|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-369 |
0e+00 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 823.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 161 LSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGSPKMN 240
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 241 FLPVKVTAAEPRQVQIELPNHQRVWLPVEGDQVQVGANMSLGIRPEHLLPSSASEVTLEGEIQVVEQLGNETQIHIQIPA 320
Cdd:PRK11000 241 FLPVKVTATAIEQVQVELPNRQQVWLPVEGRGVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGNETQIHIQIPA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488140883 321 IRQNLVYRQNDVVLVEEGATFSIGLPPHRCHLFREDGTACKRLYQELGV 369
Cdd:PRK11000 321 IRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRLHKEPGV 369
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-356 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 573.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 161 LSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGSPKMN 240
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 241 FLPVKVTAAEprqvqIELpNHQRVWLPvEGDQVQVGANMSLGIRPEHLLPSSASEVTLEGEIQVVEQLGNETQIHIQIPA 320
Cdd:COG3839 241 LLPGTVEGGG-----VRL-GGVRLPLP-AALAAAAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRLGG 313
|
330 340 350
....*....|....*....|....*....|....*.
gi 488140883 321 irQNLVYRQNDVVLVEEGATFSIGLPPHRCHLFRED 356
Cdd:COG3839 314 --QELVARVPGDTRLRPGDTVRLAFDPERLHLFDAE 347
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-357 |
5.00e-173 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 485.50 E-value: 5.00e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTLSSVYKAF--GEAVIsRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIG 78
Cdd:PRK11650 1 MAGLKLQAVRKSYdgKTQVI-KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 79 MVFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLD 158
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 159 EPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGSPK 238
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 239 MNFLPVKVTAAeprQVQIELPNHQRVWLPVEGDQVQvGANMSLGIRPEHLLPSSAsEVTLEGEIQVVEQLGNETQIHIQI 318
Cdd:PRK11650 240 MNLLDGRVSAD---GAAFELAGGIALPLGGGYRQYA-GRKLTLGIRPEHIALSSA-EGGVPLTVDTVELLGADNLAHGRW 314
|
330 340 350
....*....|....*....|....*....|....*....
gi 488140883 319 PaiRQNLVYRQNDVVLVEEGATFSIGLPPHRCHLFREDG 357
Cdd:PRK11650 315 G--GQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADT 351
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-355 |
6.59e-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: 442.23 E-value: 6.59e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 161 LSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGspKMN 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--EAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 241 FLPVKVTAAEPRQVQIElpnHQRVWLPVEGDqVQVGANMSLGIRPEHLLPSSASEV-TLEGEIQVVEQLGNETQIHIQIP 319
Cdd:COG3842 241 LLPGTVLGDEGGGVRTG---GRTLEVPADAG-LAAGGPVTVAIRPEDIRLSPEGPEnGLPGTVEDVVFLGSHVRYRVRLG 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 488140883 320 AIRQNLVYRQNDVVL-VEEGATFSIGLPPHRCHLFRE 355
Cdd:COG3842 317 DGQELVVRVPNRAALpLEPGDRVGLSWDPEDVVVLPA 353
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
4.17e-133 |
|
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: 378.91 E-value: 4.17e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQS 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488140883 164 LDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVG 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 |
1.83e-112 |
|
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: 327.27 E-value: 1.83e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQS 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 164 LDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIG 235
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-349 |
4.95e-112 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 330.57 E-value: 4.95e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMN-EVPPSERGIGMVFQ 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 163 NLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGSPkmNFL 242
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCV--NVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 243 PVKVTAAEPRQVQIELPNHQrvwlPVEGDQVQVganmslGIRPEHL--LPSSASEVTLEGEIQVVEQLGNETQIHIQIPA 320
Cdd:COG1118 241 RGRVIGGQLEADGLTLPVAE----PLPDGPAVA------GVRPHDIevSREPEGENTFPATVARVSELGPEVRVELKLED 310
|
330 340 350
....*....|....*....|....*....|....
gi 488140883 321 IRQNLVY-----RQNDVVLVEEGATFSIGLPPHR 349
Cdd:COG1118 311 GEGQPLEaevtkEAWAELGLAPGDPVYLRPRPAR 344
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
8.70e-110 |
|
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: 319.85 E-value: 8.70e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQS 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488140883 164 LDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
9-353 |
6.25e-106 |
|
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: 315.05 E-value: 6.25e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 9 VYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQSYALYP 88
Cdd:TIGR03265 10 IRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 89 HLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAAL 168
Cdd:TIGR03265 90 NLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 169 RVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGspKMNFLPVKVta 248
Cdd:TIGR03265 170 REHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG--EVNWLPGTR-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 249 AEPRQVQIelpnhQRVWLPVEGDQVQVGANMSLGIRPEHLLPSSA--SEVTLEGEIQVVEQLGNETQIHIQIP-----AI 321
Cdd:TIGR03265 246 GGGSRARV-----GGLTLACAPGLAQPGASVRLAVRPEDIRVSPAgnAANLLLARVEDMEFLGAFYRLRLRLEglpgqAL 320
|
330 340 350
....*....|....*....|....*....|..
gi 488140883 322 RQNLVYRQNDVVLVEEGATFSIGLPPHRCHLF 353
Cdd:TIGR03265 321 VADVSASEVERLGIRAGQPIWIELPAERLRAF 352
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-288 |
3.44e-105 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 314.19 E-value: 3.44e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQS 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 164 LDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGspKMNFLP 243
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINIFD 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 488140883 244 VKVtaaeprqvqIELPNHQRVWLPVEG--------DQVQVGANMSLGIRPEHL 288
Cdd:PRK09452 253 ATV---------IERLDEQRVRANVEGrecniyvnFAVEPGQKLHVLLRPEDL 296
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-304 |
2.37e-98 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 295.75 E-value: 2.37e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 2 ANVTLSSVYKAFG----EAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNE-----VPP 72
Cdd:NF040933 1 VTVRVENVTKIFKkgkkEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 73 SERGIGMVFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEP 152
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 153 DVFLLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAG 232
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 233 FIGspKMNFLPVKV---TAAEPRQVQIELPNHqrvwlPVEGDQVQvganmsLGIRPEHLLPSSASEVTLEGEIQV 304
Cdd:NF040933 241 LIG--DINLLEGKVeeeGLVDGNDLKIPLPNP-----KLEAGEVI------IGIRPEDIDISESDMRLPPGFVEV 302
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-314 |
4.91e-93 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 281.99 E-value: 4.91e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQS 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 164 LDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGSPkmNFLP 243
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIFP 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 244 VKVTA--AEPRQVQIELPNHQRVWLPvEGDqvqvganMSLGIRPEHLLPSSASEVTLEGEIQVVEQLGNETQI 314
Cdd:PRK11432 245 ATLSGdyVDIYGYRLPRPAAFAFNLP-DGE-------CTVGVRPEAITLSEQGEESQRCTIKHVAYMGPQYEV 309
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-236 |
3.36e-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: 270.75 E-value: 3.36e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQS 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHLSVAENMSFGLKLAGVK----KAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDE 159
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 160 PLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGS 236
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-210 |
1.30e-89 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 270.04 E-value: 1.30e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAF----GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSergIGM 79
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD---RGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 80 VFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDE 159
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488140883 160 PLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:COG1116 165 PFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-331 |
9.58e-89 |
|
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: 270.13 E-value: 9.58e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 35 VGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRV 114
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 115 NQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQ 194
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 195 VEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGSPKMnflpVKVTAAEPRQVQIELPNHQ------RVWLPV 268
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINV----FEATVIERKSEQVVLAGVEgrrcdiYTDVPV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 269 EGDQvqvgaNMSLGIRPEHL----LPSSASEVTLEGEIQVVEQLGNETQIHIQIPAIRQNLV--YRQND 331
Cdd:TIGR01187 238 EKDQ-----PLHVVLRPEKIvieeEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLVseFFNED 301
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-235 |
4.69e-88 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 265.51 E-value: 4.69e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQS 83
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 164 LDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIG 235
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
20-353 |
1.02e-85 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 263.47 E-value: 1.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQSYALYPHLSVAENMSFG 99
Cdd:NF040840 17 RDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 LKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRL 179
Cdd:NF040840 97 LKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 180 HKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGSPKMnflpVKVTAAEPRQVQIELP 259
Cdd:NF040840 177 HREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENI----IEGVAEKGGEGTILDT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 260 NHQRVWLPVEgdqvqVGANMSLGIRPEHLLPS------SASEVtLEGEIQVVEQLGNETQIHIQIPAIRQNLVYRQNDVV 333
Cdd:NF040840 253 GNIKIELPEE-----KKGKVRIGIRPEDITIStekvktSARNE-FKGKVEEIEDLGPLVKLTLDVGIILVAFITRSSFLD 326
|
330 340
....*....|....*....|.
gi 488140883 334 L-VEEGATFSIGLPPHRCHLF 353
Cdd:NF040840 327 LeINEGKEVYASFKASAVHVF 347
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-209 |
1.27e-85 |
|
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: 258.56 E-value: 1.27e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVIS----RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSergIGM 79
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtalEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 80 VFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488140883 160 PLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDA 209
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-272 |
1.02e-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: 256.56 E-value: 1.02e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 5 TLSSVYKAFGE---AVisRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGM 79
Cdd:COG1125 3 EFENVTKRYPDgtvAV--DDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 80 VFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQL--AHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:COG1125 81 VIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 158 DEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGS- 236
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAd 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 488140883 237 ---PKMNFLPVK-VTAAEPRQVQIELP---------NHQRVWLPVEGDQ 272
Cdd:COG1125 241 rglRRLSLLRVEdLMLPEPPTVSPDASlrealslmlERGVDWLLVVDED 289
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-235 |
3.56e-82 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 254.24 E-value: 3.56e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 3 NVTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQ 82
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SYALYPHLSVAENMSFGLKLAGVKK----AEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLD 158
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVLPRRErpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 159 EPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIG 235
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-235 |
3.61e-82 |
|
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: 250.33 E-value: 3.61e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQSYALYPHLSVAENMSFG 99
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 LKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRL 179
Cdd:cd03299 96 LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 180 HKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIG 235
Cdd:cd03299 176 RKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-238 |
7.33e-81 |
|
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: 247.21 E-value: 7.33e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGE---AVisRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIG 78
Cdd:cd03295 1 IEFENVTKRYGGgkkAV--NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 79 MVFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQL--AHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFL 156
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 157 LDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGS 236
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
..
gi 488140883 237 PK 238
Cdd:cd03295 239 DR 240
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-239 |
1.97e-76 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 240.51 E-value: 1.97e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQSYALYPHLSVAENMSFGL 100
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALFPHMTVEQNIAFGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 101 KLAGVKKAEIYQRVNqvaEVLQLAHLLD---RRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEIS 177
Cdd:PRK11607 117 KQDKLPKAEIASRVN---EMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVV 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 178 RLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGSPKM 239
Cdd:PRK11607 194 DILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-234 |
4.26e-74 |
|
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: 230.61 E-value: 4.26e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 9 VYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE------RGIGMVFQ 82
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 163 NLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFI 234
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-298 |
2.26e-72 |
|
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: 229.22 E-value: 2.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGG-------KRMNeVPPSERGIGMVFQSYALYPHLSVA 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsaRGIF-LPPHRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKLAgvKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMR 173
Cdd:COG4148 96 GNLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 174 IEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGfiGSPKMNFLPVKVTAAEPRQ 253
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAGSVLEATVAAHDPDY 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 488140883 254 --VQIELPnHQRVWLPveGDQVQVGANMSLGIRpehllpssASEVTL 298
Cdd:COG4148 252 glTRLALG-GGRLWVP--RLDLPPGTRVRVRIR--------ARDVSL 287
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-210 |
2.47e-71 |
|
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: 220.52 E-value: 2.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMN----EVPPSERGIGM 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 80 VFQSYALYPHLSVAENMSFGlklagvkkaeiyqrvnqvaevlqlahlldrrpkaLSGGQRQRVAIGRTLVSEPDVFLLDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488140883 160 PLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-216 |
4.01e-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: 4.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEID---DGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGG-------KRMNeVPPSERGIGMVFQSYALYPHL 90
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKIN-LPPQQRKIGLVFQQYALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 91 SVAENMSFGLKlaGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRV 170
Cdd:cd03297 91 NVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488140883 171 QMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
1.89e-68 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 214.91 E-value: 1.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANV-TLSSVYKAFGEAVIS----RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSER 75
Cdd:COG1136 1 MSPLlELRNLTKSYGTGEGEvtalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 76 G------IGMVFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLV 149
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488140883 150 SEPDVFLLDEPLSNLDAALRVQ-MRIeISRLHKRLERTMIYVTHDQvEAMTLADKIVVLDAGNI 212
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEvLEL-LRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-212 |
8.99e-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: 212.74 E-value: 8.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEA----VISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG--- 76
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 77 ---IGMVFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPD 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMtLADKIVVLDAGNI 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
3.47e-65 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 206.84 E-value: 3.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG-IGMVFQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 163 NLDAALRVQMRIEISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-223 |
6.22e-65 |
|
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: 206.03 E-value: 6.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQsyalYP-----HLSV 92
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQ----NPddqlfAPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 93 AENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQM 172
Cdd:COG1122 94 EEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRREL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488140883 173 RIEISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYH 223
Cdd:COG1122 174 LELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
22-235 |
1.26e-64 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 204.99 E-value: 1.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQSYALYPHLSVAENMSFG-- 99
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGlr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 --LKLAGVKKaeiyQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEIS 177
Cdd:COG3840 98 pgLKLTAEQR----AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488140883 178 RLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIG 235
Cdd:COG3840 174 ELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-210 |
6.41e-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: 200.00 E-value: 6.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVIsRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG--IGMVFQs 83
Cdd:cd03225 5 LSFSYPDGARPAL-DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLVFQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 yalYP-----HLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLD 158
Cdd:cd03225 83 ---NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488140883 159 EPLSNLDAALRVQMRIEISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-234 |
3.29e-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: 199.05 E-value: 3.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-----RGIG 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 79 MVFQSYALYPHLSVAENMSFGLK-LAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 158 DEPLSNLD---AALRVQMrieISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPaNRFVAGFI 234
Cdd:COG1127 166 DEPTAGLDpitSAVIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-232 |
5.48e-62 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 199.32 E-value: 5.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAV-ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMnEVPPSERGIgmVFQSY 84
Cdd:COG4525 9 VSVRYPGGGQPQpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADRGV--VFQKD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 85 ALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:COG4525 86 ALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 165 DAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNiaqvGKPLELYHYP-ANRFVAG 232
Cdd:COG4525 166 DALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGP----GRIVERLELDfSRRFLAG 230
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-227 |
7.17e-62 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 198.29 E-value: 7.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEvPPSE-----RGIG 78
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDinklrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 79 MVFQSYALYPHLSVAENMSFGL-KLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 158 DEPLSNLD-----AALRVqMRiEISRLHkrleRTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPAN 227
Cdd:COG1126 161 DEPTSALDpelvgEVLDV-MR-DLAKEG----MTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-217 |
2.54e-60 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 193.73 E-value: 2.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAV-ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-----RGI 77
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 GMVFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 158 DEPLSNLDAAlrvqMRIEISRLHKRLER---TMIYVTHDQ--VEAMtlADKIVVLDAGNIAQVGK 217
Cdd:COG2884 162 DEPTGNLDPE----TSWEIMELLEEINRrgtTVLIATHDLelVDRM--PKRVLELEDGRLVRDEA 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-212 |
7.88e-57 |
|
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: 184.27 E-value: 7.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMN----EVPPSERGIGM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 80 VFQSYALYPHLSVAENMSFGL-KLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 159 EPLSNLDAalrvQMRIEISRLHKRLER---TMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:cd03262 161 EPTSALDP----ELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-221 |
1.37e-56 |
|
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: 184.63 E-value: 1.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-----RGIG 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 79 MVFQSYALYPHLSVAENMSFGLKLAGV-KKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 158 DEPLSNLD-AALRVQMRIeISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:cd03261 161 DEPTAGLDpIASGVIDDL-IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-227 |
1.85e-56 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 184.53 E-value: 1.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGI----GM 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 80 VFQSYALYPHLSVAENMSFG-LKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLD 158
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 159 EPLSNLDAALRVqmriEISRLHKRLER---TMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPAN 227
Cdd:PRK09493 162 EPTSALDPELRH----EVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-212 |
3.20e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 184.10 E-value: 3.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAF-GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-----RGI 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 GMVFQSYALYPHLSVAEN--------MSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLV 149
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 150 SEPDVFLLDEPLSNLD--AALRVqMRIeISRLHKRLERTMIYVTHdQVE-AMTLADKIVVLDAGNI 212
Cdd:COG3638 163 QEPKLILADEPVASLDpkTARQV-MDL-LRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDGRV 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-237 |
9.73e-56 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 185.67 E-value: 9.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFG------EAVisRDINLEIDDGEfvVF--VGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE- 74
Cdd:COG1135 2 IELENLSKTFPtkggpvTAL--DDVSLTIEKGE--IFgiIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSEREl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 75 ----RGIGMVFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVS 150
Cdd:COG1135 78 raarRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 151 EPDVFLLDEPLSNLDAA-----LRVqmrieISRLHKRLERTMIYVTHDqveaM----TLADKIVVLDAGNIAQVGKPLEL 221
Cdd:COG1135 158 NPKVLLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLDV 228
|
250
....*....|....*.
