllDRKPKALSGGQRQRVAIGRTLVAEP 152
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLDIIKLGKREIPSRayvgrfnfkgSDQ-----------QKKVGQLSGGERNRVHLAKTLKSGG 462
|
170
....*....|...
gi 1578826625 153 SVFLLDEPLSNLD 165
Cdd:TIGR03719 463 NVLLLDEPTNDLD 475
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-192 |
4.00e-17 |
|
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: 77.96 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 14 GDVVVsKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIgekrmndtpPAERGVGMVFQSyalyPHLSva 93
Cdd:cd03223 13 GRVLL-KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR----PYLP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 enmsfglklAGAKKEvinqrvnqvaevlQLAHLLDRkpkALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMR 173
Cdd:cd03223 77 ---------LGTLRE-------------QLIYPWDD---VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|....*....
gi 1578826625 174 ieisRLHKRLGRTMIYVTH 192
Cdd:cd03223 132 ----QLLKELGITVISVGH 146
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-225 |
6.48e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 6.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTP-----PAERGVGMVFQS-YA-LYPHLSV 92
Cdd:PRK10261 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgklqALRRDIQFIFQDpYAsLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 AENMSFGLKLAGAKKEVINQRvnQVAEVLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAL 168
Cdd:PRK10261 421 GDSIMEPLRVHGLLPGKAAAA--RVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 169 RVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-221 |
1.25e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.06 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 2 ASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN--DTPPAERGVGM 79
Cdd:PRK10575 10 TTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 80 VFQSYALYPHLSVAENMSFG-------LKLAGAKKEvinQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAIGrypwhgaLGRFGAADR---EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 153 SVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-226 |
1.38e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKS----TLLRMIAGLETITSGDLFIGEKR------MNDTPPAE----RG--VGMVFQS 83
Cdd:PRK10261 33 RNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLLRRRsrqvieLSEQSAAQmrhvRGadMAMIFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 84 --YALYPHLSVAENMSFGLKL-AGAKKE---VINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:PRK10261 113 pmTSLNPVFTVGEQIAESIRLhQGASREeamVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
Cdd:PRK10261 193 DEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-213 |
1.54e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.73 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 18 VSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN-DTPPAERGVGMVF-----QSYALYPHLS 91
Cdd:PRK11288 268 LREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLcpedrKAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 92 VAENMSFGLKLAGAK-KEVINQRVNQVAEVLQLAHLLDRKPKA------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
Cdd:PRK11288 348 VADNINISARRHHLRaGCLINNRWEAENADRFIRSLNIKTPSReqlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 165 DaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
Cdd:PRK11288 428 D----VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-212 |
1.92e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.76 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGlETITSGDLFIGEK-----RMNDTPP--- 72
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLLDDGRIIYEQdlivaRLQQDPPrnv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 73 --------AErGVGMVFQSYALYPHLS--VAENMSFGL--KLAGAKKEVINQ-------RVNQVAEVLQLAHllDRKPKA 133
Cdd:PRK11147 80 egtvydfvAE-GIEEQAEYLKRYHDIShlVETDPSEKNlnELAKLQEQLDHHnlwqlenRINEVLAQLGLDP--DAALSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlrvqmRIE-ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-----TIEwLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-210 |
2.35e-16 |
|
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: 76.51 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLET--ITSGDLFIGEKRMNDTPPaeRGVGMVFQSYALYPHLSVAENMS 97
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQ--RSTGYVEQQDVHSPNLTVREALR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 98 FGLKLAGakkevinqrvnqvaevlqlahlldrkpkaLSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvQMRIEIS 177
Cdd:cd03232 102 FSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS----QAAYNIV 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 1578826625 178 RLHKRL---GRTMIYVTHdQVEAMTLA--DKIVVLDAG 210
Cdd:cd03232 149 RFLKKLadsGQAILCTIH-QPSASIFEkfDRLLLLKRG 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-212 |
2.35e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 8 NVTKAWGDVVVsKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAER---GVGMV---F 81
Cdd:COG3845 264 SVRDDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYIpedR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSYALYPHLSVAENMSFGL--KLAGAKKEVINQR-VNQVAEvlqlaHLLDR----------KPKALSGGQRQRVAIGRTL 148
Cdd:COG3845 343 LGRGLVPDMSVAENLILGRyrRPPFSRGGFLDRKaIRAFAE-----ELIEEfdvrtpgpdtPARSLSGGNQQKVILAREL 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 149 VAEPSVFLLDEPLSNLDAAlrvqmriEISRLHKRL------GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVG-------AIEFIHQRLlelrdaGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-216 |
4.32e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 79.37 E-value: 4.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigekRMNDTPPAE------RG-VGMVFQSYALYPHlSV 92
Cdd:PRK10789 332 ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI-----RFHDIPLTKlqldswRSrLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 AENMSFGLklAGAKKEvinqrvnQVAEVLQLAHLLD---RKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLD 158
Cdd:PRK10789 406 ANNIALGR--PDATQQ-------EIEHVARLASVHDdilRLPQGydtevgergvmLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 159 EPLSNLDAalrvqmRIEISRLHK----RLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:PRK10789 477 DALSAVDG------RTEHQILHNlrqwGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRG 531
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
15-195 |
5.63e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.76 E-value: 5.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 15 DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDL-FIGEKRMNDTPPAERGVGMVFQSYALYPHLSVA 93
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSFGLKLAGAkkeviNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD--AALRVQ 171
Cdd:PRK13540 93 ENCLYDIHFSPG-----AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDelSLLTII 167
|
170 180
....*....|....*....|....
