|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-345 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 593.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 161 LSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGSPAMN 240
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 241 FISGSMTEDGFRTADG-LLLPS--ERRPADAAIYGIRPEHIRLDP---GGIEVTTVVVEPTGSETLVIVRLGTQTLTCVF 314
Cdd:COG3839 241 LLPGTVEGGGVRLGGVrLPLPAalAAAAGGEVTLGIRPEHLRLADegdGGLEATVEVVEPLGSETLVHVRLGGQELVARV 320
|
330 340 350
....*....|....*....|....*....|..
gi 655334176 315 RERIRAAPGEVLRIAPIHDTVHLFGKD-EQRI 345
Cdd:COG3839 321 PGDTRLRPGDTVRLAFDPERLHLFDAEtGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-346 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 543.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDY-GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAM 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 80 VFQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDE 159
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 160 PLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGSPAM 239
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 240 NFISGSMTEDG--FRTADGLLLPSERRPA----DAAIYGIRPEHIRLDPGGIEVTTVV--VEPTGSETLVIVRLGTQTLT 311
Cdd:PRK11650 241 NLLDGRVSADGaaFELAGGIALPLGGGYRqyagRKLTLGIRPEHIALSSAEGGVPLTVdtVELLGADNLAHGRWGGQPLV 320
|
330 340 350
....*....|....*....|....*....|....*
gi 655334176 312 CVFRERIRAAPGEVLRIAPIHDTVHLFGKDEQRIT 346
Cdd:PRK11650 321 VRLPHQERPAAGSTLWLHLPANQLHLFDADTGRRI 355
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-338 |
1.04e-152 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 433.37 E-value: 1.04e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 161 LSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGSpaMN 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGE--AN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 241 FISGSMTEDGFRTAD--GLLLP----SERRPADAAIYGIRPEHIRLDP----GGIEVTTVVVEPTGSETLVIVRLGT-QT 309
Cdd:COG3842 241 LLPGTVLGDEGGGVRtgGRTLEvpadAGLAAGGPVTVAIRPEDIRLSPegpeNGLPGTVEDVVFLGSHVRYRVRLGDgQE 320
|
330 340 350
....*....|....*....|....*....|.
gi 655334176 310 LTCVF--RERIRAAPGEVLRIAPIHDTVHLF 338
Cdd:COG3842 321 LVVRVpnRAALPLEPGDRVGLSWDPEDVVVL 351
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-341 |
1.95e-146 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 417.89 E-value: 1.95e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 161 LSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGSPAMN 240
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 241 FISGSMTEDG-----FRTADGLL--LPSERR---PADAAIYGIRPEHIrLDPGGIEVT---TV-VVEPTGSETLVIVRLG 306
Cdd:PRK11000 241 FLPVKVTATAieqvqVELPNRQQvwLPVEGRgvqVGANMSLGIRPEHL-LPSDIADVTlegEVqVVEQLGNETQIHIQIP 319
|
330 340 350
....*....|....*....|....*....|....*..
gi 655334176 307 TQTLTCVFRER--IRAAPGEVLRIAPIHDTVHLFGKD 341
Cdd:PRK11000 320 AIRQNLVYRQNdvVLVEEGATFAIGLPPERCHLFRED 356
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
1.82e-133 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 379.29 E-value: 1.82e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQN 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 655334176 164 LDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSG 216
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-337 |
6.57e-122 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 354.84 E-value: 6.57e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVN-ELAPKDRDIAMVFQ 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 83 NYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 163 NLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGspAMNFI 242
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVNVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 243 SGSmTEDGFRTADGLLLP-SERRPADAAIYGIRPEHIRL-----DPGGIEVTTVVVEPTGSETLVIVRLG---TQTLTC- 312
Cdd:COG1118 241 RGR-VIGGQLEADGLTLPvAEPLPDGPAVAGVRPHDIEVsrepeGENTFPATVARVSELGPEVRVELKLEdgeGQPLEAe 319
|
330 340
....*....|....*....|....*...