gi 488140883 222 YHYPANRFVAGFIGSP 237
Cdd:COG1135 229 FANPQSELTRRFLPTV 244
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
12-212 |
2.20e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 180.40 E-value: 2.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 12 AFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPH 89
Cdd:COG4619 9 RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQEPALWGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 90 lSVAENMSFGLKLAGVKKAEiyQRVNQVAEVLQLAH-LLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAAL 168
Cdd:COG4619 89 -TVRDNLPFPFQLRERKFDR--ERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPEN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488140883 169 RVqmRIE--ISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:COG4619 166 TR--RVEelLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-218 |
2.22e-55 |
|
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: 181.22 E-value: 2.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGELLIGGKRMNE--VPPSE--RG 76
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDldVDVLElrRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 77 IGMVFQSYALYPhLSVAENMSFGLKLAGVKKAEIYQRVnqVAEVLQLAHLLD---RRPKA--LSGGQRQRVAIGRTLVSE 151
Cdd:cd03260 83 VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDER--VEEALRKAALWDevkDRLHAlgLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 152 PDVFLLDEPLSNLDAALRvqMRIE--ISRLHKrlERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKP 218
Cdd:cd03260 160 PEVLLLDEPTSALDPIST--AKIEelIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
5.88e-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: 180.47 E-value: 5.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFG----EAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE----- 74
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 75 RGIGMVFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDV 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHdQVEAM-TLADKIVVLDAGNIAQVGKPLELYHYP 225
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-221 |
6.92e-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: 180.62 E-value: 6.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 12 AFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG--IGMVFQSYALYPH 89
Cdd:COG1120 10 GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELArrIAYVPQEPPAPFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 90 LSVAENMSFG----LKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD 165
Cdd:COG1120 90 LTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488140883 166 aaLRVQMRI--EISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:COG1120 170 --LAHQLEVleLLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-213 |
1.10e-54 |
|
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: 180.00 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAV-ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQ 82
Cdd:COG1124 7 LSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRVQMVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SY--ALYPHLSVAENMSFGLKLAGVKKAEiyQRVNQVAEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDE 159
Cdd:COG1124 87 DPyaSLHPRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 160 PLSNLDAAlrVQMRI--EISRLHKRLERTMIYVTHDqVEAMT-LADKIVVLDAGNIA 213
Cdd:COG1124 165 PTSALDVS--VQAEIlnLLKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIV 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-225 |
1.40e-54 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 187.42 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-----RGIGMVFQ--SYALYPHLSV 92
Cdd:COG1123 282 DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelrRRVQMVFQdpYSSLNPRMTV 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 93 AENMSFGLKLAGV-KKAEIYQRVNQVAEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRV 170
Cdd:COG1123 362 GDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQA 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 171 QMRIEISRLHKRLERTMIYVTHD--QVEAMtlADKIVVLDAGNIAQVGKPLELYHYP 225
Cdd:COG1123 442 QILNLLRDLQRELGLTYLFISHDlaVVRYI--ADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-226 |
5.45e-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: 5.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNE------VPPSERGIGMVFQSYALYPHLSVAE 94
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 95 NMSFGLKLAGVKKAEIyqRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRI 174
Cdd:TIGR02142 95 NLRYGMKRARPSERRI--SFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488140883 175 EISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPA 226
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-209 |
7.82e-54 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 176.52 E-value: 7.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAG-LEDI--TSGELLIGGKRMNEVPPSERGIGMVFQSYALYPHLSVAENM 96
Cdd:COG4136 18 APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHLSVGENL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 97 SFGLKlAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRiei 176
Cdd:COG4136 98 AFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFR--- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488140883 177 srlhkRLERTMI--------YVTHDqVEAMTLADKIVVLDA 209
Cdd:COG4136 174 -----EFVFEQIrqrgipalLVTHD-EEDAPAAGRVLDLGN 208
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-217 |
1.66e-53 |
|
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: 175.82 E-value: 1.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 23 NLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQSYALYPHLSVAENMSFGLKL 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 103 AGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRLHKR 182
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....*
gi 488140883 183 LERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGK 217
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-216 |
2.06e-53 |
|
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: 175.76 E-value: 2.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVIsrDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQS 83
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488140883 164 LDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-221 |
7.36e-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: 175.05 E-value: 7.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 5 TLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPS-ERGIGMVFQS 83
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREaRRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488140883 164 LDAALRVQMRiEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:COG4555 163 LDVMARRLLR-EILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-226 |
1.50e-51 |
|
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: 179.33 E-value: 1.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 8 SVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDIT---SGELLIGGKRMNEVPPSERG--IGMVFQ 82
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGrrIGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 S--YALYPhLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:COG1123 91 DpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 161 LSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPA 226
Cdd:COG1123 170 TTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-212 |
3.48e-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: 170.38 E-value: 3.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG-----IGMVFQSY--ALYPHLSV 92
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrkeIQMVFQDPmsSLNPRMTI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 93 AENMSFGLKLAGV--KKAEIYQRVNQVAEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALR 169
Cdd:cd03257 102 GEQIAEPLRIHGKlsKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQ 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488140883 170 VQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:cd03257 182 AQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-221 |
1.25e-49 |
|
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: 166.59 E-value: 1.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVisRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-----RGIGMV 80
Cdd:cd03256 6 LSKTYPNGKKAL--KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYALYPHLSVAEN--------MSFGLKLAG-VKKAEIyQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSE 151
Cdd:cd03256 84 FQQFNLIERLSVLENvlsgrlgrRSTWRSLFGlFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 152 PDVFLLDEPLSNLDAALRVQ-MRIeISRLHKRLERTMIYVTHdQVE-AMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:cd03256 163 PKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLH-QVDlAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-222 |
1.39e-49 |
|
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: 167.63 E-value: 1.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMN-----EVPPSERGIGMVFQsyalYPH-----L 90
Cdd:TIGR04521 23 DVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDLRKKVGLVFQ----FPEhqlfeE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 91 SVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALR 169
Cdd:TIGR04521 99 TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488140883 170 VQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:TIGR04521 179 KEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-221 |
2.82e-49 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 165.53 E-value: 2.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 23 NLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQSYALYPHLSVAENMSFG--- 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 -LKLAGVKKAEIYQRVNQVAevlqLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISR 178
Cdd:PRK10771 99 gLKLNAAQREKLHAIARQMG----IEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488140883 179 LHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-212 |
1.77e-48 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 164.47 E-value: 1.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERgigMVFQS 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHLSVAENMSFGLKLAGVKKAEiyqrvnQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488140883 164 LDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-210 |
4.39e-48 |
|
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: 162.03 E-value: 4.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAV-ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGK-----RMNEVPPSERGI 77
Cdd:TIGR02673 2 IEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEdvnrlRGRQLPLLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 GMVFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488140883 158 DEPLSNLDAALRVQ-MRIeISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:TIGR02673 162 DEPTGNLDPDLSERiLDL-LKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-222 |
1.02e-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: 162.60 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGG-KRMNE--VPPSERGIGMVFQSyalyPH-----LS 91
Cdd:TIGR04520 19 KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEenLWEIRKKVGMVFQN----PDnqfvgAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 92 VAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQ 171
Cdd:TIGR04520 95 VEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488140883 172 MRIEISRLHKRLERTMIYVTHDQVEAmTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:TIGR04520 175 VLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-221 |
1.33e-47 |
|
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: 160.75 E-value: 1.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKaFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSER-GIGMVFQSY 84
Cdd:cd03263 6 LTKTYK-KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARqSLGYCPQFD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 85 ALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:cd03263 85 ALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 165 DAALRVQMRIEISRLhkRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:cd03263 165 DPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-232 |
3.31e-47 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 161.02 E-value: 3.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 5 TLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMnEVPPSERGIgmVFQSY 84
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAERGV--VFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 85 ALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 165 DAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNiaqvGKPLELYHYP-ANRFVAG 232
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGP----GRVVERLPLNfARRFVAG 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-221 |
4.77e-47 |
|
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: 159.94 E-value: 4.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEvPPSERGIgmVFQSYALYPHLSVAENMSFG 99
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 LK--LAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEIS 177
Cdd:TIGR01184 79 VDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488140883 178 RLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:TIGR01184 159 QIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-221 |
6.56e-47 |
|
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: 169.63 E-value: 6.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 3 NVTLSsvYKAFGEAVIsRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMV 80
Cdd:COG2274 478 NVSFR--YPGDSPPVL-DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYALYpHLSVAENMSFGLKLAGvkkaeiYQRVNQVAEVLQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLV 149
Cdd:COG2274 555 LQDVFLF-SGTIRENITLGDPDAT------DEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 150 SEPDVFLLDEPLSNLDAALrvQMRIeISRLHKRLE-RTMIYVTHDqVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:COG2274 628 RNPRILILDEATSALDAET--EAII-LENLRRLLKgRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-209 |
8.79e-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: 158.03 E-value: 8.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG-IGMVFQ 82
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SYALYPHLSVAENMSFGLKLAGVKKAEIyqRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488140883 163 NLDAAlRVQMRIEISRLHKRLERTMIYVTHDQVEAmtLADKIVVLDA 209
Cdd:COG4133 161 ALDAA-GVALLAELIAAHLARGGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
9.58e-47 |
|
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: 156.79 E-value: 9.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG-IGMVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SYALYPHLSVAENMSfglklagvkkaeiyqrvnqvaevlqlahlldrrpkaLSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:cd03230 81 EPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488140883 163 NLDAALRVQMRIEISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-216 |
1.54e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 158.64 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 3 NVTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMN-EVPPSERGI---- 77
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfSQKPSEKAIrllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 ---GMVFQSYALYPHLSVAENMSFG-LKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPD 153
Cdd:COG4161 82 qkvGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 154 VFLLDEPLSNLDAALRVQMrIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:COG4161 162 VLLFDEPTAALDPEITAQV-VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-216 |
3.55e-46 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 157.87 E-value: 3.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMN-EVPPSE-------RGI 77
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfSKTPSDkairelrRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 GMVFQSYALYPHLSVAENM-SFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFL 156
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 157 LDEPLSNLDAALRVQmrieISRLHKRLERTMI---YVTHDQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:PRK11124 165 FDEPTAALDPEITAQ----IVSIIRELAETGItqvIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
14-214 |
4.16e-46 |
|
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: 157.21 E-value: 4.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGK---RMNEVPPSE---RGIGMVFQSYALY 87
Cdd:COG4181 23 GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlfALDEDARARlraRHVGFVFQSFQLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 88 PHLSVAENMSFGLKLAGVKKAEiyqrvNQVAEVLQ---LAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:COG4181 103 PTLTALENVMLPLELAGRRDAR-----ARARALLErvgLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488140883 165 DAALRVQMrIE-ISRLHKRLERTMIYVTHDQveamTLA---DKIVVLDAGNIAQ 214
Cdd:COG4181 178 DAATGEQI-IDlLFELNRERGTTLVLVTHDP----ALAarcDRVLRLRAGRLVE 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-233 |
7.58e-46 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 161.35 E-value: 7.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE------RGIGMVFQSYALYPHLSVA 93
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMR 173
Cdd:PRK10070 125 DNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 174 IEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGF 233
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-218 |
1.88e-45 |
|
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: 155.67 E-value: 1.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 9 VYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSER---GIGMVFQSYA 85
Cdd:cd03219 6 LTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQIPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 86 LYPHLSVAENM----------SFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVF 155
Cdd:cd03219 86 LFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 156 LLDEPLSNLDAALRVQMRIEISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKP 218
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-162 |
2.54e-45 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 152.42 E-value: 2.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMN--EVPPSERGIGMVFQSYALYPHLSVAENMS 97
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTddERKSLRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 98 FGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRR----PKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
20-228 |
5.83e-45 |
|
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: 154.76 E-value: 5.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGK-----RMNEVPPSERGIGMVFQSYALYPHLSVAE 94
Cdd:TIGR02315 19 KNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditklRGKKLRKLRRRIGMIFQHYNLIERLTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 95 N--------MSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDA 166
Cdd:TIGR02315 99 NvlhgrlgyKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 167 ALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANR 228
Cdd:TIGR02315 179 KTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRH 240
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
1.00e-44 |
|
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: 151.82 E-value: 1.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 5 TLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERgigmvfqsy 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 85 alyphlsvAENMSFglklagvkkaeiyqrVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:cd03214 72 --------ARKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488140883 165 DaaLRVQMRI--EISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:cd03214 129 D--IAHQIELleLLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-216 |
1.63e-44 |
|
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: 152.91 E-value: 1.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEA----VISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVP-PSERGIG 78
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 79 MVFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLD 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488140883 159 EPLSNLDaALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:cd03266 162 EPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-210 |
1.94e-44 |
|
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: 150.47 E-value: 1.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 5 TLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 syalyphlsvaenmsfglklagvkkaeiyqrvnqvaevlqlahlldrrpkaLSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488140883 163 NLDAALRVQMRIEISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-207 |
1.98e-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: 152.00 E-value: 1.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGK---RMNEVPPSE---RGIGM 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKASKfrrEKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 80 VFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDE 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488140883 160 PLSNLDAALRvQMRIEISRLHKRLERTMIYVTHDQvEAMTLADKIVVL 207
Cdd:TIGR03608 161 PTGSLDPKNR-DEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-220 |
4.72e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.17 E-value: 4.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPpseRGIGMV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR---RRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYALYPH--LSVAENMSFGL----KLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDV 154
Cdd:COG1121 81 PQRAEVDWDfpITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 155 FLLDEPLSNLDAALRVQ-MRIeISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAGNIAQvGKPLE 220
Cdd:COG1121 161 LLLDEPFAGVDAATEEAlYEL-LRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEE 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-210 |
6.39e-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: 6.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 3 NVTLSsvYKAFGEAVIsRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMV 80
Cdd:cd03228 5 NVSFS--YPGRPKPVL-KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYALYpHLSVAENMsfglklagvkkaeiyqrvnqvaevlqlahlldrrpkaLSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:cd03228 82 PQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488140883 161 LSNLDAALRVQMRIEISRLHKrlERTMIYVTHDqVEAMTLADKIVVLDAG 210
Cdd:cd03228 124 TSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-221 |
8.66e-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: 150.98 E-value: 8.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 11 KAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGG----KRMNEVppsERGIGMVFQSYAL 86
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPREV---RRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 87 YPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDA 166
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 167 ALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-221 |
2.42e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 158.02 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 3 NVTLSsvYKAfGEAVIsRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMV 80
Cdd:COG1132 344 NVSFS--YPG-DRPVL-KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYALYpHLSVAENMSFGLKLAGvkKAEIYqrvnQVAEVLQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLV 149
Cdd:COG1132 420 PQDTFLF-SGTIRENIRYGRPDAT--DEEVE----EAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 150 SEPDVFLLDEPLSNLDAA--LRVQMRIEisRLHKrlERTMIYVTH--DQVEAmtlADKIVVLDAGNIAQVGKPLEL 221
Cdd:COG1132 493 KDPPILILDEATSALDTEteALIQEALE--RLMK--GRTTIVIAHrlSTIRN---ADRILVLDDGRIVEQGTHEEL 561
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
21-223 |
2.65e-43 |
|
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: 158.00 E-value: 2.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSyalyPHL---SVAEN 95
Cdd:COG4988 355 GLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWVPQN----PYLfagTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 96 MSFGLKLAGVkkaeiyQRVNQVAEVLQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:COG4988 431 LRLGRPDASD------EELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHL 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 165 DAALRVQMRIEISRLHKrlERTMIYVTHDQvEAMTLADKIVVLDAGNIAQVGKPLELYH 223
Cdd:COG4988 505 DAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-193 |
2.71e-43 |
|
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: 149.48 E-value: 2.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 9 VYKAFGEAVIS-RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGK-----RMNEVPPSERGIGMVFQ 82
Cdd:cd03292 6 VTKTYPNGTAAlDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlRGRAIPYLRRKIGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:cd03292 86 DFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190
....*....|....*....|....*....|....
gi 488140883 163 NLDAAlrvqMRIEISRLHKRLER---TMIYVTHD 193
Cdd:cd03292 166 NLDPD----TTWEIMNLLKKINKagtTVVVATHA 195
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-230 |
9.26e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 151.88 E-value: 9.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVIS-RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-----RGIGM 79
Cdd:PRK11153 7 ISKVFPQGGRTIHAlNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 80 VFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDE 159
Cdd:PRK11153 87 IFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 160 PLSNLDAALRVQMRIEISRLHKRLERTMIYVTH--DQVEAmtLADKIVVLDAGNIAQVGKPLELYHYP----ANRFV 230
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRELGLTIVLITHemDVVKR--ICDRVAVIDAGRLVEQGTVSEVFSHPkhplTREFI 241
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
16-226 |
6.16e-42 |
|
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: 149.05 E-value: 6.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 16 AVisRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLED---ITSGELLIGGKRMNEVPPSE------RGIGMVFQ-SY- 84
Cdd:COG0444 20 AV--DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElrkirgREIQMIFQdPMt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 85 ALYPHLSVAENMSFGLKL-AGVKKAEIYQRVnqvAEVLQLAHL------LDRRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:COG0444 98 SLNPVMTVGDQIAEPLRIhGGLSKAEARERA---IELLERVGLpdperrLDRYPHELSGGMRQRVMIARALALEPKLLIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 158 DEPLSNLDAAlrVQMRI--EISRLHKRLERTMIYVTHD--QVEAMtlADKIVVLDAGNIAQVGKPLELYHYPA 226
Cdd:COG0444 175 DEPTTALDVT--IQAQIlnLLKDLQRELGLAILFITHDlgVVAEI--ADRVAVMYAGRIVEEGPVEELFENPR 243
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1-214 |
8.03e-42 |
|
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: 145.37 E-value: 8.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTLSsvykaFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPpseRGIGMV 80
Cdd:cd03235 2 VEDLTVS-----YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---KRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYAL---YPhLSVAENMSFGL-----KLAGVKKAEiYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEP 152
Cdd:cd03235 74 PQRRSIdrdFP-ISVRDVVLMGLyghkgLFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 153 DVFLLDEPLSNLDAALRVQMRIEISRLHkRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQ 214
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-212 |
1.84e-41 |
|
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: 144.28 E-value: 1.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQS 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHLSVAENMSFGLKLAGVKKaeiyQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488140883 164 LDAALRVQMRiEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:cd03268 157 LDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-221 |
3.58e-41 |
|
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: 152.23 E-value: 3.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSyalyPHL---SVAE 94
Cdd:COG4987 352 DGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQR----PHLfdtTLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 95 NmsfgLKLA--GVKKAEIYqrvnQVAEVLQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLVSEPDVFLLDEPL 161
Cdd:COG4987 428 N----LRLArpDATDEELW----AALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488140883 162 SNLDAALRVQMrieISRLHKRL-ERTMIYVTHDQVeAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:COG4987 500 EGLDAATEQAL---LADLLEALaGRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEEL 556
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-222 |
3.65e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 145.96 E-value: 3.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGG-------KRMNEVppsERGIGMVFQ--SYALYPHlS 91
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkVKLSDI---RKKVGLVFQypEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 92 VAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAH--LLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALR 169
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488140883 170 VQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-217 |
1.06e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 144.02 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 8 SVYkaFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGELLIGGKRMN--EVPPSE--RGIG 78
Cdd:COG1117 18 NVY--YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDIYdpDVDVVElrRRVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 79 MVFQSYALYPHlSVAENMSFGLKLAGVK-KAEIYQRVNqvaEVLQLAHL-------LDRRPKALSGGQRQRVAIGRTLVS 150
Cdd:COG1117 96 MVFQKPNPFPK-SIYDNVAYGLRLHGIKsKSELDEIVE---ESLRKAALwdevkdrLKKSALGLSGGQQQRLCIARALAV 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488140883 151 EPDVFLLDEPLSNLD--AAlrvqMRIE--ISRLHKRLerTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGK 217
Cdd:COG1117 172 EPEVLLMDEPTSALDpiST----AKIEelILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGP 236
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
22-204 |
7.22e-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: 7.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG------IGMVFQSYALYPHLSVAEN 95
Cdd:TIGR02211 24 VSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnkkLGFIYQFHHLLPDFTALEN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 96 MSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIE 175
Cdd:TIGR02211 104 VAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDL 183
|
170 180
....*....|....*....|....*....
gi 488140883 176 ISRLHKRLERTMIYVTHDqveaMTLADKI 204
Cdd:TIGR02211 184 MLELNRELNTSFLVVTHD----LELAKKL 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-221 |
7.50e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 142.05 E-value: 7.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNE--VPPSERGIGMVFQSyalyPH-----LSV 92
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKKIGIIFQN----PDnqfigATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 93 AENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQM 172
Cdd:PRK13632 102 EDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488140883 173 RIEISRLHKRLERTMIYVTHDQVEAmTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:PRK13632 182 KKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
8.95e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 141.43 E-value: 8.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIG----------GKRMNEV 70
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtarslSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 71 PPSERGIGMVFQSYALYPHLSVAENMSFG-LKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLV 149
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 150 SEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYP 225
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-228 |
1.19e-39 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 143.86 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEI-DDGEFVVFvGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNE------VPPSERGIGMVFQSYALYPHLSVA 93
Cdd:PRK11144 16 TVNLTLpAQGITAIF-GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKRRIGYVFQDARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKlaGVKKAEIyqrvNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMR 173
Cdd:PRK11144 95 GNLRYGMA--KSMVAQF----DKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 174 IEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANR 228
Cdd:PRK11144 169 PYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-226 |
1.52e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 142.08 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIG------GKRMNEVPPSERGIGMVFQ--SYALYPHlSV 92
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitaGKKNKKLKPLRKKVGIVFQfpEHQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 93 AENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAH-LLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQ 171
Cdd:PRK13634 104 EKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 172 MRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPA 226
Cdd:PRK13634 184 MMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-221 |
1.74e-39 |
|
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: 139.49 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSER---GIGMVFQSYALYPHL 90
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 91 SVAENmsfgLKLAG--VKKAEIYQRVNQVAEVL-QLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAA 167
Cdd:cd03224 91 TVEEN----LLLGAyaRRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488140883 168 LRVQMRIEISRLhKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:cd03224 167 IVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-216 |
4.06e-38 |
|
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: 135.87 E-value: 4.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 9 VYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVP-------PSERGigmvf 81
Cdd:cd03269 6 VTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEERG----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 82 qsyaLYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPL 161
Cdd:cd03269 81 ----LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 162 SNLDAALRVQMRIEISRLhKRLERTMIYVTH--DQVEAMtlADKIVVLDAGNIAQVG 216
Cdd:cd03269 157 SGLDPVNVELLKDVIREL-ARAGKTVILSTHqmELVEEL--CDRVLLLNKGRAVLYG 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
5.47e-38 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 136.75 E-value: 5.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVF 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 82 QSYALYPHLSVAENMSFGL----KlaGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:COG4604 82 QENHINSRLTVRELVAFGRfpysK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488140883 158 DEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-236 |
3.13e-37 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 134.93 E-value: 3.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGG--------KRMNEVPPSER 75
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdRDGELVPADRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 76 -------GIGMVFQSYALYPHLSVAENMSFG-LKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRT 147
Cdd:COG4598 89 qlqrirtRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 148 LVSEPDVFLLDEPLSNLDAALrVQmriEISRLHKRLE---RTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHY 224
Cdd:COG4598 169 LAMEPEVMLFDEPTSALDPEL-VG---EVLKVMRDLAeegRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGN 244
|
250
....*....|..