gi 1578826625 172 MRIEisrLHKRLGRTMIYVTHDQV 195
Cdd:PRK13540 168 TKIQ---EHRAKGGAVLLTSHQDL 188
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-211 |
8.71e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.48 E-value: 8.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 6 LQNVTKAWGDVVVS-KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFI-GEKRMNDTPPAERG-VGMVFQ 82
Cdd:PRK10522 325 LRNVTFAYQDNGFSvGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVTAEQPEDYRKlFSAVFT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 SYALYPHLsvaenmsfglkLAGAKKEVINQRVNQVAEVLQLAH--------LLDRKpkaLSGGQRQRVAIGRTLVAEPSV 154
Cdd:PRK10522 405 DFHLFDQL-----------LGPEGKPANPALVEKWLERLKMAHkleledgrISNLK---LSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQvEAMTLADKIVVLDAGR 211
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQ 526
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-222 |
1.43e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.48 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAWgDVVVSK----DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGletitsgdlfigekrmnDTPPAERGVG 78
Cdd:PLN03232 614 AISIKNGYFSW-DSKTSKptlsDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSV 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 79 MVFQSYALYPHLS------VAENMSFGLKLAgakkeviNQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQR 141
Cdd:PLN03232 676 VIRGSVAYVPQVSwifnatVRENILFGSDFE-------SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 142 VAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRlHKRLGRTMIYVThDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PLN03232 749 VSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
.
gi 1578826625 222 Y 222
Cdd:PLN03232 827 S 827
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-217 |
2.39e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 76.98 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGletitSGDLFIGEKRMNDTPPA----ERG 76
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAG-----ELPLLSGERQSQFSHITrlsfEQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 VGMVFQSYALYPH--LSVAENmSFGLKLAgakkEVI------NQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTL 148
Cdd:PRK10938 76 QKLVSDEWQRNNTdmLSPGED-DTGRTTA----EIIqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGE 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-221 |
3.93e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.09 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDtpPAER-------- 75
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD--ARHRravcpria 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 76 ----GVGMvfqsyALYPHLSVAENMSFGLKLAGAKKEvinQRVNQVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTL 148
Cdd:NF033858 80 ympqGLGK-----NLYPTLSVFENLDFFGRLFGQDAA---ERRRRIDELLRatgLAPFADRPAGKLSGGMKQKLGLCCAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHK-RLGRTMIYVTHDQVEAMTLaDKIVVLDAGRVAQVGKPLEL 221
Cdd:NF033858 152 IHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAeRPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-165 |
6.82e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.93 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGE--KrmndtppaergVGMVF 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtvK-----------LAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSY-ALYPHLSVAENMSFGLklagakkEVI---NQRVNQVAEV---------LQlahlldRKPKALSGGQRQRVAIGRTL 148
Cdd:PRK11819 394 QSRdALDPNKTVWEEISGGL-------DIIkvgNREIPSRAYVgrfnfkggdQQ------KKVGVLSGGERNRLHLAKTL 460
|
170
....*....|....*..
gi 1578826625 149 VAEPSVFLLDEPLSNLD 165
Cdd:PRK11819 461 KQGGNVLLLDEPTNDLD 477
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-192 |
7.15e-15 |
|
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: 75.94 E-value: 7.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 14 GDVVVSKdINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEK-RMNDTPpaER---GVGmVFQSYALYPH 89
Cdd:TIGR00954 464 GDVLIES-LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKgKLFYVP--QRpymTLG-TLRDQIIYPD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 90 LSvaENMSfglklagaKKEVINQRVNQVAEVLQLAHLLDRK---------PKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:TIGR00954 540 SS--EDMK--------RRGLSDKDLEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 1578826625 161 LSnldaALRVQMRIEISRLHKRLGRTMIYVTH 192
Cdd:TIGR00954 610 TS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-193 |
7.20e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.93 E-value: 7.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWG-DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETItsgdlFIGEKRmndtpPAErG--VGMVF 81
Cdd:PRK11819 8 TMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE-----FEGEAR-----PAP-GikVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSYALYPHLSVAENMSFGLklaGAKKEVINqRVNQVAE-----------------VLQL------AHLLDRK-------- 130
Cdd:PRK11819 77 QEPQLDPEKTVRENVEEGV---AEVKAALD-RFNEIYAayaepdadfdalaaeqgELQEiidaadAWDLDSQleiamdal 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 131 --P------KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvqmriE-ISRLHKRLGR---TMIYVTHD 193
Cdd:PRK11819 153 rcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------EsVAWLEQFLHDypgTVVAVTHD 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-221 |
7.26e-15 |
|
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: 76.52 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAW--GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIgekrmndtppaERGVGMV 80
Cdd:TIGR00957 636 SITVHNATFTWarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----------KGSVAYV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 81 FQSyALYPHLSVAENMSFGLKLagakKEVINQRVNQVAEVLQLAHLL---DR-----KPKALSGGQRQRVAIGRTLVAEP 152
Cdd:TIGR00957 705 PQQ-AWIQNDSLRENILFGKAL----NEKYYQQVLEACALLPDLEILpsgDRteigeKGVNLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 153 SVFLLDEPLSNLDAALRVQMRIEISRLHKRL-GRTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-226 |
8.87e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.20 E-value: 8.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAwGDVVVSKDINLEIHEGEFVVFVGPSGCGKStlLRMIAGLETI------TSGDLFIGEKRMndTPPAERG- 76
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILpagvrqTAGRVLLDGKPV--APCALRGr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 -VGMVFQS--YALYPHLSVAENMSFGLKLAGakKEVINQRVNQVAEVLQL---AHLLDRKPKALSGGQRQRVAIGRTLVA 150
Cdd:PRK10418 80 kIATIMQNprSAFNPLHTMHTHARETCLALG--KPADDATLTAALEAVGLenaARVLKLYPFEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 151 EPSVFLLDEPLSNLDAAlrVQMRIE--ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
Cdd:PRK10418 158 EAPFIIADEPTTDLDVV--AQARILdlLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-225 |
1.07e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.01 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 22 INLEIHEGEFVVFVGPSGCGKSTLLRMIAGL----ETITSGDLFIGEKRMNDTPPAER------GVGMVFQS--YALYPH 89
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 90 LSVAENMSFGLKL--AGAKKEvinqRVNQVAEVLQL------AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