gi 655334176 313 VFRERIRA---APGEVLRIAPIHDTVHL 337
Cdd:COG1118 320 VTKEAWAElglAPGDPVYLRPRPARVFL 347
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-339 |
5.90e-119 |
|
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: 347.79 E-value: 5.90e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMV 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEP 160
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 161 LSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGSpaMN 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE--VN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 241 FISGSMTEDG-FRTADGLLL--PSERRPADAAIYGIRPEHIRLDPGGIEVTTVVVEPTGSE--------TLVIVRLGTQT 309
Cdd:TIGR03265 240 WLPGTRGGGSrARVGGLTLAcaPGLAQPGASVRLAVRPEDIRVSPAGNAANLLLARVEDMEflgafyrlRLRLEGLPGQA 319
|
330 340 350
....*....|....*....|....*....|....
gi 655334176 310 LTCVF----RERIRAAPGEVLRIAPIHDTVHLFG 339
Cdd:TIGR03265 320 LVADVsaseVERLGIRAGQPIWIELPAERLRAFA 353
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-235 |
1.83e-113 |
|
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: 329.20 E-value: 1.83e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQN 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 164 LDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIG 235
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
1.20e-109 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 318.69 E-value: 1.20e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQN 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 655334176 164 LDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSG 216
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-281 |
6.33e-107 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 317.66 E-value: 6.33e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQN 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 164 LDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGSpaMNFIS 243
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE--INIFD 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 655334176 244 GSMTEdgfRTADGLLLPS-ERRPADaaIYG-------------IRPEHIRLD 281
Cdd:PRK09452 253 ATVIE---RLDEQRVRANvEGRECN--IYVnfavepgqklhvlLRPEDLRVE 299
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
4-293 |
1.27e-105 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 313.86 E-value: 1.27e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFK----AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNE-----LAPKD 74
Cdd:NF040933 3 VRVENVTKIFKKGKkevvALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPPED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 75 RDIAMVFQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAV 154
Cdd:NF040933 83 RNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 155 FLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFI 234
Cdd:NF040933 163 LLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLI 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 235 GSpaMNFISGSMTEDGFRTADGLLLPSERRPADA--AIYGIRPEHI-------RLDPGGIEVTTVVVE 293
Cdd:NF040933 243 GD--INLLEGKVEEEGLVDGNDLKIPLPNPKLEAgeVIIGIRPEDIdisesdmRLPPGFVEVGKGRVK 308
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-236 |
1.34e-99 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 294.25 E-value: 1.34e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQN 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHMTVAKNMGFSLRLK----RMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDE 159
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 160 PLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGS 236
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-286 |
1.45e-96 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 290.47 E-value: 1.45e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQN 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 164 LDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGSPAM---N 240
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIfpaT 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 655334176 241 FISGSMTEDGFRtadgLLLPSE---RRPADAAIYGIRPEHIRLDPGGIE 286
Cdd:PRK11432 247 LSGDYVDIYGYR----LPRPAAfafNLPDGECTVGVRPEAITLSEQGEE 291
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-235 |
8.63e-93 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 276.68 E-value: 8.63e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQN 83
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 164 LDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIG 235
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-290 |
4.73e-91 |
|
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: 275.53 E-value: 4.73e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 34 LVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQR 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 114 VGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHD 193
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 194 QIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGSpaMNFISGSMTE--DGFRTADGLLLPSERRPADAAIY 271
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE--INVFEATVIErkSEQVVLAGVEGRRCDIYTDVPVE 238
|
250
....*....|....*....