gi 488140883 225 PANRFVAGFIGS 236
Cdd:COG4598 245 PKSERLRQFLSS 256
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-260 |
5.09e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 135.24 E-value: 5.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVP-------PSERG 76
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 77 igmvfqsyaLYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFL 156
Cdd:COG4152 82 ---------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 157 LDEPLSNLDAALRVQMRIEISRLHKRlERTMIYVTH--DQVEAmtLADKIVVLDAGNIAQVGKPLELYH-YPANRFVAGF 233
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHqmELVEE--LCDRIVIINKGRKVLSGSVDEIRRqFGRNTLRLEA 229
|
250 260
....*....|....*....|....*....
gi 488140883 234 IGSPKM--NFLPVKVTAAEPRQVQIELPN 260
Cdd:COG4152 230 DGDAGWlrALPGVTVVEEDGDGAELKLED 258
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-216 |
5.23e-37 |
|
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: 132.70 E-value: 5.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVfVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG-IGMVFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGL-LGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 163 NLDAALRVQMRIEISRLHKrlERTMIYVTH--DQVEAMtlADKIVVLDAGNIAQVG 216
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHivEDVESL--CNQVAVLNKGKLVFEG 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-226 |
8.06e-37 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 135.63 E-value: 8.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-----RGIGMVFQ-SYA-LYPHLSVA 93
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQdPYAsLNPRMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKLAGVKKAEiyQRVNQVAEVLQLAHL----LDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALR 169
Cdd:COG4608 116 DIIAEPLRIHGLASKA--ERRERVAELLELVGLrpehADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQ 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 170 VQ----MRieisRLHKRLERTMIYVTHD--QVEAMtlADKIVVLDAGNIAQVGKPLELYHYPA 226
Cdd:COG4608 194 AQvlnlLE----DLQDELGLTYLFISHDlsVVRHI--SDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-221 |
2.49e-36 |
|
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: 132.13 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTLSsvykaFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSG-ELLIGGKRMNEVPPSE--RGI 77
Cdd:COG1119 6 LRNVTVR-----RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWElrKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 GMVfqSYAL---YPHLSVAENM-------SFGLklagVKK--AEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIG 145
Cdd:COG1119 81 GLV--SPALqlrFPRDETVLDVvlsgffdSIGL----YREptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 146 RTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-222 |
7.19e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.68 E-value: 7.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNE--VPPSERGIGMVFQSyalyPH-----LSVA 93
Cdd:PRK13635 25 DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVRRQVGMVFQN----PDnqfvgATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMR 173
Cdd:PRK13635 101 DDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488140883 174 IEISRLHKRLERTMIYVTHDQVEAMTlADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13635 181 ETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-232 |
9.16e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 130.80 E-value: 9.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGL-----EDITSGELLIGGKRMNEVPPSE- 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 75 -RGIGMVFQSYALYPHLSVAENMSFGLKLAGV--KKAEIYQRVNQVAEVLQLAHLLDRRPKA----LSGGQRQRVAIGRT 147
Cdd:PRK14247 81 rRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 148 LVSEPDVFLLDEPLSNLDAalRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYP-- 225
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDP--ENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPrh 238
|
....*....
gi 488140883 226 --ANRFVAG 232
Cdd:PRK14247 239 elTEKYVTG 247
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-212 |
1.04e-35 |
|
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: 129.30 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 18 ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRmneVPPSER--GIGMVFQS--YALYPHlSVA 93
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERrkSIGYVMQDvdYQLFTD-SVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKLAGvkkaEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAAlrvQMR 173
Cdd:cd03226 91 EELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK---NME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488140883 174 iEISRLHKRL---ERTMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:cd03226 164 -RVGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-222 |
1.49e-35 |
|
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: 129.59 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 11 KAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSER---GIGMVFQSYALY 87
Cdd:cd03218 8 KRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 88 PHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDaA 167
Cdd:cd03218 88 RKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD-P 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488140883 168 LRVQmriEISRLHKRL-ERTM-IYVT-HDQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:cd03218 167 IAVQ---DIQKIIKILkDRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-212 |
1.58e-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: 129.25 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSyalyPHL---SVAE 94
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQD----VTLfygTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 95 NMSFGLKLAGVkkaeiyQRVNQVAEVLQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:cd03245 97 NITLGAPLADD------ERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488140883 164 LDaaLRVQMRIeISRLHKRL-ERTMIYVTHDQVeAMTLADKIVVLDAGNI 212
Cdd:cd03245 171 MD--MNSEERL-KERLRQLLgDKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-221 |
2.52e-35 |
|
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: 129.27 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 18 ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEV--PPSERGIGMVFQSYALYpHLSVAEN 95
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtlDSLRRAIGVVPQDTVLF-NDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 96 MSFGLKLAG-------VKKAEIYQRVNQVAEvlQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAAL 168
Cdd:cd03253 95 IRYGRPDATdeevieaAKAAQIHDKIMRFPD--GYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488140883 169 RVQMRIEISRLHKRleRTMIYVTHDQVEAMTlADKIVVLDAGNIAQVGKPLEL 221
Cdd:cd03253 173 EREIQAALRDVSKG--RTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-207 |
3.83e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 134.38 E-value: 3.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKrmnEVPPS------ERGI 77
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE---PVRFRsprdaqAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 GMVFQSYALYPHLSVAENMSFG---LKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDV 154
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGrepRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 155 FLLDEPLSNLDAAlrvqmriEISRLHKRLER------TMIYVTHDQVEAMTLADKIVVL 207
Cdd:COG1129 162 LILDEPTASLTER-------EVERLFRIIRRlkaqgvAIIYISHRLDEVFEIADRVTVL 213
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-216 |
1.72e-34 |
|
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: 126.87 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 5 TLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSER---GIGMVF 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 82 QSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQlaHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPL 161
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVLK--EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 162 SNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASG 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-221 |
1.87e-34 |
|
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: 126.64 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYkafGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSER---GIGMVFQ 82
Cdd:COG0410 9 LHAGY---GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SYALYPHLSVAENMSFGLKLAGvKKAEIYQRVNQVAEVL-QLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPL 161
Cdd:COG0410 86 GRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 162 SNLdAALRVQmriEISRLHKRLER---TMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:COG0410 165 LGL-APLIVE---EIFEIIRRLNRegvTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-216 |
3.59e-34 |
|
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: 124.97 E-value: 3.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 3 NVTLSSVYKAFGEAVIsRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELLIGGKRMNEVPPSERgIGMV 80
Cdd:cd03213 10 TVTVKSSPSKSGKQLL-KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSFRKI-IGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYALYPHLSVAENMSFGLKLAGvkkaeiyqrvnqvaevlqlahlldrrpkaLSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:cd03213 88 PQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 161 LSNLDAALRVQMRIEISRLHKrLERTMIYVTHD-QVEAMTLADKIVVLDAGNIAQVG 216
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-222 |
7.23e-34 |
|
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: 125.34 E-value: 7.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 18 ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPhLSVAEN 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 96 MSFGLKLAGV-------KKAEIYQRVNQVAEvlQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAA- 167
Cdd:cd03249 97 IRYGKPDATDeeveeaaKKANIHDFIMSLPD--GYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAEs 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 168 -LRVQMRIEisRLHKrlERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:cd03249 175 eKLVQEALD--RAMK--GRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-235 |
7.73e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 125.72 E-value: 7.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 13 FGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDIT-----SGELLIGGKRM--NEVPPSE--RGIGMVFQS 83
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEvrREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHLSVAENMSFGLKLAGV--KKAEIYQRV----NQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVewalKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 158 DEPLSNLDAAlrVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPAN----RFVAGF 233
Cdd:PRK14267 174 DEPTANIDPV--GTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHelteKYVTGA 251
|
..
gi 488140883 234 IG 235
Cdd:PRK14267 252 LG 253
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-212 |
1.53e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 125.20 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFG-----EAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG-- 76
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 77 IGMVFQSYAL--YPHLSVAENMS--------FGLKLaGVKKAEIYQRVNQVAEV-LQLAHLLDRRPKALSGGQRQRVAIG 145
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRR-GLTKKRRELFRELLATLgLGLENRLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 146 RTLVSEPDVFLLDEPLSNLD--AALRVqmrIEIS-RLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDpkTAALV---LELTeKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-221 |
1.92e-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: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPHlSVAENMS 97
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 98 FGLKLAGVKkaeiyqRVNQVAEVLQLAHLLDRRPKA-----------LSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD- 165
Cdd:cd03254 99 LGRPNATDE------EVIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARAMLRDPKILILDEATSNIDt 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 166 -AALRVQMRIEisRLHKrlERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:cd03254 173 eTEKLIQEALE--KLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
8-234 |
2.33e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 124.50 E-value: 2.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 8 SVYKAFGEAVisRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGELLIGGKrmNEVPPS------ERG 76
Cdd:PRK14239 12 SVYYNKKKAL--NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGH--NIYSPRtdtvdlRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 77 IGMVFQSYALYPhLSVAENMSFGLKLAGVKKAEIYQRVnqVAEVLQLAHLLDR-------RPKALSGGQRQRVAIGRTLV 149
Cdd:PRK14239 88 IGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEA--VEKSLKGASIWDEvkdrlhdSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 150 SEPDVFLLDEPLSNLDAAlrVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRF 229
Cdd:PRK14239 165 TSPKIILLDEPTSALDPI--SAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKE 242
|
....*
gi 488140883 230 VAGFI 234
Cdd:PRK14239 243 TEDYI 247
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-212 |
2.41e-33 |
|
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: 123.98 E-value: 2.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 15 EAVisRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGkrmnEVPPSERG-----IGMVF-QSYALYP 88
Cdd:cd03267 35 EAL--KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKkflrrIGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 89 HLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAAL 168
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488140883 169 RVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:cd03267 189 QENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-207 |
4.05e-33 |
|
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: 129.33 E-value: 4.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPHlS 91
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 92 VAENMSFGLKlaGVKKAEIYQRVNQV--AEVLQ-----LAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:TIGR02857 412 IAENIRLARP--DASDAEIREALERAglDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488140883 165 DAALRVQMRIEISRLHKRleRTMIYVTHDqVEAMTLADKIVVL 207
Cdd:TIGR02857 490 DAETEAEVLEALRALAQG--RTVLLVTHR-LALAALADRIVVL 529
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-193 |
5.49e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 123.00 E-value: 5.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG------IGMVFQSYALYPHLSVA 93
Cdd:PRK11629 26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqkLGFIYQFHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMR 173
Cdd:PRK11629 106 ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170 180
....*....|....*....|
gi 488140883 174 IEISRLHKRLERTMIYVTHD 193
Cdd:PRK11629 186 QLLGELNRLQGTAFLVVTHD 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-210 |
1.22e-32 |
|
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: 119.84 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE---RGIGMV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQsyalyphlsvaenmsfglklagvkkaeiyqrvnqvaevlqlahlldrrpkaLSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 161 LSNLDAAlrvqmriEISRLHKRLER------TMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:cd03216 110 TAALTPA-------EVERLFKVIRRlraqgvAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-228 |
1.51e-32 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 122.87 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-----RGIGMVFQSY--ALYPHLSV 92
Cdd:PRK10419 29 NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSisAVNPRKTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 93 AENMSFGLK-LAGVKKAEIYQRVNQVAEVLQLA-HLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRV 170
Cdd:PRK10419 109 REIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488140883 171 QMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNI---AQVGKPLELYHyPANR 228
Cdd:PRK10419 189 GVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvetQPVGDKLTFSS-PAGR 248
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-222 |
3.83e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 121.76 E-value: 3.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNE--VPPSERGIGMVFQSyalyPH-----LSVA 93
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenVWDIRHKIGMVFQN----PDnqfvgATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMR 173
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488140883 174 IEISRLHKRLERTMIYVTHDqVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13650 181 KTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELF 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-221 |
8.52e-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: 125.30 E-value: 8.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGEL--LIGGK--RMNEVPPSERG-----IGMVFQSYALYPHLSV 92
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDEwvDMTKPGPDGRGrakryIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 93 AENM--SFGLKLA---GVKKAEIYQRVNQVAEVlQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAA 167
Cdd:TIGR03269 383 LDNLteAIGLELPdelARMKAVITLKMVGFDEE-KAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPI 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488140883 168 LRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:TIGR03269 462 TKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-222 |
2.11e-31 |
|
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: 118.87 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 3 NVTLSsvYKAFGEAVIsRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMV 80
Cdd:cd03251 5 NVTFR--YPGDGPPVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYALYpHLSVAENMSFGLKLAGVKkaeiyqrvnQVAEVLQLAHLLD--------------RRPKALSGGQRQRVAIGR 146
Cdd:cd03251 82 SQDVFLF-NDTVAENIAYGRPGATRE---------EVEEAARAANAHEfimelpegydtvigERGVKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488140883 147 TLVSEPDVFLLDEPLSNLDaaLRVQMRIE--ISRLHKRleRTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:cd03251 152 ALLKDPPILILDEATSALD--TESERLVQaaLERLMKN--RTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
12-220 |
2.99e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 118.96 E-value: 2.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 12 AFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGigmvfQSYALYP--H 89
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-----RRLALLPqhH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 90 L-----SVAENMSFG----LKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:PRK11231 86 LtpegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 161 LSNLDaalrVQMRIEISRLHKRLE---RTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLE 220
Cdd:PRK11231 166 TTYLD----INHQVELMRLMRELNtqgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-225 |
3.29e-31 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 123.64 E-value: 3.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 16 AVisRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGELLIGGKRMNEVPPSE-----RGIGMVFQS-YA-LYP 88
Cdd:COG4172 301 AV--DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 89 HLSVAENMSFGLKL--AGVKKAEIYQRVnqvAEVLQLAHL----LDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:COG4172 378 RMTVGQIIAEGLRVhgPGLSAAERRARV---AEALEEVGLdpaaRHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 163 NLDAALRVQMrIEI-SRLHKRLERTMIYVTHDQ--VEAMtlADKIVVLDAGNIAQVGKPLELYHYP 225
Cdd:COG4172 455 ALDVSVQAQI-LDLlRDLQREHGLAYLFISHDLavVRAL--AHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-210 |
4.14e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 123.21 E-value: 4.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKrmnEVPPS------ERGI 77
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRsprdaiALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 GMVFQSYALYPHLSVAENMSFGL---KLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDV 154
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 155 FLLDEPLSNLDAAlrvqmriEISRLHKRLER------TMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:COG3845 163 LILDEPTAVLTPQ-------EADELFEILRRlaaegkSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-212 |
4.88e-31 |
|
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: 124.21 E-value: 4.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYpHLSVAENMS 97
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTLRDNIA 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 98 FGLklAGVKKAEIyQRVNQVAEVLQLAHL----LDR----RPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAalR 169
Cdd:TIGR03375 561 LGA--PYADDEEI-LRAAELAGVTEFVRRhpdgLDMqigeRGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDN--R 635
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488140883 170 VQMRIeISRLHKRLE-RTMIYVTHdQVEAMTLADKIVVLDAGNI 212
Cdd:TIGR03375 636 SEERF-KDRLKRWLAgKTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
6-222 |
5.95e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 118.75 E-value: 5.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVISrDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGL---EDITSGELLIGGKRMNE--VPPSERGIGMV 80
Cdd:PRK13640 11 VSFTYPDSKKPALN-DISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAktVWDIREKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSyalyPH-----LSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVF 155
Cdd:PRK13640 90 FQN----PDnqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 156 LLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAmTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIF 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
15-222 |
7.66e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.32 E-value: 7.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 15 EAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSyalyPH--- 89
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQN----PDnqf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 90 --LSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAA 167
Cdd:PRK13648 97 vgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 168 LRVQMRIEISRLHKRLERTMIYVTHDQVEAMTlADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-227 |
1.12e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 122.10 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELliggkrmnEVPPSERgIGMVFQSYA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLR-IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 86 LYPHLSVAENMSFGLK-LAGVKK--AEIYQ-----------------------------RVNQVAEVLQLAH-LLDRRPK 132
Cdd:COG0488 72 LDDDLTVLDTVLDGDAeLRALEAelEELEAklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEeDLDRPVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 133 ALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDaalrvqmrIE-ISRLHKRLER---TMIYVTHD-----QVeamtlADK 203
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--------LEsIEWLEEFLKNypgTVLVVSHDryfldRV-----ATR 218
|
250 260
....*....|....*....|....
gi 488140883 204 IVVLDAGniaqvgkplELYHYPAN 227
Cdd:COG0488 219 ILELDRG---------KLTLYPGN 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
7-228 |
1.97e-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: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 7 SSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-----RGIGMVF 81
Cdd:TIGR02769 15 GGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 82 Q-SY-ALYPHLSVAENMSFGLK-LAGVKKAEIYQRVNQVAEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:TIGR02769 95 QdSPsAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 158 DEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL--YHYPANR 228
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLlsFKHPAGR 247
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-203 |
2.26e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 116.81 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 8 SVYkaFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGELLIGGKRMN--EVPPSE--RGIG 78
Cdd:PRK14243 17 NVY--YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYapDVDPVEvrRRIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 79 MVFQSYALYPHlSVAENMSFGLKLAGVKKA--EIYQR-VNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVF 155
Cdd:PRK14243 95 MVFQKPNPFPK-SIYDNIAYGARINGYKGDmdELVERsLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488140883 156 LLDEPLSNLD--AALRVQmrieisRLHKRLER--TMIYVTHDQVEAMTLADK 203
Cdd:PRK14243 174 LMDEPCSALDpiSTLRIE------ELMHELKEqyTIIIVTHNMQQAARVSDM 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-207 |
2.53e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 114.64 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 12 AFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRmnevppserGIGMVFQSYAL---YP 88
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA---------RVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 89 hLSVAENMSFGL----KLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:NF040873 72 -LTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488140883 165 DAALRVQMRIEISRLHKRlERTMIYVTHDqVEAMTLADKIVVL 207
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHD-LELVRRADPCVLL 191
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-216 |
3.89e-30 |
|
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: 114.94 E-value: 3.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKrmnEVPPSERGIGMVfqsyalyPHLSVAENMSFG 99
Cdd:cd03220 39 KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---VSSLLGLGGGFN-------PELTGRENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 LKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRL 179
Cdd:cd03220 109 GRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 488140883 180 HKRlERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:cd03220 189 LKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
11-182 |
6.92e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 114.74 E-value: 6.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 11 KAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSER---GIGMVFQSYALY 87
Cdd:COG1137 11 KSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 88 PHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD-- 165
Cdd:COG1137 91 RKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpi 170
|
170
....*....|....*..
gi 488140883 166 AALRVQmRIeISRLHKR 182
Cdd:COG1137 171 AVADIQ-KI-IRHLKER 185
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-225 |
7.64e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.07 E-value: 7.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTLS--SVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE---- 74
Cdd:PRK10619 1 MSENKLNviDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 75 -----------RGIGMVFQSYALYPHLSVAEN-MSFGLKLAGVKKAEIYQR-VNQVAEVLQLAHLLDRRPKALSGGQRQR 141
Cdd:PRK10619 81 vadknqlrllrTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERaVKYLAKVGIDERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 142 VAIGRTLVSEPDVFLLDEPLSNLDAALRVqmriEISRLHKRLE---RTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKP 218
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVG----EVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
....*..
