|
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: 826.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 161 LSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 241 FLPVKVTAAEPRQVQVELPNRQLVWLPVEGAGVQPGANLSLGIRPEHLLPGEASEVRLTGDVQVVEQLGNETQIHIQIPA 320
Cdd:PRK11000 241 FLPVKVTATAIEQVQVELPNRQQVWLPVEGRGVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGNETQIHIQIPA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 515497030 321 IRQNLVYRQNDVVLVEEGATFAIGLPPHRCHLFREDGTACKRLHQEPGV 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: 572.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 161 LSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 241 FLPVKVTAAEPRQVQVELPnrqlvwLPvEGAGVQPGANLSLGIRPEHLLPGEASEVRLTGDVQVVEQLGNETQIHIQIPA 320
Cdd:COG3839 241 LLPGTVEGGGVRLGGVRLP------LP-AALAAAAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRLGG 313
|
330 340 350
....*....|....*....|....*....|....*.
gi 515497030 321 irQNLVYRQNDVVLVEEGATFAIGLPPHRCHLFRED 356
Cdd:COG3839 314 --QELVARVPGDTRLRPGDTVRLAFDPERLHLFDAE 347
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-357 |
1.56e-170 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 479.34 E-value: 1.56e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAF--GEAVIsKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIG 78
Cdd:PRK11650 1 MAGLKLQAVRKSYdgKTQVI-KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLD 158
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 159 EPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPK 238
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 239 MNFLPVKVTAAeprQVQVELPNrQLVWLPVEGAGVQPGANLSLGIRPEHLLPGEAsEVRLTGDVQVVEQLGNETQIHIQI 318
Cdd:PRK11650 240 MNLLDGRVSAD---GAAFELAG-GIALPLGGGYRQYAGRKLTLGIRPEHIALSSA-EGGVPLTVDTVELLGADNLAHGRW 314
|
330 340 350
....*....|....*....|....*....|....*....
gi 515497030 319 PaiRQNLVYRQNDVVLVEEGATFAIGLPPHRCHLFREDG 357
Cdd:PRK11650 315 G--GQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADT 351
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-355 |
1.37e-155 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 441.46 E-value: 1.37e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 161 LSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspKMN 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--EAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 241 FLPVKVTAAEPRQVQVElpnRQLVWLPVeGAGVQPGANLSLGIRPEHLLPGEASEV-RLTGDVQVVEQLGNETQIHIQIP 319
Cdd:COG3842 241 LLPGTVLGDEGGGVRTG---GRTLEVPA-DAGLAAGGPVTVAIRPEDIRLSPEGPEnGLPGTVEDVVFLGSHVRYRVRLG 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 515497030 320 AIRQNLVYRQNDVVL-VEEGATFAIGLPPHRCHLFRE 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 |
4.24e-134 |
|
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: 381.22 E-value: 4.24e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQS 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 YALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515497030 164 LDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-335 |
2.29e-112 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 331.34 E-value: 2.29e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 3 SVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMN-EVPPSERGIGMVF 81
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 82 QSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPL 161
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 162 SNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPkmNF 241
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCV--NV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 242 LPVKVTAAEPRQVQVELPnrqlvwlpvEGAGVQPGANLsLGIRPEHL-----------LPGEASEVRLTGDVQVVE-QLG 309
Cdd:COG1118 240 LRGRVIGGQLEADGLTLP---------VAEPLPDGPAV-AGVRPHDIevsrepegentFPATVARVSELGPEVRVElKLE 309
|
330 340
....*....|....*....|....*....
gi 515497030 310 NETQIHIQI---PAIRQNLVYRQNDVVLV 335
Cdd:COG1118 310 DGEGQPLEAevtKEAWAELGLAPGDPVYL 338
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-235 |
1.12e-111 |
|
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: 325.35 E-value: 1.12e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQS 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 YALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497030 164 LDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-353 |
1.41e-107 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 319.29 E-value: 1.41e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMV 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 161 LSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspKMN 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG--EVN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 241 FLPVKVtaAEPRQVQVELPNrqlvwLPVEGAGVQPGANLSLGIRPEH--LLPGEASEVRLTGDVQVVEQLGNETQIHIQI 318
Cdd:TIGR03265 240 WLPGTR--GGGSRARVGGLT-----LACAPGLAQPGASVRLAVRPEDirVSPAGNAANLLLARVEDMEFLGAFYRLRLRL 312
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 515497030 319 P-----AIRQNLVYRQNDVVLVEEGATFAIGLPPHRCHLF 353
Cdd:TIGR03265 313 EglpgqALVADVSASEVERLGIRAGQPIWIELPAERLRAF 352
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
2.06e-107 |
|
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: 313.69 E-value: 2.06e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQS 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 YALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515497030 164 LDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-296 |
2.38e-103 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 309.18 E-value: 2.38e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQS 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 YALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 164 LDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspKMNFLP 243
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINIFD 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 515497030 244 VKVTAA-EPRQVQVELPNRqlVWLPVEGAGVQPGANLSLGIRPEHLLPGEASEV 296
Cdd:PRK09452 253 ATVIERlDEQRVRANVEGR--ECNIYVNFAVEPGQKLHVLLRPEDLRVEEINDD 304
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-304 |
8.89e-98 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 294.60 E-value: 8.89e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 2 ASVTLRSVYKAFG----EAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNE-----VPP 72
Cdd:NF040933 1 VTVRVENVTKIFKkgkkEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 73 SERGIGMVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEP 152
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 153 DVFLLDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAG 232
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 233 FIGspKMNFLPVKV---TAAEPRQVQVELPNRqlvwlPVEGAGVQpganlsLGIRPEHLLPGEASEVRLTGDVQV 304
Cdd:NF040933 241 LIG--DINLLEGKVeeeGLVDGNDLKIPLPNP-----KLEAGEVI------IGIRPEDIDISESDMRLPPGFVEV 302
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-236 |
1.07e-89 |
|
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: 269.59 E-value: 1.07e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 3 SVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQ 82
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 SYALYPHLSVADNMSFGLKLAGAK----KAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLD 158
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 159 EPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS 236
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-286 |
5.48e-89 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 271.98 E-value: 5.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQS 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 YALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 164 LDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPkmNFLP 243
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIFP 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 515497030 244 VKVTaaeprQVQVELPNRQLVwLPVEGAGVQPGANLSLGIRPE 286
Cdd:PRK11432 245 ATLS-----GDYVDIYGYRLP-RPAAFAFNLPDGECTVGVRPE 281
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-215 |
6.63e-88 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 265.80 E-value: 6.63e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAF----GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSerg 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 77 IGMVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515497030 157 LDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDA--GRVAQV 215
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-331 |
1.96e-86 |
|
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: 264.36 E-value: 1.96e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 35 VGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRV 114
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 115 NQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQ 194
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 195 VEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMnflpVKVTAAEPRQVQVELPNRQLVWLPV-EGAGV 273
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINV----FEATVIERKSEQVVLAGVEGRRCDIyTDVPV 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 274 QPGANLSLGIRPEHL----LPGEASEVRLTGDVQVVEQLGNETQIHIQIPAIRQNLV--YRQND 331
Cdd:TIGR01187 238 EKDQPLHVVLRPEKIvieeEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLVseFFNED 301
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
9-235 |
2.67e-86 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 260.89 E-value: 2.67e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 9 VYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQSYALYP 88
Cdd:TIGR00968 6 ISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYALFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 89 HLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAAL 168
Cdd:TIGR00968 86 HLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 169 RVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
Cdd:TIGR00968 166 RKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-268 |
3.08e-85 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 260.41 E-value: 3.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 5 TLRSVYKAFGE---AVisKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGM 79
Cdd:COG1125 3 EFENVTKRYPDgtvAV--DDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 80 VFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQL--AHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLL 157
Cdd:COG1125 81 VIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 158 DEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS- 236
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAd 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 515497030 237 ---PKMNFLPVK-VTAAEPRQVQVELPNRQLV---------WLPV 268
Cdd:COG1125 241 rglRRLSLLRVEdLMLPEPPTVSPDASLREALslmlergvdWLLV 285
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-215 |
5.23e-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: 257.01 E-value: 5.23e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISK----DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSergIGM 79
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaleDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 80 VFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 160 PLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDA--GRVAQV 215
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
20-353 |
1.24e-81 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 252.69 E-value: 1.24e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQSYALYPHLSVADNMSFG 99
Cdd:NF040840 17 RDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 100 LKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRL 179
Cdd:NF040840 97 LKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 180 HKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMnflpVKVTAAEPRQVQVELP 259
Cdd:NF040840 177 HREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENI----IEGVAEKGGEGTILDT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 260 NRQLVWLPVEGAGvqpgaNLSLGIRPEHLL----PGEASEVR-LTGDVQVVEQLGNETQIHIQIPAIRQNLVYRQNDVVL 334
Cdd:NF040840 253 GNIKIELPEEKKG-----KVRIGIRPEDITisteKVKTSARNeFKGKVEEIEDLGPLVKLTLDVGIILVAFITRSSFLDL 327
|
330 340
....*....|....*....|
gi 515497030 335 -VEEGATFAIGLPPHRCHLF 353
Cdd:NF040840 328 eINEGKEVYASFKASAVHVF 347
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-235 |
1.40e-80 |
|
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: 246.09 E-value: 1.40e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQSYALYPHLSVADNMSFG 99
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 100 LKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRL 179
Cdd:cd03299 96 LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 180 HKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
Cdd:cd03299 176 RKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-235 |
4.17e-80 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 249.23 E-value: 4.17e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 3 SVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQ 82
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 SYALYPHLSVADNMSFGLKLAGAKK----AEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLD 158
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVLPRRErpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 159 EPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-238 |
1.70e-79 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 243.75 E-value: 1.70e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGE---AVisKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIG 78
Cdd:cd03295 1 IEFENVTKRYGGgkkAV--NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQL--AHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFL 156
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 157 LDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS 236
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
..
gi 515497030 237 PK 238
Cdd:cd03295 239 DR 240
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-239 |
4.50e-77 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 242.05 E-value: 4.50e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQSYA 85
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 86 LYPHLSVADNMSFGLKLAGAKKAEINQRVNqvsEVLQLAHLLD---RRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVN---EMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 163 NLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKM 239
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-308 |
1.69e-73 |
|
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: 232.30 E-value: 1.69e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIG-------EKRMNeVPPSERGIGMVFQSYALYPHLSVA 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqdsARGIF-LPPHRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFGLKLAGAKKAEInqRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMR 173
Cdd:COG4148 96 GNLLYGRKRAPRAERRI--SFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 174 IEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGfiGSPKMNFLPVKVTAAEPRQ 253
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAGSVLEATVAAHDPDY 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497030 254 --VQVELPNRQLvWLPveGAGVQPGANLSLGIR----------PEHL-----LPGEASEVRLTGDVQVVEQL 308
Cdd:COG4148 252 glTRLALGGGRL-WVP--RLDLPPGTRVRVRIRardvslalepPEGSsilniLPGRVVEIEPADGGQVLVRL 320
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-211 |
4.00e-72 |
|
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: 222.45 E-value: 4.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMN----EVPPSERGIGM 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 80 VFQSYALYPHLSVADNMSFGlklagakkaeinqrvnqvsevlqlahlldrrpkaLSGGQRQRVAIGRTLVAEPDVFLLDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515497030 160 PLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-234 |
4.84e-71 |
|
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: 222.90 E-value: 4.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 7 RSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE------RGIGMV 80
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 161 LSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-216 |
9.14e-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: 220.24 E-value: 9.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIeDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI-------GEKRMNeVPPSERGIGMVFQSYALYPHLSVA 93
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdSRKKIN-LPPQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFGLKlaGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMR 173
Cdd:cd03297 94 ENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515497030 174 IEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
6.89e-67 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 210.67 E-value: 6.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASV-TLRSVYKAFGEAVIS----KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSER 75
Cdd:COG1136 1 MSPLlELRNLTKSYGTGEGEvtalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 76 G------IGMVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLV 149
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 150 AEPDVFLLDEPLSNLDAALRVQ-MRIeISRLHKRLQRTMIYVTHDQvEAMTLADKIVVLDAGRV 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 |
3.43e-66 |
|
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: 208.50 E-value: 3.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEA----VISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG--- 76
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 77 ---IGMVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPD 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMtLADKIVVLDAGRV 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-235 |
6.88e-65 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 205.76 E-value: 6.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 23 NLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQSYALYPHLSVADNMSFG--- 99
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGlrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 100 -LKLAGAKKAEINQRVNQVSevlqLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISR 178
Cdd:COG3840 99 gLKLTAEQRAQVEQALERVG----LAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 179 LHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
Cdd:COG3840 175 LCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
1.55e-63 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 202.60 E-value: 1.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG-IGMVFQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 SYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 163 NLDAALRVQMRIEISRLHKRlQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-223 |
2.71e-63 |
|
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: 201.79 E-value: 2.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQsyalYP-----HLSV 92
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQ----NPddqlfAPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 ADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQM 172
Cdd:COG1122 94 EEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRREL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515497030 173 RIEISRLHKRlQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYH 223
Cdd:COG1122 174 LELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-234 |
2.31e-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: 199.44 E-value: 2.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE-----RGIG 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYPHLSVADNMSFGLK-LAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLL 157
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 158 DEPLSNLD---AALRVQMrieISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPaNRFVAGFI 234
Cdd:COG1127 166 DEPTAGLDpitSAVIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-211 |
1.96e-61 |
|
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: 196.15 E-value: 1.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAVIsKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG--IGMVFQs 83
Cdd:cd03225 5 LSFSYPDGARPAL-DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLVFQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 yalYP-----HLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLD 158
Cdd:cd03225 83 ---NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515497030 159 EPLSNLDAALRVQMRIEISRLHKRlQRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-232 |
5.53e-61 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 197.01 E-value: 5.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVISK----DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMnEVPPSERG 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQpalqDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 77 IgmVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFL 156
Cdd:COG4525 80 V--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 157 LDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDA--GRVAQVgkplelYHYP-ANRFVAG 232
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER------LELDfSRRFLAG 230
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-227 |
1.07e-60 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 195.21 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIG-------EKRMNEVppsERG 76
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDgedltdsKKDINKL---RRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 77 IGMVFQSYALYPHLSVADNMSFGL-KLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVF 155
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 156 LLDEPLSNLDAALrVQmriEISRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAN 227
Cdd:COG1126 159 LFDEPTSALDPEL-VG---EVLDVMRDLAKegmTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 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 515497030 4 VTLRSVYKAFGEAV-ISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE-----RGI 77
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 78 GMVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLL 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 158 DEPLSNLDAAlrvqMRIEISRLHKRLQR---TMIYVTHDQ--VEAMtlADKIVVLDAGRVAQVGK 217
Cdd:COG2884 162 DEPTGNLDPE----TSWEIMELLEEINRrgtTVLIATHDLelVDRM--PKRVLELEDGRLVRDEA 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-221 |
1.67e-57 |
|
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: 186.94 E-value: 1.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE-----RGIG 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYPHLSVADNMSFGLKLAGA-KKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLL 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 158 DEPLSNLD-AALRVQMRIeISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03261 161 DEPTAGLDpIASGVIDDL-IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-234 |
1.37e-56 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 184.91 E-value: 1.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGI----GM 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 80 VFQSYALYPHLSVADNMSFG-LKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLD 158
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 159 EPLSNLDAALRVqmriEISRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
Cdd:PRK09493 162 EPTSALDPELRH----EVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-212 |
4.40e-56 |
|
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: 182.34 E-value: 4.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMN----EVPPSERGIGM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 80 VFQSYALYPHLSVADNMSFGL-KLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 159 EPLSNLDAalrvQMRIEISRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03262 161 EPTSALDP----ELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-212 |
1.43e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 181.17 E-value: 1.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 5 TLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQ 82
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 SYALYPHlSVADNMSFGLKLAGAKKAEinQRVNQVSEVLQLAH-LLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPL 161
Cdd:COG4619 82 EPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515497030 162 SNLDAALRVqmRIE--ISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:COG4619 159 SALDPENTR--RVEelLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-237 |
1.64e-55 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 184.90 E-value: 1.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFG------EAVisKDVNLTIEDGEfvVF--VGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE- 74
Cdd:COG1135 2 IELENLSKTFPtkggpvTAL--DDVSLTIEKGE--IFgiIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSEREl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 75 ----RGIGMVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNqvsEVLQLAHLLDRR---PKALSGGQRQRVAIGRT 147
Cdd:COG1135 78 raarRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVA---ELLELVGLSDKAdayPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 148 LVAEPDVFLLDEPLSNLDAA-----LRVqmrieISRLHKRLQRTMIYVTHDqveaM----TLADKIVVLDAGRVAQVGKP 218
Cdd:COG1135 155 LANNPKVLLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPV 225
|
250
....*....|....*....
gi 515497030 219 LELYHYPANRFVAGFIGSP 237
Cdd:COG1135 226 LDVFANPQSELTRRFLPTV 244
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-212 |
9.38e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 180.25 E-value: 9.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAF-GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE-----RGI 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 78 GMVFQSYALYPHLSVADN--------MSFGLKLAGA-KKAEInQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTL 148
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNvlagrlgrTSTWRSLLGLfPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 149 VAEPDVFLLDEPLSNLD--AALRVqMRIeISRLHKRLQRTMIYVTHdQVE-AMTLADKIVVLDAGRV 212
Cdd:COG3638 162 VQEPKLILADEPVASLDpkTARQV-MDL-LRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDGRV 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-218 |
1.25e-54 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 179.30 E-value: 1.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGDLLIGEKRMNE--VPPSE--RG 76
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDldVDVLElrRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 77 IGMVFQSYALYPhLSVADNMSFGLKLAG-AKKAEINQRvnqVSEVLQLAHLLD---RRPKA--LSGGQRQRVAIGRTLVA 150
Cdd:cd03260 83 VGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDER---VEEALRKAALWDevkDRLHAlgLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 151 EPDVFLLDEPLSNLDAALRvqMRIE--ISRLHKRLqrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:cd03260 159 EPEVLLLDEPTSALDPIST--AKIEelIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-284 |
4.31e-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: 181.85 E-value: 4.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNE------VPPSERGIGMVFQSYALYPHLSVAD 94
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 95 NMSFGLKLAGAKKAEINQrvNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRI 174
Cdd:TIGR02142 95 NLRYGMKRARPSERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 175 EISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAgfiGSPKMNFLPVKVTAAEPRQ- 253
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA---REDQGSLIEGVVAEHDQHYg 249
|
250 260 270
....*....|....*....|....*....|..