gi 655334176 272 GIRPEHIRLDPGGIEVTTV 290
Cdd:TIGR01187 239 KDQPLHVVLRPEKIVIEEE 257
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
1.15e-86 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 261.95 E-value: 1.15e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDY----GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPkdrD 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 77 IAMVFQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 655334176 157 FDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-235 |
1.13e-83 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 253.41 E-value: 1.13e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 6 VNNARKDYGAFKaIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNeLAPKDRDIAMVFQNY 84
Cdd:cd03299 3 VENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDITN-LPPEKRDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 85 ALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:cd03299 81 ALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 165 DAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIG 235
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-207 |
5.77e-83 |
|
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: 251.24 E-value: 5.77e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYG----AFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPkdrDIAM 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 80 VFQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 655334176 160 PLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVM 207
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
6-286 |
3.65e-81 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 251.15 E-value: 3.65e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 6 VNNARKDYGAFKaIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQNYA 85
Cdd:NF040840 4 IENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 86 LYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:NF040840 83 LFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 166 AKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGspAMNFISGS 245
Cdd:NF040840 163 VQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG--FENIIEGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 655334176 246 MTEDGFRT---ADGLLLPSERRPADAAIYGIRPEHIRLDPGGIE 286
Cdd:NF040840 241 AEKGGEGTildTGNIKIELPEEKKGKVRIGIRPEDITISTEKVK 284
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-235 |
5.06e-81 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 250.77 E-value: 5.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQN 83
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHMTVAKNMGFSL----RLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDE 159
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655334176 160 PLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIG 235
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-285 |
4.06e-79 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 246.67 E-value: 4.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 6 VNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQNYA 85
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 86 LYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 166 AKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGSpaMNFISGS 245
Cdd:PRK11607 182 KKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVFEGV 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 655334176 246 MTEdgfRTADGLLL--PSERRP----ADAAIYGIRPEHIRLDPGGI 285
Cdd:PRK11607 260 LKE---RQEDGLVIdsPGLVHPlkvdADASVVDNVPVHVALRPEKI 302
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-236 |
7.80e-77 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 238.45 E-value: 7.80e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 8 NARKDY-GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIvNELAPKD--RDIAMVFQN 83
Cdd:COG1125 6 NVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIdGEDI-RDLDPVElrRRIGYVIQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGL--ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:COG1125 85 IGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 162 SNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGS 236
Cdd:COG1125 165 GALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-237 |
1.90e-74 |
|
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: 230.27 E-value: 1.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGA-FKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMV 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLE--SLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 159 EPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGSP 237
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-216 |
1.39e-69 |
|
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: 216.78 E-value: 1.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 28 DGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNE------LAPKDRDIAMVFQNYALYPHMTVAKNMGFSLR 101
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 102 LKRmpRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQ 181
Cdd:cd03297 102 RKR--NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 655334176 182 RLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSG 216
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
10-234 |
5.75e-69 |
|
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: 217.13 E-value: 5.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 10 RKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD------RDIAMVFQN 83
Cdd:cd03294 31 LKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:cd03294 111 FALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 164 LDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFI 234
Cdd:cd03294 191 LDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-213 |
5.79e-69 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 215.68 E-value: 5.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYG----AFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRD--- 76
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 77 ---IAMVFQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPA 153
Cdd:COG1136 85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 154 VFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQiEAMTMADKIVVMKDGLIE 213
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-210 |
4.64e-68 |
|
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: 211.66 E-value: 4.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 6 VNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELA----PKDRDIAMVF 81
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 82 QNYALYPHMTVAKNMGFSLrlkrmprteidqrvgnaakilglesllerypkqlSGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:cd03229 83 QDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 655334176 162 SNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-212 |
3.40e-67 |
|
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: 210.81 E-value: 3.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGA----FKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRD--- 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 77 ---IAMVFQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPA 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 154 VFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQiEAMTMADKIVVMKDGLI 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-228 |