gi 488140883 219 LELYHYP 225
Cdd:PRK10619 237 EQLFGNP 243
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-225 |
1.79e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 115.96 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGK---RMNEVPPSE--RGIGMVFQS--YALYPHLSVA 93
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdllGMKDDEWRAvrSDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKL--AGVKKAEIYQRV-NQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRV 170
Cdd:PRK15079 119 EIIAEPLRTyhPKLSRQEVKDRVkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 171 QmrieISRLHKRLERTM----IYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYP 225
Cdd:PRK15079 199 Q----VVNLLQQLQREMglslIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-212 |
4.13e-29 |
|
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: 110.77 E-value: 4.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG--IGMVFQSYALYPHlS 91
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGYLPQDDELFSG-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 92 VAENMsfglklagvkkaeiyqrvnqvaevlqlahlldrrpkaLSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQ 171
Cdd:cd03246 92 IAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488140883 172 MRIEISRLHKRlERTMIYVTHdQVEAMTLADKIVVLDAGNI 212
Cdd:cd03246 135 LNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-222 |
5.71e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 113.26 E-value: 5.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGG---KRMNEVPPSERGIGMVFQSyalyPHLS-----V 92
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PDNQivatiV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 93 AENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQM 172
Cdd:PRK13633 104 EEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488140883 173 RIEISRLHKRLERTMIYVTHDQVEAMTlADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13633 184 VNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-207 |
7.26e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 111.73 E-value: 7.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPHlS 91
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 92 VAENMSFGLKLAGvkkaeiyQRVNQVAEVLQLA------HLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD 165
Cdd:PRK10247 97 VYDNLIFPWQIRN-------QQPDPAIFLDDLErfalpdTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488140883 166 AALRVQMRIEISRLHKRLERTMIYVTHDQVEaMTLADKIVVL 207
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-224 |
1.02e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 111.71 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRmneVPPSERGIGMVfqsyalyPHLSVAENMSFG 99
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV---SALLELGAGFH-------PELTGRENIYLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 LKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALR--VQMRIEis 177
Cdd:COG1134 113 GRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQkkCLARIR-- 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488140883 178 rlhKRLE--RTMIYVTHD--QVEamTLADKIVVLDAGNIAQVGKP---LELYHY 224
Cdd:COG1134 191 ---ELREsgRTVIFVSHSmgAVR--RLCDRAIWLEKGRLVMDGDPeevIAAYEA 239
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-212 |
2.08e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 112.87 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 15 EAVisRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRmnevpPSE------RGIGMVF-QSYALY 87
Cdd:COG4586 36 EAV--DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKrrkefaRRIGVVFgQRSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 88 PHLSVAEnmSFGL--KLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD 165
Cdd:COG4586 109 WDLPAID--SFRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488140883 166 AALRVQMRIEISRLHKRLERTMIYVTHD--QVEAmtLADKIVVLDAGNI 212
Cdd:COG4586 187 VVSKEAIREFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHGRI 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-222 |
2.24e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 111.72 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMN--EVPPSERGIGMVFQSY-ALYPHLSVAENMSF 98
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNPdNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 99 GLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISR 178
Cdd:PRK13642 106 GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488140883 179 LHKRLERTMIYVTHDQVEAMTlADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13642 186 IKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-222 |
2.71e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 112.02 E-value: 2.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 23 NLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGG-------KRMNEVPPSERGIGMVFQ--SYALYPHlSVA 93
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVFQfpEYQLFQE-TIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAH-LLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQM 172
Cdd:PRK13645 110 KDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDF 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488140883 173 RIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13645 190 INLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-222 |
3.53e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 111.37 E-value: 3.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMN------EVPPSERGIGMVFQsyalYPHL---- 90
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPESqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 91 -SVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAH-LLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAal 168
Cdd:PRK13649 101 eTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP-- 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 169 rvQMRIEISRLHKRLER---TMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13649 179 --KGRKELMTLFKKLHQsgmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-193 |
4.48e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 109.48 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVIS--RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGK---RMNEVPPSE---RGIGMVFQSYA 85
Cdd:PRK10584 19 GEHELSilTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhQMDEEARAKlraKHVGFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 86 LYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD 165
Cdd:PRK10584 99 LIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180
....*....|....*....|....*...
gi 488140883 166 AALRVQMRIEISRLHKRLERTMIYVTHD 193
Cdd:PRK10584 179 RQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-216 |
5.61e-28 |
|
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: 109.28 E-value: 5.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 3 NVTLSSVyKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLED---ITSGELLIGGKRMN--EVPPSergI 77
Cdd:cd03234 8 DVGLKAK-NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKpdQFQKC---V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 GMVFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVnQVAEVLQLAHLLDRRP-----KALSGGQRQRVAIGRTLVSEP 152
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRK-KRVEDVLLRDLALTRIggnlvKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 153 DVFLLDEPLSNLDAALRVQMRIEISRLHKRlERTMIYVTHD-QVEAMTLADKIVVLDAGNIAQVG 216
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-221 |
6.26e-28 |
|
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: 109.50 E-value: 6.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFG--EAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPS--ERGIGM 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 80 VFQSYALYpHLSVAENMSFGLKLAGVKKAEIYQRVNQVAE-VLQLAH----LLDRRPKALSGGQRQRVAIGRTLVSEPDV 154
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALADPGMSMERVIEAAKLAGAHDfISELPEgydtIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488140883 155 FLLDEPLSNLDAAlrvQMRIEISRLHKRLE-RTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:cd03252 160 LIFDEATSALDYE---SEHAIMRNMHDICAgRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-238 |
6.88e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 110.59 E-value: 6.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGG------KRMNEVPPSERGIGMVFQ--SYALYPHlSV 92
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstSKQKEIKPVRKKVGVVFQfpESQLFEE-TV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 93 AENMSFGLKLAGVKKAEIYQRVNQVAEVLQLA-HLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQ 171
Cdd:PRK13643 103 LKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 172 MRIEISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHyPANRFVAGFIGSPK 238
Cdd:PRK13643 183 MMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ-EVDFLKAHELGVPK 247
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-230 |
1.01e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.08 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGG---KRMNEVPPSERGIGMVFQS-YALYPHLSVAEN 95
Cdd:PRK13644 19 ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKLQGIRKLVGIVFQNpETQFVGRTVEED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 96 MSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIE 175
Cdd:PRK13644 99 LAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLER 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 176 ISRLHKRlERTMIYVTHDqVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFV 230
Cdd:PRK13644 179 IKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-286 |
1.03e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 112.24 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIG 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 79 MVFQSYALYPHLSVAENMSFGL-----KLAGVKKAEiYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPD 153
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRtphrsRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 154 VFLLDEPLSNLDAALRVQMrIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELyhYPANRFVAGF 233
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRT-LELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV--LTADTLRAAF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488140883 234 -----------IGSPKMNFLPVKVTAAEPRQVQIELPNHQRVWLPVEGDQVQVGANMSLGIRPE 286
Cdd:PRK09536 237 dartavgtdpaTGAPTVTPLPDPDRTEAAADTRVHVVGGGQPAARAVSRLVAAGASVSVGPVPE 300
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-193 |
1.04e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 108.42 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGK-----RMNEVPPSERGIGMVFQSYALYPHLSVAENM 96
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditrlKNREVPFLRRQIGMIFQDHHLLMDRTVYDNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 97 SFGLKLAGVKKAEIYQRVnqvAEVLQLAHLLDRR---PKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVqmr 173
Cdd:PRK10908 101 AIPLIIAGASGDDIRRRV---SAALDKVGLLDKAknfPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE--- 174
|
170 180
....*....|....*....|...
gi 488140883 174 iEISRLHKRLER---TMIYVTHD 193
Cdd:PRK10908 175 -GILRLFEEFNRvgvTVLMATHD 196
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-222 |
1.06e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.94 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEvppSERG-------IGMVFQS--YALYPhL 90
Cdd:PRK13636 23 KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY---SRKGlmklresVGMVFQDpdNQLFS-A 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 91 SVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRV 170
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488140883 171 QMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-167 |
1.64e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 107.65 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERgIGMVFQSYALYPHLSVA 93
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488140883 94 ENMSFGLKLAGVKKAEIYQrvnqVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAA 167
Cdd:PRK13539 92 ENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-221 |
2.15e-27 |
|
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: 107.63 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 24 LEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNevpPSERGIGMVFQSYAL---YPhLSVAEN-MSFG 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPG---KGWRHIGYVPQRHEFawdFP-ISVAHTvMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 LKLAGV----KKAEiYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD---AALRVQM 172
Cdd:TIGR03771 77 TGHIGWlrrpCVAD-FAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDmptQELLTEL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488140883 173 RIEISrlhkRLERTMIYVTHDQVEAMTLADKIVVLDaGNIAQVGKPLEL 221
Cdd:TIGR03771 156 FIELA----GAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQL 199
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-212 |
2.21e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 113.67 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGI------GMVFQSYALYPHLSVA 93
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrrehfGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQ-M 172
Cdd:PRK10535 105 QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEvM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488140883 173 RIeisrLHKRLER--TMIYVTHD-QVEAMtlADKIVVLDAGNI 212
Cdd:PRK10535 185 AI----LHQLRDRghTVIIVTHDpQVAAQ--AERVIEIRDGEI 221
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-234 |
2.64e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 108.21 E-value: 2.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDI------TSGELLIGGKRMNEVPPSE--RGI 77
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKDIFQIDAIKlrKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 GMVFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVnqVAEVLQLAHL-------LDRRPKALSGGQRQRVAIGRTLVS 150
Cdd:PRK14246 93 GMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKVGLwkevydrLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 151 EPDVFLLDEPLSNLDAALRVQMRIEISRLHKrlERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFV 230
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
....
gi 488140883 231 AGFI 234
Cdd:PRK14246 249 EKYV 252
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
3.47e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 109.12 E-value: 3.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 2 ANVTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG-IGMV 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488140883 161 LSNLDAALRVQMrieISRLHKRLER--TMIYVTHDQVEAMTLADKIVVLDAG-NIAQvGKPLEL 221
Cdd:PRK13537 166 TTGLDPQARHLM---WERLRSLLARgkTILLTTHFMEEAERLCDRLCVIEEGrKIAE-GAPHAL 225
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-217 |
3.85e-27 |
|
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: 112.44 E-value: 3.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG--IGMVFQSYALYPHlS 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 92 VAENMS-FGlklAGVKKAEIYQrvnqvAEVLQLAH-LLDRRPK-----------ALSGGQRQRVAIGRTLVSEPDVFLLD 158
Cdd:TIGR01842 408 VAENIArFG---ENADPEKIIE-----AAKLAGVHeLILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLD 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 159 EPLSNLDAALRVQMRIEISRLHKRlERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGK 217
Cdd:TIGR01842 480 EPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGE 536
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-220 |
4.62e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.51 E-value: 4.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPHLSVAENMS 97
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLAFPFTVEEVVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 98 FGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTL--VSEPDVF-----LLDEPLSNLDaaLRV 170
Cdd:COG4559 98 LGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVDGgprwlFLDEPTSALD--LAH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488140883 171 QMRI-EISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLE 220
Cdd:COG4559 176 QHAVlRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-221 |
6.54e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 107.38 E-value: 6.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 12 AFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPH 89
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 90 LSVAENMSFG----LKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD 165
Cdd:PRK10253 96 ITVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 166 AALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-210 |
9.89e-27 |
|
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: 105.24 E-value: 9.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGkrmnevppserGIGMVFQSyalyPHL---SVAENM 96
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQE----PWIqngTIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 97 SFGLKLagvkkaeIYQRVNQVAEVLQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD 165
Cdd:cd03250 87 LFGKPF-------DEERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488140883 166 AalRVQMRIeISRL---HKRLERTMIYVTHdQVEAMTLADKIVVLDAG 210
Cdd:cd03250 160 A--HVGRHI-FENCilgLLLNNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-225 |
2.16e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.43 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVisRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQS 83
Cdd:PRK13652 9 LCYSYSGSKEAL--NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 ---YALYPhlSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:PRK13652 87 pddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 161 LSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYP 225
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-221 |
3.08e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 105.15 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 18 ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELLIGGKRMNEVPPSER---GIGMVFQsyalYPhlsv 92
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIFLAFQ----YP---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 93 AE-----NMSFgLKLA-------GVKKAEIYQRVNQVAEVLQLAHLLDRRP--KALSGGQRQRVAIGRTLVSEPDVFLLD 158
Cdd:COG0396 87 VEipgvsVSNF-LRTAlnarrgeELSAREFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 159 EPLSNLDA-ALRVqMRIEISRLHKRlERTMIYVTH-----DQVEamtlADKIVVLDAGNIAQVGKPlEL 221
Cdd:COG0396 166 ETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHyqrilDYIK----PDFVHVLVDGRIVKSGGK-EL 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-167 |
3.36e-26 |
|
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: 103.59 E-value: 3.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPS-ERGIGMVFQSYALYPHLSV 92
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 93 AENMSFGLKLAGVKKAEIYQRVNQVAevlqLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAA 167
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIEDALAAVG----LTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-227 |
4.90e-26 |
|
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: 103.99 E-value: 4.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGELLIGGKRMNEVPPSERGIGMVFQS--YALYPHLSVAE 94
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 95 NMSFGLKLAGVKKAEIYQRVNQVAEVLQLAH---LLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQ 171
Cdd:TIGR02770 84 HAIETLRSLGKLSKQARALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 172 MRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPAN 227
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-222 |
7.77e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.91 E-value: 7.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE------RGIGMVFQsyalYPHL---- 90
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklrKKVSLVFQ----FPEAqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 91 -SVAENMSFGLKLAGV--KKAEIyQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAA 167
Cdd:PRK13641 101 nTVLKDVEFGPKNFGFseDEAKE-KALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 168 LRVQMrIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13641 180 GRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-221 |
1.14e-25 |
|
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: 108.37 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 18 ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYpHLSVAEN 95
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 96 MSFGlkLAGVKKAEiyqrvnqVAEVLQLAHLLD---RRPKA-----------LSGGQRQRVAIGRTLVSEPDVFLLDEPL 161
Cdd:COG5265 452 IAYG--RPDASEEE-------VEAAARAAQIHDfieSLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488140883 162 SNLD--------AALRvqmriEISRlhkrlERTMIYVTH------DqveamtlADKIVVLDAGNIAQVGKPLEL 221
Cdd:COG5265 523 SALDsrteraiqAALR-----EVAR-----GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAEL 579
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
16-221 |
1.28e-25 |
|
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: 108.29 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 16 AVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPS--ERGIGMVFQSYALYPHlSVA 93
Cdd:TIGR01846 470 PEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFG------------LKLAGVKKAEIYQRVNQVAEVlqlahllDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPL 161
Cdd:TIGR01846 549 DNIALCnpgapfehvihaAKLAGAHDFISELPQGYNTEV-------GEKGANLSGGQRQRIAIARALVGNPRILIFDEAT 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488140883 162 SNLD----AALRVQMRiEISRlhkrlERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:TIGR01846 622 SALDyeseALIMRNMR-EICR-----GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-222 |
1.36e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.48 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMN------EVPPSERGIGMVFQsyalYPHL--- 90
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkYIRPVRKRIGMVFQ----FPESqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 91 --SVAENMSFGLKLAGVKKAEIYQRVNQVaeVLQLA---HLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD 165
Cdd:PRK13646 100 edTVEREIIFGPKNFKMNLDEVKNYAHRL--LMDLGfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488140883 166 AalrvQMRIEISRLHKRLE----RTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13646 178 P----QSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-222 |
1.55e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.93 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVY--KAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGL----------EDITSGELLIGGKRMNEVPPS 73
Cdd:PRK13631 27 LYCVFdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELITNPYSK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 74 E--------RGIGMVFQ--SYALYPHlSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAH-LLDRRPKALSGGQRQRV 142
Cdd:PRK13631 107 KiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 143 AIGRTLVSEPDVFLLDEPLSNLDAALRVQMrIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-222 |
1.60e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.00 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPS----ERGIGMVFQS-----YAlyPhl 90
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevRKTVGIVFQNpddqlFA--P-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 91 SVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAalrv 170
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP---- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 171 QMRIEISRLHKRLER---TMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13639 171 MGASQIMKLLYDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
14-218 |
1.69e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.31 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPHLS 91
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 92 VAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLV------SEPDVFLLDEPLSNLD 165
Cdd:PRK13548 93 VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 166 aaLRVQmrIEISRLHKRLER----TMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKP 218
Cdd:PRK13548 173 --LAHQ--HHVLRLARQLAHerglAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-216 |
1.89e-25 |
|
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: 107.53 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG--IGMVFQSYALYPHlS 91
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 92 VAENMS-FG----------LKLAGVKKAeiyqrvnqvaeVLQLAH----LLDRRPKALSGGQRQRVAIGRTLVSEPDVFL 156
Cdd:COG4618 422 IAENIArFGdadpekvvaaAKLAGVHEM-----------ILRLPDgydtRIGEGGARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488140883 157 LDEPLSNLD----AALRVQmrieISRLHKRlERTMIYVTHDQvEAMTLADKIVVLDAGNIAQVG 216
Cdd:COG4618 491 LDEPNSNLDdegeAALAAA----IRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFG 548
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-221 |
3.19e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 102.81 E-value: 3.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 18 ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDItSGELLIGGK----------RMNEVPPSERGIGMVFQSYALY 87
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRveffnqniyeRRVNLNRLRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 88 PhLSVAENMSFGLKLAG----VKKAEIYQRVNQVAEVL-QLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:PRK14258 101 P-MSVYDNVAYGVKIVGwrpkLEIDDIVESALKDADLWdEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 163 NLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADkIVVLDAGNIAQVGKPLEL 221
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD-FTAFFKGNENRIGQLVEF 237
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-223 |
3.80e-25 |
|
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: 101.06 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELLIGGKRMNEVPPSER---GIGMVFQSYALYP 88
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 89 hlsvaenmsfglklaGVKKAEIYQRVNqvaevlqlahlldrrpKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDA-A 167
Cdd:cd03217 91 ---------------GVKNADFLRYVN----------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIdA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488140883 168 LRVQMRIeISRLHKRlERTMIYVTH-----DQVEamtlADKIVVLDAGNIAQVGkPLELYH 223
Cdd:cd03217 140 LRLVAEV-INKLREE-GKSVLIITHyqrllDYIK----PDRVHVLYDGRIVKSG-DKELAL 193
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-218 |
4.33e-25 |
|
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: 102.10 E-value: 4.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 25 EIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPsergigmvfQSYALYPhlSVAENMSFGlKLAG 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQ---------YIKADYE--GTVRDLLSS-ITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 105 VKKAEIYQrvNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDaalrVQMRIEISRLHKRL- 183
Cdd:cd03237 89 FYTHPYFK--TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD----VEQRLMASKVIRRFa 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 488140883 184 ---ERTMIYVTHDQVEAMTLADKIVVLDagniaqvGKP 218
Cdd:cd03237 163 ennEKTAFVVEHDIIMIDYLADRLIVFE-------GEP 193
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-269 |
5.16e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.51 E-value: 5.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-----RGIGMVFQS-YA-LYPHLSVA 93
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNPRKKVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKL-AGVKKAEiyqRVNQVAEVLQLAHL----LDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAAL 168
Cdd:PRK11308 113 QILEEPLLInTSLSAAE---RREKALAMMAKVGLrpehYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 169 RVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGS-PKMNflpvkvt 247
Cdd:PRK11308 190 QAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSAtPRLN------- 262
|
250 260 270
....*....|....*....|....*....|....*.
gi 488140883 248 aAEPRQVQI----ELPN----------HQRVWLPVE 269
Cdd:PRK11308 263 -PDDRRERIkltgELPSplnpppgcafNARCPRAFG 297
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-219 |
7.61e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.12 E-value: 7.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVisRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-RG-IGMVFQS 83
Cdd:PRK13647 10 LHFRYKDGTKAL--KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSkVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 yalyPH-----LSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLD 158
Cdd:PRK13647 88 ----PDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 159 EPLSNLDAALRVQMRIEISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAGN-IAQVGKPL 219
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRvLAEGDKSL 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-193 |
7.87e-25 |
|
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: 105.52 E-value: 7.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSyalyPHL- 90
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQD----AHLf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 91 --SVAENMSFGLKlaGVKKAEIYQrvnqVAEVLQLAHLLDRRP-----------KALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:TIGR02868 422 dtTVRENLRLARP--DATDEELWA----ALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*..