gi 515497030 254 -VQVELPNrqlVWLPVEGAGVQPGANLSLGIR 284
Cdd:TIGR02142 250 lTALRLGG---GHLWVPENLGPTGARLRLRVP 278
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
4.51e-54 |
|
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: 178.16 E-value: 4.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFG----EAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE----- 74
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 75 RGIGMVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDV 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497030 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHdQVEAM-TLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-225 |
4.81e-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: 185.88 E-value: 4.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE-----RGIGMVFQ--SYALYPHLSV 92
Cdd:COG1123 282 DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelrRRVQMVFQdpYSSLNPRMTV 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 ADNMSFGLKLAG-AKKAEINQRVNQVSEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRV 170
Cdd:COG1123 362 GDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQA 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 171 QMRIEISRLHKRLQRTMIYVTHD--QVEAMtlADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:COG1123 442 QILNLLRDLQRELGLTYLFISHDlaVVRYI--ADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-221 |
1.14e-53 |
|
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: 177.54 E-value: 1.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG--IGMVF 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELArrIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 82 QSYALYPHLSVADNMSFG----LKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLL 157
Cdd:COG1120 82 QEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 158 DEPLSNLDaaLRVQMRI--EISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG1120 162 DEPTSHLD--LAHQLEVleLLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-216 |
1.59e-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: 1.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQSYALYPHLSVADNMSFGL 100
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 101 KLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRLH 180
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 515497030 181 KRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-213 |
1.69e-53 |
|
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: 176.92 E-value: 1.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEA----VISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGI 77
Cdd:COG1124 2 LEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 78 GMVFQSY--ALYPHLSVADNMSFGLKLAGakKAEINQRVNQVSEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVAEPDV 154
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515497030 155 FLLDEPLSNLDAAlrVQMRI--EISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
Cdd:COG1124 160 LLLDEPTSALDVS--VQAEIlnLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-217 |
2.29e-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: 175.43 E-value: 2.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 23 NLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQSYALYPHLSVADNMSFGLKL 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 103 AGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRLHKR 182
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....*
gi 515497030 183 LQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-209 |
1.45e-52 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 173.44 E-value: 1.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAG-LEDI--TSGDLLIGEKRMNEVPPSERGIGMVFQSYALYPHL 90
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 91 SVADNMSFGLKlAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRV 170
Cdd:COG4136 92 SVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515497030 171 QMRIEI-SRLHKRlQRTMIYVTHDqVEAMTLADKIVVLDA 209
Cdd:COG4136 171 QFREFVfEQIRQR-GIPALLVTHD-EEDAPAAGRVLDLGN 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-221 |
1.01e-51 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 172.35 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 5 TLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI-GEKRMNEVPPSERGIGMVFQS 83
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDVRKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 YALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 164 LDAALRVQMRiEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG4555 163 LDVMARRLLR-EILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-212 |
1.25e-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: 171.53 E-value: 1.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG-----IGMVFQSY--ALYPHLSV 92
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrkeIQMVFQDPmsSLNPRMTI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 ADNMSFGLKLAGA--KKAEINQRVNQVSEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALR 169
Cdd:cd03257 102 GEQIAEPLRIHGKlsKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQ 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515497030 170 VQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03257 182 AQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-226 |
3.14e-50 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 175.48 E-value: 3.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 8 SVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDIT---SGDLLIGEKRMNEVPPSERG--IGMVFQ 82
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGrrIGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 S--YALYPhLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:COG1123 91 DpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 161 LSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
Cdd:COG1123 170 TTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-221 |
1.62e-49 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 166.30 E-value: 1.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 23 NLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQSYALYPHLSVADNMSFG--- 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 100 -LKLAGAKKAEINQRVNQVSevlqLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISR 178
Cdd:PRK10771 99 gLKLNAAQREKLHAIARQMG----IEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515497030 179 LHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-222 |
1.66e-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: 1.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMN-----EVPPSERGIGMVFQsyalYPH----- 89
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDLRKKVGLVFQ----FPEhqlfe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 90 LSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAAL 168
Cdd:TIGR04521 98 ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKG 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515497030 169 RVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:TIGR04521 178 RKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
20-221 |
1.93e-48 |
|
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: 163.51 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE-----RGIGMVFQSYALYPHLSVAD 94
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIGMIFQQFNLIERLSVLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 95 N--------MSFGLKLAGA-KKAEInQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLD 165
Cdd:cd03256 98 NvlsgrlgrRSTWRSLFGLfPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 166 AALRVQ-MRIeISRLHKRLQRTMIYVTHdQVE-AMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03256 177 PASSRQvMDL-LKRINREEGITVIVSLH-QVDlAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-212 |
3.34e-48 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 163.69 E-value: 3.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERgigMVFQS 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 YALYPHLSVADNMSFGLKLAGAKKAEinqrvnQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515497030 164 LDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-222 |
8.34e-48 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 162.98 E-value: 8.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI-GEKRMNE--VPPSERGIGMVFQSyalyPH-----LS 91
Cdd:TIGR04520 19 KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVdGLDTLDEenLWEIRKKVGMVFQN----PDnqfvgAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 92 VADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQ 171
Cdd:TIGR04520 95 VEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515497030 172 MRIEISRLHKRLQRTMIYVTHDQVEAmTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:TIGR04520 175 VLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-211 |
3.48e-47 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 159.72 E-value: 3.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAV-ISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEK-----RMNEVPPSERGI 77
Cdd:TIGR02673 2 IEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEdvnrlRGRQLPLLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 78 GMVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLL 157
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 158 DEPLSNLDAALRVQ-MRIeISRLHKRlQRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:TIGR02673 162 DEPTGNLDPDLSERiLDL-LKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
7.18e-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: 158.82 E-value: 7.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGE----AVisKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSER-GIG 78
Cdd:cd03263 1 LQIRNLTKTYKKgtkpAV--DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARqSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLD 158
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515497030 159 EPLSNLDAALRVQMRIEISRLhkRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
1.47e-46 |
|
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: 156.40 E-value: 1.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG-IGMVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 SYALYPHLSVADNMSfglklagakkaeinqrvnqvsevlqlahlldrrpkaLSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:cd03230 81 EPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515497030 163 NLDAALRVQMRIEISRLHKRlQRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-221 |
1.59e-46 |
|
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: 168.47 E-value: 1.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 3 SVTLRSV---YKAFGEAVIsKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGI 77
Cdd:COG2274 473 DIELENVsfrYPGDSPPVL-DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 78 GMVFQSYALYpHLSVADNMSFGlklagakKAEINQrvNQVSEVLQLAHLLD---RRPK-----------ALSGGQRQRVA 143
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENITLG-------DPDATD--EEIIEAARLAGLHDfieALPMgydtvvgeggsNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 144 IGRTLVAEPDVFLLDEPLSNLDAALrvQMRIeISRLHKRLQ-RTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAET--EAII-LENLRRLLKgRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-221 |
1.71e-46 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 158.40 E-value: 1.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEvPPSERGIgmVFQSYALYPHLSVADNMSFG 99
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 100 LK--LAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEIS 177
Cdd:TIGR01184 79 VDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515497030 178 RLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR01184 159 QIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-233 |
1.77e-46 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 163.28 E-value: 1.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE------RGIGMVFQSYALYPHLSVA 93
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMR 173
Cdd:PRK10070 125 DNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 174 IEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGF 233
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-216 |
2.53e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 158.25 E-value: 2.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 3 SVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMN-EVPPSERGI---- 77
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfSQKPSEKAIrllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 78 ---GMVFQSYALYPHLSVADNMSFG-LKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPD 153
Cdd:COG4161 82 qkvGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515497030 154 VFLLDEPLSNLDAALRVQMrIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:COG4161 162 VLLFDEPTAALDPEITAQV-VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-216 |
7.89e-46 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 157.10 E-value: 7.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 3 SVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMN-EVPPSE------- 74
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfSKTPSDkairelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 75 RGIGMVFQSYALYPHLSVADNM-SFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPD 153
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 154 VFLLDEPLSNLDAALRVQmrieISRLHKRLQRTMI---YVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQ----IVSIIRELAETGItqvIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
21-232 |
1.15e-45 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 156.78 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMnEVPPSERGIgmVFQSYALYPHLSVADNMSFGL 100
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAERGV--VFQNEGLLPWRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 101 KLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRLH 180
Cdd:PRK11248 96 QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLW 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515497030 181 KRLQRTMIYVTHDQVEAMTLADKIVVL--DAGRVAQvGKPLELyhypANRFVAG 232
Cdd:PRK11248 176 QETGKQVLLITHDIEEAVFMATELVLLspGPGRVVE-RLPLNF----ARRFVAG 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-218 |
1.20e-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: 156.06 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSER---GIGMVFQ 82
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 SYALYPHLSVADNM----------SFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEP 152
Cdd:cd03219 83 IPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 153 DVFLLDEPLSNLDAALRVQMRIEISRLHKRlQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
20-228 |
5.53e-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: 5.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLL-----IGEKRMNEVPPSERGIGMVFQSYALYPHLSVAD 94
Cdd:TIGR02315 19 KNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILlegtdITKLRGKKLRKLRRRIGMIFQHYNLIERLTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 95 N--------MSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDA 166
Cdd:TIGR02315 99 NvlhgrlgyKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497030 167 ALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANR 228
Cdd:TIGR02315 179 KTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRH 240
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-216 |
1.39e-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: 1.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEA----VISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVP-PSERGIG 78
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLD 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 159 EPLSNLDaALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03266 162 EPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-211 |
1.76e-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: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 5 TLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 syalyphlsvadnmsfglklagakkaeinqrvnqvsevlqlahlldrrpkaLSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515497030 163 NLDAALRVQMRIEISRLHKRlQRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-207 |
2.75e-44 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 151.61 E-value: 2.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEK---RMNEVPPSE---RGIGM 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKASKfrrEKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 80 VFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDE 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515497030 160 PLSNLDAALRvQMRIEISRLHKRLQRTMIYVTHDQvEAMTLADKIVVL 207
Cdd:TIGR03608 161 PTGSLDPKNR-DEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-162 |
3.05e-44 |
|
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: 149.72 E-value: 3.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMN--EVPPSERGIGMVFQSYALYPHLSVADNMS 97
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTddERKSLRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 98 FGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRR----PKALSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-214 |
4.38e-44 |
|
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: 152.20 E-value: 4.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAF----GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI-GEK--RMNEVPPSE-- 74
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLaGQDlfALDEDARARlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 75 -RGIGMVFQSYALYPHLSVADNMSFGLKLAGAKKAEinQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPD 153
Cdd:COG4181 89 aRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR--ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 154 VFLLDEPLSNLDAALRVQMrIE-ISRLHKRLQRTMIYVTHDQveamTLA---DKIVVLDAGRVAQ 214
Cdd:COG4181 167 ILFADEPTGNLDAATGEQI-IDlLFELNRERGTTLVLVTHDP----ALAarcDRVLRLRAGRLVE 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
5.01e-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: 150.28 E-value: 5.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 5 TLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERgigmvfqsy 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 85 alyphlsvADNMSFglklagakkaeinqrVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNL 164
Cdd:cd03214 72 --------ARKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515497030 165 DaaLRVQMRI--EISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03214 129 D--IAHQIELleLLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-221 |
1.42e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 158.79 E-value: 1.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSYALYpHLSVADNMS 97
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGTIRENIR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 98 FGLKLAG-------AKKAEINQRVNQVSEvlQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAA--L 168
Cdd:COG1132 436 YGRPDATdeeveeaAKAAQAHEFIEALPD--GYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTEteA 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 169 RVQMRIEisRLHKrlQRTMIYVTH--DQVEAmtlADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG1132 514 LIQEALE--RLMK--GRTTIVIAHrlSTIRN---ADRILVLDDGRIVEQGTHEEL 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
2.00e-43 |
|
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: 148.30 E-value: 2.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSV---YKAFGEAVIsKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIG 78
Cdd:cd03228 1 IEFKNVsfsYPGRPKPVL-KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYpHLSVADNMsfglklagakkaeinqrvnqvsevlqlahlldrrpkaLSGGQRQRVAIGRTLVAEPDVFLLD 158
Cdd:cd03228 80 YVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515497030 159 EPLSNLDAALRVQMRIEISRLHKRlqRTMIYVTHDqVEAMTLADKIVVLDAGR 211
Cdd:cd03228 122 EATSALDPETEALILEALRALAKG--KTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-211 |
4.45e-43 |
|
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: 148.40 E-value: 4.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 2 ASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG-IGMV 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQSYALYPHLSVADNMSFGLKLAGAKKAEInqRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515497030 161 LSNLDAAlRVQMRIEISRLHKRLQRTMIYVTHDQVEAmtLADKIVVLDAGR 211
Cdd:COG4133 159 FTALDAA-GVALLAELIAAHLARGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-220 |
1.22e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 148.70 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPpseRGIGMV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR---RRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQSYALYPH--LSVADNMSFGL----KLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDV 154
Cdd:COG1121 81 PQRAEVDWDfpITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 155 FLLDEPLSNLDAAlrvqMRIEISRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGRVAQvGKPLE 220
Cdd:COG1121 161 LLLDEPFAGVDAA----TEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEE 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
20-223 |
3.39e-42 |
|
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: 154.92 E-value: 3.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSyalyPHL---SVAD 94
Cdd:COG4988 354 DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWVPQN----PYLfagTIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 95 NMSFGlkLAGAKKAEINQRVNQVsevlQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:COG4988 430 NLRLG--RPDASDEELEAALEAA----GLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAH 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 164 LDAALRVQMRIEISRLHKrlQRTMIYVTHDQvEAMTLADKIVVLDAGRVAQVGKPLELYH 223
Cdd:COG4988 504 LDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-230 |
2.72e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 148.03 E-value: 2.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFG------EAVisKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--- 74
Cdd:PRK11153 2 IELKNISKVFPqggrtiHAL--NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 75 --RGIGMVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEP 152
Cdd:PRK11153 80 arRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 153 DVFLLDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTH--DQVEAmtLADKIVVLDAGRVAQVGKPLELYHYP----A 226
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHemDVVKR--ICDRVAVIDAGRLVEQGTVSEVFSHPkhplT 237
|
....
gi 515497030 227 NRFV 230
Cdd:PRK11153 238 REFI 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-212 |
2.98e-41 |
|
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: 144.09 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVIS-KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEK-----RMNEVPPSERGI 77
Cdd:cd03292 1 IEFINVTKTYPNGTAAlDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 78 GMVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLL 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 158 DEPLSNLDAAlrvqMRIEISRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03292 161 DEPTGNLDPD----TTWEIMNLLKKINKagtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-222 |
3.02e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 146.35 E-value: 3.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIG-----EKRMNeVPPSERGIGMVFQ--SYALYPHlSV 92
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvditDKKVK-LSDIRKKVGLVFQypEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 ADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAH--LLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRV 170
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515497030 171 QMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-217 |
3.94e-41 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 145.18 E-value: 3.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 8 SVYkaFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGDLLIGEKRMN--EVPPSE--RGIG 78
Cdd:COG1117 18 NVY--YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDIYdpDVDVVElrRRVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYPHlSVADNMSFGLKLAGAK-KAEINQRVnqvSEVLQLAHL-------LDRRPKALSGGQRQRVAIGRTLVA 150
Cdd:COG1117 96 MVFQKPNPFPK-SIYDNVAYGLRLHGIKsKSELDEIV---EESLRKAALwdevkdrLKKSALGLSGGQQQRLCIARALAV 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515497030 151 EPDVFLLDEPLSNLD--AAlrvqMRIE--ISRLHKRLqrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:COG1117 172 EPEVLLMDEPTSALDpiST----AKIEelILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGP 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-212 |
8.36e-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: 142.74 E-value: 8.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQS 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 YALYPHLSVADNMSFGLKLAGAKKaeinQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515497030 164 LDAALRVQMRiEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03268 157 LDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-221 |
9.29e-41 |
|
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: 142.89 E-value: 9.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 11 KAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI-GEKRMNEVPPSERGIGMVFQSYALYPH 89
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVVREPREVRRRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 90 LSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALR 169
Cdd:cd03265 88 LTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515497030 170 VQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03265 168 AHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-221 |
3.61e-40 |
|
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: 149.15 E-value: 3.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSyalyPHL---SVAD 94
Cdd:COG4987 352 DGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQR----PHLfdtTLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 95 NmsfgLKLA--GAKKAEINQRVNQVsevlQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLVAEPDVFLLDEPL 161
Cdd:COG4987 428 N----LRLArpDATDEELWAALERV----GLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515497030 162 SNLDAALRVQMrieISRLHKRLQ-RTMIYVTHDQVeAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG4987 500 EGLDAATEQAL---LADLLEALAgRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEEL 556
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-226 |
4.64e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 143.24 E-value: 4.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGE------KRMNEVPPSERGIGMVFQ--SYALYPHlS 91
Cdd:PRK13634 24 YDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitagKKNKKLKPLRKKVGIVFQfpEHQLFEE-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 92 VADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAH-LLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRV 170
Cdd:PRK13634 103 VEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 171 QMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-228 |
1.25e-39 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 143.86 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIG-------EKRMNeVPPSERGIGMVFQSYALYPHLSVA 93
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNgrvlfdaEKGIC-LPPEKRRIGYVFQDARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFGLKlagakkAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMR 173
Cdd:PRK11144 95 GNLRYGMA------KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 174 IEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANR 228
Cdd:PRK11144 169 PYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-226 |
2.57e-39 |
|
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: 142.11 E-value: 2.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLED---ITSGDLLIGEKRMNEVPPSE------RGIGMVFQ-SY-ALYPH 89
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElrkirgREIQMIFQdPMtSLNPV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 90 LSVADNMSFGLKL-AGAKKAEINQRVnqvSEVLQLAHL------LDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:COG0444 103 MTVGDQIAEPLRIhGGLSKAEARERA---IELLERVGLpdperrLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTT 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 163 NLDAALRVQmrieISRLHKRLQR----TMIYVTHD--QVEAMtlADKIVVLDAGRVAQVGKPLELYHYPA 226
Cdd:COG0444 180 ALDVTIQAQ----ILNLLKDLQRelglAILFITHDlgVVAEI--ADRVAVMYAGRIVEEGPVEELFENPR 243
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-221 |
3.00e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 140.51 E-value: 3.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNE--VPPSERGIGMVFQSyalyPH-----LSV 92
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKKIGIIFQN----PDnqfigATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 ADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQM 172
Cdd:PRK13632 102 EDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515497030 173 RIEISRLHKRLQRTMIYVTHDQVEAmTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK13632 182 KKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
5.58e-39 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 139.06 E-value: 5.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVF 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 82 QSYALYPHLSVADNMSFGL----KlaGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLL 157
Cdd:COG4604 82 QENHINSRLTVRELVAFGRfpysK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 158 DEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
6.76e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 139.11 E-value: 6.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPP--SERG-- 76
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsQQKGli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 77 ------IGMVFQSYALYPHLSVADNMSFG-LKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLV 149
Cdd:PRK11264 81 rqlrqhVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 150 AEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRlQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-222 |
6.80e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 137.07 E-value: 6.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNE--VPPSERGIGMVFQSyalyPH-----LSV 92
Cdd:PRK13635 24 KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVRRQVGMVFQN----PDnqfvgATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 ADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQM 172
Cdd:PRK13635 100 QDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515497030 173 RIEISRLHKRLQRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13635 180 LETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-204 |
1.31e-37 |
|
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: 134.79 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAV-ISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG------IG 78
Cdd:TIGR02211 7 LGKRYQEGKLDTrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnkkLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLD 158
Cdd:TIGR02211 87 FIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLAD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515497030 159 EPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDqveaMTLADKI 204
Cdd:TIGR02211 167 EPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHD----LELAKKL 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-221 |
1.70e-37 |
|
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: 134.48 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 5 TLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSER---GIGMVF 81
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 82 QSYALYPHLSVADNmsfgLKLAG--AKKAEINQRVNQVSEVL-QLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLD 158
Cdd:cd03224 82 EGRRIFPELTVEEN----LLLGAyaRRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515497030 159 EPLSNLDAALRVQMRIEISRLhKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-221 |
3.54e-37 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 134.44 E-value: 3.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRsvykaFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD--LLIGEKR------------ 66
Cdd:COG1119 6 LRNVTVR-----RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLFGERRggedvwelrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 67 -------MNEVPPSERGIGMV----FQSYALYPHLSVADNmsfglklagakkaeinQRVNQVSEVLQLAHLLDRRPKALS 135
Cdd:COG1119 81 glvspalQLRFPRDETVLDVVlsgfFDSIGLYREPTDEQR----------------ERARELLELLGLAHLADRPFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 136 GGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
....*.