Cdd:PRK11022 106 YTVGFQIMEAIKVhqGGNKKT----RRQRAIDLLNQvgipdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 162 SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-207 |
1.15e-14 |
|
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: 75.21 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 28 EGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigekrmnDTPPAERGVGMVFQSYALYPHLS-VAENmsfGLKLA--- 103
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKRFRGTELQDYFKkLANG---EIKVAhkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 104 -----------GAKKEV---INQR--VNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaa 167
Cdd:COG1245 167 qyvdlipkvfkGTVRELlekVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD-- 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1578826625 168 lrVQMRIEISRLHKRL---GRTMIYVTHDQveAM--TLADKIVVL 207
Cdd:COG1245 245 --IYQRLNVARLIRELaeeGKYVLVVEHDL--AIldYLADYVHIL 285
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-243 |
1.42e-14 |
|
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: 75.44 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFI-GEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAG 104
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 105 AKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLhKRLG 184
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI-IREG 2120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 185 RTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGF-IGSPKMNFLP 243
Cdd:TIGR01257 2121 RAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMkIKSPKDDLLP 2180
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
3-216 |
1.83e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 72.54 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAW----------GDVVVSK----------DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfi 62
Cdd:PRK13546 4 SVNIKNVTKEYriyrtnkermKDALIPKhknktffaldDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 63 geKRMNDtppaergVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRV 142
Cdd:PRK13546 82 --DRNGE-------VSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 143 AIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:PRK13546 153 GFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-221 |
2.21e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 74.28 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTllrmIAGLET----ITSGDLFIGEKRMND-TPPAERG-VGMVFQSYALYpHLSVA 93
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKST----IANLLTrfydIDEGEILLDGHDLRDyTLASLRNqVALVSQNVHLF-NDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSFglklagAKKEVINQRvnQVAEVLQLAHLLDRKPK--------------ALSGGQRQRVAIGRTLVAEPSVFLLDE 159
Cdd:PRK11176 435 NNIAY------ARTEQYSRE--QIEEAARMAYAMDFINKmdngldtvigengvLLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 160 PLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK11176 507 ATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-207 |
2.78e-14 |
|
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: 72.01 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 28 EGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigekrmnDTPPAERGVGMVFQSYALYPHLS--VAENMSFGLK---- 101
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--------DDPPDWDEILDEFRGSELQNYFTklLEGDVKVIVKpqyv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 102 ------LAGAKKEVINQR-----VNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
Cdd:cd03236 97 dlipkaVKGKVGELLKKKdergkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 1578826625 171 QMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVL 207
Cdd:cd03236 177 NAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-212 |
4.31e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAErGV--GMVFQSY-----ALYPHLSV 92
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD-GLanGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 AENMSFGlklagAKKEVINQ--RVNQVAEVLQLAHLLD----RKPKA------LSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:PRK10762 348 KENMSLT-----ALRYFSRAggSLKHADEQQAVSDFIRlfniKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 161 LSNLDaalrVQMRIEISRL---HKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:PRK10762 423 TRGVD----VGAKKEIYQLinqFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-165 |
4.46e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.65 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 22 INLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIgekrmnDTPPAERGVGMVFQSY-----ALYPHLSVAENM 96
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI------DGKTATRGDRSRFMAYlghlpGLKADLSTLENL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 97 SFGLKLAGAKKEvinQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
Cdd:PRK13543 104 HFLCGLHGRRAK---QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-221 |
1.11e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.85 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGletitsgdlfigekrmnDTPPAERGVGMVFQSYALYPHLS------VAE 94
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLG-----------------ELPPRSDASVVIRGTVAYVPQVSwifnatVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 95 NMSFGLKLAGAkkevinqRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:PLN03130 698 NILFGSPFDPE-------RYERAIDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 164 LDAALRVQ-----MRIEISrlhkrlGRTMIYVThDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PLN03130 771 LDAHVGRQvfdkcIKDELR------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-207 |
1.24e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.37 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWG---DVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKR-MNDTPPA--ERGV 77
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnLKDINLKwwRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSYALYPHlSVAENMSFGL--------------------------------KLAGA---------KKEVINQRVN- 115
Cdd:PTZ00265 463 GVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscraKCAGDlndmsnttdSNELIEMRKNy 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 116 ------QVAEVLQ--LAH------------LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIE 175
Cdd:PTZ00265 542 qtikdsEVVDVSKkvLIHdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250 260 270
....*....|....*....|....*....|..
gi 1578826625 176 ISRLHKRLGRTMIYVTHdQVEAMTLADKIVVL 207
Cdd:PTZ00265 622 INNLKGNENRITIIIAH-RLSTIRYANTIFVL 652
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-248 |
1.44e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.45 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGlETITSGDLFIGEKRMNDTPPAE-----RG-VGMVFQSYALYPHLSVA 93
Cdd:TIGR00956 78 KPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS-NTDGFHIGVEGVITYDGITPEEikkhyRGdVVYNAETDVHFPHLTVG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSFGLKLAG--------AKKEVINQRVNQVAEVLQLAHLLDRKP-----KALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:TIGR00956 157 ETLDFAARCKTpqnrpdgvSREEYAKHIADVYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 161 LSNLDAALRVQMrIEISRLHKRLGRTMIYVTHDQV--EAMTLADKIVVLDAGRvaqvgkplELYHYPADRFVAGFIgspK 238
Cdd:TIGR00956 237 TRGLDSATALEF-IRALKTSANILDTTPLVAIYQCsqDAYELFDKVIVLYEGY--------QIYFGPADKAKQYFE---K 304
|
250
....*....|..