gi 488140883 158 DEPLSNLDAALRVQMrieISRLHKRL-ERTMIYVTHD 193
Cdd:TIGR02868 496 DEPTEHLDAETADEL---LEDLLAALsGRTVVLITHH 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-233 |
1.24e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 104.88 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDI--TSGELLIGGKRMNEV----PPSERG- 76
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHVALCEKCgyveRPSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 77 ------------------------------IGMVFQ-SYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAH 125
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdklrrrirkrIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 126 LLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIV 205
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260
....*....|....*....|....*...
gi 488140883 206 VLDAGNIAQVGKPLELyhypANRFVAGF 233
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV----VAVFMEGV 264
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-212 |
1.33e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.76 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKrmnevppsergigmVFQS 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET--------------VKIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 Y------ALYPHLSVAENMSFGLKlaGVKKAEIYQRvnqvaevlqLAHLL------DRRPKALSGGQRQRVAIGRTLVSE 151
Cdd:COG0488 382 YfdqhqeELDPDKTVLDELRDGAP--GGTEQEVRGY---------LGRFLfsgddaFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 152 PDVFLLDEPLSNLDaalrVQMRiEIsrlhkrLER-------TMIYVTHDQ--VEamTLADKIVVLDAGNI 212
Cdd:COG0488 451 PNVLLLDEPTNHLD----IETL-EA------LEEalddfpgTVLLVSHDRyfLD--RVATRILEFEDGGV 507
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-221 |
1.45e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.60 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKrmnEVPPSER----GIGM 79
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV---PVPARARlaraRIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 80 VFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDE 159
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 160 PLSNLDAALRvqmRIEISRLHKRLER--TMIYVTHDQVEAMTLADKIVVLDAG-NIAQvGKPLEL 221
Cdd:PRK13536 199 PTTGLDPHAR---HLIWERLRSLLARgkTILLTTHFMEEAERLCDRLCVLEAGrKIAE-GRPHAL 259
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-220 |
1.72e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 101.70 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSG-----------------------ELLIG---GKRMNEVPPSE 74
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekekvleKLVIQktrFKKIKKIKEIR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 75 RGIGMVFQ--SYALYPHlSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVSE 151
Cdd:PRK13651 105 RRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAME 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 152 PDVFLLDEPLSNLDAALRVQMRIEISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLE 220
Cdd:PRK13651 184 PDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-264 |
2.32e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 103.98 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPS---ERGIGMVFQ 82
Cdd:PRK15439 14 ARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkahQLGIYLVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SYALYPHLSVAENMSFGLKlagvKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:PRK15439 94 EPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 163 NLDAAlrvqmriEISRLHKRLERT------MIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLElyhYPANRFVAGFigS 236
Cdd:PRK15439 170 SLTPA-------ETERLFSRIRELlaqgvgIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD---LSTDDIIQAI--T 237
|
250 260
....*....|....*....|....*...
gi 488140883 237 PKMNflpvKVTAAEPRQVQIELPNHQRV 264
Cdd:PRK15439 238 PAAR----EKSLSASQKLWLELPGNRRQ 261
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-221 |
2.87e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 99.58 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSER---GI 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 GMVFQSYALYPHLSVAENMSFGLKLAGVKKAEIYQ-RVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFL 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 157 LDEPLSNLDAALRVQMRIEISRLHKRLERTMIyVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLI-TDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-221 |
3.85e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.77 E-value: 3.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITsGELLIGGKRMNEVPPSE--RGIGMVFQSYALyPHLSVAENMSFG 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 LKLAGvkKAEIYQRVNQ--VAE-VLQLAHLLDRRPK----ALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDA------ 166
Cdd:PRK11174 447 NPDAS--DEQLQQALENawVSEfLPLLPQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAhseqlv 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 167 --ALRVQMRieisrlhkrlERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:PRK11174 525 mqALNAASR----------RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
17-221 |
3.94e-24 |
|
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: 103.88 E-value: 3.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 17 VISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPHlSVAE 94
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAvrRQLGVVLQNGRLMSG-SIFE 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 95 NMSFGLKLAgvkkaeiyqrVNQVAEVLQLAHL---LDRRP-----------KALSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:TIGR03797 546 NIAGGAPLT----------LDEAWEAARMAGLaedIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILLFDEA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488140883 161 LSNLDAalRVQmRIEISRLhKRLERTMIYVTHDQVEAMTlADKIVVLDAGNIAQVGKPLEL 221
Cdd:TIGR03797 616 TSALDN--RTQ-AIVSESL-ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDEL 671
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-210 |
5.45e-24 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 98.66 E-value: 5.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLI----GGKRMNEVPPSE------RGIGMVFQSYALYPH 89
Cdd:COG4778 28 DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPREilalrrRTIGYVSQFLRVIPR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 90 LS----VAEnmsfGLKLAGVKKAEIYQRvnqvAEVLqLAHL-LDRR-----PKALSGGQRQRVAIGRTLVSEPDVFLLDE 159
Cdd:COG4778 108 VSaldvVAE----PLLERGVDREEARAR----AREL-LARLnLPERlwdlpPATFSGGEQQRVNIARGFIADPPLLLLDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488140883 160 PLSNLDAALRvqmRIEISRLHKRLER--TMIYVTHDQvEAM-TLADKIVVLDAG 210
Cdd:COG4778 179 PTASLDAANR---AVVVELIEEAKARgtAIIGIFHDE-EVReAVADRVVDVTPF 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-192 |
6.45e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.96 E-value: 6.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 17 VISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELliggkrmnEVPPSERgigMVF---QSY--------A 85
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR---VLFlpqRPYlplgtlreA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 86 L-YPHLsvAENMSfglklagvkKAEIyqrvnqvAEVLQ---LAHLLDR------RPKALSGGQRQRVAIGRTLVSEPDVF 155
Cdd:COG4178 446 LlYPAT--AEAFS---------DAEL-------REALEavgLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190
....*....|....*....|....*....|....*...
gi 488140883 156 LLDEPLSNLDAALRVQMrieISRLHKRLER-TMIYVTH 192
Cdd:COG4178 508 FLDEATSALDEENEAAL---YQLLREELPGtTVISVGH 542
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-233 |
6.71e-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: 103.94 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVISRdINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRM-NEVPPSERGIGMVFQSY 84
Cdd:TIGR01257 934 LVKIFEPSGRPAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 85 ALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:TIGR01257 1013 ILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 165 DAALRvqMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELyhypANRFVAGF 233
Cdd:TIGR01257 1093 DPYSR--RSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-221 |
1.14e-23 |
|
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: 102.51 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 13 FGEAVISrDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPHl 90
Cdd:TIGR01193 485 YGSNILS-DISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFINYLPQEPYIFSG- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 91 SVAENMSFGLK--------LAGVKKAEIYQRVNQVAEVLQLAhlLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:TIGR01193 563 SILENLLLGAKenvsqdeiWAACEIAEIKDDIENMPLGYQTE--LSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 163 NLDAALrvQMRIeISRLHKRLERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:TIGR01193 641 NLDTIT--EKKI-VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-212 |
1.33e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 98.55 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGL--EDITSG---ELL-----IGGKRMNEVPPSERGIGMVFQSYALYPHLS 91
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGshiELLgrtvqREGRLARDIRKSRANTGYIFQQFNLVNRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 92 VAENMSFGLK------------LAGVKKAEIYQRVNQVAevlqLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDE 159
Cdd:PRK09984 103 VLENVLIGALgstpfwrtcfswFTREQKQRALQALTRVG----MVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 160 PLSNLDAAlrvQMRIEISRLH--KRLERTMIYVTHDQVE-AMTLADKIVVLDAGNI 212
Cdd:PRK09984 179 PIASLDPE---SARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-221 |
1.86e-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: 101.72 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPHlSVAENMS 97
Cdd:TIGR02203 349 DSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVALVSQDVVLFND-TIANNIA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 98 FGlKLAGVKKAEIyqrvNQVAEVLQLAHLLDRRPKA-----------LSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDA 166
Cdd:TIGR02203 428 YG-RTEQADRAEI----ERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARALLKDAPILILDEATSALDN 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 167 ALRVQMRIEISRLHKrlERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:TIGR02203 503 ESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-212 |
2.06e-23 |
|
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: 101.30 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 15 EAVisRDINLEIDDGEFVVFVGPSGCGKS----TLLRMIAGLEDITSGELLIGGKRMNEVPPSE----RG--IGMVFQ-- 82
Cdd:COG4172 24 EAV--KGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrriRGnrIAMIFQep 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SYALYPHLSVAENMSFGLKL-AGVKKAEIYQRVnqvAEVLQLAHL------LDRRPKALSGGQRQRVAIGRTLVSEPDVF 155
Cdd:COG4172 102 MTSLNPLHTIGKQIAEVLRLhRGLSGAAARARA---LELLERVGIpdperrLDAYPHQLSGGQRQRVMIAMALANEPDLL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 156 LLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQ--VEAMtlADKIVVLDAGNI 212
Cdd:COG4172 179 IADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLgvVRRF--ADRVAVMRQGEI 235
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-222 |
4.03e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.39 E-value: 4.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 13 FGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEvppSERG-------IGMVFQSya 85
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY---SKRGllalrqqVATVFQD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 86 lyP-----HLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:PRK13638 86 --PeqqifYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 161 LSNLDAALRVQMRIEISRLHKRLERTMIyVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
3-222 |
4.19e-23 |
|
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: 100.79 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 3 NVTLSsvYKAFGEAVISrDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMV 80
Cdd:TIGR03796 482 NITFG--YSPLEPPLIE-NFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVlaNSVAMV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYALYPHlSVAENMS--------FGLKLAgVKKAEIYQRVnqVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEP 152
Cdd:TIGR03796 559 DQDIFLFEG-TVRDNLTlwdptipdADLVRA-CKDAAIHDVI--TSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNP 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 153 DVFLLDEPLSNLDAAlrVQMRIEisrlhKRLER---TMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:TIGR03796 635 SILILDEATSALDPE--TEKIID-----DNLRRrgcTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELW 699
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-237 |
4.46e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 97.14 E-value: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-----RGIG 78
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytvrKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 79 MVFQSYALYPHLSVAENMSFGLK-LAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 158 DEPLSNLDA-ALRVQMRIeISRLHKRLERTMIYVTHDQVEAMTLAD-KIVVLDAGNIAQvGKPLELYHYPANR---FVAG 232
Cdd:PRK11831 168 DEPFVGQDPiTMGVLVKL-ISELNSALGVTCVVVSHDVPEVLSIADhAYIVADKKIVAH-GSAQALQANPDPRvrqFLDG 245
|
....*
gi 488140883 233 FIGSP 237
Cdd:PRK11831 246 IADGP 250
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-221 |
1.47e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 99.43 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 13 FGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKrmnEVPPSE----RGIGMVFQSYALYP 88
Cdd:NF033858 276 FGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---PVDAGDiatrRRVGYMSQAFSLYG 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 89 HLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQR----VAIgrtlVSEPDVFLLDEPLSNL 164
Cdd:NF033858 353 ELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRlslaVAV----IHKPELLILDEPTSGV 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488140883 165 DAALR---VQMRIEISrlhkRLERTMIYV-THDQVEAMtLADKIVVLDAGNIAQVGKPLEL 221
Cdd:NF033858 429 DPVARdmfWRLLIELS----REDGVTIFIsTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-238 |
1.55e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 95.93 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 34 FVGPSGCGKSTLLRMIAGLEDITSG-----ELLIGGKRM---NEVPPSERGIGMVFQSYALYPhLSVAENMSFGLKLAGV 105
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 106 KKAEIYQRVNQ--VAEVLQLAHLLDR---RPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRLH 180
Cdd:PRK14271 131 VPRKEFRGVAQarLTEVGLWDAVKDRlsdSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 181 KRLerTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPAN----RFVAGFIGSPK 238
Cdd:PRK14271 211 DRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHaetaRYVAGLSGDVK 270
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-222 |
2.76e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.26 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 18 ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPS--ERGIGMVFQSYALYPHlSVAEN 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 96 MSFGLKLAgvKKAEIyqrvnQVAEVLQLAH------------LLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:TIGR00958 575 IAYGLTDT--PDEEI-----MAAAKAANAHdfimefpngydtEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 164 LDAalRVQMRIEISRlhKRLERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:TIGR00958 648 LDA--ECEQLLQESR--SRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLM 701
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-209 |
4.50e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 92.56 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSergigmvFQSYALY------ 87
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDLLYlghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 88 --PHLSVAENMSFGLKLAGVKKAEiyqrvnQVAEVLQLAHLLDRR--P-KALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:PRK13538 85 ikTELTALENLRFYQRLHGPGDDE------ALWEALAQVGLAGFEdvPvRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488140883 163 NLDAAlrvqmriEISRLHKRLER------TMIYVTHDQVEAMTLADKIVVLDA 209
Cdd:PRK13538 159 AIDKQ-------GVARLEALLAQhaeqggMVILTTHQDLPVASDKVRKLRLGQ 204
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-212 |
7.22e-22 |
|
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: 92.53 E-value: 7.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 3 NVTLSsvYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPS--ERGIGMV 80
Cdd:cd03248 16 NVTFA--YPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYALYPHlSVAENMSFGLKLAGVKK-AEIYQRVNQVAEVLQLAHLLD----RRPKALSGGQRQRVAIGRTLVSEPDVF 155
Cdd:cd03248 94 GQEPVLFAR-SLQDNIAYGLQSCSFECvKEAAQKAHAHSFISELASGYDtevgEKGSQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 156 LLDEPLSNLDAALRVQMRIEISRLHKRleRTMIYVTHdQVEAMTLADKIVVLDAGNI 212
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-212 |
8.92e-22 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 91.34 E-value: 8.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSER---GIGMV---FQSYALYPHLSVA 93
Cdd:cd03215 17 RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYVpedRKREGLVLDLSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSfglklagvkkaeiyqrvnqvaevlqLAHLLdrrpkalSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD-AAlrvqm 172
Cdd:cd03215 97 ENIA-------------------------LSSLL-------SGGNQQKVVLARWLARDPRVLILDEPTRGVDvGA----- 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488140883 173 rieISRLHKRLER------TMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:cd03215 140 ---KAEIYRLIREladagkAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-167 |
9.51e-22 |
|
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: 91.79 E-value: 9.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRdINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPS-ERGIGMVFQSYALYPHLSV 92
Cdd:cd03231 12 GRALFSG-LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 93 AENMSFGLKLAGvkKAEIYQRVNQVAevlqLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAA 167
Cdd:cd03231 91 LENLRFWHADHS--DEQVEEALARVG----LNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-212 |
1.33e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 92.25 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE---RGI 77
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 GMVFQSYALYPHLSVAENMSFGLKLAgvKKAEIYQRVNQVAEVL-QLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFL 156
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 157 LDEPLSNLDAALRVQMRIEISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-210 |
2.24e-21 |
|
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: 89.04 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGgkrmnevppsergigmvfqs 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 yalyphlsvaenmsfglklagvkkaeiyqrvnQVAEVLQLAHlldrrpkaLSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:cd03221 61 --------------------------------STVKIGYFEQ--------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488140883 164 LDaalrVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:cd03221 101 LD----LESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-233 |
2.82e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 91.71 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELliggkrmnEVPPSERgIGMVFQS 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR-IGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHLSVAENMSFGLKlAGVKKAEIYQRVNQVaevlQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:PRK09544 76 LYLDTTLPLTVNRFLRLR-PGTKKEDILPALKRV----QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 164 LDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDaGNIAQVGKPLELYHYPanRFVAGF 233
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN-HHICCSGTPEVVSLHP--EFISMF 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-210 |
3.07e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.85 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTlssvyKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPP---SERGI 77
Cdd:PRK09700 8 MAGIG-----KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 GMVFQSYALYPHLSVAENMSFGL----KLAGVKKAEiYQRVNQVAEVLQLAHLLDRRPKA----LSGGQRQRVAIGRTLV 149
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGRhltkKVCGVNIID-WREMRVRAAMMLLRVGLKVDLDEkvanLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488140883 150 SEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-229 |
4.20e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.39 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKST----LLRMIAglediTSGELLIGGK-----RMNEVPPSERGIGMVFQ-- 82
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQplhnlNRRQLLPVRHRIQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SYALYPHLSVAENMSFGLKL--AGVKKAEIYQRVNQVAEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDE 159
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 160 PLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRF 229
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-221 |
4.59e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.51 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPHlSVAENms 97
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAISVVSQRVHLFSA-TLRDN-- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 98 fgLKLAGVKKAEiyqrvNQVAEVLQ---LAHLLDR------------RPkaLSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:PRK11160 434 --LLLAAPNASD-----EALIEVLQqvgLEKLLEDdkglnawlgeggRQ--LSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 163 NLDAALRVQMrIEISRLHKRlERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:PRK11160 505 GLDAETERQI-LELLAEHAQ-NKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
16-220 |
5.00e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 90.67 E-value: 5.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 16 AVISR--DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGELLIGGKRMNEVPPSE----RG---------IGM- 79
Cdd:COG4138 7 AVAGRlgPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElarhRAylsqqqsppFAMp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 80 VFQSYALYPHLSVAEnmsfglklagvkkAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLV-------SEP 152
Cdd:COG4138 86 VFQYLALHQPAGASS-------------EAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488140883 153 DVFLLDEPLSNLDAALRVQMRIEISRLHkRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLE 220
Cdd:COG4138 153 QLLLLDEPMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-212 |
1.12e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.14 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 15 EAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIggkrmNEVPPSErgigmvfqsyalyphlsVAE 94
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL-----DGVPVSD-----------------LEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 95 NMSfglklagvkkaeiyqrvNQVAEVLQLAHLLD--------RRpkaLSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDA 166
Cdd:cd03247 72 ALS-----------------SLISVLNQRPYLFDttlrnnlgRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488140883 167 ALRVQMrieISRLHKRLE-RTMIYVTHdQVEAMTLADKIVVLDAGNI 212
Cdd:cd03247 132 ITERQL---LSLIFEVLKdKTLIWITH-HLTGIEHMDKILFLENGKI 174
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
15-237 |
1.20e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.23 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 15 EAVisRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERG--IGMVFQ--SYALYPHL 90
Cdd:PRK15112 27 EAV--KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrIRMIFQdpSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 91 SVAENMSFGLKLAGVKKAEiyQRVNQVAEVLQLAHLLDRR----PKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDA 166
Cdd:PRK15112 105 RISQILDFPLRLNTDLEPE--QREKQIIETLRQVGLLPDHasyyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 167 ALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYP----ANRFVAGFIGSP 237
Cdd:PRK15112 183 SMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPlhelTKRLIAGHFGEA 257
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-208 |
1.39e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 92.95 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 25 EIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKrmnevppsergIgmvfqSYAlyP-HLSVAENMSFGLKLA 103
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-----------I-----SYK--PqYIKPDYDGTVEDLLR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 104 GVKKA---EIYQrvNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDaalrVQMRIEISRLH 180
Cdd:PRK13409 423 SITDDlgsSYYK--SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VEQRLAVAKAI 496
|
170 180 190
....*....|....*....|....*....|..