gi 515497030 216 GKPLEL 221
Cdd:COG1119 225 GPKEEV 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-214 |
7.82e-37 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 132.27 E-value: 7.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 12 AFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI-GEKRMNEVppseRGIGMVFQSYAL---Y 87
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLEKER----KRIGYVPQRRSIdrdF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 88 PhLSVADNMSFGL-----KLAGAKKAEInQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:cd03235 84 P-ISVRDVVLMGLyghkgLFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 163 NLDaalrVQMRIEISRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGRVAQ 214
Cdd:cd03235 162 GVD----PKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-236 |
8.74e-37 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 133.77 E-value: 8.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI-GE-------KRMNEVPPSER 75
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVgGEeirlkpdRDGELVPADRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 76 -------GIGMVFQSYALYPHLSVADNMSFG-LKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRT 147
Cdd:COG4598 89 qlqrirtRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 148 LVAEPDVFLLDEPLSNLDAALrVQmriEISRLHKRL---QRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHY 224
Cdd:COG4598 169 LAMEPEVMLFDEPTSALDPEL-VG---EVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGN 244
|
250
....*....|..
gi 515497030 225 PANRFVAGFIGS 236
Cdd:COG4598 245 PKSERLRQFLSS 256
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
21-226 |
1.25e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 135.24 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE-----RGIGMVFQ-SYA-LYPHLSVA 93
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQdPYAsLNPRMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFGLKLAG-AKKAEINQRVNQVSEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQ 171
Cdd:COG4608 116 DIIAEPLRIHGlASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQ 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515497030 172 mrieISRLHKRLQR----TMIYVTHD--QVEAMtlADKIVVLDAGRVAQVGKPLELYHYPA 226
Cdd:COG4608 196 ----VLNLLEDLQDelglTYLFISHDlsVVRHI--SDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-221 |
1.74e-36 |
|
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: 132.35 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFG-EAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEV--PPSERGIGMV 80
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQSYALYpHLSVADNMSFGLKLAG-------AKKAEINQRVNQVSEvlQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPD 153
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYGRPDATdeevieaAKAAQIHDKIMRFPD--GYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRlqRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-216 |
2.18e-36 |
|
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: 131.25 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 9 VYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVP-------PSERGigmvf 81
Cdd:cd03269 6 VTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEERG----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 82 qsyaLYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPL 161
Cdd:cd03269 81 ----LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 162 SNLDAALRVQMRIEISRLhKRLQRTMIYVTH--DQVEAMtlADKIVVLDAGRVAQVG 216
Cdd:cd03269 157 SGLDPVNVELLKDVIREL-ARAGKTVILSTHqmELVEEL--CDRVLLLNKGRAVLYG 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-212 |
2.89e-36 |
|
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: 131.17 E-value: 2.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSyalyPHL---SVAD 94
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQD----VTLfygTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 95 NMSFGLKLAGakkaeiNQRVNQVSEVLQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:cd03245 97 NITLGAPLAD------DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515497030 164 LDaaLRVQMRIeISRLHKRL-QRTMIYVTHDQVeAMTLADKIVVLDAGRV 212
Cdd:cd03245 171 MD--MNSEERL-KERLRQLLgDKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-260 |
3.69e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 132.93 E-value: 3.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 3 SVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVP-------PSER 75
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 76 GigmvfqsyaLYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVF 155
Cdd:COG4152 81 G---------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 156 LLDEPLSNLDAALRVQMRIEISRLHKRlQRTMIYVTH--DQVEAmtLADKIVVLDAGRVAQVGKPLELYH-YPANRFVAG 232
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHqmELVEE--LCDRIVIINKGRKVLSGSVDEIRRqFGRNTLRLE 228
|
250 260 270
....*....|....*....|....*....|
gi 515497030 233 FIGSPKM--NFLPVKVTAAEPRQVQVELPN 260
Cdd:COG4152 229 ADGDAGWlrALPGVTVVEEDGDGAELKLED 258
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-212 |
4.93e-36 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 130.07 E-value: 4.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 18 ISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRmneVPPSER--GIGMVFQS--YALYPHlSVA 93
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERrkSIGYVMQDvdYQLFTD-SVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFGLKLAGAKkaeiNQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAAlrvQMR 173
Cdd:cd03226 91 EELLLGLKELDAG----NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK---NME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515497030 174 iEISRLHKRLQ---RTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03226 164 -RVGELIRELAaqgKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-221 |
1.01e-34 |
|
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: 127.34 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSYALYPHlSVADNMS 97
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 98 FGLKLAGAKkaeinqRVNQVSEVLQLAHLLDRRPKA-----------LSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLD- 165
Cdd:cd03254 99 LGRPNATDE------EVIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARAMLRDPKILILDEATSNIDt 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 166 -AALRVQMRIEisRLHKrlQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03254 173 eTEKLIQEALE--KLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-216 |
1.61e-34 |
|
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: 126.15 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVfVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG-IGMVFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGL-LGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 SYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 163 NLDAALRVQMRIEISRLHKrlQRTMIYVTH--DQVEAMtlADKIVVLDAGRVAQVG 216
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHivEDVESL--CNQVAVLNKGKLVFEG 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-222 |
2.74e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 126.12 E-value: 2.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 11 KAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSER---GIGMVFQSYALY 87
Cdd:cd03218 8 KRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 88 PHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDaA 167
Cdd:cd03218 88 RKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD-P 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 168 LRVQmriEISRLHKRL-QRTM-IYVT-HDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:cd03218 167 IAVQ---DIQKIIKILkDRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-221 |
5.27e-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: 125.48 E-value: 5.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 5 TLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSER---GIGMVF 81
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 82 QSYALYPHLSVADNMSFGLKlAGAKKAEINQRVNQVSEVL-QLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:COG0410 85 EGRRIFPSLTVEENLLLGAY-ARRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 161 LSNLdAALRVQmriEISRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG0410 164 SLGL-APLIVE---EIFEIIRRLNRegvTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-222 |
1.18e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.00 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNE--VPPSERGIGMVFQSyalyPH-----LSV 92
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenVWDIRHKIGMVFQN----PDnqfvgATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 ADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQM 172
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515497030 173 RIEISRLHKRLQRTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13650 180 IKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELF 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-216 |
2.27e-33 |
|
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: 122.66 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 3 SVTLRSVYKAFGEAVIsKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGDLLIGEKRMNEVPPSERgIGMV 80
Cdd:cd03213 10 TVTVKSSPSKSGKQLL-KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSFRKI-IGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQSYALYPHLSVADNMSFGLKLAGakkaeinqrvnqvsevlqlahlldrrpkaLSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:cd03213 88 PQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 161 LSNLDAALRVQMRIEISRLHKrLQRTMIYVTHD-QVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-235 |
2.81e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 124.18 E-value: 2.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 13 FGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRM-------NEVPPSE--RGIGMVFQS 83
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLfgrniysPDVDPIEvrREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 YALYPHLSVADNMSFGLKLAG--AKKAEINQRVNQVsevLQLAHLLDR-------RPKALSGGQRQRVAIGRTLVAEPDV 154
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWA---LKKAALWDEvkdrlndYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLqrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAN----RFV 230
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHelteKYV 248
|
....*
gi 515497030 231 AGFIG 235
Cdd:PRK14267 249 TGALG 253
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-212 |
3.26e-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: 123.60 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 15 EAVisKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLligeKRMNEVPPSERG-----IGMVF-QSYALYP 88
Cdd:cd03267 35 EAL--KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV----RVAGLVPWKRRKkflrrIGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 89 HLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAAL 168
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515497030 169 RVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03267 189 QENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
3.26e-33 |
|
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: 121.38 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE---RGIGMV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQsyalyphlsvadnmsfglklagakkaeinqrvnqvsevlqlahlldrrpkaLSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 161 LSNLDAAlrvqmriEISRLHKRLQR------TMIYVTHDQVEAMTLADKIVVLDAGRVA 213
Cdd:cd03216 110 TAALTPA-------EVERLFKVIRRlraqgvAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-232 |
6.62e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 123.10 E-value: 6.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGL-----EDITSGDLLIGEKRMNEVPPSE- 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 75 -RGIGMVFQSYALYPHLSVADNMSFGLKL--AGAKKAEINQRVNQVSEVLQLAHLLDRRPKA----LSGGQRQRVAIGRT 147
Cdd:PRK14247 81 rRRVQMVFQIPNPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 148 LVAEPDVFLLDEPLSNLDAalRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP-- 225
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDP--ENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPrh 238
|
....*....
gi 515497030 226 --ANRFVAG 232
Cdd:PRK14247 239 elTEKYVTG 247
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-212 |
9.53e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.83 E-value: 9.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKrmnEVPPS------ERGI 77
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE---PVRFRsprdaqAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 78 GMVFQSYALYPHLSVADNMSFGLKLAGA---KKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDV 154
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 155 FLLDEPLSNLDAAlrvqmriEISRLHKRLQR------TMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:COG1129 162 LILDEPTASLTER-------EVERLFRIIRRlkaqgvAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-222 |
2.50e-32 |
|
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: 121.11 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 18 ISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSYALYPhLSVADN 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 96 MSFGLKLA-------GAKKAEINqrvnqvSEVLQLAHLLD----RRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNL 164
Cdd:cd03249 97 IRYGKPDAtdeeveeAAKKANIH------DFIMSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 165 DAA--LRVQMRIEisRLHKrlQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:cd03249 171 DAEseKLVQEALD--RAMK--GRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-218 |
3.21e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 126.29 E-value: 3.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKrmnEVPPS------ERGI 77
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRsprdaiALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 78 GMVFQSYALYPHLSVADNMSFGL---KLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDV 154
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 155 FLLDEPLSNLDAAlrvqmriEISRLHKRLQR------TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:COG3845 163 LILDEPTAVLTPQ-------EADELFEILRRlaaegkSIIFITHKLREVMAIADRVTVLRRGKVVGTVDT 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-216 |
4.90e-32 |
|
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: 120.32 E-value: 4.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 5 TLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSER---GIGMVF 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 82 QSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQlaHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPL 161
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVLK--EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 162 SNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASG 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-221 |
6.86e-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: 125.69 E-value: 6.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL--LIGEK--RMNEVPPSERG-----IGMVFQSYALYPHLSV 92
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDEwvDMTKPGPDGRGrakryIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 ADNM--SFGLKLA---GAKKAEINQRVNQVSEVlQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAA 167
Cdd:TIGR03269 383 LDNLteAIGLELPdelARMKAVITLKMVGFDEE-KAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPI 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515497030 168 LRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR03269 462 TKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-227 |
8.42e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 125.18 E-value: 8.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLligekrmnEVPPSERgIGMVFQSYA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLR-IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 86 LYPHLSVADN--MSFG-LKLAGAKKAEINQRVNQVSEVL-QLAHL-----------------------------LDRRPK 132
Cdd:COG0488 72 LDDDLTVLDTvlDGDAeLRALEAELEELEAKLAEPDEDLeRLAELqeefealggweaearaeeilsglgfpeedLDRPVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 133 ALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDaalrvqmrIE-ISRLHKRLQR---TMIYVTHD-----QVeamtlADK 203
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--------LEsIEWLEEFLKNypgTVLVVSHDryfldRV-----ATR 218
|
250 260
....*....|....*....|....
gi 515497030 204 IVVLDAGRvaqvgkpleLYHYPAN 227
Cdd:COG0488 219 ILELDRGK---------LTLYPGN 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-225 |
8.67e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 125.57 E-value: 8.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFgEAVisKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGDLLIGEKRMNEVPPSE-----RGIGMV 80
Cdd:COG4172 292 FRRTVGHV-KAV--DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQS-YA-LYPHLSVADNMSFGLKL--AGAKKAEINQRVNQV-SEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVF 155
Cdd:COG4172 368 FQDpFGsLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEAlEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 156 LLDEPLSNLDAALRVQmrieISRLHKRLQR----TMIYVTHDQ--VEAMtlADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:COG4172 448 VLDEPTSALDVSVQAQ----ILDLLRDLQRehglAYLFISHDLavVRAL--AHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
10-222 |
9.30e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.06 E-value: 9.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 10 YKAFGEAVIsKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGL--------EDITSGDLLIGEKRMNEVppSERgIGMVF 81
Cdd:PRK13640 15 YPDSKKPAL-NDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWDI--REK-VGIVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 82 QSyalyPH-----LSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFL 156
Cdd:PRK13640 91 QN----PDnqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 157 LDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAmTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIF 231
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-212 |
1.23e-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: 126.13 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSYALYpHLSVADNMS 97
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTLRDNIA 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 98 FGLklAGAKKAEINQRVNQ--VSEVLQ-----LAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAalRV 170
Cdd:TIGR03375 561 LGA--PYADDEEILRAAELagVTEFVRrhpdgLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDN--RS 636
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515497030 171 QMRIeISRLHKRLQ-RTMIYVTHdQVEAMTLADKIVVLDAGRV 212
Cdd:TIGR03375 637 EERF-KDRLKRWLAgKTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-212 |
1.31e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 120.19 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFG-----EAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG-- 76
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 77 IGMVFQSYAL--YPHLSVADNMS--------FGLKLaGAKKAEINQRVNQVSEV-LQLAHLLDRRPKALSGGQRQRVAIG 145
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRR-GLTKKRRELFRELLATLgLGLENRLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 146 RTLVAEPDVFLLDEPLSNLD--AALRVqmrIEIS-RLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDpkTAALV---LELTeKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
12-220 |
2.84e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 118.96 E-value: 2.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 12 AFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGigmvfQSYALYP--H 89
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-----RRLALLPqhH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 90 L-----SVADNMSFG----LKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:PRK11231 86 LtpegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515497030 161 LSNLDaalrVQMRIEISRLHKRLQ---RTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
Cdd:PRK11231 166 TTYLD----INHQVELMRLMRELNtqgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-207 |
5.57e-31 |
|
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: 123.17 E-value: 5.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSYALYPHlS 91
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 92 VADNMSFGLKlaGAKKAEINQRVNQV--SEVLQ-----LAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNL 164
Cdd:TIGR02857 412 IAENIRLARP--DASDAEIREALERAglDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515497030 165 DAALRVQMRIEISRLHKRlqRTMIYVTHDqVEAMTLADKIVVL 207
Cdd:TIGR02857 490 DAETEAEVLEALRALAQG--RTVLLVTHR-LALAALADRIVVL 529
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
8-234 |
7.71e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.57 E-value: 7.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 8 SVYKAFGEAVisKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNE----VPPSE-----RGIG 78
Cdd:PRK14239 12 SVYYNKKKAL--NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGhniySPRTDtvdlrKEIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYPhLSVADNMSFGLKLAGAKKAEINQRVnqVSEVLQLAHLLDR-------RPKALSGGQRQRVAIGRTLVAE 151
Cdd:PRK14239 90 MVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEA--VEKSLKGASIWDEvkdrlhdSALGLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 152 PDVFLLDEPLSNLDAAlrVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVA 231
Cdd:PRK14239 167 PKIILLDEPTSALDPI--SAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETE 244
|
...
gi 515497030 232 GFI 234
Cdd:PRK14239 245 DYI 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-193 |
8.40e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 117.22 E-value: 8.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG------IGMVFQSYALYPHLSVA 93
Cdd:PRK11629 26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqkLGFIYQFHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMR 173
Cdd:PRK11629 106 ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170 180
....*....|....*....|
gi 515497030 174 IEISRLHKRLQRTMIYVTHD 193
Cdd:PRK11629 186 QLLGELNRLQGTAFLVVTHD 205
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
15-222 |
9.71e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.93 E-value: 9.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 15 EAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSyalyPH--- 89
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQN----PDnqf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 90 --LSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAA 167
Cdd:PRK13648 97 vgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 168 LRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-222 |
1.11e-30 |
|
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: 116.95 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSV---YKAFGEAVIsKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIG 78
Cdd:cd03251 1 VEFKNVtfrYPGDGPPVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYpHLSVADNMSFGLKLAGAKkaeinqrvnQVSEVLQLAHLLD--------------RRPKALSGGQRQRVAI 144
Cdd:cd03251 80 LVSQDVFLF-NDTVAENIAYGRPGATRE---------EVEEAARAANAHEfimelpegydtvigERGVKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 145 GRTLVAEPDVFLLDEPLSNLDaaLRVQMRIE--ISRLHKRlqRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:cd03251 150 ARALLKDPPILILDEATSALD--TESERLVQaaLERLMKN--RTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-228 |
1.96e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 117.10 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLL-----IGEKRMNEVPPSERGIGMVFQSY--ALYPHLSV 92
Cdd:PRK10419 29 NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwrgepLAKLNRAQRKAFRRDIQMVFQDSisAVNPRKTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 ADNMSFGLK-LAGAKKAEINQRVNQVSEVLQLA-HLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRV 170
Cdd:PRK10419 109 REIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515497030 171 QMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRV---AQVGKPLELYHyPANR 228
Cdd:PRK10419 189 GVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvetQPVGDKLTFSS-PAGR 248
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-207 |
4.09e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 115.20 E-value: 4.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQS 83
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 YALYPHlSVADNMSFGLKLAGaKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:PRK10247 90 PTLFGD-TVYDNLIFPWQIRN-QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515497030 164 LDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEaMTLADKIVVL 207
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-182 |
4.48e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 115.13 E-value: 4.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSER---GI 77
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 78 GMVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLL 157
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180
....*....|....*....|....*..