gi 1578826625 239 MNFL--PVKVTA 248
Cdd:TIGR00956 305 MGFKcpDRQTTA 316
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-210 |
1.69e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.57 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDL-FIGEKRMNDTPPA--ERGVGMVF 81
Cdd:PRK10762 6 QLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlYLGKEVTFNGPKSsqEAGIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 82 QSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEVLqLAHL-LDRKPKALSG----GQRQRVAIGRTLVAEPSVFL 156
Cdd:PRK10762 86 QELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKL-LARLnLRFSSDKLVGelsiGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1578826625 157 LDEPLSNL-----DAALRVqmrieISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:PRK10762 165 MDEPTDALtdtetESLFRV-----IREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-218 |
1.85e-13 |
|
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: 71.37 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 22 INLEIHEGEfVVF-VGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMN-DTPPAER---GVgmVFQSYALYPHlsvaenm 96
Cdd:COG4615 351 IDLTIRRGE-LVFiVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTaDNREAYRqlfSA--VFSDFHLFDR------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 97 sfglkLAGAKKEVINQRVNQVAEVLQLAH--------LLDRkpkALSGGQRQRVAIgrtLVA---EPSVFLLDEPLSNLD 165
Cdd:COG4615 421 -----LLGLDGEADPARARELLERLELDHkvsvedgrFSTT---DLSQGQRKRLAL---LVAlleDRPILVFDEWAADQD 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 166 AALRvqmRI---EI-SRLhKRLGRTMIYVTHDQvEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:COG4615 490 PEFR---RVfytELlPEL-KARGKTVIAISHDD-RYFDLADRVLKMDYGKLVELTGP 541
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
113-207 |
1.45e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 113 RVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRL--GRTMIYV 190
Cdd:PRK13409 192 KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD----IRQRLNVARLIRELaeGKYVLVV 267
|
90
....*....|....*..
gi 1578826625 191 THDQVEAMTLADKIVVL 207
Cdd:PRK13409 268 EHDLAVLDYLADNVHIA 284
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
283-355 |
2.76e-12 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 61.48 E-value: 2.76e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 283 LGIRPEHLLPSDIADViLEGEVQVVEQLGNETQIHIQIPSIRQNLVYRQS-DVVLVEEGATFAIGLPPERCHLF 355
Cdd:pfam08402 1 LAIRPEKIRLAAAANG-LSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNaHARPPAPGDRVGLGWDPEDAHVL 73
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
89-208 |
2.97e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 89 HLSVAENMSFGlklagaKKEVINQRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:PTZ00265 1309 NMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLL 1382
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLD 208
Cdd:PTZ00265 1383 DEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFN 1432
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-210 |
4.03e-12 |
|
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: 66.03 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 18 VSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGlETITSGDLFIGEKRMNDTPpaergvgmvfQSYALYPHlSVAENMS 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILG-ELEPSEGKIKHSGRISFSS----------QFSWIMPG-TIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 98 FGLKLAgakkeviNQRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
Cdd:cd03291 120 FGVSYD-------EYRYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1578826625 167 AlrVQMRIEISRLHKRLG-RTMIYVThDQVEAMTLADKIVVLDAG 210
Cdd:cd03291 193 F--TEKEIFESCVCKLMAnKTRILVT-SKMEHLKKADKILILHEG 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-214 |
5.52e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 5.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAER-GVGMVF-----QSYALYPHLSVA 93
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMS------FGLKLAGAKKEVINQRVNQvAEVLQLAHLlDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaa 167
Cdd:PRK15439 360 WNVCalthnrRGFWIKPARENAVLERYRR-ALNIKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD-- 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1578826625 168 lrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQ 214
Cdd:PRK15439 436 --VSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEISG 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-213 |
5.65e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE---RGVGMVFQ---SYALYPHLSVA 93
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainHGFALVTEerrSTGIYAYLDIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENM----------SFGLkLAGAKKEVINQRVNQVAEVLQLAHllDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:PRK10982 345 FNSlisnirnyknKVGL-LDNSRMKSDTQWVIDSMRVKTPGH--RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1578826625 164 LDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-165 |
7.76e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 63.74 E-value: 7.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 36 GPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTppAERGVGMVFQSYALYPHLSVAENMSFGlklagakKEVINQRVN 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI--AKPYCTYIGHNLGLKLEMTVFENLKFW-------SEIYNSAET 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 116 QVAEV--LQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
Cdd:PRK13541 104 LYAAIhyFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-210 |
8.85e-12 |
|
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: 66.86 E-value: 8.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 18 VSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGlETITSGDLFIGEKRMNDTPpaergvgmvfQSYALYPHlSVAENMS 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG-ELEPSEGKIKHSGRISFSP----------QTSWIMPG-TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 98 FGLKLAGAK-KEVINqrVNQVAEVLQLAHLLDRKPK-----ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaaLRVQ 171
Cdd:TIGR01271 509 FGLSYDEYRyTSVIK--ACQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD--VVTE 584
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1578826625 172 MRIEISRLHKRL-GRTMIYVThDQVEAMTLADKIVVLDAG 210
Cdd:TIGR01271 585 KEIFESCLCKLMsNKTRILVT-SKLEHLKKADKILLLHEG 623
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-165 |
9.52e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKrmndtppAERGvgmVFQSY 84
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK-------LEVA---YFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 85 --ALYPHLSVAENmsfglkLAGAKKEV-INQRVNQVAEVLQ--LAH-LLDRKP-KALSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:PRK11147 391 raELDPEKTVMDN------LAEGKQEVmVNGRPRHVLGYLQdfLFHpKRAMTPvKALSGGERNRLLLARLFLKPSNLLIL 464
|
....*...
gi 1578826625 158 DEPLSNLD 165
Cdd:PRK11147 465 DEPTNDLD 472
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-192 |
1.77e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 66.02 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 29 GEFVVFVGPSGCGKSTLLRMIAGLETitsGDLFIGEKRMNDTPPAE----RGVGMVFQSYALYPHLSVAENMSFG--LKL 102
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKT---GGYIEGDIRISGFPKKQetfaRISGYCEQNDIHSPQVTVRESLIYSafLRL 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 103 AgakKEVINQR----VNQVAEVLQLAHLLDR-----KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA-ALRVQM 172
Cdd:PLN03140 983 P---KEVSKEEkmmfVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDArAAAIVM 1059
|
170 180
....*....|....*....|
gi 1578826625 173 RieISRLHKRLGRTMIYVTH 192
Cdd:PLN03140 1060 R--TVRNTVDTGRTVVCTIH 1077
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-208 |
2.42e-11 |
|
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: 61.82 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 25 EIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLfigekrmndtppaergvgmvfqsyalyphlsvaenmsfglKLAG 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND----------------------------------------EWDG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 105 AKKEVINQRVNqvaevlqlahlldrkpkaLSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLG 184
Cdd:cd03222 61 ITPVYKPQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|....