5.98e-64 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 202.95 E-value: 5.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDY-GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMV 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNyalyP-----HMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVF 155
Cdd:COG1122 81 FQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655334176 156 LFDEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNL 228
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
1.09e-63 |
|
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: 202.73 E-value: 1.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGA----FKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDI 77
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 AMVFQNY--ALYPHMTVAKNMGFSLRLKRMPrtEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMGRAIVRDPAV 154
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 155 FLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDqIEAMT-MADKIVVMKDGLIEQSGSPLELYDRPNN 227
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-225 |
2.35e-63 |
|
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: 209.76 E-value: 2.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDY-----GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD---- 74
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 75 -RDIAMVFQN--YALYPHMTVAKNMGFSLRL-KRMPRTEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMGRAIV 149
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 150 RDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDqIEAM-TMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHD-LAVVrYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-227 |
2.38e-63 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 201.38 E-value: 2.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNeLAPKD-----RDIA 78
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDinklrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 79 MVFQNYALYPHMTVAKNMGFSLR-LKRMPRTEIDQRvgnAAKIL---GLESLLERYPKQLSGGQRQRVAMGRAIVRDPAV 154
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEER---AMELLervGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 155 FLFDEPLSNLDAklrvQMRSE----IKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNN 227
Cdd:COG1126 158 MLFDEPTSALDP----ELVGEvldvMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
8-310 |
1.45e-62 |
|
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: 203.41 E-value: 1.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 8 NARKDYGAFkAIKgVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHI-------VNeLAPKDRDIAMV 80
Cdd:COG4148 6 DFRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargIF-LPPHRRRIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPHMTVAKNMGFSLRlkRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEP 160
Cdd:COG4148 83 FQEARLFPHLSVRGNLLYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 161 LSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGfiGSPAMN 240
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 241 FISGS---------MTEdgFRTADG-LLLPSERRPADAAIY-GIRPEHIRL---DPGGI------EVTTVVVEPT-GSET 299
Cdd:COG4148 239 VLEATvaahdpdygLTR--LALGGGrLWVPRLDLPPGTRVRvRIRARDVSLalePPEGSsilnilPGRVVEIEPAdGGQV 316
|
330
....*....|.
gi 655334176 300 LVIVRLGTQTL 310
Cdd:COG4148 317 LVRLDLGGQTL 327
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-226 |
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: 199.05 E-value: 2.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRD-----IA 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrrIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 79 MVFQNYALYPHMTVAKNMGFSLR-LKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLF 157
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 158 DEPLSNLD---AKLRVQMrseIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPN 226
Cdd:COG1127 166 DEPTAGLDpitSAVIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDD 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-224 |
3.53e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 198.36 E-value: 3.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKDRDIAMVFQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 83 NYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 163 NLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-210 |
4.63e-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: 194.61 E-value: 4.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 5 SVNNARKDY--GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMV 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNyalyP-HM----TVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVF 155
Cdd:cd03225 81 FQN----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 156 LFDEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-235 |
1.45e-60 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 194.20 E-value: 1.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 6 VNNARKDYGAFkaIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQNYA 85
Cdd:COG3840 4 LDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 86 LYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:COG3840 82 LFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 166 AKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIG 235
Cdd:COG3840 162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-221 |
1.77e-59 |
|
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: 191.56 E-value: 1.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD-----RDIA 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 79 MVFQNYALYPHMTVAKNMGFSLRLK-RMPRTEIDQRVgnAAKI--LGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVF 155
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIV--LEKLeaVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655334176 156 LFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-214 |
5.18e-59 |
|
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: 190.02 E-value: 5.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDY----GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDR---- 75
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 76 -DIAMVFQNY--ALYPHMTVAKNMGFSLRLKRMPR--TEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMGRAIV 149
Cdd:cd03257 82 kEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSkkEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 150 RDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDqIEAM-TMADKIVVMKDG-LIEQ 214
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHD-LGVVaKIADRVAVMYAGkIVEE 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-228 |
1.33e-56 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 192.04 E-value: 1.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDY--GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL---EGITSGQIQIGKHIVNELAPKDR--D 76
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 77 IAMVFQN--YALYPhMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAV 154
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 155 FLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNL 228
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-212 |
1.63e-56 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 183.33 E-value: 1.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDY-GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD-----RDI 77