gi 515497030 158 DEPLSNLD--AALRVQmRIeISRLHKR 182
Cdd:COG1137 161 DEPFAGVDpiAVADIQ-KI-IRHLKER 185
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-203 |
6.08e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 115.65 E-value: 6.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 8 SVYkaFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGDLLIGEKRMN--EVPPSE--RGIG 78
Cdd:PRK14243 17 NVY--YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYapDVDPVEvrRRIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYPHlSVADNMSFGLKLAGAKkAEINQRVNQVsevLQLAHLLDR-RPK------ALSGGQRQRVAIGRTLVAE 151
Cdd:PRK14243 95 MVFQKPNPFPK-SIYDNIAYGARINGYK-GDMDELVERS---LRQAALWDEvKDKlkqsglSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515497030 152 PDVFLLDEPLSNLD--AALRVQmriEISRLHKRlQRTMIYVTHDQVEAMTLADK 203
Cdd:PRK14243 170 PEVILMDEPCSALDpiSTLRIE---ELMHELKE-QYTIIIVTHNMQQAARVSDM 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-225 |
7.54e-30 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 117.11 E-value: 7.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSG-------DLL-IGEKRMNEVppsERGIGMVFQS--YALYPH 89
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGevawlgkDLLgMKDDEWRAV---RSDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 90 LSVADNMSFGLKLAGAK--KAEINQRV-NQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDA 166
Cdd:PRK15079 115 MTIGEIIAEPLRTYHPKlsRQEVKDRVkAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515497030 167 ALRVQmrieISRLHKRLQRTM----IYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK15079 195 SIQAQ----VVNLLQQLQREMglslIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-207 |
4.01e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.17 E-value: 4.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 12 AFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGekrmnevppSERGIGMVFQSYAL---YP 88
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA---------GGARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 89 hLSVADNMSFGL----KLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNL 164
Cdd:NF040873 72 -LTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515497030 165 DAALRVQMRIEISRLHKRlQRTMIYVTHDqVEAMTLADKIVVL 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 |
4.42e-29 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 112.24 E-value: 4.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLligEKRMNEVPPSERGIGMVfqsyalyPHLSVADNMSFG 99
Cdd:cd03220 39 KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV---TVRGRVSSLLGLGGGFN-------PELTGRENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 100 LKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRL 179
Cdd:cd03220 109 GRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 515497030 180 HKRlQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03220 189 LKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-224 |
6.15e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 112.48 E-value: 6.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIgekRMNEVPPSERGIGMVfqsya 85
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV---NGRVSALLELGAGFH----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 86 lyPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLD 165
Cdd:COG1134 101 --PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 166 AALR--VQMRIEisRLHKRlQRTMIYVTHD--QVEamTLADKIVVLDAGRVAQVGKP---LELYHY 224
Cdd:COG1134 179 AAFQkkCLARIR--ELRES-GRTVIFVSHSmgAVR--RLCDRAIWLEKGRLVMDGDPeevIAAYEA 239
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-212 |
8.40e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 111.51 E-value: 8.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLL-----IGEKRMNEVPPSERGIGMVFQSYALYPHLSVADNM 96
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWfsghdITRLKNREVPFLRRQIGMIFQDHHLLMDRTVYDNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 97 SFGLKLAGAKKAEINQRVnqvSEVLQLAHLLDRR---PKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVqmr 173
Cdd:PRK10908 101 AIPLIIAGASGDDIRRRV---SAALDKVGLLDKAknfPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE--- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515497030 174 iEISRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:PRK10908 175 -GILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-222 |
8.82e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 113.18 E-value: 8.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGE-------KRMNEVPPSERGIGMVFQ--SYALYPHlS 91
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVFQfpEYQLFQE-T 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 92 VADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAH-LLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRV 170
Cdd:PRK13645 108 IEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515497030 171 QMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13645 188 DFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-216 |
1.01e-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: 111.21 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 11 KAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLED---ITSGDLLIgekrmNEVPPS----ERGIGMVFQS 83
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILF-----NGQPRKpdqfQKCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 YALYPHLSVADNMSFGLKLAG---AKKAEINQRVNQVSEV-LQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDE 159
Cdd:cd03234 90 DILLPGLTVRETLTYTAILRLprkSSDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 160 PLSNLDAALRVQMRIEISRLHKRlQRTMIYVTHD-QVEAMTLADKIVVLDAGRVAQVG 216
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
8-228 |
1.04e-28 |
|
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: 112.21 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 8 SVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE-----RGIGMVFQ 82
Cdd:TIGR02769 16 GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 -SY-ALYPHLSVADNMSFGLK-LAGAKKAEINQRVNQVSEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLD 158
Cdd:TIGR02769 96 dSPsAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497030 159 EPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL--YHYPANR 228
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLlsFKHPAGR 247
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-212 |
1.47e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 113.26 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 15 EAVisKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIgekrMNEVPPSER-----GIGMVF-QSYALYP 88
Cdd:COG4586 36 EAV--DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV----LGYVPFKRRkefarRIGVVFgQRSQLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 89 HLSVADnmSFGL--KLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDA 166
Cdd:COG4586 110 DLPAID--SFRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515497030 167 ALRVQMRIEISRLHKRLQRTMIYVTHD--QVEAmtLADKIVVLDAGRV 212
Cdd:COG4586 188 VSKEAIREFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHGRI 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-225 |
3.42e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.83 E-value: 3.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 9 VYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE-------------- 74
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrll 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 75 -RGIGMVFQSYALYPHLSVADN-MSFGLKLAGAKKAEINQR-VNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAE 151
Cdd:PRK10619 91 rTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERaVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 152 PDVFLLDEPLSNLDAALRVqmriEISRLHKRLQ---RTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVG----EVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-222 |
3.46e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 111.37 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMN------EVPPSERGIGMVFQsyalYPHL---- 90
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPESqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 91 -SVADNMSFGLKLAGAKKAEINQRVNqvsEVLQLA----HLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLD 165
Cdd:PRK13649 101 eTVLKDVAFGPQNFGVSQEEAEALAR---EKLALVgiseSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 166 AalrvQMRIEISRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13649 178 P----KGRKELMTLFKKLHQsgmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-193 |
4.72e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 109.48 E-value: 4.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVIS--KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-LIGE--KRMNEVPPSE---RGIGMVFQSYA 85
Cdd:PRK10584 19 GEHELSilTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVsLVGQplHQMDEEARAKlraKHVGFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 86 LYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLD 165
Cdd:PRK10584 99 LIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180
....*....|....*....|....*...
gi 515497030 166 AALRVQMRIEISRLHKRLQRTMIYVTHD 193
Cdd:PRK10584 179 RQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
8.06e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 111.05 E-value: 8.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 2 ASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-LIGEKRMNEVPPSERGIGMV 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIsLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515497030 161 LSNLDAALRVQMrieISRLHKRLQR--TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK13537 166 TTGLDPQARHLM---WERLRSLLARgkTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-222 |
1.29e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.79 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGE---KRMNEVPPSERGIGMVFQSyalyPHLS----- 91
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PDNQivati 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 92 VADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQ 171
Cdd:PRK13633 103 VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515497030 172 MRIEISRLHKRLQRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13633 183 VVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-222 |
1.43e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.80 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMN--EVPPSERGIGMVFQSY-ALYPHLSVADNMSF 98
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNPdNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 99 GLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISR 178
Cdd:PRK13642 106 GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515497030 179 LHKRLQRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13642 186 IKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-212 |
2.12e-27 |
|
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: 106.15 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG--IGMVFQSYALYPHlS 91
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGYLPQDDELFSG-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 92 VADNMsfglklagakkaeinqrvnqvsevlqlahlldrrpkaLSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQ 171
Cdd:cd03246 92 IAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515497030 172 MRIEISRLHKRlQRTMIYVTHdQVEAMTLADKIVVLDAGRV 212
Cdd:cd03246 135 LNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-238 |
6.91e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 107.90 E-value: 6.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGE------KRMNEVPPSERGIGMVFQ--SYALYPHlSV 92
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstSKQKEIKPVRKKVGVVFQfpESQLFEE-TV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 ADNMSFGLKLAGAKKAEINQRVNQVSEVLQLA-HLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQ 171
Cdd:PRK13643 103 LKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 172 MRIEISRLHKRLQrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHyPANRFVAGFIGSPK 238
Cdd:PRK13643 183 MMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ-EVDFLKAHELGVPK 247
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-221 |
1.11e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 106.13 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSER---GI 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 78 GMVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQ-RVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFL 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 157 LDEPLSNLDAALRVQMRIEISRLHKRLQRTMIyVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLI-TDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-230 |
1.23e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.00 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIgeKRMNEVPPSE-----RGIGMVFQS-YALYPHLSVA 93
Cdd:PRK13644 19 ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDFSKlqgirKLVGIVFQNpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMR 173
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 174 IEISRLHKRlQRTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFV 230
Cdd:PRK13644 177 ERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-222 |
1.26e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 107.24 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEvppSERG-------IGMVFQS--YALYPhL 90
Cdd:PRK13636 23 KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY---SRKGlmklresVGMVFQDpdNQLFS-A 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 91 SVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRV 170
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515497030 171 QMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-222 |
1.33e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.17 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMN------EVPPSERGIGMVFQsyalYPHL--- 90
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkYIRPVRKRIGMVFQ----FPESqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 91 --SVADNMSFGLKLAGAKKAEINQRVNQVseVLQLA---HLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLD 165
Cdd:PRK13646 100 edTVEREIIFGPKNFKMNLDEVKNYAHRL--LMDLGfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515497030 166 AalrvQMRIEISRLHKRLQ----RTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13646 178 P----QSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
20-225 |
2.08e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.43 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI-GE----KRMNEVppsERGIGMVFQS---YALYPhlS 91
Cdd:PRK13652 21 NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEpitkENIREV---RKFVGLVFQNpddQIFSP--T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 92 VADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQ 171
Cdd:PRK13652 96 VEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515497030 172 MRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK13652 176 LIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-222 |
2.08e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 107.24 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 15 EAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGL----------EDITSGDLLIGEKRMNEVPPSE--------RG 76
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELITNPYSKKiknfkelrRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 77 IGMVFQ--SYALYPHlSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAH-LLDRRPKALSGGQRQRVAIGRTLVAEPD 153
Cdd:PRK13631 118 VSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 154 VFLLDEPLSNLDAALRVQMrIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-220 |
2.11e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.97 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSYALYPHLSVADNMS 97
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLAFPFTVEEVVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 98 FGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTL--VAEPDVF-----LLDEPLSNLDaaLRV 170
Cdd:COG4559 98 LGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVDGgprwlFLDEPTSALD--LAH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515497030 171 QMRI-EISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
Cdd:COG4559 176 QHAVlRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-221 |
2.15e-26 |
|
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: 105.26 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFG--EAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPS--ERGIGM 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 80 VFQSYALYpHLSVADNMSFGLKLAGAKKAEINQRVNQVSE-VLQLAH----LLDRRPKALSGGQRQRVAIGRTLVAEPDV 154
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALADPGMSMERVIEAAKLAGAHDfISELPEgydtIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 155 FLLDEPLSNLDAAlrvQMRIEISRLHKRLQ-RTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03252 160 LIFDEATSALDYE---SEHAIMRNMHDICAgRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-167 |
2.38e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 104.19 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERgIGMVFQSYALYPHLSVA 93
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 94 DNMSFGLKLAGAKKAEINQRVNQVsevlQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAA 167
Cdd:PRK13539 92 ENLEFWAAFLGGEELDIAAALEAV----GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-211 |
3.92e-26 |
|
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: 103.70 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLligekrmnEVPPSergIGMVFQSyalyPHL---SVADNM 96
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV--------SVPGS---IAYVSQE----PWIqngTIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 97 SFGLKLagakkaeINQRVNQVSEVLQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLD 165
Cdd:cd03250 87 LFGKPF-------DEERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515497030 166 AalRVQMRIeISRL---HKRLQRTMIYVTHdQVEAMTLADKIVVLDAGR 211
Cdd:cd03250 160 A--HVGRHI-FENCilgLLLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-212 |
4.90e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 109.43 E-value: 4.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAV-ISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGI------G 78
Cdd:PRK10535 10 IRRSYPSGEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrrehfG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLD 158
Cdd:PRK10535 90 FIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 159 EPLSNLDAALRVQ-MRIeisrLHKRLQR--TMIYVTHD-QVEAMtlADKIVVLDAGRV 212
Cdd:PRK10535 170 EPTGALDSHSGEEvMAI----LHQLRDRghTVIIVTHDpQVAAQ--AERVIEIRDGEI 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-218 |
5.16e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.20 E-value: 5.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE-RG-IGMVFQSyalyPH-----LSV 92
Cdd:PRK13647 22 KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSkVGLVFQD----PDdqvfsSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 ADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQM 172
Cdd:PRK13647 98 WDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515497030 173 RIEISRLHKRlQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:PRK13647 178 MEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-221 |
6.69e-26 |
|
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: 109.14 E-value: 6.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 18 ISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSYALYpHLSVADN 95
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 96 MSFGlkLAGAKKAEINqrvnqvsEVLQLAHLLD---RRPKA-----------LSGGQRQRVAIGRTLVAEPDVFLLDEPL 161
Cdd:COG5265 452 IAYG--RPDASEEEVE-------AAARAAQIHDfieSLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 162 SNLD--------AALRvqmriEISRlhkrlQRTMIYVTH------DqveamtlADKIVVLDAGRVAQVGKPLEL 221
Cdd:COG5265 523 SALDsrteraiqAALR-----EVAR-----GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAEL 579
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-212 |
1.17e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.84 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKrmnevppsergigmVFQS 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET--------------VKIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 Y------ALYPHLSVADNMSFGLKlaGAKKAEINQRvnqvsevlqLAHLL------DRRPKALSGGQRQRVAIGRTLVAE 151
Cdd:COG0488 382 YfdqhqeELDPDKTVLDELRDGAP--GGTEQEVRGY---------LGRFLfsgddaFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 152 PDVFLLDEPLSNLDaalrVQMRiEIsrLHKRLQR---TMIYVTHDQ--VEamTLADKIVVLDAGRV 212
Cdd:COG0488 451 PNVLLLDEPTNHLD----IETL-EA--LEEALDDfpgTVLLVSHDRyfLD--RVATRILEFEDGGV 507
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-218 |
1.22e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.70 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 7 RSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSY 84
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 85 ALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLV------AEPDVFLLD 158
Cdd:PRK13548 86 SLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 159 EPLSNLDaaLRVQmrIEISRLHKRLQR----TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:PRK13548 166 EPTSALD--LAHQ--HHVLRLARQLAHerglAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-286 |
2.00e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.08 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIG 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYAL--------------YPHLSVADNMSfglklaGAKKAEINQRVNQVsEVLQLAhllDRRPKALSGGQRQRVAI 144
Cdd:PRK09536 81 SVPQDTSLsfefdvrqvvemgrTPHRSRFDTWT------ETDRAAVERAMERT-GVAQFA---DRPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 145 GRTLVAEPDVFLLDEPLSNLDAALRVQMrIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhY 224
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRT-LELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV--L 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515497030 225 PANRFVAGF-----------IGSPKMNFLPVKVTAAEPRQVQVELPNRQLVWLPVEGAGVQPGANLSLGIRPE 286
Cdd:PRK09536 228 TADTLRAAFdartavgtdpaTGAPTVTPLPDPDRTEAAADTRVHVVGGGQPAARAVSRLVAAGASVSVGPVPE 300
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-221 |
2.16e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 102.84 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 18 ISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGDLLIGEKRMNEVPPSER---GIGMVFQSYALYPHLSV 92
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 ADnmsFgLKLAGAKKAEIN-------QRVNQVSEVLQLAHLLDRRP--KALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:COG0396 95 SN---F-LRTALNARRGEElsareflKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDETDSG 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 164 LDA-ALRVqMRIEISRLHKRlQRTMIYVTH-----DQVEamtlADKIVVLDAGRVAQVGKPlEL 221
Cdd:COG0396 171 LDIdALRI-VAEGVNKLRSP-DRGILIITHyqrilDYIK----PDFVHVLVDGRIVKSGGK-EL 227
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
16-221 |
2.33e-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: 107.52 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 16 AVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPS--ERGIGMVFQSYALYPHlSVA 93
Cdd:TIGR01846 470 PEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFG------------LKLAGAKKAEINQRVNQVSEVlqlahllDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPL 161
Cdd:TIGR01846 549 DNIALCnpgapfehvihaAKLAGAHDFISELPQGYNTEV-------GEKGANLSGGQRQRIAIARALVGNPRILIFDEAT 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 162 SNLD----AALRVQMRiEISRlhkrlQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR01846 622 SALDyeseALIMRNMR-EICR-----GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-227 |
2.89e-25 |
|
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: 102.06 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGDLLIGEKRMNEVPPSERGIGMVFQS--YALYPHLSVAD 94
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 95 NMSFGLKLAGAKKAEINQRVNQVSEVLQLAH---LLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQ 171
Cdd:TIGR02770 84 HAIETLRSLGKLSKQARALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 172 MRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAN 227
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-202 |
3.09e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 102.81 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 18 ISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIG----------EKRMNeVPPSERGIGMVFQSYALY 87
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrveffnqniyERRVN-LNRLRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 88 PhLSVADNMSFGLKLAGAK-KAEINQRVNQVSEVLQL----AHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:PRK14258 101 P-MSVYDNVAYGVKIVGWRpKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515497030 163 NLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLAD 202
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-225 |
4.58e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.89 E-value: 4.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE-----RGIGMVFQS-YA-LYPHLSVA 93
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNPRKKVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFGLklagakkaEIN------QRVNQVSEVLQLAHL----LDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:PRK11308 113 QILEEPL--------LINtslsaaERREKALAMMAKVGLrpehYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 164 LDAALRVQmrieISRLHKRLQRTM----IYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK11308 185 LDVSVQAQ----VLNLMMDLQQELglsyVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-234 |
5.14e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.05 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 9 VYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDI------TSGDLLIGEKRMNEVPPSE--RGIGMV 80
Cdd:PRK14246 16 LYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKDIFQIDAIKlrKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQSYALYPHLSVADNMSFGLKLAGAK-KAEINQRVNQ----VSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVF 155
Cdd:PRK14246 96 FQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEEclrkVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 156 LLDEPLSNLDAALRVQMRIEISRLHKRLqrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-223 |
5.27e-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: 100.68 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGDLLIGEKRMNEVPPSER---GIGMVFQSYALYP 88
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 89 HLSVADNMSFglklagakkaeinqrVNqvsevlqlahlldrrpKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDA-A 167
Cdd:cd03217 91 GVKNADFLRY---------------VN----------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIdA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515497030 168 LRVQMRIeISRLHKRlQRTMIYVTH-----DQVEamtlADKIVVLDAGRVAQVGkPLELYH 223
Cdd:cd03217 140 LRLVAEV-INKLREE-GKSVLIITHyqrllDYIK----PDRVHVLYDGRIVKSG-DKELAL 193
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-216 |
7.17e-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: 105.60 E-value: 7.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG--IGMVFQSYALYPHlS 91
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 92 VADNMS-FG----------LKLAGAKKAeinqrvnqvseVLQLAH----LLDRRPKALSGGQRQRVAIGRTLVAEPDVFL 156
Cdd:COG4618 422 IAENIArFGdadpekvvaaAKLAGVHEM-----------ILRLPDgydtRIGEGGARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 157 LDEPLSNLDAALRVQMRIEISRLHKRlQRTMIYVTHDQvEAMTLADKIVVLDAGRVAQVG 216
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFG 548
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-192 |
9.04e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 105.66 E-value: 9.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 17 VISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLligekrmnEVPPSERgigMVF---QSY--------A 85
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR---VLFlpqRPYlplgtlreA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 86 L-YPHLsvADNMSfglklagakkaeiNQRVNQVSEVLQLAHLLDR------RPKALSGGQRQRVAIGRTLVAEPDVFLLD 158
Cdd:COG4178 446 LlYPAT--AEAFS-------------DAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190
....*....|....*....|....*....|....*
gi 515497030 159 EPLSNLDAALRVQMrieISRLHKRLQR-TMIYVTH 192
Cdd:COG4178 511 EATSALDEENEAAL---YQLLREELPGtTVISVGH 542
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1-221 |
1.04e-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: 105.81 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRsvYKAFGEAVIsKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSG----------DLLIGEKRmnev 70
Cdd:TIGR03797 454 VDRVTFR--YRPDGPLIL-DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGsvfydgqdlaGLDVQAVR---- 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 71 ppseRGIGMVFQSYALYPHlSVADNMSFGLKLAgakkaeinqrVNQVSEVLQLAHL---LDRRP-----------KALSG 136
Cdd:TIGR03797 527 ----RQLGVVLQNGRLMSG-SIFENIAGGAPLT----------LDEAWEAARMAGLaedIRAMPmgmhtviseggGTLSG 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 137 GQRQRVAIGRTLVAEPDVFLLDEPLSNLDAalRVQmRIEISRLhKRLQRTMIYVTHDQVEAMTlADKIVVLDAGRVAQVG 216
Cdd:TIGR03797 592 GQRQRLLIARALVRKPRILLFDEATSALDN--RTQ-AIVSESL-ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
....*
gi 515497030 217 KPLEL 221
Cdd:TIGR03797 667 TYDEL 671
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-217 |
1.24e-24 |
|
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: 105.12 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG--IGMVFQSYALYPHlS 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 92 VADNMSFGLKLAGAKKAEINQRVNQVSEVLQlahlldRRPK-----------ALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:TIGR01842 408 VAENIARFGENADPEKIIEAAKLAGVHELIL------RLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 161 LSNLDAALRVQMRIEISRLHKRlQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGE 536
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-218 |
1.30e-24 |
|
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: 100.56 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 25 TIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLligEKRMNEVPPSERGIGMVFQSyalyphlSVADNMSFGLKLAG 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKPQYIKADYEG-------TVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 105 akkaEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDaalrVQMRIEISRLHKRL- 183
Cdd:cd03237 91 ----THPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD----VEQRLMASKVIRRFa 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 515497030 184 ---QRTMIYVTHDQVEAMTLADKIVVLDagrvaqvGKP 218
Cdd:cd03237 163 ennEKTAFVVEHDIIMIDYLADRLIVFE-------GEP 193
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-221 |
1.50e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 101.22 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 12 AFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSYALYPH 89
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 90 LSVADNMSFG----LKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLD 165
Cdd:PRK10253 96 ITVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 166 AALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-221 |
1.89e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.22 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-LIGEKRMNEVPPSERGIGM 79
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 80 VFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDE 159
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 160 PLSNLDAALRvqmRIEISRLHKRLQR--TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK13536 199 PTTGLDPHAR---HLIWERLRSLLARgkTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-222 |
2.64e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.67 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE------RGIGMVFQsyalYPHL---- 90
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklrKKVSLVFQ----FPEAqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 91 -SVADNMSFGLKLAGA--KKAEiNQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAA 167
Cdd:PRK13641 101 nTVLKDVEFGPKNFGFseDEAK-EKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 168 LRVQMrIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13641 180 GRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
4-222 |
3.08e-24 |
|
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: 104.26 E-value: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSV---YKAFGEAVISkDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIG 78
Cdd:TIGR03796 478 VELRNItfgYSPLEPPLIE-NFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVlaNSVA 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYPHlSVADNMS--------FGLKLAgAKKAEINQRVnqVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVA 150
Cdd:TIGR03796 557 MVDQDIFLFEG-TVRDNLTlwdptipdADLVRA-CKDAAIHDVI--TSRPGGYDAELAEGGANLSGGQRQRLEIARALVR 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 151 EPDVFLLDEPLSNLDAAlrVQMRIEisrlhKRLQR---TMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:TIGR03796 633 NPSILILDEATSALDPE--TEKIID-----DNLRRrgcTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELW 699
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-222 |
4.07e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.03 E-value: 4.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 18 ISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIgekrmNEVPPSE-------RGIGMVFQSYALYPHl 90
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-----DGVPLVQydhhylhRQVALVGQEPVLFSG- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 91 SVADNMSFGLK-------LAGAKKAEINqrvNQVSEVLQLAHL-LDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:TIGR00958 570 SVRENIAYGLTdtpdeeiMAAAKAANAH---DFIMEFPNGYDTeVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 163 NLDAalRVQMRIEISRlhKRLQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:TIGR00958 647 ALDA--ECEQLLQESR--SRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLM 701
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-221 |
4.55e-24 |
|
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: 98.77 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 24 LTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNevpPSERGIGMVFQSYAL---YPhLSVADN-MSFG 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPG---KGWRHIGYVPQRHEFawdFP-ISVAHTvMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 100 LKLAG----AKKAEInQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMrIE 175
Cdd:TIGR03771 77 TGHIGwlrrPCVADF-AAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL-TE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515497030 176 ISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDaGRVAQVGKPLEL 221
Cdd:TIGR03771 155 LFIELAGAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQL 199
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-233 |
6.73e-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: 102.57 E-value: 6.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDI--TSGDLLIGEKRMNEV----PPSERG- 76
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHVALCEKCgyveRPSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 77 ------------------------------IGMVFQ-SYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAH 125
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdklrrrirkrIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 126 LLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIV 205
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260
....*....|....*....|....*...