gi 1578826625 185 RTMIYVTHDQVEAMTLADKIVVLD 208
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-225 |
3.52e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.67 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 1 MASVQLQNVT----KAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGletITSGDLFIGEKRM--ND----- 69
Cdd:PRK15093 1 MPLLDIRNLTiefkTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG---VTKDNWRVTADRMrfDDidllr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 70 -TPPAER-----GVGMVFQSyalyPHLSVAENMSFGLKLA---------GAKKEVINQRVNQVAEVLQLAHLLDRK---- 130
Cdd:PRK15093 78 lSPRERRklvghNVSMIFQE----PQSCLDPSERVGRQLMqnipgwtykGRWWQRFGWRKRRAIELLHRVGIKDHKdamr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 131 --PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLD 208
Cdd:PRK15093 154 sfPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLY 233
|
250 260
....*....|....*....|
gi 1578826625 209 AGRVAQVGKPLELY---HYP 225
Cdd:PRK15093 234 CGQTVETAPSKELVttpHHP 253
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-218 |
4.42e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.92 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 17 VVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLET---ITSGDLFIGEKRMNDTPPAERGVGMVFQSYALYPH---- 89
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggAPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQaaqp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 90 ---LSVAENMSFG----LKLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTL---------VAEPS 153
Cdd:PRK13547 95 afaFSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1578826625 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-221 |
4.67e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.60 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 3 SVQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCG--KSTLLRMIAGLETITSGDLFI----GEKRMNDTPPAERG 76
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*twcaNRRALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 VgmvfqSYALYPHLSVAENM-SFGLKLAGAKKEViNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
Cdd:NF000106 93 V-----R*GRRESFSGRENLyMIGR*LDLSRKDA-RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1578826625 156 LLDEPLSNLDAALRVQMRIEIsRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEV-RSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-211 |
7.87e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.27 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 5 QLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITS--GD-LFIGE----KRMNDTppAERGV 77
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEiLFDGEvcrfKDIRDS--EALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 78 GMVFQSYALYPHLSVAENMSFGLKLagAKKEVIN-QRVNQVAEVLqLAHL-LDRKPKALSG----GQRQRVAIGRTLVAE 151
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNER--AKRGVIDwNETNRRAREL-LAKVgLDESPDTLVTdigvGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 152 PSVFLLDEPLSNLD----AALrvqmrIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:NF040905 158 VKLLILDEPTAALNeedsAAL-----LDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-205 |
1.60e-10 |
|
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: 60.35 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLlrmiaGLETITSGdlfiGEKRMNDT--PPAERGVGMVFQSY-----ALYPHLSV 92
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKSSL-----AFDTIYAE----GQRRYVESlsAYARQFLGQMDKPDvdsieGLSPAIAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 AENMS-----------------FGLKLAgakKEVINQRVNQVAEVlQLAHL-LDRKPKALSGGQRQRVAIGRTLVAEPS- 153
Cdd:cd03270 83 DQKTTsrnprstvgtvteiydyLRLLFA---RVGIRERLGFLVDV-GLGYLtLSRSAPTLSGGEAQRIRLATQIGSGLTg 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 154 -VFLLDEPLSNLDAALRVQMRIEISRLhKRLGRTMIYVTHDQvEAMTLADKIV 205
Cdd:cd03270 159 vLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHVI 209
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-212 |
2.15e-10 |
|
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: 61.76 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGL-ETITSGDLFIGEKRMNDTPPA---ERGVGMVFQS---YALYPHLSVA 93
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAqaiRAGIAMVPEDrkrHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSFGLKLAGAKKEVINQRVNQ--VAEVLQLAHLLDRKP----KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaa 167
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAAELqiIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD-- 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1578826625 168 lrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:TIGR02633 436 --VGAKYEIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-210 |
2.48e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 29 GEFVVFVGPSGCGKSTLLRMIAGLET---ITSGDLFIGEKRMNDTppAERGVGMVFQSYALYPHLSVAENMSFGLKLAGA 105
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDSS--FQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQP 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 106 KKEVINQRVNQVAEVLQLAHLLDRKP-------KALSGGQRQRVAIGRTLVAEPSVFL-LDEPLSNLDAalrvQMRIEIS 177
Cdd:TIGR00956 867 KSVSKSEKMEYVEEVIKLLEMESYADavvgvpgEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS----QTAWSIC 942
|
170 180 190
....*....|....*....|....*....|....*...
gi 1578826625 178 RLHKRL---GRTMIYVTHdQVEAMTLA--DKIVVLDAG 210
Cdd:TIGR00956 943 KLMRKLadhGQAILCTIH-QPSAILFEefDRLLLLQKG 979
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-217 |
2.63e-10 |
|
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: 58.87 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLrmiagLETITSGdlfiGEKRMNDTPPAergvgmvfqsyaLYPHLSVaenmsfg 99
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLV-----NEGLYAS----GKARLISFLPK------------FSRNKLI------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 100 lklagakkeVINQRVNQVAevLQLAHL-LDRKPKALSGGQRQRVAIGRTLVAEP--SVFLLDEPLSNLDAALRVQMRIEI 176
Cdd:cd03238 64 ---------FIDQLQFLID--VGLGYLtLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1578826625 177 SRLhKRLGRTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:cd03238 133 KGL-IDLGNTVILIEHN-LDVLSSADWIIDFGPGSGKSGGK 171
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-212 |
4.44e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKrmndtppAErgVGMVFQ- 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN-------AN--IGYYAQd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 SYALYPH-LSVAENMSfglklaGAKKEVIN-QRVNQVaevlqLAHLL------DRKPKALSGGQRQRVAIGRTLVAEPSV 154
Cdd:PRK15064 391 HAYDFENdLTLFDWMS------QWRQEGDDeQAVRGT-----LGRLLfsqddiKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1578826625 155 FLLDEPLSNLDaalrvqMR-IEI--SRLHKRLGrTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:PRK15064 460 LVMDEPTNHMD------MEsIESlnMALEKYEG-TLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-216 |
5.12e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.42 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLE--TITSGDLFIGEKRMNDTPPAER---GVGMVFQSYALYPHLSvae 94
Cdd:PRK09580 18 RGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAFQYPVEIPGVS--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 95 NMSFglkLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKAL---------------SGGQRQRVAIGRTLVAEPSVFLLDE 159
Cdd:PRK09580 95 NQFF---LQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCILDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 160 PLSNLDA-ALR-VQMRIEISRLHKrlgRTMIYVTHDQ-VEAMTLADKIVVLDAGRVAQVG 216
Cdd:PRK09580 172 SDSGLDIdALKiVADGVNSLRDGK---RSFIIVTHYQrILDYIKPDYVHVLYQGRIVKSG 228
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
235-290 |
1.30e-09 |
|
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK transport protein.