gi 488140883 181 KRL----ERTMIYVTHDQVEAMTLADKIVVLD 208
Cdd:PRK13409 497 RRIaeerEATALVVDHDIYMIDYISDRLMVFE 528
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-212 |
2.88e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 92.32 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAG---LEDitsGELLIGG----KRMNEVPPS 73
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDD---GRIIYEQdlivARLQQDPPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 74 ERGiGMVF---------QSYAL--YPHLS--VAENMSFGL--KLAGVKK----AEIYQRVNQVAEVLQLAHL-LDRRPKA 133
Cdd:PRK11147 78 NVE-GTVYdfvaegieeQAEYLkrYHDIShlVETDPSEKNlnELAKLQEqldhHNLWQLENRINEVLAQLGLdPDAALSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 134 LSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAAlrvqmRIE-ISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-----TIEwLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-221 |
3.60e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.03 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 29 GEFVVFVGPSGCGKSTLLRMIA-----GLEdiTSGELLIGGKRMNEVPPSERGiGMVFQSYALYPHLSVAENMSFG--LK 101
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAfrspkGVK--GSGSVLLNGMPIDAKEMRAIS-AYVQQDDLFIPTLTVREHLMFQahLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 102 L-AGVKKAEIYQRVNQVAEVLQL---AHLL---DRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAAlrvqMRI 174
Cdd:TIGR00955 128 MpRRVTKKEKRERVDEVLQALGLrkcANTRigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF----MAY 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488140883 175 EISRLHKRLE---RTMIYVTHD-QVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:TIGR00955 204 SVVQVLKGLAqkgKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-225 |
4.22e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.84 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-----RGIGMVFQS-YA-LYPHLSVAENMSFGLK 101
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 102 LAGVKKAEIYQRvnQVAEVLQLAHLLD----RRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEIS 177
Cdd:PRK10261 430 VHGLLPGKAAAA--RVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488140883 178 RLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYP 225
Cdd:PRK10261 508 DLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-215 |
5.18e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.38 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE---RGIGMVFQSY---ALYPHLSVA 93
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdnGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFG--LKLAGVKKA-------EIYQRVNQVAEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:PRK09700 360 QNMAISrsLKDGGYKGAmglfhevDEQRTAENQRELLALkCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 164 LDaalrVQMRIEISRLHKRLE---RTMIYVTHDQVEAMTLADKIVVLDAGNIAQV 215
Cdd:PRK09700 440 ID----VGAKAEIYKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-210 |
8.57e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.36 E-value: 8.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRM---NEVPPSERGIGMVFQSYALYPHLSVAENMS 97
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGVAIIYQELHLVPEMTVAENLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 98 FGL---KLAGVKKAEIYQRVnqvaeVLQLAHL-LDRRP----KALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDA-AL 168
Cdd:PRK11288 102 LGQlphKGGIVNRRLLNYEA-----REQLEHLgVDIDPdtplKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488140883 169 RVQMRIeISRLhkRLE-RTMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:PRK11288 177 EQLFRV-IREL--RAEgRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-218 |
1.29e-19 |
|
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: 86.39 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 3 NVTLSsvYKAFGEAVIsRDINLEIDDGEFVVFVGPSGCGKST----LLRMIagleDITSGELLIGGKRMNEVPPSE--RG 76
Cdd:cd03244 7 NVSLR--YRPNLPPVL-KNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlrSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 77 IGMVFQSyalyPHL---SVAENM-SFG----------LKLAGVKKAeiyqrVNQVAEvlQLAHLLDRRPKALSGGQRQRV 142
Cdd:cd03244 80 ISIIPQD----PVLfsgTIRSNLdPFGeysdeelwqaLERVGLKEF-----VESLPG--GLDTVVEEGGENLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 143 AIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISrlHKRLERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKP 218
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-213 |
1.35e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.69 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE---RGIGMV---FQSYALYPHLSVA 93
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVpedRKGEGLVLDLSIR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGL--KLAG---VKKAEIYQRVNQVAEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAA 167
Cdd:COG1129 349 ENITLASldRLSRgglLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVG 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488140883 168 LRVqmriEISRLHKRLER---TMIYVTHDQVEAMTLADKIVVLDAGNIA 213
Cdd:COG1129 429 AKA----EIYRLIRELAAegkAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-220 |
3.45e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 85.75 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGELLIGGKRMNEVPPSE----RG---------IGM-VFQSYALY 87
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMpVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 88 PHlsvaenmsfglklAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRV-------AIGRTLVSEPDVFLLDEP 160
Cdd:PRK03695 94 QP-------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 161 LSNLDAALRVQMRIEISRLhKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLE 220
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
11-216 |
5.34e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 85.36 E-value: 5.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 11 KAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGK--------RMNEvppSERGI----- 77
Cdd:PRK11701 14 KLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyALSE---AERRRllrte 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 -GMVFQSYA--LYPHLSVAENMSFGLKLAGVKKaeiYQRVNQVA-----EVLQLAHLLDRRPKALSGGQRQRVAIGRTLV 149
Cdd:PRK11701 91 wGFVHQHPRdgLRMQVSAGGNIGERLMAVGARH---YGDIRATAgdwleRVEIDAARIDDLPTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 150 SEPDVFLLDEPLSNLDAAlrVQMRI--EISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVS--VQARLldLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-221 |
7.10e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 88.09 E-value: 7.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 3 NVTLSsvYKAFGEAVisRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPS--ERGIGMV 80
Cdd:PRK13657 339 DVSFS--YDNSRQGV--EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 81 FQSYALYPHlSVAENMSFGLklAGVKKAEIYQrvnqVAEVLQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLV 149
Cdd:PRK13657 415 FQDAGLFNR-SIEDNIRVGR--PDATDEEMRA----AAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 150 SEPDVFLLDEPLSNLDAALRVQMRIEISRLHKrlERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDEL 556
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-221 |
8.43e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.77 E-value: 8.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPS--ERGIGMVFQSYALYpHLSVAENMS 97
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAslRNQVALVSQNVHLF-NDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 98 FGLKlagvkkaEIYQRvNQVAEVLQLAHLLDRRPK--------------ALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:PRK11176 439 YART-------EQYSR-EQIEEAARMAYAMDFINKmdngldtvigengvLLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488140883 164 LDAALRVQMRIEISRLHKrlERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:PRK11176 511 LDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-208 |
1.68e-18 |
|
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: 86.76 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 25 EIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKrmnevppsergIgmvfqSYAlyP-HLSVAENMSFGLKLA 103
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-----------I-----SYK--PqYISPDYDGTVEEFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 104 GVKKAEI----YQrvNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDaalrVQMRIEISRL 179
Cdd:COG1245 424 SANTDDFgssyYK--TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VEQRLAVAKA 497
|
170 180 190
....*....|....*....|....*....|...
gi 488140883 180 HKRL----ERTMIYVTHDQVEAMTLADKIVVLD 208
Cdd:COG1245 498 IRRFaenrGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-210 |
1.76e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.08 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 9 VYKAFG------EAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSgelligGKRMNEVPPSErgigmvfq 82
Cdd:COG2401 30 VLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTP------VAGCVDVPDNQ-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 syaLYPHLSVAENMSfglklagvkkaeIYQRVNQVAEVLQLAHLLD-----RRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:COG2401 96 ---FGREASLIDAIG------------RKGDFKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488140883 158 DEPLSNLDAALRVQMRIEISRLHKRLERTMIYVT-HDQVEAMTLADKIVVLDAG 210
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGITLVVAThHYDVIDDLQPDLLIFVGYG 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-210 |
4.94e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 85.37 E-value: 4.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 1 MANVTlssvyKAFGeAVISRD-INLEIDDGEFVVFVGPSGCGKSTLLRMIAGL--EDITSGELLIGGK--RMNEVPPSER 75
Cdd:PRK13549 8 MKNIT-----KTFG-GVKALDnVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEelQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 76 -GIGMVFQSYALYPHLSVAENMSFGLKL--AGVKK-AEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSE 151
Cdd:PRK13549 82 aGIAIIHQELALVKELSVLENIFLGNEItpGGIMDyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 152 PDVFLLDEPLSNLDAAlRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:PRK13549 162 ARLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-216 |
4.96e-18 |
|
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: 82.57 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLI-----GGKRMNEVPPSERGI- 77
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERRRl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 78 -----GMVFQSYA--LYPHLSVAENMSFGLKLAGVKKaeiYQRVNQVA-----EVLQLAHLLDRRPKALSGGQRQRVAIG 145
Cdd:TIGR02323 84 mrtewGFVHQNPRdgLRMRVSAGANIGERLMAIGARH---YGNIRATAqdwleEVEIDPTRIDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488140883 146 RTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-225 |
5.12e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.73 E-value: 5.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPP---SERGIGMVFQSYALYPHLSVAEN--- 95
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqiARMGVVRTFQHVRLFREMTVIENllv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 96 -----MSFGLkLAGVKKAEIYQRVNQVA--------EVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:PRK11300 104 aqhqqLKTGL-FSGLLKTPAFRRAESEAldraatwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 163 NLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYP 225
Cdd:PRK11300 183 GLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-240 |
5.54e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 83.62 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGL---EDITSGELLIGGKRMNEVPPSE------RGIGMVFQS--YALYPH 89
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKElnklraEQISMIFQDpmTSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 90 LSVAENMSFGLKL-AGVKKAEIYQRVNQVAEVLQLAHLLDRR---PKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD 165
Cdd:PRK09473 114 MRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 166 AALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAGFIGS-PKMN 240
Cdd:PRK09473 194 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAvPRLD 269
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-212 |
1.23e-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: 80.38 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 11 KAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDIT---SGELLIGG---KRMNEVPPSErgIGMVFQSY 84
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGipyKEFAEKYPGE--IIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 85 ALYPHLSVAENMSFGLKLAGvkkaeiyqrvNQVAevlqlahlldrrpKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:cd03233 93 VHFPTLTVRETLDFALRCKG----------NEFV-------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488140883 165 DAALRVQMrIEISRLHKRLERTMIYVTHDQ--VEAMTLADKIVVLDAGNI 212
Cdd:cd03233 150 DSSTALEI-LKCIRTMADVLKTTTFVSLYQasDEIYDLFDKVLVLYEGRQ 198
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-216 |
1.86e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 84.06 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 17 VISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLiggkrmnevppSERGIGMVFQSyALYPHLSVAENM 96
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 97 SF-----GLKLAGVKkaeiyqRVNQV-AEVLQLAHLLD----RRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDA 166
Cdd:PTZ00243 742 LFfdeedAARLADAV------RVSQLeADLAQLGGGLEteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488140883 167 AL--RVQMRIEISRLHKrleRTMIYVTHdQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:PTZ00243 816 HVgeRVVEECFLGALAG---KTRVLATH-QVHVVPRADYVVALGDGRVEFSG 863
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-216 |
2.22e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 83.61 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE-RG-IGMVFQSYALYPHlSVAENMS 97
Cdd:PRK10789 332 ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSrLAVVSQTPFLFSD-TVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 98 FGLKLAGVKKAEIYQRVNQVAE-VLQLAHLLD----RRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAalrvqm 172
Cdd:PRK10789 411 LGRPDATQQEIEHVARLASVHDdILRLPQGYDtevgERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG------ 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488140883 173 RIEISRLHK----RLERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:PRK10789 485 RTEHQILHNlrqwGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRG 531
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-227 |
2.45e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.37 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKS----TLLRMI--AGLEdITSGELLIGGKRMNEVPPSE---------RG--IGMVFQ 82
Cdd:PRK10261 33 RNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGL-VQCDKMLLRRRSRQVIELSEqsaaqmrhvRGadMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 S--YALYPHLSVAENMSFGLKL-AGVKKAEIYQRVNQVAEVLQLAH---LLDRRPKALSGGQRQRVAIGRTLVSEPDVFL 156
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488140883 157 LDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPAN 227
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
14-224 |
2.60e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 80.46 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLE--DITSGELLIGGKRMNEVPPSER---GIGMVFQsyalYP 88
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERahlGIFLAFQ----YP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 89 -HLSVAENMSFgLKLA--GVKKA---------EIYQRVNQVAEVLQL-AHLLDRR-PKALSGGQRQRVAIGRTLVSEPDV 154
Cdd:CHL00131 94 iEIPGVSNADF-LRLAynSKRKFqglpeldplEFLEIINEKLKLVGMdPSFLSRNvNEGFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 155 FLLDEPLSNLDA-ALRVqMRIEISRLhKRLERTMIYVTHDQveamTLADKIV-----VLDAGNIAQVG-----KPLELYH 223
Cdd:CHL00131 173 AILDETDSGLDIdALKI-IAEGINKL-MTSENSIILITHYQ----RLLDYIKpdyvhVMQNGKIIKTGdaelaKELEKKG 246
|
.
gi 488140883 224 Y 224
Cdd:CHL00131 247 Y 247
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-210 |
2.74e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 82.95 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGL--EDITSGELLIGGKRM--NEVPPSER-GIG 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkaSNIRDTERaGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 79 MVFQSYALYPHLSVAENMSFG--LKLAGVKK--AEIYQRVNQVAEVLQLAHLLDRRPKA-LSGGQRQRVAIGRTLVSEPD 153
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGneITLPGGRMayNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 154 VFLLDEPLSNLDAAlRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:TIGR02633 162 LLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-217 |
1.04e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.30 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPS--ERGIGMVFQSYALYPHlSVAENMS 97
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPVVLAD-TFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 98 FGLKLAgvkkaeiYQRVNQVAEVLQLAHLLDRRPKA-----------LSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDA 166
Cdd:PRK10790 437 LGRDIS-------EEQVWQALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488140883 167 ALR--VQMRIEISRLHKrlerTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGK 217
Cdd:PRK10790 510 GTEqaIQQALAAVREHT----TLVVIAH-RLSTIVEADTILVLHRGQAVEQGT 557
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-193 |
1.30e-16 |
|
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: 81.13 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 5 TLSSVYKAF-GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGElliggkrmnEVPPSERGIGMVFQS 83
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE---------ARPQPGIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHLSVAENMSFGLKlagvKKAEIYQRVNQV--------AEVLQL---------------AHLLDRR---------- 130
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVA----EIKDALDRFNEIsakyaepdADFDKLaaeqaelqeiidaadAWDLDSQleiamdalrc 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 131 P------KALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAAlrvqmriEISRLHKRLER---TMIYVTHD 193
Cdd:TIGR03719 153 PpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-------SVAWLERHLQEypgTVVAVTHD 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-222 |
1.66e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 81.18 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGleditsgelliggkrmnEVPPSERGIGMVFQSYALYPHLS------VAE 94
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVVIRGSVAYVPQVSwifnatVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 95 NMSFGLKLAGvkkaeiyQRVNQVAEVLQLAHLLD-----------RRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:PLN03232 698 NILFGSDFES-------ERYWRAIDVTALQHDLDllpgrdlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 164 LDAalRVQMRIEISRLHKRLE-RTMIYVThDQVEAMTLADKIVVLDAGNIAQVGKPLELY 222
Cdd:PLN03232 771 LDA--HVAHQVFDSCMKDELKgKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-221 |
2.05e-16 |
|
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: 81.15 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKrmnevppsergIGMVFQSyALYPHLSVAENMSFGLK 101
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------VAYVPQQ-AWIQNDSLRENILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 102 LagvkKAEIYQRVNQVAEVLQLAHLL---DR-----RPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMR 173
Cdd:TIGR00957 725 L----NEKYYQQVLEACALLPDLEILpsgDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488140883 174 IEISRLHKRLE-RTMIYVTHDqVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:TIGR00957 801 EHVIGPEGVLKnKTRILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-225 |
2.67e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 78.63 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGELLIGGKRMNEVPPSER------GIGMVFQS--YALYPH 89
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 90 LSVAENMSFGLKL-AGVKKAEIYQRVnqvAEVLQL------AHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:PRK11022 106 YTVGFQIMEAIKVhQGGNKKTRRQRA---IDLLNQvgipdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 163 NLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYP 225
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-210 |
4.57e-16 |
|
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: 76.22 E-value: 4.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSERGIGMVFQ-SYALY-PHL---SVAEN 95
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSvAYAAQkPWLlnaTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 96 MSFGLKLAGvkkaeiyQRVNQVAEVLQLAHLLDRRPKA-----------LSGGQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:cd03290 99 ITFGSPFNK-------QRYKAVTDACSLQPDIDLLPFGdqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488140883 165 DAALRVQ-MRIEISRLHKRLERTMIYVTHdQVEAMTLADKIVVLDAG 210
Cdd:cd03290 172 DIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-273 |
6.53e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKS----TLLRMIAGLEDI-TSGELLIGGKRMNEVPPSE----RG--IGMVFQS--YALY 87
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHASEQTlrgvRGnkIAMIFQEpmVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 88 PHLSVAENMSFGLKL-AGVKK----AEIYQRVNQVAeVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:PRK15134 107 PLHTLEKQLYEVLSLhRGMRReaarGEILNCLDRVG-IRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 163 NLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRFVAgfigspkmnfl 242
Cdd:PRK15134 186 ALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ----------- 254
|
250 260 270
....*....|....*....|....*....|.
gi 488140883 243 pvKVTAAEPRQVQIELPNHQRVWLPVEGDQV 273
Cdd:PRK15134 255 --KLLNSEPSGDPVPLPEPASPLLDVEQLQV 283
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-217 |
6.81e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.15 E-value: 6.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 5 TLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGL--EDITSGELLIGGKRMNEvpPSERGIGMVFQ 82
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTK--QILKRTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SYALYPHLSVAENMSFG--LKLA-GVKKAEIYQRVNQVAEVLQLAH-----LLDRRPKALSGGQRQRVAIGRTLVSEPDV 154
Cdd:PLN03211 148 DDILYPHLTVRETLVFCslLRLPkSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGK 217
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-210 |
7.97e-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: 74.97 E-value: 7.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELLIGGKRMNEVPPseRGIGMVFQSYALYPHLSVAENMSF 98
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQ--RSTGYVEQQDVHSPNLTVREALRF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 99 GLKLAGvkkaeiyqrvnqvaevlqlahlldrrpkaLSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAalrvQMRIEISR 178
Cdd:cd03232 103 SALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS----QAAYNIVR 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 488140883 179 LHKRLERT--MIYVTHDQVEAMTLA--DKIVVLDAG 210
Cdd:cd03232 150 FLKKLADSgqAILCTIHQPSASIFEkfDRLLLLKRG 185
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-221 |
9.56e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 79.01 E-value: 9.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGleditsgelliggkrmnEVPPSERGIGMVFQSYALYPHLS------VAE 94
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLG-----------------ELPPRSDASVVIRGTVAYVPQVSwifnatVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 95 NMSFGLKLAGVkkaeiyqRVNQVAEVLQLAHLLDRRPKA-----------LSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:PLN03130 698 NILFGSPFDPE-------RYERAIDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 164 LDAALRVQ-----MRIEISRlhkrleRTMIYVThDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:PLN03130 771 LDAHVGRQvfdkcIKDELRG------KTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-165 |
9.74e-16 |
|
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: 78.44 E-value: 9.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 9 VYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGgkrmnevppSERGIGMVFQSY-ALY 87
Cdd:TIGR03719 328 LTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG---------ETVKLAYVDQSRdALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 88 PHLSVAENMSFGLKLAGVKKAEIYQR----------VNQvaevlqlahllDRRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:TIGR03719 399 PNKTVWEEISGGLDIIKLGKREIPSRayvgrfnfkgSDQ-----------QKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
....*...