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 AMVFQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLF 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 158 DEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-207 |
6.85e-55 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 180.44 E-value: 6.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFK----AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNelAPkDRD 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GP-GAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 77 IAMVFQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFL 156
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 655334176 157 FDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVM 207
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-212 |
8.97e-55 |
|
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: 178.49 E-value: 8.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVN----ELAPKDRDIAM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 80 VFQNYALYPHMTVAKNMGFSLR-LKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 159 EPLSNLDAklrvQMRSEIKELHQRL---QTTTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:cd03262 161 EPTSALDP----ELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-238 |
5.81e-54 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 180.66 E-value: 5.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 3 HVSVNNARKDY----GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD---- 74
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 75 -RDIAMVFQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPA 153
Cdd:COG1135 81 rRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 154 VFLFDEPLSNLDAK-----LRVqmrseIKELHQRLQTTTIYVTHD-----QIeamtmADKIVVMKDGLIEQSGSPLELYD 223
Cdd:COG1135 161 VLLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHEmdvvrRI-----CDRVAVLENGRIVEQGPVLDVFA 230
|
250
....*....|....*
gi 655334176 224 RPNNLFVAGFIGSPA 238
Cdd:COG1135 231 NPQSELTRRFLPTVL 245
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-224 |
9.21e-54 |
|
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: 176.97 E-value: 9.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 6 VNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKDRDIAMVFQNY 84
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDVRKEPREARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 85 ALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:COG4555 84 GLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 165 DAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:COG4555 164 DVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
1.53e-53 |
|
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: 176.23 E-value: 1.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYG----AFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD----- 74
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 75 RDIAMVFQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAV 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 155 FLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHdQIEAM-TMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-210 |
2.19e-52 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 173.70 E-value: 2.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDY-GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD-----RDI 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 AMVFQNYALYPHMTVAKN--------MGF--SLrLKRMPRTEIDQrvgnAAKIL---GLESLLERYPKQLSGGQRQRVAM 144
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNvlagrlgrTSTwrSL-LGLFPPEDRER----ALEALervGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 145 GRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHdQIE-AMTMADKIVVMKDG 210
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDG 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-227 |
4.45e-51 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 169.89 E-value: 4.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDI----AM 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 80 VFQNYALYPHMTVAKNMGFS-LRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFD 158
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 159 EPLSNLDAKLRVQMRSEIKELHQRLQTTTIyVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNN 227
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-216 |
7.71e-51 |
|
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: 168.50 E-value: 7.71e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 23 SVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQNYALYPHMTVAKNMGFSLRL 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 103 KRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQR 182
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 655334176 183 LQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSG 216
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-223 |
1.90e-50 |
|
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: 168.52 E-value: 1.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 6 VNNARKDYGA-FKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD-----RDIAM 79
Cdd:cd03256 3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 80 VFQNYALYPHMTVAKN--MGfslRLKRMPR--------TEIDQRVGNAA-KILGLESLLERYPKQLSGGQRQRVAMGRAI 148
Cdd:cd03256 83 IFQQFNLIERLSVLENvlSG---RLGRRSTwrslfglfPKEEKQRALAAlERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655334176 149 VRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHdQIE-AMTMADKIVVMKDGLIEQSGSPLELYD 223
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLH-QVDlAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
14-210 |
1.99e-50 |
|
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: 167.43 E-value: 1.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 14 GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD-----RDIAMVFQNYALYP 88
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRIGVVFQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 89 HMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL 168
Cdd:TIGR02673 93 DRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 655334176 169 RVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:TIGR02673 173 SERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-221 |
2.24e-50 |
|
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: 168.68 E-value: 2.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVF 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 82 QNYALYPHMTVAKN--MGFS--LRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLF 157
Cdd:COG1120 82 QEPPAPFGLTVRELvaLGRYphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 158 DEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-228 |
7.01e-50 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 167.61 E-value: 7.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDY--GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIqigkhIVNELAPKDRD----- 76
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKV-----TVDGLDTLDEEnlwei 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 77 ---IAMVFQNyalyPH-----MTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAI 148
Cdd:TIGR04520 76 rkkVGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 149 VRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDqIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNL 228
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHD-MEEAVLADRVIVMNKGKIVAEGTPREIFSQVELL 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-216 |