gi 515497030 206 VLDAGRVAQVGKPLELyhypANRFVAGF 233
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV----VAVFMEGV 264
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-222 |
7.04e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.38 E-value: 7.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPS----ERGIGMVFQS-----YAlyPhl 90
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevRKTVGIVFQNpddqlFA--P-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 91 SVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAalrv 170
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP---- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 171 QMRIEISRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13639 171 MGASQIMKLLYDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-212 |
7.58e-24 |
|
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: 102.46 E-value: 7.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 15 EAVisKDVNLTIEDGEFVVFVGPSGCGKS----TLLRMIAGLEDITSG-------DLL-IGEKRMNEVppseRG--IGMV 80
Cdd:COG4172 24 EAV--KGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGsilfdgqDLLgLSERELRRI----RGnrIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQ--SYALYPHLSVADNMSFGLKL-AGAKKAEINQRVnqvSEVLQLAHL------LDRRPKALSGGQRQRVAIGRTLVAE 151
Cdd:COG4172 98 FQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARA---LELLERVGIpdperrLDAYPHQLSGGQRQRVMIAMALANE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 152 PDVFLLDEPLSNLDAALRVQmrieISRLHKRLQRT----MIYVTHDQ--VEAMtlADKIVVLDAGRV 212
Cdd:COG4172 175 PDLLIADEPTTALDVTVQAQ----ILDLLKDLQRElgmaLLLITHDLgvVRRF--ADRVAVMRQGEI 235
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-237 |
7.92e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 99.07 E-value: 7.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI-GEkrmnEVPPSERG------ 76
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGE----NIPAMSRSrlytvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 77 --IGMVFQSYALYPHLSVADNMSFGLKLAGAKKAEI-NQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPD 153
Cdd:PRK11831 84 krMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLlHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 154 VFLLDEPLSNLDA-ALRVQMRIeISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANR---F 229
Cdd:PRK11831 164 LIMFDEPFVGQDPiTMGVLVKL-ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRvrqF 242
|
....*...
gi 515497030 230 VAGFIGSP 237
Cdd:PRK11831 243 LDGIADGP 250
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-221 |
9.86e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 102.90 E-value: 9.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 13 FGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD-LLIGEkrmnEVPPSE----RGIGMVFQSYALY 87
Cdd:NF033858 276 FGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEaWLFGQ----PVDAGDiatrRRVGYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 88 PHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQR----VAIgrtlVAEPDVFLLDEPLSN 163
Cdd:NF033858 352 GELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRlslaVAV----IHKPELLILDEPTSG 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497030 164 LDAALR---VQMRIEISrlhkRLQRTMIYV-THDQVEAMtLADKIVVLDAGRVAQVGKPLEL 221
Cdd:NF033858 428 VDPVARdmfWRLLIELS----REDGVTIFIsTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-233 |
1.39e-23 |
|
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: 102.78 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAVISKdVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRM-NEVPPSERGIGMVFQSY 84
Cdd:TIGR01257 934 LVKIFEPSGRPAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 85 ALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNL 164
Cdd:TIGR01257 1013 ILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 165 DAALRvqMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhypANRFVAGF 233
Cdd:TIGR01257 1093 DPYSR--RSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-167 |
1.70e-23 |
|
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: 96.27 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPS-ERGIGMVFQSYALYPHLSV 92
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 93 ADNMSFGLKLAGAKKAEINQRVNQVSevlqLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAA 167
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIEDALAAVG----LTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-238 |
1.94e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 98.24 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSvykAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSG-----DLLIGEKRM---NEVPP 72
Cdd:PRK14271 22 MAAVNLTL---GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 73 SERGIGMVFQSYALYPhLSVADNMSFGL---KLAGAK--KAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRT 147
Cdd:PRK14271 99 FRRRVGMLFQRPNPFP-MSIMDNVLAGVrahKLVPRKefRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 148 LVAEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLqrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAN 227
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
250
....*....|....*
gi 515497030 228 ----RFVAGFIGSPK 238
Cdd:PRK14271 256 aetaRYVAGLSGDVK 270
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-221 |
3.34e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.07 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITsGDLLIGEKRMNEVPPSE--RGIGMVFQSYALyPHLSVADNMSFG 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 100 LKLAGakKAEINQRVNQ--VSE-VLQLAHLLDRRPK----ALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDA------ 166
Cdd:PRK11174 447 NPDAS--DEQLQQALENawVSEfLPLLPQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAhseqlv 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 167 --ALRVQMRieisrlhkrlQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK11174 525 mqALNAASR----------RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-229 |
3.71e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.55 E-value: 3.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKST----LLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQ--SYALY 87
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQdpNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 88 PHLSVADNMSFGLKL--AGAKKAEINQRVNQVSEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNL 164
Cdd:PRK15134 377 PRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 165 DAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRF 229
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
15-237 |
3.74e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 97.17 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 15 EAVisKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERG--IGMVFQ--SYALYPHL 90
Cdd:PRK15112 27 EAV--KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrIRMIFQdpSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 91 SVADNMSFGLKL-----AGAKKAEINQRVNQVSEVLQLAHLLdrrPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLD 165
Cdd:PRK15112 105 RISQILDFPLRLntdlePEQREKQIIETLRQVGLLPDHASYY---PHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 166 AALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP----ANRFVAGFIGSP 237
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPlhelTKRLIAGHFGEA 257
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-193 |
4.20e-23 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 100.51 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSyalyPHL- 90
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQD----AHLf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 91 --SVADNMSFGLKlaGAKKAEINQRVNQVsevlQLAHLLDRRP-----------KALSGGQRQRVAIGRTLVAEPDVFLL 157
Cdd:TIGR02868 422 dtTVRENLRLARP--DATDEELWAALERV----GLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*..
gi 515497030 158 DEPLSNLDAALRVQMrieISRLHKRLQ-RTMIYVTHD 193
Cdd:TIGR02868 496 DEPTEHLDAETADEL---LEDLLAALSgRTVVLITHH 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-212 |
5.14e-23 |
|
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: 96.00 E-value: 5.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPS--ERGIGMVFQSYALYPHlSVADNMS 97
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 98 FGLKLAGAKK-AEINQRVNQVSEVLQLAHLLD----RRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQM 172
Cdd:cd03248 110 YGLQSCSFECvKEAAQKAHAHSFISELASGYDtevgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515497030 173 RIEISRLHKRlqRTMIYVTHdQVEAMTLADKIVVLDAGRV 212
Cdd:cd03248 190 QQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-220 |
5.23e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.46 E-value: 5.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSG-----------------------DLLIGE---KRMNEVPPS 73
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekekvleKLVIQKtrfKKIKKIKEI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 74 ERGIGMVFQ--SYALYPHlSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVA 150
Cdd:PRK13651 104 RRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 151 EPDVFLLDEPLSNLDAALRVQMRIEISRLHKRlQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-211 |
9.09e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 95.19 E-value: 9.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAF-----GEAVIS--KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI----GEKRMNEVPPSE 74
Cdd:COG4778 7 VENLSKTFtlhlqGGKRLPvlDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 75 ------RGIGMVFQSYALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVsevlqLAHL-LDRR-----PKALSGGQRQRV 142
Cdd:COG4778 87 ilalrrRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARAREL-----LARLnLPERlwdlpPATFSGGEQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497030 143 AIGRTLVAEPDVFLLDEPLSNLDAALRvqmRIEISRLHKRLQR--TMIYVTHDQvEAM-TLADKIVVLDAGR 211
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANR---AVVVELIEEAKARgtAIIGIFHDE-EVReAVADRVVDVTPFS 229
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-221 |
1.25e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 99.43 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 13 FGEAVISkDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSYALYPHl 90
Cdd:TIGR01193 485 YGSNILS-DISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFINYLPQEPYIFSG- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 91 SVADNMSFGLK--------LAGAKKAEINQRVNQVSEVLQLAhlLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:TIGR01193 563 SILENLLLGAKenvsqdeiWAACEIAEIKDDIENMPLGYQTE--LSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 163 NLDAALrvQMRIeISRLHKRLQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR01193 641 NLDTIT--EKKI-VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-217 |
1.36e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.97 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPS---ERGIGMVFQ 82
Cdd:PRK15439 14 ARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkahQLGIYLVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 SYALYPHLSVADNMSFGLklagAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:PRK15439 94 EPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515497030 163 NLDAAlrvqmriEISRLHKRLQRT------MIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:PRK15439 170 SLTPA-------ETERLFSRIRELlaqgvgIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-221 |
2.67e-22 |
|
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: 98.25 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRsvYKAFGEAVISkDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLigekrMNEVPPSE-------RG 76
Cdd:TIGR02203 336 VTFR--YPGRDRPALD-SISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIL-----LDGHDLADytlaslrRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 77 IGMVFQSYALYPHlSVADNMSFGlKLAGAKKAEInqrvnqvSEVLQLAHLL---DRRPKA-----------LSGGQRQRV 142
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIAYG-RTEQADRAEI-------ERALAAAYAQdfvDKLPLGldtpigengvlLSGGQRQRL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 143 AIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRLHKrlQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-212 |
7.04e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.54 E-value: 7.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGL--EDITSGDL--LIG-----EKRM-NEVPPSERGIGMVFQSYALYPHLS 91
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSHieLLGrtvqrEGRLaRDIRKSRANTGYIFQQFNLVNRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 92 VADNMSFGlKLAGAK---------KAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:PRK09984 103 VLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515497030 163 NLDAAlrvQMRIEISRLHKRLQR--TMIYVTHDQVE-AMTLADKIVVLDAGRV 212
Cdd:PRK09984 182 SLDPE---SARIVMDTLRDINQNdgITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-211 |
2.13e-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: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKrmnevppsergigmvfQS 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------------VK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 YALYPHlsvadnmsfglklagakkaeinqrvnqvsevlqlahlldrrpkaLSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:cd03221 65 IGYFEQ--------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515497030 164 LDaalrVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:cd03221 101 LD----LESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-222 |
4.87e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.61 E-value: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 13 FGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEvppSERG-------IGMVFQSya 85
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY---SKRGllalrqqVATVFQD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 86 lyP-----HLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:PRK13638 86 --PeqqifYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497030 161 LSNLDAALRVQMRIEISRLHKRLQRTMIyVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-220 |
6.11e-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: 6.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGDLLIGEKRMNEVPPSE----RG---------IGM-VFQSYALY 87
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElarhRAylsqqqsppFAMpVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 88 PHlsvadnmsfglklAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLV-------AEPDVFLLDEP 160
Cdd:COG4138 94 QP-------------AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 161 LSNLDAALRVQMRIEISRLHkRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-221 |
8.24e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.74 E-value: 8.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSYALYPHlSVADNms 97
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAISVVSQRVHLFSA-TLRDN-- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 98 fgLKLAGAKKAEinqrvNQVSEVLQ---LAHLLDR------------RPkaLSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:PRK11160 434 --LLLAAPNASD-----EALIEVLQqvgLEKLLEDdkglnawlgeggRQ--LSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 163 NLDAALRVQMrieISRLHKRLQ-RTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK11160 505 GLDAETERQI---LELLAEHAQnKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-212 |
8.77e-21 |
|
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: 88.64 E-value: 8.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSER---GIGMV---FQSYALYPHLSVA 93
Cdd:cd03215 17 RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYVpedRKREGLVLDLSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSfglklagakkaeinqrvnqvsevlqLAHLLdrrpkalSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLD-AAlrvqm 172
Cdd:cd03215 97 ENIA-------------------------LSSLL-------SGGNQQKVVLARWLARDPRVLILDEPTRGVDvGA----- 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515497030 173 rieISRLHKRLQR------TMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:cd03215 140 ---KAEIYRLIREladagkAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-212 |
1.42e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 93.09 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAG---LED---ITSGDLLIGekRMNEVPPSE 74
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDDgriIYEQDLIVA--RLQQDPPRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 75 RGiGMVF---------QSYAL--YPHLS--VADNMSFGL--KLAGAK-KAEIN---QRVNQVSEVLQLAHL-LDRRPKAL 134
Cdd:PRK11147 79 VE-GTVYdfvaegieeQAEYLkrYHDIShlVETDPSEKNlnELAKLQeQLDHHnlwQLENRINEVLAQLGLdPDAALSSL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 135 SGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAAlrvqmRIE-ISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-----TIEwLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-212 |
1.76e-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: 87.75 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 15 EAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIgekrmNEVPPSErgigmvfqsyalyphlsVAD 94
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL-----DGVPVSD-----------------LEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 95 NMSfglklagakkaeinqrvNQVSEVLQLAHLLD--------RRpkaLSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDA 166
Cdd:cd03247 72 ALS-----------------SLISVLNQRPYLFDttlrnnlgRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515497030 167 ALRVQMrieISRLHKRLQ-RTMIYVTHdQVEAMTLADKIVVLDAGRV 212
Cdd:cd03247 132 ITERQL---LSLIFEVLKdKTLIWITH-HLTGIEHMDKILFLENGKI 174
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-212 |
1.99e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 89.17 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE---RGI 77
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 78 GMVFQSYALYPHLSVADNMSFGLKLAgaKKAEINQRVNQVSEVL-QLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFL 156
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 157 LDEPLSNLDAALRVQMRIEISRLHKRlQRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-208 |
4.06e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 88.25 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLligekrmnEVPPSERgIGMVFQS 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR-IGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 YALYPHLSVADNMSFGLKlAGAKKAEINQRVNQVsevlQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:PRK09544 76 LYLDTTLPLTVNRFLRLR-PGTKKEDILPALKRV----QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515497030 164 LDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLD 208
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-221 |
7.32e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.88 E-value: 7.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 18 ISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIA-----GLEdiTSGDLLIGEKRMNEVPPSERGiGMVFQSYALYPHLSV 92
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkGVK--GSGSVLLNGMPIDAKEMRAIS-AYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 ADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLD---------RRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKcantrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497030 164 LDAAlrvqMRIEISRLHKRLQ---RTMIYVTHD-QVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR00955 197 LDSF----MAYSVVQVLKGLAqkgKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-215 |
8.74e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 86.94 E-value: 8.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 3 SVTLRSVYKAFG------EAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGdlligeKRMNEVPPSErg 76
Cdd:COG2401 24 SERVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV------AGCVDVPDNQ-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 77 igmvfqsyaLYPHLSVADNMSfglklagakkaeINQRVNQVSEVLQLAHLLD-----RRPKALSGGQRQRVAIGRTLVAE 151
Cdd:COG2401 96 ---------FGREASLIDAIG------------RKGDFKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAER 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 152 PDVFLLDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVT-HDQVEAMTLADKIVVLDAGRVAQV 215
Cdd:COG2401 155 PKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVAThHYDVIDDLQPDLLIFVGYGGVPEE 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-210 |
1.09e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.23 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPP---SERGIGMV 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQSYALYPHLSVADNMSFGLKLagAKK---------AEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAE 151
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHL--TKKvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 152 PDVFLLDEPLSNLDAALRVQMRIEISRLHKRlQRTMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-221 |
1.26e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 90.25 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 25 TIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKrmnevppsergIgmvfqSYAlyP-HLSVADNMSFGLKLA 103
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-----------I-----SYK--PqYIKPDYDGTVEDLLR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 104 GAK--------KAEINQRvnqvsevLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDaalrVQMRIE 175
Cdd:PRK13409 423 SITddlgssyyKSEIIKP-------LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VEQRLA 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515497030 176 ISRLHKRLQR----TMIYVTHDQVEAMTLADKIVVLD--AGRVAQVGKPLEL 221
Cdd:PRK13409 492 VAKAIRRIAEereaTALVVDHDIYMIDYISDRLMVFEgePGKHGHASGPMDM 543
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-216 |
2.20e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 89.39 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE-RG-IGMVFQSYALYPHlSVADNMS 97
Cdd:PRK10789 332 ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSrLAVVSQTPFLFSD-TVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 98 FGlkLAGAKKAEINQ--RVNQVSE-VLQLAHLLD----RRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAalrv 170
Cdd:PRK10789 411 LG--RPDATQQEIEHvaRLASVHDdILRLPQGYDtevgERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG---- 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515497030 171 qmRIEISRLHK----RLQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:PRK10789 485 --RTEHQILHNlrqwGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRG 531
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-218 |
5.96e-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: 84.47 E-value: 5.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKST----LLRMIagleDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSyalyPHL--- 90
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQD----PVLfsg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 91 SVADNM-SFGL----KLAGA-KKAEINQRVNQVSEvlQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNL 164
Cdd:cd03244 93 TIRSNLdPFGEysdeELWQAlERVGLKEFVESLPG--GLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515497030 165 DAALRVQMRIEISrlHKRLQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:cd03244 171 DPETDALIQKTIR--EAFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-215 |
6.32e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 6.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE---RGIGMVFQSY---ALYPHLSVA 93
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdnGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFG--LKLAGAKKA-------EINQRVNQVSEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:PRK09700 360 QNMAISrsLKDGGYKGAmglfhevDEQRTAENQRELLALkCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 164 LDaalrVQMRIEISRLHKRLQ---RTMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
Cdd:PRK09700 440 ID----VGAKAEIYKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-216 |
7.03e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.98 E-value: 7.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 7 RSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEK--------RMNEvppSERGI- 77
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyALSE---AERRRl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 78 -----GMVFQSYA--LYPHLSVADNMSFGLKLAGAKK-AEINQRVNQ-VSEVLQLAHLLDRRPKALSGGQRQRVAIGRTL 148
Cdd:PRK11701 87 lrtewGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHyGDIRATAGDwLERVEIDAARIDDLPTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 149 VAEPDVFLLDEPLSNLDAAlrVQMRI--EISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVS--VQARLldLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-167 |
7.34e-19 |
|
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: 83.70 E-value: 7.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKdVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPS-ERGIGMVFQSYALYPHLSV 92
Cdd:cd03231 12 GRALFSG-LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 93 ADNMSFGLKLAGakKAEINQRVNQVSevlqLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAA 167
Cdd:cd03231 91 LENLRFWHADHS--DEQVEEALARVG----LNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-225 |
1.49e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.22 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE-----RGIGMVFQS-YA-LYPHLSVADNMSFGLK 101
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 102 LAGAKKAEINQRvnQVSEVLQLAHLLD----RRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQmrieIS 177
Cdd:PRK10261 430 VHGLLPGKAAAA--RVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ----II 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515497030 178 RLHKRLQRTM----IYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK10261 504 NLLLDLQRDFgiayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-213 |
1.55e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.61 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE---RGIGMV---FQSYALYPHLSVA 93
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVpedRKGEGLVLDLSIR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFGL--KLAGA---KKAEINQRVNQVSEVLQL-AHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAA 167
Cdd:COG1129 349 ENITLASldRLSRGgllDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVG 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515497030 168 LRVqmriEISRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGRVA 213
Cdd:COG1129 429 AKA----EIYRLIRELAAegkAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-216 |
1.75e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 87.53 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 17 VISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLigekrmnevppSERGIGMVFQSyALYPHLSVADNM 96
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 97 SFGLKLAGAKKAEInQRVNQV-SEVLQLAHLLD----RRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAAL--R 169
Cdd:PTZ00243 742 LFFDEEDAARLADA-VRVSQLeADLAQLGGGLEteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeR 820
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515497030 170 VQMRIEISRLHKrlqRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:PTZ00243 821 VVEECFLGALAG---KTRVLATH-QVHVVPRADYVVALGDGRVEFSG 863
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-221 |
3.11e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.17 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPS--ERGIGMVFQSYALYPHlSVADNMSF 98
Cdd:PRK13657 353 DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVVFQDAGLFNR-SIEDNIRV 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 99 GLklAGAKKAEinqrVNQVSEVLQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAA 167
Cdd:PRK13657 432 GR--PDATDEE----MRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515497030 168 LRVQMRIEISRLHKrlQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK13657 506 TEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDEL 556
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-216 |
6.46e-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: 82.19 E-value: 6.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 11 KAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI-----GEKRMNEVPPSERGI------GM 79
Cdd:TIGR02323 11 KSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERRRlmrtewGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 80 VFQSYA--LYPHLSVADNMSFGLKLAGAKK-AEINQR-VNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVF 155
Cdd:TIGR02323 91 VHQNPRdgLRMRVSAGANIGERLMAIGARHyGNIRATaQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515497030 156 LLDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:TIGR02323 171 FMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-212 |
7.98e-18 |
|
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: 80.77 E-value: 7.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 11 KAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDIT---SGDLL---IGEKRMNEVPPSErgIGMVFQSY 84
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHyngIPYKEFAEKYPGE--IIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 85 ALYPHLSVADNMSFGLKLAGakkaeiNQRVnqvsevlqlahlldrrpKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNL 164
Cdd:cd03233 93 VHFPTLTVRETLDFALRCKG------NEFV-----------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515497030 165 DAALRVQMrIEISRLHKRLQRTMIYVTHDQ--VEAMTLADKIVVLDAGRV 212
Cdd:cd03233 150 DSSTALEI-LKCIRTMADVLKTTTFVSLYQasDEIYDLFDKVLVLYEGRQ 198
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
14-224 |
8.30e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 82.00 E-value: 8.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLE--DITSGDLLIGEKRMNEVPPSER---GIGMVFQsyalYP 88
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERahlGIFLAFQ----YP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 89 -HLSVADNMSFgLKLA-GAKKAEINQR-------VNQVSEVLQL----AHLLDRR-PKALSGGQRQRVAIGRTLVAEPDV 154
Cdd:CHL00131 94 iEIPGVSNADF-LRLAyNSKRKFQGLPeldplefLEIINEKLKLvgmdPSFLSRNvNEGFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 155 FLLDEPLSNLDA-ALRVqMRIEISRLhKRLQRTMIYVTHDQveamTLADKIV-----VLDAGRVAQVG-----KPLELYH 223
Cdd:CHL00131 173 AILDETDSGLDIdALKI-IAEGINKL-MTSENSIILITHYQ----RLLDYIKpdyvhVMQNGKIIKTGdaelaKELEKKG 246
|
.