Pssm-ID: 465563 [Multi-domain] Cd Length: 53 Bit Score: 53.36 E-value: 1.30e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 235 GSPKMNFLPVKVTA--VAIDQVQVELPMPNLQQVWLPVEshnvqVGANMSLGIRPEHL 290
Cdd:pfam17912 1 GSPPMNFLPATVVEdgLLVLGGGVTLPLPEGQVLALKLY-----VGKEVILGIRPEHI 53
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
22-216 |
1.92e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 58.38 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 22 INLEIHEGEFVVFVGPSGCGKSTLLRMIAGLE----TITSGDLFIGEKRMNDTPPAER------GVGMVFQ--SYALYPH 89
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQepSSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 90 LSVAENMSFGL---KLAGAKKEVINQRVNQVAEVL------QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
Cdd:COG4170 106 AKIGDQLIEAIpswTFKGKWWQRFKWRKKRAIELLhrvgikDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEP 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1578826625 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDqVEAMT-LADKIVVLDAGRVAQVG 216
Cdd:COG4170 186 TNAMESTTQAQIFRLLARLNQLQGTSILLISHD-LESISqWADTITVLYCGQTVESG 241
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-218 |
5.21e-09 |
|
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: 55.50 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 18 VSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTP--PAERGVGMVFQSYALYPHlSVAEN 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLTIIPQDPTLFSG-TIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 96 MsfglklagakkEVINQRVN-QVAEVLQLAHLLDRkpkaLSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL----DAALRV 170
Cdd:cd03369 102 L-----------DPFDEYSDeEIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASIdyatDALIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1578826625 171 QMRIEISrlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:cd03369 167 TIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-221 |
6.91e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.65 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 17 VVSKDINLEIHEGEFVVFVGPSGCGKST----LLRM---------IAGLE-------------TITSGD--LFIGEKRMN 68
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRInesaegeiiIDGLNiakiglhdlrfkiTIIPQDpvLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 69 DTPpaergvgmvFQSYAlyphlsvAENMSFGLKLAGAKKEVINQRVnqvaevlQLAHLLDRKPKALSGGQRQRVAIGRTL 148
Cdd:TIGR00957 1380 LDP---------FSQYS-------DEEVWWALELAHLKTFVSALPD-------KLDHECAEGGENLSVGQRQLVCLARAL 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 149 VAEPSVFLLDEPLSNLD--------AALRVQMR-IEISRLHKRLGRTMIYVthdqveamtladKIVVLDAGRVAQVGKPL 219
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDletdnliqSTIRTQFEdCTVLTIAHRLNTIMDYT------------RVIVLDKGEVAEFGAPS 1504
|
..
gi 1578826625 220 EL 221
Cdd:TIGR00957 1505 NL 1506
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-207 |
7.22e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.04 E-value: 7.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPpAERGVGMVFQSYAL---YPHLsVAENM 96
Cdd:PRK15056 24 RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL-QKNLVAYVPQSEEVdwsFPVL-VEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 97 SFG-------LKLAGAKKEvinQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalr 169
Cdd:PRK15056 102 MMGryghmgwLRRAKKRDR---QIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD---- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1578826625 170 VQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVL 207
Cdd:PRK15056 175 VKTEARIISLLRELrdeGKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-216 |
7.35e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIgekrmndtppaERGVGMVFQSYALYPHLSVAENMSFGL 100
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-----------KGSAALIAISSGLNGQLTGIENIELKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 101 KLAGAKKEVINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLh 180
Cdd:PRK13545 111 LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF- 189
|
170 180 190
....*....|....*....|....*....|....*.
gi 1578826625 181 KRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:PRK13545 190 KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
28-205 |
7.87e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 54.92 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 28 EGEFVVFVGPSGCGKSTLlrmIAGLETITSGDLfigekrmndtPPAERGVgmvfqsyALYPHL----SVAENMSFGLKLA 103
Cdd:cd03240 21 FSPLTLIVGQNGAGKTTI---IEALKYALTGEL----------PPNSKGG-------AHDPKLiregEVRAQVKLAFENA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 104 GAKKEVINQRVNQVAEVL-----QLAHLLDRKPKALSGGQRQ------RVAIGRTLVAEPSVFLLDEPLSNLDAALRVQM 172
Cdd:cd03240 81 NGKKYTITRSLAILENVIfchqgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEES 160
|
170 180 190
....*....|....*....|....*....|....