gi 488140883 158 DEPLSNLD 165
Cdd:TIGR03719 468 DEPTNDLD 475
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-213 |
1.06e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSErGI--GMVF-----QSYALYPHLSVAE 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD-AIraGIMLcpedrKAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 95 NMS---------FGLKLAGVKKAEIYQRvnqvaevlQLAHLLDRRPKA------LSGGQRQRVAIGRTLVSEPDVFLLDE 159
Cdd:PRK11288 351 NINisarrhhlrAGCLINNRWEAENADR--------FIRSLNIKTPSReqlimnLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 160 PLSNLDaalrVQMRIEISRLHKRLE---RTMIYVTHDQVEAMTLADKIVVLDAGNIA 213
Cdd:PRK11288 423 PTRGID----VGAKHEIYNVIYELAaqgVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-165 |
1.46e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.89 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKrmnEVPPSERGIGMVFQSY--ALYPHLSVAENMSFg 99
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRFMAYLGHlpGLKADLSTLENLHF- 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 100 lkLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD 165
Cdd:PRK13543 106 --LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-221 |
1.73e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.86 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEvpPSER-------- 75
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD--ARHRravcpria 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 76 ----GIGMvfqsyALYPHLSVAENMSFGLKLAGVKKAEIYQRvnqVAEVLQ---LAHLLDRRPKALSGGQRQRVAIGRTL 148
Cdd:NF033858 80 ympqGLGK-----NLYPTLSVFENLDFFGRLFGQDAAERRRR---IDELLRatgLAPFADRPAGKLSGGMKQKLGLCCAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 149 VSEPDVFLLDEPLSNLDAALRVQMRIEISRLhkRLER---TMIYVTHDQVEAMTLaDKIVVLDAGNIAQVGKPLEL 221
Cdd:NF033858 152 IHDPDLLILDEPTTGVDPLSRRQFWELIDRI--RAERpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
29-221 |
3.92e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLiggkrMNEVPPSERGIGMVFQSYALYPH-LSVAENMSFGLKLA---- 103
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIL-----LDAQPLESWSSKAFARKVAYLPQqLPAAEGMTVRELVAigry 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 104 ------GVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEIS 177
Cdd:PRK10575 112 pwhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVH 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488140883 178 RLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:PRK10575 192 RLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-182 |
4.27e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 76.21 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 23 NLEIDDGEFVVFVGPSGCGKSTLLRMIagleditSGEL-LIGGKRMNEvppsergigmvFQSYALyphLS-------VAE 94
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARAL-------AGELpLLSGERQSQ-----------FSHITR---LSfeqlqklVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 95 N--------MSFGLKLAGVKKAEIYQ-------RVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDE 159
Cdd:PRK10938 82 EwqrnntdmLSPGEDDTGRTTAEIIQdevkdpaRCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180
....*....|....*....|...
gi 488140883 160 PLSNLDAALRVQMRIEISRLHKR 182
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQS 184
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-192 |
4.63e-15 |
|
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: 72.19 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIggkrmnevpPSERGIGMVFQ-SYalyphlsvaenMSF 98
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQrPY-----------LPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 99 GLkLAGvkkaeiyqrvnqvaevlQLAHLLDRRpkaLSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRieisR 178
Cdd:cd03223 78 GT-LRE-----------------QLIYPWDDV---LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY----Q 132
|
170
....*....|....
gi 488140883 179 LHKRLERTMIYVTH 192
Cdd:cd03223 133 LLKELGITVISVGH 146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-243 |
5.15e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 76.98 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVISRdINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKR-MNEVPPSERGIGMVFQSY 84
Cdd:TIGR01257 1943 LTKVYSGTSSPAVDR-LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISDVHQNMGYCPQFD 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 85 ALYPHLSVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:TIGR01257 2022 AIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 165 DAALRVQMRIEISRLhKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL-YHYPANRFVAGFIGSPKMNFLP 243
Cdd:TIGR01257 2102 DPQARRMLWNTIVSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLkSKFGDGYIVTMKIKSPKDDLLP 2180
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-193 |
9.10e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.54 E-value: 9.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 5 TLSSVYKAFGEA-VISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGE--LLIGGKrmnevppsergIGMVF 81
Cdd:PRK11819 8 TMNRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarPAPGIK-----------VGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 82 QSYALYPHLSVAENMSFGLKlagvKKAEIYQRVNQVAE-----------------VLQL------AHLLDRR-------- 130
Cdd:PRK11819 77 QEPQLDPEKTVRENVEEGVA----EVKAALDRFNEIYAayaepdadfdalaaeqgELQEiidaadAWDLDSQleiamdal 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 131 --P------KALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAalrvqmriE-ISRLHKRLER---TMIYVTHD 193
Cdd:PRK11819 153 rcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------EsVAWLEQFLHDypgTVVAVTHD 219
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-226 |
1.14e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.81 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKS----TLLRMI-AGLEDiTSGELLIGGKRMneVPPSERG--IGMVFQS--YALYPHL 90
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRVLLDGKPV--APCALRGrkIATIMQNprSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 91 SVAENMSFGLKLAGVKKAEiyqrvNQVAEVLQLAHL------LDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:PRK10418 97 TMHTHARETCLALGKPADD-----ATLTAALEAVGLenaarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488140883 165 DAAlrVQMRI--EISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPA 226
Cdd:PRK10418 172 DVV--AQARIldLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-207 |
1.71e-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: 72.40 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 28 DGEFVVFVGPSGCGKSTLLRMIAGLeditsgelLIGGKRMNEVPPSERGIGMVFQSYALYPHLS--VAENMSFGLKLAGV 105
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGK--------LKPNLGKFDDPPDWDEILDEFRGSELQNYFTklLEGDVKVIVKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 106 ---------KKAEIYQRV------NQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRV 170
Cdd:cd03236 97 dlipkavkgKVGELLKKKdergklDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 488140883 171 QMRIEISRLHKRlERTMIYVTHDQVEAMTLADKIVVL 207
Cdd:cd03236 177 NAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-178 |
2.57e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.75 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMN-EVPPSERGIGMVFQSYALYPHLSVAENMSF 98
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkDLCTYQKQLCFVGHRSGINPYLTLRENCLY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 99 GLKLAGVKKAeiyqrVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD--AALRVQMRIEI 176
Cdd:PRK13540 98 DIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDelSLLTIITKIQE 172
|
..
gi 488140883 177 SR 178
Cdd:PRK13540 173 HR 174
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-208 |
3.05e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 74.30 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 18 ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLI-----------------------GGKRMNEVPPSE 74
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVfknehtndmtneqdyqgdeeqnvGMKNVNEFSLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 75 RG---------------------------------IGMVFQSYALYpHLSVAENMSFGLK---LAGVKKAEIYQRVNQVA 118
Cdd:PTZ00265 1263 EGgsgedstvfknsgkilldgvdicdynlkdlrnlFSIVSQEPMLF-NMSIYENIKFGKEdatREDVKRACKFAAIDEFI 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 119 EVLQLAHLLDRRP--KALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHdQVE 196
Cdd:PTZ00265 1342 ESLPNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIA 1420
|
250
....*....|..
gi 488140883 197 AMTLADKIVVLD 208
Cdd:PTZ00265 1421 SIKRSDKIVVFN 1432
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-210 |
3.71e-14 |
|
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: 71.81 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKrmnevppsergIGMVFQSYALYPHlSVAENMSFG 99
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 LK------LAGVKKAEIYQRVNQVAEvlQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAAlrVQMR 173
Cdd:cd03291 122 VSydeyryKSVVKACQLEEDITKFPE--KDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF--TEKE 197
|
170 180 190
....*....|....*....|....*....|....*...
gi 488140883 174 IEISRLHKRL-ERTMIYVThDQVEAMTLADKIVVLDAG 210
Cdd:cd03291 198 IFESCVCKLMaNKTRILVT-SKMEHLKKADKILILHEG 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-212 |
7.61e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSErGI--GMVFQSY-----ALYPHLSV 92
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD-GLanGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 93 AENMS------FGLKLAGVKKAEiyqRVNQVAEVLQLAHL----LDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:PRK10762 348 KENMSltalryFSRAGGSLKHAD---EQQAVSDFIRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488140883 163 NLDaalrVQMRIEISRLHKRLER---TMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:PRK10762 425 GVD----VGAKKEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-207 |
1.05e-13 |
|
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: 72.12 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 29 GEFVVFVGPSGCGKSTLLRmiagledITSGELL--IGgkrMNEVPPSERGIGMVFQSYALYPHLS-VAENmsfGLKLA-- 103
Cdd:COG1245 99 GKVTGILGPNGIGKSTALK-------ILSGELKpnLG---DYDEEPSWDEVLKRFRGTELQDYFKkLANG---EIKVAhk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 104 ------------GV-----KKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDa 166
Cdd:COG1245 166 pqyvdlipkvfkGTvrellEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD- 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488140883 167 alrVQMRIEISRLHKRL---ERTMIYVTHDQveAM--TLADKIVVL 207
Cdd:COG1245 245 ---IYQRLNVARLIRELaeeGKYVLVVEHDL--AIldYLADYVHIL 285
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
21-165 |
2.11e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 68.36 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVP-PSERGIGmvfQSYALYPHLSVAENMSFG 99
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPYCTYIG---HNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 100 lklagvkkAEIYQRVNQVAEVL---QLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD 165
Cdd:PRK13541 95 --------SEIYNSAETLYAAIhyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-165 |
2.58e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.92 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 9 VYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGgkrmNEVPpsergIGMVFQSY-ALY 87
Cdd:PRK11819 330 LSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG----ETVK-----LAYVDQSRdALD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 88 PHLSVAENMSFGLKLAGVKKAEIYQRvnqvaevlqlAHL-------LDRRPKA--LSGGQRQRVAIGRTLVSEPDVFLLD 158
Cdd:PRK11819 401 PNKTVWEEISGGLDIIKVGNREIPSR----------AYVgrfnfkgGDQQKKVgvLSGGERNRLHLAKTLKQGGNVLLLD 470
|
....*..
gi 488140883 159 EPLSNLD 165
Cdd:PRK11819 471 EPTNDLD 477
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
113-207 |
3.57e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 113 RVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDaalrVQMRIEISRLHKRL--ERTMIYV 190
Cdd:PRK13409 192 KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD----IRQRLNVARLIRELaeGKYVLVV 267
|
90
....*....|....*..
gi 488140883 191 THDQVEAMTLADKIVVL 207
Cdd:PRK13409 268 EHDLAVLDYLADNVHIA 284
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-218 |
8.03e-13 |
|
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: 66.67 E-value: 8.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPHlSVAENMs 97
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLFSG-TIRSNL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 98 fglklagvkkaEIYQRVN--QVAEVLQLAHLLDRrpkaLSGGQRQRVAIGRTLVSEPDVFLLDEPLSNL----DAALRVQ 171
Cdd:cd03369 103 -----------DPFDEYSdeEIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASIdyatDALIQKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488140883 172 MRIEISrlhkrlERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKP 218
Cdd:cd03369 168 IREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-212 |
1.27e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.90 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSER---GIGMV---FQSYALYPHLSVA 93
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYIpedRLGRGLVPDMSVA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGL-------KLAGVKKAEIYQRVNQVAEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLD 165
Cdd:COG3845 355 ENLILGRyrrppfsRGGFLDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488140883 166 AAlrvqmriEISRLHKRL--ERTM----IYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:COG3845 435 VG-------AIEFIHQRLleLRDAgaavLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-210 |
1.31e-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: 69.17 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKrmnevppsergIGMVFQSYALYPHlSVAENMSFG 99
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 LKLAGVKKAEIYQRVnQVAEVLQLAHLLDRRPK-----ALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDaaLRVQMRI 174
Cdd:TIGR01271 511 LSYDEYRYTSVIKAC-QLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD--VVTEKEI 587
|
170 180 190
....*....|....*....|....*....|....*..
gi 488140883 175 EISRLHKRL-ERTMIYVThDQVEAMTLADKIVVLDAG 210
Cdd:TIGR01271 588 FESCLCKLMsNKTRILVT-SKLEHLKKADKILLLHEG 623
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
18-194 |
1.38e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.74 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 18 ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELLIGGKRMNEVPPSER---GIGMVFQSYALYPhlSV 92
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageGIFMAFQYPVEIP--GV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 93 AENMSFGLKLAGVKK---AEIYQR------VNQVAEVLQL-AHLLDRRPK-ALSGGQRQRVAIGRTLVSEPDVFLLDEPL 161
Cdd:PRK09580 94 SNQFFLQTALNAVRSyrgQEPLDRfdfqdlMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESD 173
|
170 180 190
....*....|....*....|....*....|....*
gi 488140883 162 SNLDA-ALR-VQMRIEISRLHKrleRTMIYVTHDQ 194
Cdd:PRK09580 174 SGLDIdALKiVADGVNSLRDGK---RSFIIVTHYQ 205
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-218 |
1.96e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.77 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 17 VISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGleDIT----------SGELLIGGKRMNEVPPSE----RGIgMVFQ 82
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTgggaprgarvTGDVTLNGEPLAAIDAPRlarlRAV-LPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 SYALYPhLSVAENMSFGLKLAGVKKAEIYQRVNQVA-EVLQLAH---LLDRRPKALSGGQRQRVAIGRTL---------V 149
Cdd:PRK13547 92 AQPAFA-FSAREIVLLGRYPHARRAGALTHRDGEIAwQALALAGataLVGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488140883 150 SEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKP 218
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-192 |
2.31e-12 |
|
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: 68.24 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISrDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGK-RMNEVPpsER---GIGmVFQSYALYPh 89
Cdd:TIGR00954 464 GDVLIE-SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKgKLFYVP--QRpymTLG-TLRDQIIYP- 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 90 lsvaeNMSFGLKLAGVKKAEIyqrvNQVAEVLQLAHLLDRR---------PKALSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:TIGR00954 539 -----DSSEDMKRRGLSDKDL----EQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 488140883 161 LSnldaALRVQMRIEISRLHKRLERTMIYVTH 192
Cdd:TIGR00954 610 TS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
281-353 |
3.02e-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: 3.02e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488140883 281 LGIRPEHLLPSSASEvTLEGEIQVVEQLGNETQIHIQIPAIRQNLVYRQN-DVVLVEEGATFSIGLPPHRCHLF 353
Cdd:pfam08402 1 LAIRPEKIRLAAAAN-GLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNaHARPPAPGDRVGLGWDPEDAHVL 73
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-208 |
3.07e-12 |
|
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: 64.52 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 25 EIDDGEFVVFVGPSGCGKSTLLRMIAGLEDitsgelliggkrmnevpPSErgigmvfqsyalyphlsvaENMSFGLKLAG 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLI-----------------PNG-------------------DNDEWDGITPV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 105 VKKAEIyqrvnqvaevlqlahlldrrpkALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLE 184
Cdd:cd03222 65 YKPQYI----------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|....
gi 488140883 185 RTMIYVTHDQVEAMTLADKIVVLD 208
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-210 |
3.26e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.21 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 29 GEFVVFVGPSGCGKSTLLRMIAGLED---ITSGELLIGGKRMNEvpPSERGIGMVFQSYALYPHLSVAENMSFGLKL--- 102
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDS--SFQRSIGYVQQQDLHLPTSTVRESLRFSAYLrqp 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 103 AGVKKAEIYQRVNQVAEVLQLAHLLDrrpkALSG--------GQRQRVAIGRTLVSEPDVFL-LDEPLSNLDAalrvQMR 173
Cdd:TIGR00956 867 KSVSKSEKMEYVEEVIKLLEMESYAD----AVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS----QTA 938
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488140883 174 IEISRLHKRLERT--MIYVTHDQVEAMTLA--DKIVVLDAG 210
Cdd:TIGR00956 939 WSICKLMRKLADHgqAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-216 |
3.43e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.99 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELliggKRMNEVppsergiGMVFQSYALYPHLSVAENMSFGL 100
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----DRNGEV-------SVIAISAGLSGQLTGIENIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 101 KLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRLh 180
Cdd:PRK13546 111 LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF- 189
|
170 180 190
....*....|....*....|....*....|....*.
gi 488140883 181 KRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:PRK13546 190 KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-214 |
4.45e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.30 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPHLsvaenmsfg 99
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAVFTDFHLFDQL--------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 lkLAGVKKAEIYQRVNQVAEVLQLAH--------LLDRRpkaLSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQ 171
Cdd:PRK10522 413 --LGPEGKPANPALVEKWLERLKMAHkleledgrISNLK---LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRRE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488140883 172 MRIEISRLHKRLERTMIYVTHDQvEAMTLADKIVVLDAGNIAQ 214
Cdd:PRK10522 488 FYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLSE 529
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-218 |
5.11e-12 |
|
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: 67.13 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEfVVF-VGPSGCGKSTLLRMIAGLEDITSGELLIGGKRmneVPPSERG-----IGMVFQSYALYPHlsvaen 95
Cdd:COG4615 351 IDLTIRRGE-LVFiVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREayrqlFSAVFSDFHLFDR------ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 96 msfglkLAGVKKAEIYQRVNQVAEVLQLAHLL---DRR--PKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRv 170
Cdd:COG4615 421 ------LLGLDGEADPARARELLERLELDHKVsveDGRfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFR- 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488140883 171 qmRI---EI-SRLhKRLERTMIYVTHDQvEAMTLADKIVVLDAGNIAQVGKP 218
Cdd:COG4615 494 --RVfytELlPEL-KARGKTVIAISHDD-RYFDLADRVLKMDYGKLVELTGP 541
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-207 |
5.90e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.36 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 18 ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGG----KRMNeVPPSERGIGMVFQSYALYPHlSVA 93
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDIN-LKWWRSKIGVVSQDPLLFSN-SIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGL--------------------------------KLAG--------------VKKAEIYQRV--NQVAEVLQ--L 123
Cdd:PTZ00265 478 NNIKYSLyslkdlealsnyynedgndsqenknkrnscraKCAGdlndmsnttdsnelIEMRKNYQTIkdSEVVDVSKkvL 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 124 AH------------LLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVT 191
Cdd:PTZ00265 558 IHdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
|
250
....*....|....*.