gi 515497030 224 Y 224
Cdd:CHL00131 247 Y 247
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-240 |
1.09e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 82.85 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGL---EDITSGD--------LLIGEKRMNEVPPSErgIGMVFQS--YALY 87
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSatfngreiLNLPEKELNKLRAEQ--ISMIFQDpmTSLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 88 PHLSVADNMSFGLKL-AGAKKAEINQRVNQVSEVLQLAHLLDRR---PKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:PRK09473 112 PYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 164 LDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS-PKMN 240
Cdd:PRK09473 192 LDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAvPRLD 269
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-211 |
1.44e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.81 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRM---NEVPPSERGIGMVFQSYALYPHLSVADNMS 97
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGVAIIYQELHLVPEMTVAENLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 98 FGL---KLAGAKKAEINQRVnqvseVLQLAHL-LDRRP----KALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAAlr 169
Cdd:PRK11288 102 LGQlphKGGIVNRRLLNYEA-----REQLEHLgVDIDPdtplKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR-- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515497030 170 vqmriEISRLHK---RLQ---RTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:PRK11288 175 -----EIEQLFRvirELRaegRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-220 |
1.83e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.75 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGDLLIGEKRMNEVPPSE----RG---------IGM-VFQSYALY 87
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMpVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 88 PHlsvadnmsfglklAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRV-------AIGRTLVAEPDVFLLDEP 160
Cdd:PRK03695 94 QP-------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 161 LSNLDAALRVQMRIEISRLhKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-208 |
2.98e-17 |
|
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: 82.91 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 25 TIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEK---RMNEVPPSergIGMVFQSYalyphLSVADNMSFGLK 101
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisyKPQYISPD---YDGTVEEF-----LRSANTDDFGSS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 102 LAgakKAEINQRvnqvsevLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDaalrVQMRIEISRLHK 181
Cdd:COG1245 434 YY---KTEIIKP-------LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VEQRLAVAKAIR 499
|
170 180 190
....*....|....*....|....*....|..
gi 515497030 182 RL----QRTMIYVTHD-QVEAMtLADKIVVLD 208
Cdd:COG1245 500 RFaenrGKTAMVVDHDiYLIDY-ISDRLMVFE 530
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-227 |
4.64e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.60 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKS----TLLRMI--AGLEdITSGDLLIGEKRMNEVPPSE---------RG--IGMVFQ 82
Cdd:PRK10261 33 RNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGL-VQCDKMLLRRRSRQVIELSEqsaaqmrhvRGadMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 S--YALYPHLSVADNMSFGLKL-AGAKK----AEINQRVNQVsEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVF 155
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLhQGASReeamVEAKRMLDQV-RIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497030 156 LLDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAN 227
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-273 |
4.75e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.45 E-value: 4.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKS----TLLRMIAGLEDI-TSGDLLI-GEKRMNEVPPSERG-----IGMVFQS------ 83
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFhGESLLHASEQTLRGvrgnkIAMIFQEpmvsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 ------YALYPHLSVADNMSfglklAGAKKAEINQRVNQVSeVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLL 157
Cdd:PRK15134 107 plhtleKQLYEVLSLHRGMR-----REAARGEILNCLDRVG-IRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 158 DEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAgfigsp 237
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ------ 254
|
250 260 270
....*....|....*....|....*....|....*.
gi 515497030 238 kmnflpvKVTAAEPRQVQVELPNRQLVWLPVEGAGV 273
Cdd:PRK15134 255 -------KLLNSEPSGDPVPLPEPASPLLDVEQLQV 283
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-167 |
6.04e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.31 E-value: 6.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSergigmvFQSYALY------ 87
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDLLYlghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 88 --PHLSVADNMSFGLKLAG-AKKAEINQRVNQVSevlqLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNL 164
Cdd:PRK13538 85 ikTELTALENLRFYQRLHGpGDDEALWEALAQVG----LAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
...
gi 515497030 165 DAA 167
Cdd:PRK13538 161 DKQ 163
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-211 |
1.42e-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: 80.75 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 5 TLRSVYKAF-GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGdlligekrmnEVPPSE-RGIGMVFQ 82
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----------EARPQPgIKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 SYALYPHLSVADNMSFGLklagAKKAEINQRVNQVSEVL-----------------------QLAHLLDRR--------- 130
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEGV----AEIKDALDRFNEISAKYaepdadfdklaaeqaelqeiidaADAWDLDSQleiamdalr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 131 -P------KALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAAlrvqmriEISRLHKRLQR---TMIYVTHDQVEAMTL 200
Cdd:TIGR03719 152 cPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-------SVAWLERHLQEypgTVVAVTHDRYFLDNV 224
|
250
....*....|.
gi 515497030 201 ADKIVVLDAGR 211
Cdd:TIGR03719 225 AGWILELDRGR 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-225 |
1.81e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.11 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPP---SERGIGMVFQSYALYPHLSVADNM-- 96
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqiARMGVVRTFQHVRLFREMTVIENLlv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 97 -----------SFGLKLAGAKKAEIN--QRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:PRK11300 104 aqhqqlktglfSGLLKTPAFRRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAG 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497030 164 LDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK11300 184 LNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-211 |
2.06e-16 |
|
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: 80.25 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGL--EDITSGDLLIGEKRM--NEVPPSER-GIG 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkaSNIRDTERaGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYPHLSVADNMSFG--LKLAGAKK--AEINQRVNQVSEVLQLAHLLDRRPKA-LSGGQRQRVAIGRTLVAEPD 153
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGneITLPGGRMayNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 154 VFLLDEPLSNLDAAlRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:TIGR02633 162 LLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-211 |
3.27e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.59 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 5 TLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGL--EDITSGDLLI-GEK-RMNEVPPSER-GIGM 79
Cdd:PRK13549 7 EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFeGEElQASNIRDTERaGIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 80 VFQSYALYPHLSVADNMSFGLKLAGAKK---AEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFL 156
Cdd:PRK13549 87 IHQELALVKELSVLENIFLGNEITPGGImdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 157 LDEPLSNLDAAlRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:PRK13549 167 LDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-225 |
3.97e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 78.24 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGDLLIGEKRMNEVPPSER------GIGMVFQS--YALYPH 89
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 90 LSVADNMSFGLKL-AGAKKAEINQRVnqvSEVLQL------AHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLS 162
Cdd:PRK11022 106 YTVGFQIMEAIKVhQGGNKKTRRQRA---IDLLNQvgipdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515497030 163 NLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-221 |
4.11e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.68 E-value: 4.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPS--ERGIGMVFQSYALYpHLSVADNMS 97
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAslRNQVALVSQNVHLF-NDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 98 FglklagAKKAEINQRvnQVSEVLQLAHLLDRRPK--------------ALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:PRK11176 439 Y------ARTEQYSRE--QIEEAARMAYAMDFINKmdngldtvigengvLLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 164 LDAALRVQMRIEISRLHKrlQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK11176 511 LDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-217 |
5.16e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 79.38 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPS--ERGIGMVFQSYALYPHlSVADNMS 97
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPVVLAD-TFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 98 FGLKLAgakkaeiNQRVNQVSEVLQLAHLLDRRPKA-----------LSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDA 166
Cdd:PRK10790 437 LGRDIS-------EEQVWQALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515497030 167 ALR--VQMRIEISRLHKrlqrTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:PRK10790 510 GTEqaIQQALAAVREHT----TLVVIAH-RLSTIVEADTILVLHRGQAVEQGT 557
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-221 |
8.19e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.36 E-value: 8.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLigekrMNEVPPSERGIGMVFQSYALYPH-LSVADNMSFGL 100
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIL-----LDAQPLESWSSKAFARKVAYLPQqLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 101 KLA----------GAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRV 170
Cdd:PRK10575 105 LVAigrypwhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515497030 171 QMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-165 |
9.30e-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: 78.44 E-value: 9.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 9 VYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMnevppsergIGMVFQSY-ALY 87
Cdd:TIGR03719 328 LTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK---------LAYVDQSRdALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 88 PHLSVADNMSFGLKLAGAKKAEINQR----------VNQvsevlqlahllDRRPKALSGGQRQRVAIGRTLVAEPDVFLL 157
Cdd:TIGR03719 399 PNKTVWEEISGGLDIIKLGKREIPSRayvgrfnfkgSDQ-----------QKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
....*...
gi 515497030 158 DEPLSNLD 165
Cdd:TIGR03719 468 DEPTNDLD 475
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-217 |
1.02e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.38 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 11 KAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGL--EDITSGDLLIGEKRMNEvpPSERGIGMVFQSYALYP 88
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTK--QILKRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 89 HLSVADNMSFG--LKLAGAKKAEINQRVNQ--VSEvLQLAH-----LLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDE 159
Cdd:PLN03211 154 HLTVRETLVFCslLRLPKSLTKQEKILVAEsvISE-LGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 160 PLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-221 |
1.49e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 78.24 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGleditsgdlligekrmnEVPPSERGIGMVFQSYALYPHLS------VAD 94
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLG-----------------ELPPRSDASVVIRGTVAYVPQVSwifnatVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 95 NMSFGLKLAGAkkaeinqRVNQVSEVLQLAHLLDRRPKA-----------LSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:PLN03130 698 NILFGSPFDPE-------RYERAIDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515497030 164 LDAALRVQ-----MRIEISrlhkrlQRTMIYVThDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PLN03130 771 LDAHVGRQvfdkcIKDELR------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-222 |
2.76e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.71 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGleditsgdlligekrmnEVPPSERGIGMVFQSYALYPHLS------VAD 94
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVVIRGSVAYVPQVSwifnatVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 95 NMSFGLKLAgakkaeiNQRVNQVSEVLQLAHLLD-----------RRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:PLN03232 698 NILFGSDFE-------SERYWRAIDVTALQHDLDllpgrdlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 164 LDAalRVQMRIEISRLHKRLQ-RTMIYVThDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
Cdd:PLN03232 771 LDA--HVAHQVFDSCMKDELKgKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-192 |
3.76e-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: 72.57 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIgekrmnevpPSERGIGMVFQ-SYalyphlsvadnMSF 98
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQrPY-----------LPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 99 GLkLAGakkaeinqrvnqvsevlQLAHLLDRRpkaLSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRieiSR 178
Cdd:cd03223 78 GT-LRE-----------------QLIYPWDDV---LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY---QL 133
|
170
....*....|....
gi 515497030 179 LHKRLQrTMIYVTH 192
Cdd:cd03223 134 LKELGI-TVISVGH 146
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-210 |
4.21e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 73.52 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSERGIGMVFQ-SYALY-PHL---SVADN 95
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSvAYAAQkPWLlnaTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 96 MSFGLKLAgakkaeiNQRVNQVSEVLQLAHLLDRRPKA-----------LSGGQRQRVAIGRTLVAEPDVFLLDEPLSNL 164
Cdd:cd03290 99 ITFGSPFN-------KQRYKAVTDACSLQPDIDLLPFGdqteigerginLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515497030 165 DAALRVQ-MRIEISRLHKRLQRTMIYVTHdQVEAMTLADKIVVLDAG 210
Cdd:cd03290 172 DIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-213 |
4.83e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.10 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSErGI--GMVF-----QSYALYPHLSVAD 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD-AIraGIMLcpedrKAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 95 NMS---------FGLKLAGAKKAEINQRvnqvsevlQLAHLLDRRPKA------LSGGQRQRVAIGRTLVAEPDVFLLDE 159
Cdd:PRK11288 351 NINisarrhhlrAGCLINNRWEAENADR--------FIRSLNIKTPSReqlimnLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 160 PLSNLDaalrVQMRIEISRLHKRLQ---RTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
Cdd:PRK11288 423 PTRGID----VGAKHEIYNVIYELAaqgVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-217 |
6.92e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 75.82 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 23 NLTIEDGEFVVFVGPSGCGKSTLLRMIAGleditSGDLLIGEKRMNevppsergigmvFQSYALyphLSV---------- 92
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG-----ELPLLSGERQSQ------------FSHITR---LSFeqlqklvsde 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 -----ADNMSFGLKLAGAKKAEI-------NQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:PRK10938 83 wqrnnTDMLSPGEDDTGRTTAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 161 LSNLDAALRVQMRIEISRLHKRlQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGE 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-207 |
1.40e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.45 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGE----KRMNeVPPSERGIGMVF 81
Cdd:PTZ00265 388 VRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDIN-LKWWRSKIGVVS 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 82 QSYALYPHlSVADNMSFGL--------------------------------KLAGA-------------KKAEINQRVNQ 116
Cdd:PTZ00265 467 QDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscraKCAGDlndmsnttdsnelIEMRKNYQTIK 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 117 VSEVLQ-----LAH------------LLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRL 179
Cdd:PTZ00265 546 DSEVVDvskkvLIHdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
|
250 260
....*....|....*....|....*...
gi 515497030 180 HKRLQRTMIYVTHdQVEAMTLADKIVVL 207
Cdd:PTZ00265 626 KGNENRITIIIAH-RLSTIRYANTIFVL 652
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-193 |
1.78e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.38 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 5 TLRSVYKAFGEA-VISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGdlligekrmnEVPPSErG--IGMVF 81
Cdd:PRK11819 8 TMNRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG----------EARPAP-GikVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 82 QSYALYPHLSVADNMSFGLklagAKKAEINQRVNQVSE-----------------VLQL------AHLLDRR-------- 130
Cdd:PRK11819 77 QEPQLDPEKTVRENVEEGV----AEVKAALDRFNEIYAayaepdadfdalaaeqgELQEiidaadAWDLDSQleiamdal 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 131 --P------KALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAalrvqmriE-ISRLHKRLQR---TMIYVTHD 193
Cdd:PRK11819 153 rcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------EsVAWLEQFLHDypgTVVAVTHD 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-221 |
1.80e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.78 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLL-----IGEKR-MNEVPPseR-- 75
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdMADARhRRAVCP--Ria 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 76 ----GIGMvfqsyALYPHLSVADNMSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAE 151
Cdd:NF033858 80 ympqGLGK-----NLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515497030 152 PDVFLLDEPLSNLDAALRVQMRIEISRLhkRLQR---TMIYVTHDQVEAMTLaDKIVVLDAGRVAQVGKPLEL 221
Cdd:NF033858 155 PDLLILDEPTTGVDPLSRRQFWELIDRI--RAERpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-207 |
1.83e-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: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 27 EDGEFVVFVGPSGCGKSTLLRMIAGLeditsgdlLIGEKRMNEVPPSERGIGMVFQSYALYPHLS--VADNMSFGLK--- 101
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGK--------LKPNLGKFDDPPDWDEILDEFRGSELQNYFTklLEGDVKVIVKpqy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 102 ------------LAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALR 169
Cdd:cd03236 96 vdlipkavkgkvGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 515497030 170 VQMRIEISRLHKRlQRTMIYVTHDQVEAMTLADKIVVL 207
Cdd:cd03236 176 LNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-165 |
2.56e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.00 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 9 VYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGE--KrmnevppsergIGMVFQSY-A 85
Cdd:PRK11819 330 LSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtvK-----------LAYVDQSRdA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 86 LYPHLSVADNMSFGLKLAGAKKAEINQRvnqvsevlqlAHL-------LDRRPKA--LSGGQRQRVAIGRTLVAEPDVFL 156
Cdd:PRK11819 399 LDPNKTVWEEISGGLDIIKVGNREIPSR----------AYVgrfnfkgGDQQKKVgvLSGGERNRLHLAKTLKQGGNVLL 468
|
....*....