gi 1578826625 173 RIEISRLHKRLG-RTMIYVTHDQvEAMTLADKIV 205
Cdd:cd03240 161 LAEIIEERKSQKnFQLIVITHDE-ELVDAADHIY 193
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-211 |
9.07e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 9.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 6 LQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE---RGVGMVFQ 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaleNGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 83 SYALYPHLSVAENMSFG---LKLAGAKKEVINQRVNQVAEVLQLAhlLDRKPKA--LSGGQRQRVAIGRTLVAEPSVFLL 157
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDID--IDPRAKVatLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 158 DEPLSNLDAAlRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:PRK10982 159 DEPTSSLTEK-EVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-212 |
2.90e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 21 DINLEIHEGEFVVFVGPSGCGKSTLLRMIAGL-ETITSGDLFIGEKRMNDTPPAE---RGVGMVFQS---YALYPHLSVA 93
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 94 ENMSfglkLAGAKKEVINQRVNQVAEVLQLAHLLDR-KPKA---------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:PRK13549 360 KNIT----LAALDRFTGGSRIDDAAELKTILESIQRlKVKTaspelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 164 LDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:PRK13549 436 ID----VGAKYEIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-221 |
3.56e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 17 VVSKDINLEIHEGEFVVFVGPSGCGKSTLL----RMIagletitsgDLFIGEKRMNDTPPAERGVGMVFQSYALYPHL-- 90
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMV---------EVCGGEIRVNGREIGAYGLRELRRQFSMIPQDpv 1394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 91 ----SVAENMSFGLKLAGAkkevinqrvnQVAEVLQLAHLLDR--------KPKALSG------GQRQRVAIGRTLVAEP 152
Cdd:PTZ00243 1395 lfdgTVRQNVDPFLEASSA----------EVWAALELVGLRERvasesegiDSRVLEGgsnysvGQRQLMCMARALLKKG 1464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 153 SVF-LLDEPLSNLDAALRVQmrIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PTZ00243 1465 SGFiLMDEATANIDPALDRQ--IQATVMSAFSAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-197 |
9.93e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 4 VQLQNVTKAWGDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETIT-SGDL-FIGEKRMN-----DTppaERG 76
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLtLFGRRRGSgetiwDI---KKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 77 VGMVFQSYAL-YPHLSVAENM-------SFGLKLAGAKKEviNQRVNQVAEVLQLAHLLDRKP-KALSGGQRQRVAIGRT 147
Cdd:PRK10938 338 IGYVSSSLHLdYRVSTSVRNVilsgffdSIGIYQAVSDRQ--QKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRA 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1578826625 148 LVAEPSVFLLDEPLSNLDAALR--VQMRIEISRLHkrlGRT-MIYVTHDQVEA 197
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLDPLNRqlVRRFVDVLISE---GETqLLFVSHHAEDA 465
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-204 |
2.33e-07 |
|
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: 49.68 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 29 GEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIgekrmndtppaergvgmvfqsyalyphlsvaenmsfglklagakke 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 109 vIN-QRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEIS-----RLHKR 182
Cdd:smart00382 36 -IDgEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSE 114
|
170 180
....*....|....*....|..
gi 1578826625 183 LGRTMIYVTHDQVEAMTLADKI 204
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRR 136
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-165 |
3.21e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 14 GDVVVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEK-RMndtppaergvgMVFQSYalypHLSv 92
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRM-----------AVFSQH----HVD- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 93 aenmsfGLKLAGAKKEVINQRVNQVAEVLQLAHL--------LDRKPK-ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
Cdd:PLN03073 584 ------GLDLSSNPLLYMMRCFPGVPEQKLRAHLgsfgvtgnLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657
|
..
gi 1578826625 164 LD 165
Cdd:PLN03073 658 LD 659
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
90-221 |
5.86e-06 |
|
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: 48.47 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 90 LSVAENMSF--GLKLAGAKKEVINQRVNQVAEVLQ------LAHL-LDRKPKALSGGQRQRVA----IGRTLVAepSVFL 156
Cdd:TIGR00630 436 LSIREAHEFfnQLTLTPEEKKIAEEVLKEIRERLGflidvgLDYLsLSRAAGTLSGGEAQRIRlatqIGSGLTG--VLYV 513
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 157 LDEPLSNLDAalRVQMR-IEISRLHKRLGRTMIYVTHDQvEAMTLADKIVVL------DAGRVAQVGKPLEL 221
Cdd:TIGR00630 514 LDEPSIGLHQ--RDNRRlINTLKRLRDLGNTLIVVEHDE-DTIRAADYVIDIgpgageHGGEVVASGTPEEI 582
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-221 |
6.66e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIgekrmNDTPPAERGVGMVFQSYALYPHLSV--AENMSFGLKLA 103
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMI-----DDCDVAKFGLTDLRRVLSIIPQSPVlfSGTVRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 104 GAKKEVinqrvnQVAEVLQLAHL---LDRKPKAL-----------SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaaLR 169
Cdd:PLN03232 1334 SEHNDA------DLWEALERAHIkdvIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVD--VR 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1578826625 170 VQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PLN03232 1406 TDSLIQRTIREEFKSCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
103-192 |
1.72e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 103 AGAKKEVINQRVNQVAEVLQL--------------------AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
Cdd:PLN03073 294 DGVDKDAVSQRLEEIYKRLELidaytaearaasilaglsftPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTN 373
|
90 100 110
....*....|....*....|....*....|
gi 1578826625 163 NLDaaLRVQMRIEISRLhkRLGRTMIYVTH 192
Cdd:PLN03073 374 HLD--LHAVLWLETYLL--KWPKTFIVVSH 399
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-205 |
4.49e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 24 LEIHEGEFVVFVGPSGCGKSTLLRMIAgletitsgdlfigekrmndtppaergvgmvfqsyalyphLSVAENMSfglklA 103
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------------LALGGAQS-----A 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 104 GAKKEVINQRVNQVAEVLQLAHLLDRkpkaLSGGQRQRVAI----GRTLVAEPSVFLLDEPLSNLDaaLRVQMRI-EISR 178
Cdd:cd03227 52 TRRRSGVKAGCIVAAVSAELIFTRLQ----LSGGEKELSALalilALASLKPRPLYILDEIDRGLD--PRDGQALaEAIL 125
|
170 180
....*....|....*....|....*..