gi 488140883 192 HdQVEAMTLADKIVVL 207
Cdd:PTZ00265 638 H-RLSTIRYANTIFVL 652
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-214 |
1.46e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAF-GEAVISrDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPP---SERGIGMVF 81
Cdd:PRK10762 7 LKGIDKAFpGVKALS-GAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAGIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 82 QSYALYPHLSVAENMSFGL----KLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:PRK10762 86 QELNLIPQLTIAENIFLGRefvnRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488140883 158 DEPLSNL-----DAALRVqmrieISRLhKRLERTMIYVTHDQVEAMTLADKIVVL-DAGNIAQ 214
Cdd:PRK10762 166 DEPTDALtdtetESLFRV-----IREL-KSQGRGIVYISHRLKEIFEICDDVTVFrDGQFIAE 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-207 |
2.25e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNE---------VPPSERgigmVFQSYALYPHL 90
Cdd:PRK15056 24 RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQalqknlvayVPQSEE----VDWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 91 SVAENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDaalrV 170
Cdd:PRK15056 100 VVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD----V 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488140883 171 QMRIEISRLHKRLE---RTMIYVTHDQVEAMTLADKIVVL 207
Cdd:PRK15056 176 KTEARIISLLRELRdegKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-217 |
3.14e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.13 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 18 ISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGELLIGGKRMNEVPPSERGiGMVFQSYA--LYPHLS 91
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYRG-DVVYNAETdvHFPHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 92 VAENMSFGLKLAGV--------KKAEIYQRVNQVAEVLQLAHLLDRRP-----KALSGGQRQRVAIGRTLVSEPDVFLLD 158
Cdd:TIGR00956 155 VGETLDFAARCKTPqnrpdgvsREEYAKHIADVYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKIQCWD 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488140883 159 EPLSNLDAALRVQMrIEISRLHKRLERTMIYVTHDQV--EAMTLADKIVVLDAGNIAQVGK 217
Cdd:TIGR00956 235 NATRGLDSATALEF-IRALKTSANILDTTPLVAIYQCsqDAYELFDKVIVLYEGYQIYFGP 294
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-214 |
1.01e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSER-GIGMVF-----QSYALYPHLSVA 93
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMS------FGLKLAGVKKAEIYQRVNQvAEVLQLAHLlDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDaa 167
Cdd:PRK15439 360 WNVCalthnrRGFWIKPARENAVLERYRR-ALNIKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD-- 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488140883 168 lrVQMRIEISRLHKRLER---TMIYVTHDQVEAMTLADKIVVLDAGNIAQ 214
Cdd:PRK15439 436 --VSARNDIYQLIRSIAAqnvAVLFISSDLEEIEQMADRVLVMHQGEISG 483
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
22-216 |
1.69e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 61.46 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGELLIGGKRMNEVPPSER------GIGMVFQ--SYALYPH 89
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQepSSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 90 LSVAENMSFGLkLAGVKKAEIYQRVNQVAE-VLQLAH---------LLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDE 159
Cdd:COG4170 106 AKIGDQLIEAI-PSWTFKGKWWQRFKWRKKrAIELLHrvgikdhkdIMNSYPHELTEGECQKVMIAMAIANQPRLLIADE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 160 PLSNLDAALRVQmrieISRLHKRLER----TMIYVTHDqVEAMT-LADKIVVLDAGNIAQVG 216
Cdd:COG4170 185 PTNAMESTTQAQ----IFRLLARLNQlqgtSILLISHD-LESISqWADTITVLYCGQTVESG 241
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-213 |
1.89e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE---RGIGMVFQ---SYALYPHLSVA 93
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainHGFALVTEerrSTGIYAYLDIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENM----------SFGLkLAGVKKAEIYQRVNQVAEVLQLAHllDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:PRK10982 345 FNSlisnirnyknKVGL-LDNSRMKSDTQWVIDSMRVKTPGH--RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488140883 164 LDAALRVQMRIEISRLHKRlERTMIYVTHDQVEAMTLADKIVVLDAGNIA 213
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
235-288 |
3.28e-10 |
|
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: 55.28 E-value: 3.28e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488140883 235 GSPKMNFLPVKVT----AAEPRQVQIELPNHQRVwlpveGDQVQVGANMSLGIRPEHL 288
Cdd:pfam17912 1 GSPPMNFLPATVVedglLVLGGGVTLPLPEGQVL-----ALKLYVGKEVILGIRPEHI 53
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
19-205 |
6.18e-10 |
|
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: 58.39 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 19 SRDINLEID-DGEFVVFVGPSGCGKSTLlrmIAGLEDITSGELliggkrmnevPPSERGIgmvfqsyALYPHL----SVA 93
Cdd:cd03240 11 SFHERSEIEfFSPLTLIVGQNGAGKTTI---IEALKYALTGEL----------PPNSKGG-------AHDPKLiregEVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKLAGVKKAEIYQRVNQVAEVL-----QLAHLLDRRPKALSGGQRQ------RVAIGRTLVSEPDVFLLDEPLS 162
Cdd:cd03240 71 AQVKLAFENANGKKYTITRSLAILENVIfchqgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTT 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488140883 163 NLDAALRVQMRIEISRLHKRLE-RTMIYVTHDQvEAMTLADKIV 205
Cdd:cd03240 151 NLDEENIEESLAEIIEERKSQKnFQLIVITHDE-ELVDAADHIY 193
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-210 |
1.05e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE---RGIGMVFQSYALYPHLSVAENMS 97
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaleNGISMVHQELNLVLQRSVMDNMW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 98 FG---LKLAGVKKAEIYQRVNQVAEVLQLAhlLDRRPKA--LSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAAlrvqm 172
Cdd:PRK10982 96 LGrypTKGMFVDQDKMYRDTKAIFDELDID--IDPRAKVatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK----- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488140883 173 riEISRLHKRLER------TMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:PRK10982 169 --EVNHLFTIIRKlkergcGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-225 |
1.29e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.05 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGledITSGELLIGGKRMN-------EVPPSER------GIGMVFQSyalyP 88
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICG---VTKDNWRVTADRMRfddidllRLSPRERrklvghNVSMIFQE----P 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 89 HLSVAENMSFGLKL-----AGVKKAEIYQRVN----QVAEVLQLAHLLDRR------PKALSGGQRQRVAIGRTLVSEPD 153
Cdd:PRK15093 99 QSCLDPSERVGRQLmqnipGWTYKGRWWQRFGwrkrRAIELLHRVGIKDHKdamrsfPYELTEGECQKVMIAIALANQPR 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLELY---HYP 225
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVttpHHP 253
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-212 |
1.32e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 4 VTLSSVYKAFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGelliggkrmnEVPPSERG-IGMVFQ 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG----------TVKWSENAnIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 83 --SYALYPHLSVAENMSfglKLAGVKKAEiyQRVNQVaevlqLAHLL------DRRPKALSGGQRQRVAIGRTLVSEPDV 154
Cdd:PRK15064 390 dhAYDFENDLTLFDWMS---QWRQEGDDE--QAVRGT-----LGRLLfsqddiKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 155 FLLDEPLSNLDaalrvqmrIE-ISRLHKRLER---TMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:PRK15064 460 LVMDEPTNHMD--------MEsIESLNMALEKyegTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-173 |
2.64e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.09 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 29 GEFVVFVGPSGCGKSTLLRMIAGLEditSGELLIGGKRMNEVPPSE----RGIGMVFQSYALYPHLSVAENMSFG--LKL 102
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRK---TGGYIEGDIRISGFPKKQetfaRISGYCEQNDIHSPQVTVRESLIYSafLRL 982
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488140883 103 AG-VKKAEIYQRVNQVAEVLQLAHLLDR---RP--KALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDA-ALRVQMR 173
Cdd:PLN03140 983 PKeVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDArAAAIVMR 1060
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-193 |
4.86e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 12 AFGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRmnEVPpsergigmVFQSY--ALYPH 89
Cdd:PRK11147 328 QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL--EVA--------YFDQHraELDPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 90 LSVAENMSFGlklagvkKAEIyqRVNQVAEVLqLAHLLD--------RRP-KALSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:PRK11147 398 KTVMDNLAEG-------KQEV--MVNGRPRHV-LGYLQDflfhpkraMTPvKALSGGERNRLLLARLFLKPSNLLILDEP 467
|
170 180 190
....*....|....*....|....*....|....*..
gi 488140883 161 LSNLDaalrvqmrIEISRLHKRL----ERTMIYVTHD 193
Cdd:PRK11147 468 TNDLD--------VETLELLEELldsyQGTVLLVSHD 496
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-212 |
9.20e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGL-EDITSGELLIGGKRMNEVPPS---ERGIGMVFQS---YALYPHLSVA 93
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAqaiRAGIAMVPEDrkrHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSfglkLAGVKKAEIYQRVNQVAEV------LQLAHLLDRRP----KALSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:TIGR02633 358 KNIT----LSVLKSFCFKMRIDAAAELqiigsaIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488140883 164 LDaalrVQMRIEISRLHKRLER---TMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:TIGR02633 434 VD----VGAKYEIYKLINQLAQegvAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-216 |
1.01e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.82 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKrmnevppsergIGMVFQSYALYPHLSVAENMSFGL 100
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIAISSGLNGQLTGIENIELKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 101 KLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRLh 180
Cdd:PRK13545 111 LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF- 189
|
170 180 190
....*....|....*....|....*....|....*.
gi 488140883 181 KRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVG 216
Cdd:PRK13545 190 KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-205 |
3.50e-08 |
|
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: 53.42 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTL----------LRMIAGLE-------------DITSGELL-----IGGKRMNEVP 71
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSayarqflgqmdkpDVDSIEGLspaiaIDQKTTSRNP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 72 PSERGigmvfqsyalyphlSVAE-NMSFGLKLAgvkKAEIYQRVNQVAEVlQLAHL-LDRRPKALSGGQRQRVAIGRTLV 149
Cdd:cd03270 92 RSTVG--------------TVTEiYDYLRLLFA---RVGIRERLGFLVDV-GLGYLtLSRSAPTLSGGEAQRIRLATQIG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488140883 150 SEPD--VFLLDEPLSNLDAALRVQMRIEISRLhKRLERTMIYVTHDQvEAMTLADKIV 205
Cdd:cd03270 154 SGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHVI 209
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
94-221 |
5.31e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMR 173
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488140883 174 IEIsRLHKRLERTMIYVTHDQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:NF000106 185 DEV-RSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-197 |
7.07e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 13 FGEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAG------LEDIT-------SGELLIGGKRMnevppsergIGM 79
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgySNDLTlfgrrrgSGETIWDIKKH---------IGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 80 VFQSYAL-YPHLSVAENM-------SFGlklagvkkaeIYQRV----NQVA-EVLQLAHLLDRRPKA----LSGGQRQRV 142
Cdd:PRK10938 341 VSSSLHLdYRVSTSVRNVilsgffdSIG----------IYQAVsdrqQKLAqQWLDILGIDKRTADApfhsLSWGQQRLA 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 143 AIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLERTMIYVTHDQVEA 197
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-165 |
8.63e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.10 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGleditsgelliggkrmnEVPPSErgiGMVFQSyalyPHLSVA 93
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG-----------------ELQPSS---GTVFRS----AKVRMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ---ENMSFGLKLAGVKKAEIYQRVNQVAEVLQLAHL--------LDRRPK-ALSGGQRQRVAIGRTLVSEPDVFLLDEPL 161
Cdd:PLN03073 576 vfsQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLgsfgvtgnLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
....
gi 488140883 162 SNLD 165
Cdd:PLN03073 656 NHLD 659
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-221 |
1.05e-07 |
|
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: 53.80 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVppserGIGMVFQSYALYPHLSVAENMSFG 99
Cdd:TIGR00957 1303 RHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI-----GLHDLRFKITIIPQDPVLFSGSLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 LKL---AGVKKAEIYQrvnqvaeVLQLAHL----------LDRR----PKALSGGQRQRVAIGRTLVSEPDVFLLDEPLS 162
Cdd:TIGR00957 1378 MNLdpfSQYSDEEVWW-------ALELAHLktfvsalpdkLDHEcaegGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488140883 163 NLD--------AALRVQMR-IEISRLHKRLERTMIYVthdqveamtladKIVVLDAGNIAQVGKPLEL 221
Cdd:TIGR00957 1451 AVDletdnliqSTIRTQFEdCTVLTIAHRLNTIMDYT------------RVIVLDKGEVAEFGAPSNL 1506
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-229 |
1.11e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLL----RMIagleDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYPHlSVA 93
Cdd:PTZ00243 1327 RGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSFGLKlagVKKAEIYQRVNQVA---EVLQLAHLLDRRpkALSGG------QRQRVAIGRTLVSEPDVF-LLDEPLSN 163
Cdd:PTZ00243 1402 QNVDPFLE---ASSAEVWAALELVGlreRVASESEGIDSR--VLEGGsnysvgQRQLMCMARALLKKGSGFiLMDEATAN 1476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 164 LDAALRVQmrIEISRLHKRLERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLELYHYPANRF 229
Cdd:PTZ00243 1477 IDPALDRQ--IQATVMSAFSAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-204 |
4.52e-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: 48.91 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIggkrmnevppsergigmvfqsyalyphlsvaenmsfglkLAGvkka 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------IDG---- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 109 eiyQRVNQVAEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDAALRVQMRIEIS-----RLHKRL 183
Cdd:smart00382 39 ---EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEK 115
|
170 180
....*....|....*....|.
gi 488140883 184 ERTMIYVTHDQVEAMTLADKI 204
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLRR 136
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-214 |
5.65e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 50.24 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 6 LSSVYKAFGEAVIsRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGELLIGGKRMNEVPPSE--RGIGMVFQS 83
Cdd:cd03289 8 LTAKYTEGGNAVL-ENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKwrKAFGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 84 YALYPHlSVAENMSfglKLAGVKKAEIYqrvnQVAEVLQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLVSEP 152
Cdd:cd03289 86 VFIFSG-TFRKNLD---PYGKWSDEEIW----KVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 153 DVFLLDEPLSNLDAalrvqmrIEISRLHKRLER-----TMIYVTHdQVEAMTLADKIVVLDAGNIAQ 214
Cdd:cd03289 158 KILLLDEPSAHLDP-------ITYQVIRKTLKQafadcTVILSEH-RIEAMLECQRFLVIEENKVRQ 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-164 |
5.71e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITS--GELLIGGK--RMNEVPPSE-RGIGMVFQSYALYPHLSVAEN 95
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcRFKDIRDSEaLGIVIIHQELALIPYLSIAEN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488140883 96 MSFGLKLAgvKKAEI-YQRVNQVAEVLqLAHL-LDRRPKALSG----GQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:NF040905 99 IFLGNERA--KRGVIdWNETNRRAREL-LAKVgLDESPDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-221 |
6.52e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 30 EFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYphlsvAENMSFGLK-LAGVK 106
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLF-----SGTVRFNIDpFSEHN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 107 KAEIYqrvnqvaEVLQLAHL---LDRRPKAL-----------SGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDaaLRVQM 172
Cdd:PLN03232 1338 DADLW-------EALERAHIkdvIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVD--VRTDS 1408
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488140883 173 RIEISRLHKRLERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:PLN03232 1409 LIQRTIREEFKSCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-212 |
7.30e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 21 DINLEIDDGEFVVFVGPSGCGKSTLLRMIAGL-EDITSGELLIGGKRMNEVPPSE---RGIGMVFQS---YALYPHLSVA 93
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 ENMSfglkLAGVKKAEIYQRVNQVAEVLQLAHLLDR-RPKA---------LSGGQRQRVAIGRTLVSEPDVFLLDEPLSN 163
Cdd:PRK13549 360 KNIT----LAALDRFTGGSRIDDAAELKTILESIQRlKVKTaspelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488140883 164 LDaalrVQMRIEISRLHKRLER---TMIYVTHDQVEAMTLADKIVVLDAGNI 212
Cdd:PRK13549 436 ID----VGAKYEIYKLINQLVQqgvAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
91-192 |
1.97e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 91 SVAENMSFGLKLAGVKKAEIYQRVNQV---------AEVLQ----LAHLLDRRPKALSGGQRQRVAIGRTLVSEPDVFLL 157
Cdd:PLN03073 289 KGANKDGVDKDAVSQRLEEIYKRLELIdaytaearaASILAglsfTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLL 368
|
90 100 110
....*....|....*....|....*....|....*
gi 488140883 158 DEPLSNLDaaLRVQMRIEISRLhkRLERTMIYVTH 192
Cdd:PLN03073 369 DEPTNHLD--LHAVLWLETYLL--KWPKTFIVVSH 399
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-217 |
3.06e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.93 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRmiAGLEdiTSGELLIGGKRMNevpPSERGIGMVFQsyalyphLSVAENMSFG 99
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--ASGKARLISFLPK---FSRNKLIFIDQ-------LQFLIDVGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 lklagvkkaeiYQRVNQVAEvlqlahlldrrpkALSGGQRQRVAIGRTLVSEPD--VFLLDEPLSNLDAALRVQMRIEIS 177
Cdd:cd03238 78 -----------YLTLGQKLS-------------TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIK 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488140883 178 RLhKRLERTMIYVTHDqVEAMTLADKIVVLDAGNIAQVGK 217
Cdd:cd03238 134 GL-IDLGNTVILIEHN-LDVLSSADWIIDFGPGSGKSGGK 171
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
20-221 |
3.69e-05 |
|
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: 44.90 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVP--PSERGIGMVFQSYALYPHlSVAENMS 97
Cdd:cd03288 38 KHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlhTLRSRLSIILQDPILFSG-SIRFNLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 98 FGLKLAGvkkaeiyQRVNQVAEVLQLAHLLDRRPKAL-----------SGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDA 166
Cdd:cd03288 117 PECKCTD-------DRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDM 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488140883 167 ALR-VQMRIEISRLhkrLERTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:cd03288 190 ATEnILQKVVMTAF---ADRTVVTIAH-RVSTILDADLVLVLSRGILVECDTPENL 241
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-205 |
6.27e-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: 42.73 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 14 GEAVISRDINLEIDDGEFVVFVGPSGCGKSTLLRMIAgleditsgeLLIGGKRMNEVPPSERGIGmVFQSYAlyphlsva 93
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------LALGGAQSATRRRSGVKAG-CIVAAV-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 94 enmsfglklagvkKAEIYQRVNQvaevlqlahlldrrpkaLSGGQRQRVAI-----GRTLVSEPdVFLLDEPLSNLDaaL 168
Cdd:cd03227 68 -------------SAELIFTRLQ-----------------LSGGEKELSALalilaLASLKPRP-LYILDEIDRGLD--P 114
|
170 180 190
....*....|....*....|....*....|....*...
gi 488140883 169 RVQMRI-EISRLHKRLERTMIYVTHDQvEAMTLADKIV 205
Cdd:cd03227 115 RDGQALaEAILEHLVKGAQVIVITHLP-ELAELADKLI 151
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-205 |
6.69e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 26 IDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKR----MN------EVPPSERGIGMVFQSYALYPHLSVAEN 95
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWqlawVNqetpalPQPALEYVIDGDREYRQLEAQLHDANE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 96 MSFGL-------KLAGVKKAEIYQRVNQVAEVLQLAH-LLDRRPKALSGGQRQRVAIGRTLVSEPDVFLLDEPLSNLDaa 167
Cdd:PRK10636 104 RNDGHaiatihgKLDAIDAWTIRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD-- 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 488140883 168 lrVQMRIEISRLHKRLERTMIYVTHDQVEAMTLADKIV 205
Cdd:PRK10636 182 --LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
90-205 |
9.12e-05 |
|
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: 44.62 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 90 LSVAENMSF--GLKLAGVKKA-------EIYQRVNQVAEVlQLAHL-LDRRPKALSGGQRQRVA----IGRTLVSEpdVF 155
Cdd:TIGR00630 436 LSIREAHEFfnQLTLTPEEKKiaeevlkEIRERLGFLIDV-GLDYLsLSRAAGTLSGGEAQRIRlatqIGSGLTGV--LY 512
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488140883 156 LLDEPLSNLDAalRVQMR-IEISRLHKRLERTMIYVTHDQvEAMTLADKIV 205
Cdd:TIGR00630 513 VLDEPSIGLHQ--RDNRRlINTLKRLRDLGNTLIVVEHDE-DTIRAADYVI 560
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-221 |
1.02e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 22 INLEIDDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELLIGGKRMNEVPPSE--RGIGMVFQSYALYphlsvAENMSFG 99
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGIIPQAPVLF-----SGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 100 LK-LAGVKKAEIYqrvnqvaEVLQLAHLLD---RRPKAL-----------SGGQRQRVAIGRTLVSEPDVFLLDEPLSNL 164
Cdd:PLN03130 1333 LDpFNEHNDADLW-------ESLERAHLKDvirRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488140883 165 D----AALRVQMRIEISRLhkrlerTMIYVTHdQVEAMTLADKIVVLDAGNIAQVGKPLEL 221
Cdd:PLN03130 1406 DvrtdALIQKTIREEFKSC------TMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
141-193 |
8.74e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 8.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 488140883 141 RVAIGRTLVSEPDVFLLDEPLSNLDaalrvqmrIE-ISRLHKRL-ER--TMIYVTHD 193
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD--------INtIRWLEDVLnERnsTMIIISHD 211
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
29-59 |
1.33e-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: 39.69 E-value: 1.33e-03
10 20 30
....*....|....*....|....*....|.
gi 488140883 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGE 59
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGE 115
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
10-215 |
2.62e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 10 YKAFgeavisRDINLEIddGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELliggkrmNEVPPSERGIGMVFQSYAlyph 89
Cdd:COG4637 10 FKSL------RDLELPL--GPLTVLIGANGSGKSNLLDALRFLSDAARGGL-------QDALARRGGLEELLWRGP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488140883 90 LSVAENMSFGLKLAGVKKAEI-Y----------QRVNQVAEVLQLAHLLDRRPkALSGGQRQRVAIGRTlvsepdvFLLD 158
Cdd:COG4637 71 RTITEPIRLELEFAEEDERDLrYelelglpepgGRPEVKEERLWLKRGSGGRP-FLDFRPKGRAVGGEP-------ERLD 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488140883 159 EPLSNLDAALRVQMRIEISRLHKRLERTMIYvtHDQVEAMTLADKIV---VL--DAGNIAQV 215
Cdd:COG4637 143 SPESLLSQLGDPERFPELRALREALRSWRFY--DFHPAPLRQPQPAGrtpVLapDGSNLAAV 202
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-45 |
2.68e-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: 40.00 E-value: 2.68e-03
10 20
....*....|....*....|....*.
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTL 45
Cdd:TIGR00630 13 KNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
14-50 |
6.60e-03 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 37.61 E-value: 6.60e-03
10 20 30
....*....|....*....|....*....|....*..
gi 488140883 14 GEAVISRDINLEidDGEFVVFVGPSGCGKSTLLRMIA 50
Cdd:cd03243 16 GETFVPNDINLG--SGRLLLITGPNMGGKSTYLRSIG 50
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
20-45 |
6.85e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 6.85e-03
10 20
....*....|....*....|....*.
gi 488140883 20 RDINLEIDDGEFVVFVGPSGCGKSTL 45
Cdd:COG0178 17 KNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
134-160 |
7.63e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.23 E-value: 7.63e-03
10 20
....*....|....*....|....*..
gi 488140883 134 LSGGQRQRVAIGRTLVSEPDVFLLDEP 160
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEP 431
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