gi 515497030 157 LDEPLSNLD 165
Cdd:PRK11819 469 LDEPTNDLD 477
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-210 |
3.61e-14 |
|
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: 70.35 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGDLLIGEKRMNEVPPseRGIGMVFQSYALYPHLSVADNMS 97
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQ--RSTGYVEQQDVHSPNLTVREALR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 98 FGLKLAGakkaeinqrvnqvsevlqlahlldrrpkaLSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAalrvQMRIEIS 177
Cdd:cd03232 102 FSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS----QAAYNIV 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 515497030 178 RLHKRLQRT--MIYVTHDQVEAMTLA--DKIVVLDAG 210
Cdd:cd03232 149 RFLKKLADSgqAILCTIHQPSASIFEkfDRLLLLKRG 185
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-226 |
5.13e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.27 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKS----TLLRMI-AGLEDiTSGDLLIGEKRMneVPPSERG--IGMVFQS--YALYPHL 90
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQ-TAGRVLLDGKPV--APCALRGrkIATIMQNprSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 91 SVADNMSFGLKLAGakKAEINQRVNQVSEVLQL---AHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAA 167
Cdd:PRK10418 97 TMHTHARETCLALG--KPADDATLTAALEAVGLenaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515497030 168 lrVQMRI--EISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
Cdd:PRK10418 175 --AQARIldLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-216 |
1.44e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 69.84 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLligeKRMNEVppsergiGMVFQSYALYPHLSVADNMSFGL 100
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----DRNGEV-------SVIAISAGLSGQLTGIENIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 101 KLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRLh 180
Cdd:PRK13546 111 LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF- 189
|
170 180 190
....*....|....*....|....*....|....*.
gi 515497030 181 KRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:PRK13546 190 KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-221 |
1.61e-13 |
|
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: 72.29 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIgekrmnevppsERGIGMVFQSyALYPHLSVADNMSFGLK 101
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----------KGSVAYVPQQ-AWIQNDSLRENILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 102 LAgakkaeiNQRVNQVSEVLQLAHLLDRRPKA-----------LSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRV 170
Cdd:TIGR00957 725 LN-------EKYYQQVLEACALLPDLEILPSGdrteigekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515497030 171 QMRIEISRLHKRLQ-RTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR00957 798 HIFEHVIGPEGVLKnKTRILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-212 |
2.13e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSErGI--GMVFQSY-----ALYPHLSV 92
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD-GLanGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 ADNMSF-GLKLAGAKKAEINQRVNQ--VSEVLQLAHL----LDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLD 165
Cdd:PRK10762 348 KENMSLtALRYFSRAGGSLKHADEQqaVSDFIRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515497030 166 aalrVQMRIEISRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:PRK10762 428 ----VGAKKEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-207 |
3.94e-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: 70.58 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 25 TIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLligekrmnEVPPSERGIGMVFQSYALYPHLS-VADNmsfglKLA 103
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKRFRGTELQDYFKkLANG-----EIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 104 GAKKaeiNQRVNQVSEV------------------------LQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDE 159
Cdd:COG1245 162 VAHK---PQYVDLIPKVfkgtvrellekvdergkldelaekLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515497030 160 PLSNLDaalrVQMRIEISRLHKRLQ---RTMIYVTHDQveAM--TLADKIVVL 207
Cdd:COG1245 239 PSSYLD----IYQRLNVARLIRELAeegKYVLVVEHDL--AIldYLADYVHIL 285
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-211 |
4.22e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.39 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAVIS-KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI-GEKRMNEVPPSERG-IGMVFQ 82
Cdd:PRK10522 325 LRNVTFAYQDNGFSvGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVTAEQPEDYRKlFSAVFT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 SYALYPHLsvadnmsfglkLAGAKKAEINQRVNQVSEVLQLAH--------LLDRRpkaLSGGQRQRVAIGRTLVAEPDV 154
Cdd:PRK10522 405 DFHLFDQL-----------LGPEGKPANPALVEKWLERLKMAHkleledgrISNLK---LSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 155 FLLDEPLSNLDAALRvqmRIEISRLHKRLQ---RTMIYVTHDQvEAMTLADKIVVLDAGR 211
Cdd:PRK10522 471 LLLDEWAADQDPHFR---REFYQVLLPLLQemgKTIFAISHDD-HYFIHADRLLEMRNGQ 526
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-210 |
5.08e-13 |
|
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: 70.71 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIagleditsgdlligekrMNEVPPSERGI---GMVfqSYAlyPHLS----- 91
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMI-----------------MGELEPSEGKIkhsGRI--SFS--PQTSwimpg 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 92 -VADNMSFGLKLAgakkaeiNQRVNQVSEVLQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLVAEPDVFLLDE 159
Cdd:TIGR01271 502 tIKDNIIFGLSYD-------EYRYTSVIKACQLEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515497030 160 PLSNLDaaLRVQMRIEISRLHKRL-QRTMIYVThDQVEAMTLADKIVVLDAG 210
Cdd:TIGR01271 575 PFTHLD--VVTEKEIFESCLCKLMsNKTRILVT-SKLEHLKKADKILLLHEG 623
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-210 |
6.71e-13 |
|
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: 68.34 E-value: 6.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGdlligekrmnEVPPSERgIGMVFQSYALYPHlSVADNMSFG 99
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG----------KIKHSGR-ISFSSQFSWIMPG-TIKENIIFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 100 LKLAgakkaeiNQRVNQVSEVLQLAHLLDRRPK-----------ALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAAl 168
Cdd:cd03291 122 VSYD-------EYRYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF- 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515497030 169 rVQMRIEISRLHKRL-QRTMIYVThDQVEAMTLADKIVVLDAG 210
Cdd:cd03291 194 -TEKEIFESCVCKLMaNKTRILVT-SKMEHLKKADKILILHEG 234
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
21-165 |
7.85e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 66.43 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVP-PSERGIGmvfQSYALYPHLSVADNMSFG 99
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPYCTYIG---HNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 100 lklagakkAEINQRVNQVSEVL---QLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLD 165
Cdd:PRK13541 95 --------SEIYNSAETLYAAIhyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-243 |
8.60e-13 |
|
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: 70.04 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 26 IEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI-GEKRMNEVPPSERGIGMVFQSYALYPHLSVADNMSFGLKLAG 104
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 105 AKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRLhKRLQ 184
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI-IREG 2120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 185 RTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL-YHYPANRFVAGFIGSPKMNFLP 243
Cdd:TIGR01257 2121 RAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLkSKFGDGYIVTMKIKSPKDDLLP 2180
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-178 |
1.05e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.13 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI-GEKRMNEVPPSERGIGMVFQSYALYPHLSVADNMSF 98
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 99 GLKLAGAkkaeiNQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLD--AALRVQMRIEI 176
Cdd:PRK13540 98 DIHFSPG-----AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDelSLLTIITKIQE 172
|
..
gi 515497030 177 SR 178
Cdd:PRK13540 173 HR 174
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
106-207 |
1.39e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 106 KKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDaalrVQMRIEISRLHKRLQ- 184
Cdd:PRK13409 185 KKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD----IRQRLNVARLIRELAe 260
|
90 100
....*....|....*....|....
gi 515497030 185 -RTMIYVTHDQVEAMTLADKIVVL 207
Cdd:PRK13409 261 gKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-208 |
1.80e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.90 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 18 ISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI-----------------------GEKRMNEVPPSE 74
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVfknehtndmtneqdyqgdeeqnvGMKNVNEFSLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 75 RG---------------------------------IGMVFQSYALYpHLSVADNMSFGlklagaKKAEINQRVNQVSEVL 121
Cdd:PTZ00265 1263 EGgsgedstvfknsgkilldgvdicdynlkdlrnlFSIVSQEPMLF-NMSIYENIKFG------KEDATREDVKRACKFA 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 122 QLAHLLDRRP-----------KALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYV 190
Cdd:PTZ00265 1336 AIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415
|
250
....*....|....*...
gi 515497030 191 THdQVEAMTLADKIVVLD 208
Cdd:PTZ00265 1416 AH-RIASIKRSDKIVVFN 1432
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-193 |
2.84e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.05 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 12 AFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRmnEVPpsergigmVFQSY--ALYPH 89
Cdd:PRK11147 328 QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL--EVA--------YFDQHraELDPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 90 LSVADNmsfglkLA-GAKKAEINQRVNQVsevlqLAHLLD--------RRP-KALSGGQRQRVAIGRTLVAEPDVFLLDE 159
Cdd:PRK11147 398 KTVMDN------LAeGKQEVMVNGRPRHV-----LGYLQDflfhpkraMTPvKALSGGERNRLLLARLFLKPSNLLILDE 466
|
170 180 190
....*....|....*....|....*....|....*...
gi 515497030 160 PLSNLDaalrvqmrIEISRLHKRL----QRTMIYVTHD 193
Cdd:PRK11147 467 PTNDLD--------VETLELLEELldsyQGTVLLVSHD 496
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-218 |
5.30e-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: 66.75 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEfVVF-VGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRmneVPPSERG-----IGMVFQSYALYPHlsvadn 95
Cdd:COG4615 351 IDLTIRRGE-LVFiVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREayrqlFSAVFSDFHLFDR------ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 96 msfglkLAGAKKAEINQRVNQVSEVLQLAHLL---DRR--PKALSGGQRQRVAIgrtLVA---EPDVFLLDEPLSNLDAA 167
Cdd:COG4615 421 ------LLGLDGEADPARARELLERLELDHKVsveDGRfsTTDLSQGQRKRLAL---LVAlleDRPILVFDEWAADQDPE 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 168 LRvqmRI---EI-SRLhKRLQRTMIYVTHDQvEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:COG4615 492 FR---RVfytELlPEL-KARGKTVIAISHDD-RYFDLADRVLKMDYGKLVELTGP 541
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-250 |
7.55e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.06 E-value: 7.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 18 ISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDlLIGEKRMNEVPPSErgIGMVFQSYALY--------PH 89
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIG-VEGVITYDGITPEE--IKKHYRGDVVYnaetdvhfPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 90 LSVADNMSFGLKLAG--------AKKAEINQRVNQVSEVLQLAHLLDRRP-----KALSGGQRQRVAIGRTLVAEPDVFL 156
Cdd:TIGR00956 153 LTVGETLDFAARCKTpqnrpdgvSREEYAKHIADVYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 157 LDEPLSNLDAALRVQMrIEISRLHKRLQRTMIYVTHDQV--EAMTLADKIVVLDAGRvaqvgkplELYHYPANRFVAGFI 234
Cdd:TIGR00956 233 WDNATRGLDSATALEF-IRALKTSANILDTTPLVAIYQCsqDAYELFDKVIVLYEGY--------QIYFGPADKAKQYFE 303
|
250
....*....|....*..
gi 515497030 235 gspKMNFL-PVKVTAAE 250
Cdd:TIGR00956 304 ---KMGFKcPDRQTTAD 317
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-192 |
7.62e-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: 66.70 E-value: 7.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKdVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEK-RMNEVPpsER---GIGmVFQSYALYPH 89
Cdd:TIGR00954 464 GDVLIES-LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKgKLFYVP--QRpymTLG-TLRDQIIYPD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 90 lSVADNMSFGLKlagakkaeiNQRVNQVSEVLQLAHLLDRR---------PKALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:TIGR00954 540 -SSEDMKRRGLS---------DKDLEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 515497030 161 LSnldaALRVQMRIEISRLHKRLQRTMIYVTH 192
Cdd:TIGR00954 610 TS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-165 |
1.06e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 26 IEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKrmnEVPPSERGIGMVFQSY--ALYPHLSVADNMSFglkLA 103
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRFMAYLGHlpGLKADLSTLENLHF---LC 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497030 104 GAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLD 165
Cdd:PRK13543 108 GLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
281-353 |
1.42e-11 |
|
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: 59.56 E-value: 1.42e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 281 LGIRPEHLLPGEASEvRLTGDVQVVEQLGNETQIHIQIPAIRQNLVYRQN-DVVLVEEGATFAIGLPPHRCHLF 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 ... |
26-233 |
1.70e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 62.20 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 26 IEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLligekrmnevppsergigmvfqsyalyphlsvadnmsfglKLAGA 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND----------------------------------------EWDGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 106 KKAEINQRVNqvsevlqlahlldrrpkaLSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLQR 185
Cdd:cd03222 62 TPVYKPQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515497030 186 TMIYVTHDQVEAMTLADKIVVLDA--GRVAQVGKPLELYHyPANRFVAGF 233
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVFEGepGVYGIASQPKGTRE-GINRFLRGY 172
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-218 |
2.17e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.69 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 17 VISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGleDIT----------SGDLLIGEKRMNEVPP-------------S 73
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTgggaprgarvTGDVTLNGEPLAAIDAprlarlravlpqaA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 74 ERGIGMVFQSYAL---YPHLsvadnmsfglKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTL-- 148
Cdd:PRK13547 93 QPAFAFSAREIVLlgrYPHA----------RRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515497030 149 -------VAEPDVFLLDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
18-216 |
2.20e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.27 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 18 ISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGDLLIGEKRMNEVPPSER---GIGMVFQSYALYPHLSv 92
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageGIFMAFQYPVEIPGVS- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 adNMSFGLKLAGAKKAEINQR----------VNQVSEVLQL-AHLLDRRPK-ALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:PRK09580 95 --NQFFLQTALNAVRSYRGQEpldrfdfqdlMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDES 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515497030 161 LSNLDA-ALR-VQMRIEISRLHKrlqRTMIYVTHDQ-VEAMTLADKIVVLDAGRVAQVG 216
Cdd:PRK09580 173 DSGLDIdALKiVADGVNSLRDGK---RSFIIVTHYQrILDYIKPDYVHVLYQGRIVKSG 228
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-212 |
2.25e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGdlligekrmnEVPPSERG-IGMVFQ 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG----------TVKWSENAnIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 -SYALYPH-LSVADNMSfglKLAGAKKAEinQRVNQVsevlqLAHLL------DRRPKALSGGQRQRVAIGRTLVAEPDV 154
Cdd:PRK15064 390 dHAYDFENdLTLFDWMS---QWRQEGDDE--QAVRGT-----LGRLLfsqddiKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497030 155 FLLDEPLSNLDaalrvqmrIE-ISRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:PRK15064 460 LVMDEPTNHMD--------MEsIESLNMALEKyegTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-218 |
2.86e-11 |
|
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: 62.43 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSYALyphlsvadnms 97
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTL----------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 98 fglkLAGAKKAEINqRVNQVSEVLQLAHL-LDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDaalrVQMRIEI 176
Cdd:cd03369 94 ----FSGTIRSNLD-PFDEYSDEEIYGALrVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASID----YATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515497030 177 SR-LHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
Cdd:cd03369 165 QKtIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-212 |
4.96e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.89 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSER---GIGMV---FQSYALYPHLSVA 93
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYIpedRLGRGLVPDMSVA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFGL--KLAGAKKAEINQRvnqvsEVLQLA-HLLDR---RP-------KALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:COG3845 355 ENLILGRyrRPPFSRGGFLDRK-----AIRAFAeELIEEfdvRTpgpdtpaRSLSGGNQQKVILARELSRDPKLLIAAQP 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 161 LSNLDAAlrvqmriEISRLHKRL--QRTM----IYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:COG3845 430 TRGLDVG-------AIEFIHQRLleLRDAgaavLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-210 |
1.21e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLED---ITSGDLLIGEKRMNEvpPSERGIGMVFQSYALYPHL 90
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDS--SFQRSIGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 91 SVADNMSFGLKL---AGAKKAEINQRVNQVSEVLQLAHLLDrrpkALSG--------GQRQRVAIGRTLVAEPDVFL-LD 158
Cdd:TIGR00956 852 TVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYAD----AVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 159 EPLSNLDAalrvQMRIEISRLHKRLQRT--MIYVTHDQVEAMTLA--DKIVVLDAG 210
Cdd:TIGR00956 928 EPTSGLDS----QTAWSICKLMRKLADHgqAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-207 |
2.37e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.67 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 3 SVTLRSVYKAFgeavisKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPpSERGIGMVFQ 82
Cdd:PRK15056 13 TVTWRNGHTAL------RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL-QKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 SYAL---YPHLsVADNMSFG-------LKLAGAKKAEInqrvnqVSEVLQLAHLLDRRPKA---LSGGQRQRVAIGRTLV 149
Cdd:PRK15056 86 SEEVdwsFPVL-VEDVVMMGryghmgwLRRAKKRDRQI------VTAALARVDMVEFRHRQigeLSGGQKKRVFLARAIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515497030 150 AEPDVFLLDEPLSNLDaalrVQMRIEISRLHKRLQ---RTMIYVTHDQVEAMTLADKIVVL 207
Cdd:PRK15056 159 QQGQVILLDEPFTGVD----VKTEARIISLLRELRdegKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-213 |
2.70e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE---RGIGMVFQ---SYALYPHLSVA 93
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainHGFALVTEerrSTGIYAYLDIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNM----------SFGLkLAGAKKAEINQRVNQVSEVLQLAHllDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:PRK10982 345 FNSlisnirnyknKVGL-LDNSRMKSDTQWVIDSMRVKTPGH--RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515497030 164 LDAALRVQMRIEISRLHKRlQRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
22-216 |
3.74e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 60.30 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGDLLIGEKRMNEVPPSER------GIGMVFQ--SYALYPH 89
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQepSSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 90 LSVADNMSFGL---KLAGAKKAEINQRVNQVSEVL------QLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:COG4170 106 AKIGDQLIEAIpswTFKGKWWQRFKWRKKRAIELLhrvgikDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515497030 161 LSNLDAALRVQmrieISRLHKRLQR----TMIYVTHDqVEAMT-LADKIVVLDAGRVAQVG 216
Cdd:COG4170 186 TNAMESTTQAQ----IFRLLARLNQlqgtSILLISHD-LESISqWADTITVLYCGQTVESG 241
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-173 |
4.47e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.40 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEditSGDLLIGEKRMNEVPPSE----RGIGMVFQSYALYPHLSVADN 95
Cdd:PLN03140 897 REVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK---TGGYIEGDIRISGFPKKQetfaRISGYCEQNDIHSPQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 96 MSFGLKLAGAKKAEINQRVNQVSEVLQLAHLLDRRPK--------ALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDA- 166
Cdd:PLN03140 974 LIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAivglpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAr 1053
|
....*..