gi 1578826625 179 LHKRLGRTMIYVTHDQvEAMTLADKIV 205
Cdd:cd03227 126 EHLVKGAQVIVITHLP-ELAELADKLI 151
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-221 |
7.73e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 22 INLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTPPAE--RGVGMVFQSYALYphlsvAENMSFG 99
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGIIPQAPVLF-----SGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 100 LKLAGAKKEVinqrvnQVAEVLQLAHLLD---RKPKAL-----------SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
Cdd:PLN03130 1333 LDPFNEHNDA------DLWESLERAHLKDvirRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 166 ----AALRVQMRIEISRLhkrlgrTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PLN03130 1407 vrtdALIQKTIREEFKSC------TMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
89-221 |
1.30e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 89 HLSVAENMSF--GLKLAGAKKEV-------INQRV---NQVAevlqLAHL-LDRKPKALSGGQRQRV----AIGRTLVAe 151
Cdd:COG0178 432 ALSIDEALEFfeNLELTEREAEIaerilkeIRSRLgflVDVG----LDYLtLDRSAGTLSGGEAQRIrlatQIGSGLVG- 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 152 pSVFLLDEP---L-----SNLDAALRvqmrieisRLhKRLGRTMIYVTHDQvEAMTLADKIVvlD----AGR-----VAQ 214
Cdd:COG0178 507 -VLYVLDEPsigLhqrdnDRLIETLK--------RL-RDLGNTVIVVEHDE-DTIRAADYII--DigpgAGEhggevVAQ 573
|
....*..
gi 1578826625 215 vGKPLEL 221
Cdd:COG0178 574 -GTPEEI 579
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
20-45 |
4.41e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 4.41e-04
10 20
....*....|....*....|....*.
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTL 45
Cdd:COG0178 17 KNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
107-205 |
4.57e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 107 KEVI---NQRVNQVAEvLQLAHL-LDRKPKALSGGQRQRVAIGRTLVAEPS--VFLLDEPLSNLDAALRVQMRIEISRLH 180
Cdd:PRK00635 447 EEVLqglKSRLSILID-LGLPYLtPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLR 525
|
90 100
....*....|....*....|....*
gi 1578826625 181 KRlGRTMIYVTHDQvEAMTLADKIV 205
Cdd:PRK00635 526 DQ-GNTVLLVEHDE-QMISLADRII 548
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-45 |
5.29e-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: 41.92 E-value: 5.29e-04
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-205 |
6.66e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDL-FIG---------EKRMNDTPPAERGVGMVFQSYALYPHLSVAEN 95
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtFPGnwqlawvnqETPALPQPALEYVIDGDREYRQLEAQLHDANE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 96 MSFGL-------KLAGAKKEVINQRVNQVAEVLQLAH-LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaa 167
Cdd:PRK10636 104 RNDGHaiatihgKLDAIDAWTIRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD-- 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1578826625 168 lrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIV 205
Cdd:PRK10636 182 --LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
90-205 |
1.09e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 90 LSVAENMSF--GLKLAGAKKEVINQRVNQVAEVLQ------LAHL-LDRKPKALSGG--QRQRVA--IGRTLVAepsV-F 155
Cdd:PRK00349 437 LSIGEALEFfeNLKLSEQEAKIAEPILKEIRERLKflvdvgLDYLtLSRSAGTLSGGeaQRIRLAtqIGSGLTG---VlY 513
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 156 LLDEPlsnldaalrvqmriEISrLHKR--------------LGRTMIYVTHDQvEAMTLADKIV 205
Cdd:PRK00349 514 VLDEP--------------SIG-LHQRdndrlietlkhlrdLGNTLIVVEHDE-DTIRAADYIV 561
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
36-85 |
1.17e-03 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 39.40 E-value: 1.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 36 GPSGCGKSTLLRMIA---GLETITSGDLFigeKRMndtpPAERGVGMV-FQSYA 85
Cdd:PRK04182 7 GPPGSGKTTVARLLAeklGLKHVSAGEIF---REL----AKERGMSLEeFNKYA 53
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-212 |
1.20e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 17 VVSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLE--TITSGDLFIG--EKRMNDTPPA-ERGVGMVFQ---SYALYP 88
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDgkEVDVSTVSDAiDAGLAYVTEdrkGYGLNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 89 HLSVAENMSfglkLAG----AKKEVINQ-RVNQVAE------------VLQLAhlldrkpKALSGGQRQRVAIGRTLVAE 151
Cdd:NF040905 354 IDDIKRNIT----LANlgkvSRRGVIDEnEEIKVAEeyrkkmniktpsVFQKV-------GNLSGGNQQKVVLSKWLFTD 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1578826625 152 PSVFLLDEPLSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:NF040905 423 PDVLILDEPTRGID----VGAKYEIYTIINELaaeGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
20-45 |
1.69e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 1.69e-03
10 20
....*....|....*....|....*.
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTL 45
Cdd:PRK00349 17 KNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
127-238 |
2.01e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 127 LDRKPKALSGGQRQRVAIGRTLV---AEPSVFLLDEPLSNLD----AALRVQMRIEISrlhkrLGRTMIYVTHDqVEAMT 199
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDnqqkSALLVQLRTLVS-----LGHSVIYIDHD-PALLK 1766
|
90 100 110
....*....|....*....|....*....|....*....
gi 1578826625 200 LADKIVVLDAGRVAQVGKPLelyhypadrfvagFIGSPK 238
Cdd:PRK00635 1767 QADYLIEMGPGSGKTGGKIL-------------FSGPPK 1792
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-221 |
2.05e-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: 39.51 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 18 VSKDINLEIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGEKRMNDTP--PAERGVGMVFQSYALYphlsvAEN 95
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlhTLRSRLSIILQDPILF-----SGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1578826625 96 MSFGLKlagAKKEVINQRVNQVAEVLQLAHLLDRKPKAL-----------SGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
Cdd:cd03288 111 IRFNLD---PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1578826625 165 DAALR-VQMRIEISRLHKrlgRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03288 188 DMATEnILQKVVMTAFAD---RTVVTIAH-RVSTILDADLVLVLSRGILVECDTPENL 241
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
28-59 |
7.00e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.38 E-value: 7.00e-03
10 20 30
....*....|....*....|....*....|..
gi 1578826625 28 EGEFVVFVGPSGCGKSTLLRMIAGLETITSGD 59
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGE 115
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
26-50 |
8.61e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.46 E-value: 8.61e-03
10 20
....*....|....*....|....*.
gi 1578826625 26 IHEGE-FVVFVGPSGCGKSTLLRMIA 50
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRRLL 64
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-46 |
8.65e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 8.65e-03
10 20
....*....|....*....|....*..
gi 1578826625 20 KDINLEIHEGEFVVFVGPSGCGKSTLL 46
Cdd:TIGR00630 625 KNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| |