gi 515497030 167 ALRVQMR 173
Cdd:PLN03140 1054 AAAIVMR 1060
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-225 |
4.52e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.20 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGledITSGDLLIGEKRMN-------EVPPSER------GIGMVFQSyalyP 88
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICG---VTKDNWRVTADRMRfddidllRLSPRERrklvghNVSMIFQE----P 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 89 HLSVADNMSFGLKLAGA-----KKAEINQRVN----QVSEVLQLAHLLDRR------PKALSGGQRQRVAIGRTLVAEPD 153
Cdd:PRK15093 99 QSCLDPSERVGRQLMQNipgwtYKGRWWQRFGwrkrRAIELLHRVGIKDHKdamrsfPYELTEGECQKVMIAIALANQPR 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY---HYP 225
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVttpHHP 253
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
19-205 |
6.99e-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: 58.00 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 19 SKDVNLTIE-DGEFVVFVGPSGCGKSTLlrmIAGLEDITSGDLligekrmnevPPSERGIgmvfqsyALYPHL----SVA 93
Cdd:cd03240 11 SFHERSEIEfFSPLTLIVGQNGAGKTTI---IEALKYALTGEL----------PPNSKGG-------AHDPKLiregEVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFGLKLAGAKKAEINQRVNQVSEVL-----QLAHLLDRRPKALSGGQRQ------RVAIGRTLVAEPDVFLLDEPLS 162
Cdd:cd03240 71 AQVKLAFENANGKKYTITRSLAILENVIfchqgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTT 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515497030 163 NLDAALRVQMRIEISRLHKRL-QRTMIYVTHDQvEAMTLADKIV 205
Cdd:cd03240 151 NLDEENIEESLAEIIEERKSQkNFQLIVITHDE-ELVDAADHIY 193
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
235-288 |
8.24e-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: 54.13 E-value: 8.24e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 235 GSPKMNFLPVKVT----AAEPRQVQVELPNRQlvwlpVEGAGVQPGANLSLGIRPEHL 288
Cdd:pfam17912 1 GSPPMNFLPATVVedglLVLGGGVTLPLPEGQ-----VLALKLYVGKEVILGIRPEHI 53
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-214 |
1.32e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSER-GIGMVF-----QSYALYPHLSVA 93
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMS------FGLKLAGAKKAEINQRVNQVSEVlQLAHLlDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDaa 167
Cdd:PRK15439 360 WNVCalthnrRGFWIKPARENAVLERYRRALNI-KFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD-- 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515497030 168 lrVQMRIEISRLHKRL---QRTMIYVTHDQVEAMTLADKIVVLDAGRVAQ 214
Cdd:PRK15439 436 --VSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEISG 483
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
107-221 |
9.19e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.28 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 107 KAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEIsRLHKRLQRT 186
Cdd:NF000106 118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVRDGAT 196
|
90 100 110
....*....|....*....|....*....|....*
gi 515497030 187 MIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-212 |
9.36e-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: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGL-EDITSGDLLIGEKRMNEVPPS---ERGIGMVFQS---YALYPHLSVA 93
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAqaiRAGIAMVPEDrkrHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFGLKLAGAKKAEINQRVNQ--VSEVLQLAHLLDRRP----KALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDaa 167
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAAELqiIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD-- 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515497030 168 lrVQMRIEISRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:TIGR02633 436 --VGAKYEIYKLINQLAQegvAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-211 |
1.63e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE---RGIGMVFQ 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaleNGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 83 SYALYPHLSVADNMSFG---LKLAGAKKAEINQRVNQVSEVLQLAhlLDRRPKA--LSGGQRQRVAIGRTLVAEPDVFLL 157
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDID--IDPRAKVatLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515497030 158 DEPLSNLDAAlRVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:PRK10982 159 DEPTSSLTEK-EVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-205 |
2.64e-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: 53.80 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLlrmiagleditSGDLLI--GEKRMNE-VPPSER-GIGMVFQSY-----ALYPHL 90
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKSSL-----------AFDTIYaeGQRRYVEsLSAYARqFLGQMDKPDvdsieGLSPAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 91 SVaDNMSFG----------------LKLAGAKkAEINQRVNQVSEVlQLAHL-LDRRPKALSGGQRQRVAIGRTLVAEPD 153
Cdd:cd03270 81 AI-DQKTTSrnprstvgtvteiydyLRLLFAR-VGIRERLGFLVDV-GLGYLtLSRSAPTLSGGEAQRIRLATQIGSGLT 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515497030 154 --VFLLDEPLSNLDAALRVQMRIEISRLhKRLQRTMIYVTHDQvEAMTLADKIV 205
Cdd:cd03270 158 gvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHVI 209
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-210 |
4.28e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAF-GEAVISKdVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLL-IGEKRMNEVPPS--ERGIGMVF 81
Cdd:PRK10762 7 LKGIDKAFpGVKALSG-AALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEVTFNGPKSsqEAGIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 82 QSYALYPHLSVADNMSFGL----KLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLL 157
Cdd:PRK10762 86 QELNLIPQLTIAENIFLGRefvnRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 158 DEPLSNL-----DAALRVqmrieISRLhKRLQRTMIYVTHDQVEAMTLADKIVVLDAG 210
Cdd:PRK10762 166 DEPTDALtdtetESLFRV-----IREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-197 |
9.47e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 9.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 4 VTLRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGleDITSG---DL-LIGEKRMN--EVPPSERGI 77
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysnDLtLFGRRRGSgeTIWDIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 78 GMVFQSYalypHL------SVADNM------SFGLKLAGAKKAeiNQRVNQVSEVLQLAHLLDRRP-KALSGGQRQRVAI 144
Cdd:PRK10938 339 GYVSSSL----HLdyrvstSVRNVIlsgffdSIGIYQAVSDRQ--QKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515497030 145 GRTLVAEPDVFLLDEPLSNLDAALR--VQMRIEISRLHKRLQrtMIYVTHDQVEA 197
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPLNRqlVRRFVDVLISEGETQ--LLFVSHHAEDA 465
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-217 |
1.19e-07 |
|
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: 51.17 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRmiAGLEDItsgdlliGEKRMNEVPPsergigmvfqsyALYPHLSVA-DNMSF 98
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYAS-------GKARLISFLP------------KFSRNKLIFiDQLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 99 GLKLAgakkaeinqrvnqvsevlqLAHL-LDRRPKALSGGQRQRVAIGRTLVAEPD--VFLLDEPLSNLDAALRVQMRIE 175
Cdd:cd03238 71 LIDVG-------------------LGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEV 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515497030 176 ISRLhKRLQRTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGK 217
Cdd:cd03238 132 IKGL-IDLGNTVILIEHN-LDVLSSADWIIDFGPGSGKSGGK 171
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-204 |
1.47e-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: 50.45 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIgekrmnevppsergigmvfqsyalyphlsvadnmsfglklagakka 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 109 eIN-QRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEIS-----RLHKR 182
Cdd:smart00382 36 -IDgEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSE 114
|
170 180
....*....|....*....|..
gi 515497030 183 LQRTMIYVTHDQVEAMTLADKI 204
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRR 136
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-213 |
3.34e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEK-RMnevppsergigMVFQSYalypHLSv 92
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRM-----------AVFSQH----HVD- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 93 adnmsfGLKLAGAKKAEINQRVNQVSEVLQLAHL--------LDRRPK-ALSGGQRQRVAIGRTLVAEPDVFLLDEPLSN 163
Cdd:PLN03073 584 ------GLDLSSNPLLYMMRCFPGVPEQKLRAHLgsfgvtgnLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515497030 164 LDAAlRVQMRIEISRLhkrLQRTMIYVTHDQVEAMTLADKIVVLDAGRVA 213
Cdd:PLN03073 658 LDLD-AVEALIQGLVL---FQGGVLMVSHDEHLISGSVDELWVVSEGKVT 703
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-211 |
3.84e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 6 LRSVYKAFGEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITS--GDLLI--GEKRMNEVPPSE-RGIGMV 80
Cdd:NF040905 4 MRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFdgEVCRFKDIRDSEaLGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 81 FQSYALYPHLSVADNMSFGLKLagAKKAEIN-QRVNQVSEVLqLAHL-LDRRPKALSG----GQRQRVAIGRTLVAEPDV 154
Cdd:NF040905 84 HQELALIPYLSIAENIFLGNER--AKRGVIDwNETNRRAREL-LAKVgLDESPDTLVTdigvGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 155 FLLDEPLSNLD----AALRvqmrieisRLHKRLQR---TMIYVTHDQVEAMTLADKIVVLDAGR 211
Cdd:NF040905 161 LILDEPTAALNeedsAALL--------DLLLELKAqgiTSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-229 |
4.78e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLL----RMI--AGLEDITSGDLlIGEKRMNEVppsERGIGMVFQSYALYPHlSVADN 95
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLltfmRMVevCGGEIRVNGRE-IGAYGLREL---RRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 96 MSFGLKlagAKKAEI---------NQRVNQVSEVLqlahllDRRpkALSGG------QRQRVAIGRTLVAEPDVF-LLDE 159
Cdd:PTZ00243 1404 VDPFLE---ASSAEVwaalelvglRERVASESEGI------DSR--VLEGGsnysvgQRQLMCMARALLKKGSGFiLMDE 1472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 160 PLSNLDAALRVQmrIEISRLHKRLQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRF 229
Cdd:PTZ00243 1473 ATANIDPALDRQ--IQATVMSAFSAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-221 |
1.09e-06 |
|
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: 50.71 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKST----LLRMIAGLEditsgdlliGEKRMNEVPPSERGIGMVFQSYALYPHLSV--A 93
Cdd:TIGR00957 1303 RHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINESAE---------GEIIIDGLNIAKIGLHDLRFKITIIPQDPVlfS 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNMSFGLKLAGAKKAEinqrvnQVSEVLQLAHL----------LDRR----PKALSGGQRQRVAIGRTLVAEPDVFLLDE 159
Cdd:TIGR00957 1374 GSLRMNLDPFSQYSDE------EVWWALELAHLktfvsalpdkLDHEcaegGENLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515497030 160 PLSNLD--------AALRVQMR-IEISRLHKRLQRTMIYVthdqveamtladKIVVLDAGRVAQVGKPLEL 221
Cdd:TIGR00957 1448 ATAAVDletdnliqSTIRTQFEdCTVLTIAHRLNTIMDYT------------RVIVLDKGEVAEFGAPSNL 1506
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-216 |
1.09e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.27 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIgekrmnevppsERGIGMVFQSYALYPHLSVADNMSFGL 100
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-----------KGSAALIAISSGLNGQLTGIENIELKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 101 KLAGAKKAEINQRVNQVSEVLQLAHLLDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDAALRVQMRIEISRLh 180
Cdd:PRK13545 111 LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF- 189
|
170 180 190
....*....|....*....|....*....|....*.
gi 515497030 181 KRLQRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
Cdd:PRK13545 190 KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYG 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-221 |
2.68e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.59 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 30 EFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVPPSE--RGIGMVFQSYALYphlsvADNMSFGLKlagaKK 107
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLF-----SGTVRFNID----PF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 108 AEINQRvnQVSEVLQLAHL---LDRRPKAL-----------SGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDaaLRVQMR 173
Cdd:PLN03232 1334 SEHNDA--DLWEALERAHIkdvIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVD--VRTDSL 1409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515497030 174 IEISRLHKRLQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
129-192 |
3.51e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 3.51e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497030 129 RRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDaaLRVQMRIEISRLhkRLQRTMIYVTH 192
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWLETYLL--KWPKTFIVVSH 399
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-212 |
6.28e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGL-EDITSGDLLIGEKRMNEVPPSE---RGIGMVFQS---YALYPHLSVA 93
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 94 DNM--------SFGLKL-AGAKKAEINQRVNQVSevLQLAHLlDRRPKALSGGQRQRVAIGRTLVAEPDVFLLDEPLSNL 164
Cdd:PRK13549 360 KNItlaaldrfTGGSRIdDAAELKTILESIQRLK--VKTASP-ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515497030 165 DaalrVQMRIEISRLHKRL-QRTM--IYVTHDQVEAMTLADKIVVLDAGRV 212
Cdd:PRK13549 437 D----VGAKYEIYKLINQLvQQGVaiIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-205 |
6.52e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 14 GEAVISKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLI----------GEKRMNEVPPSERGIGMVFQS 83
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgnwqlawvnQETPALPQPALEYVIDGDREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 84 YALYPHLSVADNMSFGL-------KLAGAKKAEINQRVNQVSEVLQLAH-LLDRRPKALSGGQRQRVAIGRTLVAEPDVF 155
Cdd:PRK10636 92 RQLEAQLHDANERNDGHaiatihgKLDAIDAWTIRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515497030 156 LLDEPLSNLDaalrVQMRIEISRLHKRLQRTMIYVTHDQVEAMTLADKIV 205
Cdd:PRK10636 172 LLDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-214 |
1.46e-05 |
|
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: 46.00 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 1 MASVTLRSVYKAFGEAVIsKDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGDLLIGEKRMNEVPPSE--RGIG 78
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVL-ENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKwrKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 79 MVFQSYALYphlsvadNMSFGLKLAGAKKAEiNQRVNQVSEVLQLAHLLDRRPK-----------ALSGGQRQRVAIGRT 147
Cdd:cd03289 81 VIPQKVFIF-------SGTFRKNLDPYGKWS-DEEIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497030 148 LVAEPDVFLLDEPLSNLDAalrvqmrIEISRLHKRLQR-----TMIYVTHdQVEAMTLADKIVVLDAGRVAQ 214
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDP-------ITYQVIRKTLKQafadcTVILSEH-RIEAMLECQRFLVIEENKVRQ 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-221 |
6.32e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 22 VNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIgekrmNEVPPSERGI-------GMVFQSYALYphlsvAD 94
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILI-----DGCDISKFGLmdlrkvlGIIPQAPVLF-----SG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 95 NMSFGLK-LAGAKKAEInqrvnqvSEVLQLAHLLD---RRPKAL-----------SGGQRQRVAIGRTLVAEPDVFLLDE 159
Cdd:PLN03130 1328 TVRFNLDpFNEHNDADL-------WESLERAHLKDvirRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 160 PLSNLD----AALRVQMRIEISRLhkrlqrTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:PLN03130 1401 ATAAVDvrtdALIQKTIREEFKSC------TMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-205 |
8.91e-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: 42.35 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 21 DVNLTieDGEFVVFVGPSGCGKSTLLRMIAgleditsgdLLIGEKRMNEVPPSERGIGMVfqsyalyphlsvadnmsfgl 100
Cdd:cd03227 15 DVTFG--EGSLTIITGPNGSGKSTILDAIG---------LALGGAQSATRRRSGVKAGCI-------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 101 klAGAKKAEINQRVNQvsevlqlahlldrrpkaLSGGQRQRVAI----GRTLVAEPDVFLLDEPLSNLDaaLRVQMRI-E 175
Cdd:cd03227 64 --VAAVSAELIFTRLQ-----------------LSGGEKELSALalilALASLKPRPLYILDEIDRGLD--PRDGQALaE 122
|
170 180 190
....*....|....*....|....*....|
gi 515497030 176 ISRLHKRLQRTMIYVTHDQvEAMTLADKIV 205
Cdd:cd03227 123 AILEHLVKGAQVIVITHLP-ELAELADKLI 151
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
90-221 |
2.16e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 90 LSVADNMSF--GLKLAGAKKA-------EINQRVNQVSEVlQLAHL-LDRRPKALSGGQRQRVA----IGRTLVAEpdVF 155
Cdd:TIGR00630 436 LSIREAHEFfnQLTLTPEEKKiaeevlkEIRERLGFLIDV-GLDYLsLSRAAGTLSGGEAQRIRlatqIGSGLTGV--LY 512
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515497030 156 LLDEPLSNLDAalRVQMR-IEISRLHKRLQRTMIYVTHDQvEAMTLADKIVVL------DAGRVAQVGKPLEL 221
Cdd:TIGR00630 513 VLDEPSIGLHQ--RDNRRlINTLKRLRDLGNTLIVVEHDE-DTIRAADYVIDIgpgageHGGEVVASGTPEEI 582
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
20-221 |
3.37e-04 |
|
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: 41.82 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLLIGEKRMNEVP--PSERGIGMVFQSYALYphlsvadNMS 97
Cdd:cd03288 38 KHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlhTLRSRLSIILQDPILF-------SGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 98 FGLKLAGAKKAEiNQRVNQVSEVLQLAHLLDRRPKAL-----------SGGQRQRVAIGRTLVAEPDVFLLDEPLSNLDA 166
Cdd:cd03288 111 IRFNLDPECKCT-DDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDM 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515497030 167 ALR-VQMRIEISRLhkrLQRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
Cdd:cd03288 190 ATEnILQKVVMTAF---ADRTVVTIAH-RVSTILDADLVLVLSRGILVECDTPENL 241
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
141-193 |
1.01e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 1.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497030 141 RVAIGRTLVAEPDVFLLDEPLSNLDaalrvqmrIEISR-----LHKRlQRTMIYVTHD 193
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD--------INTIRwledvLNER-NSTMIIISHD 211
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
89-221 |
1.71e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 89 HLSVADNMSF--GLKLAGAKKA-------EINQRVNQVSEVlQLAHL-LDRRPKALSGGQRQRV----AIGRTLVaepDV 154
Cdd:COG0178 432 ALSIDEALEFfeNLELTEREAEiaerilkEIRSRLGFLVDV-GLDYLtLDRSAGTLSGGEAQRIrlatQIGSGLV---GV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 155 -FLLDEPlSnldaalrvqmrieISrLHKR--------LQR------TMIYVTHDQvEAMTLADKIVvlD----AGR---- 211
Cdd:COG0178 508 lYVLDEP-S-------------IG-LHQRdndrlietLKRlrdlgnTVIVVEHDE-DTIRAADYII--DigpgAGEhgge 569
|
170
....*....|.
gi 515497030 212 -VAQvGKPLEL 221
Cdd:COG0178 570 vVAQ-GTPEEI 579
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
20-45 |
2.42e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 2.42e-03
10 20
....*....|....*....|....*.
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTL 45
Cdd:COG0178 17 KNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
29-59 |
3.19e-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: 38.53 E-value: 3.19e-03
10 20 30
....*....|....*....|....*....|.
gi 515497030 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGD 59
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGE 115
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
134-160 |
4.25e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 4.25e-03
10 20
....*....|....*....|....*..
gi 515497030 134 LSGGQRQRVAIGRTLVAEPDVFLLDEP 160
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
23-194 |
4.57e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.76 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 23 NLTIEDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLligekrmNEVPPSERGIGMVFQSYAlyphLSVADNMSFGLKL 102
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALRFLSDAARGGL-------QDALARRGGLEELLWRGP----RTITEPIRLELEF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497030 103 AGAKKAEI-----------NQRVNQVSEVLQLAHLLDRRPkALSGGQRQRVAIGRTlvaepdvFLLDEPLSNLDAALRVQ 171
Cdd:COG4637 84 AEEDERDLryelelglpepGGRPEVKEERLWLKRGSGGRP-FLDFRPKGRAVGGEP-------ERLDSPESLLSQLGDPE 155
|
170 180
....*....|....*....|...
gi 515497030 172 MRIEISRLHKRLQRTMIYVTHDQ 194
Cdd:COG4637 156 RFPELRALREALRSWRFYDFHPA 178
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
20-45 |
5.25e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.90 E-value: 5.25e-03
10 20
....*....|....*....|....*.
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTL 45
Cdd:PRK00349 17 KNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| AAA_17 |
pfam13207 |
AAA domain; |
35-64 |
5.32e-03 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 36.83 E-value: 5.32e-03
10 20 30
....*....|....*....|....*....|...
gi 515497030 35 VGPSGCGKSTLLRMIA---GLEDITSGDLLIGE 64
Cdd:pfam13207 1 TGVPGSGKTTQLKKLAeklGFPHISAGDLLREE 33
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-46 |
8.43e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 8.43e-03
10 20
....*....|....*....|....*..
gi 515497030 20 KDVNLTIEDGEFVVFVGPSGCGKSTLL 46
Cdd:TIGR00630 625 KNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| |