1.06e-49 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 165.74 E-value: 1.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 23 SVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQNYALYPHMTVAKNMGfslrL 102
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVG----L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 103 KRMPR---TEID-QRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKE 178
Cdd:cd03298 94 GLSPGlklTAEDrQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 655334176 179 LHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSG 216
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-210 |
1.61e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 164.99 E-value: 1.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 5 SVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQ 82
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 83 NYALYPhMTVAKNMGFSLRLKRMPRTEidQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 655334176 162 SNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-214 |
2.02e-49 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 165.96 E-value: 2.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKH---IVNELAPKD-----R 75
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdFSKTPSDKAirelrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 76 DIAMVFQNYALYPHMTVAKNM-GFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAV 154
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 155 FLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIyVTHDQIEAMTMADKIVVMKDG-LIEQ 214
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGhIVEQ 222
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-228 |
3.09e-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: 166.47 E-value: 3.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 15 AFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD-----RDIAMVFQnyalYPH 89
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrKKVGLVFQ----FPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 90 M-----TVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:TIGR04521 93 HqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 164 LDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNL 228
Cdd:TIGR04521 173 LDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDEL 237
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-225 |
8.97e-49 |
|
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: 166.38 E-value: 8.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDY----GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLE---GITSGQIQI-GKHIVnELAPKD- 74
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFdGEDLL-KLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 75 -----RDIAMVFQN-Y-ALYPHMTVAKNMGFSLRL-KRMPRTEIDQRVGNAAKILGL---ESLLERYPKQLSGGQRQRVA 143
Cdd:COG0444 81 rkirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 144 MGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDqIEAM-TMADKIVVMKDGLIEQSGSPLELY 222
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHD-LGVVaEIADRVAVMYAGRIVEEGPVEELF 239
|
...
gi 655334176 223 DRP 225
Cdd:COG0444 240 ENP 242
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-226 |
1.20e-48 |
|
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: 167.21 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 8 NARKDYGAFKAikGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNE------LAPKDRDIAMVF 81
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 82 QNYALYPHMTVAKNMGFSLRlkrmpRTEIDQRVGNAAKI---LGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFD 158
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMK-----RARPSERRISFERVielLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 159 EPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPN 226
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
1.60e-48 |
|
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: 161.03 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKDRDIAMVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 83 NYALYPHMTVAKNMgfslrlkrmprteidqrvgnaakilglesllerypkQLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 655334176 163 NLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-214 |
3.09e-47 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 160.18 E-value: 3.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVN---ELAPKD-----R 75
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAirllrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 76 DIAMVFQNYALYPHMTVAKNM-GFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAV 154
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 155 FLFDEPLSNLDAKLRVQMRSEIKELHQrLQTTTIYVTHDQIEAMTMADKIVVMKDG-LIEQ 214
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGrIIEQ 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
4.82e-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: 4.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYG--AFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKH-IVNELAPKDRDIAMV 80
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEP 160
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 161 LSNLDAKLRVQMRSEIKELhqRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-212 |
3.19e-46 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 157.92 E-value: 3.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 6 VNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKhivNELAPKDRDIAMVFQNYA 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT---APLAEAREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 86 LYPHMTVAKNMGFSLRLKRMPRTEidqrvgNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:PRK11247 92 LLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 655334176 166 AKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-225 |
3.77e-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: 156.86 E-value: 3.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPkdrDIAMVFQNYALYPHMTVAKNMGF 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 99 SLR--LKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEI 176
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 655334176 177 KELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLEL-YDRP 225
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-221 |
3.84e-46 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 157.05 E-value: 3.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 23 SVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQNYALYPHMTVAKNMGF---- 98
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLglnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 99 SLRLKRMPRTEIDQRvgnaAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKE 178
Cdd:PRK10771 99 GLKLNAAQREKLHAI----ARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 655334176 179 LHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-193 |
9.37e-46 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 155.33 E-value: 9.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAG-LEGI--TSGQIQIGKHIVNELAPKDRDIAMVFQNYALYPHMTVAKN 95
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MGFSLRlKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSE 175
Cdd:COG4136 97 LAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175
|
170
....*....|....*...
gi 655334176 176 IKELHQRLQTTTIYVTHD 193
Cdd:COG4136 176 VFEQIRQRGIPALLVTHD 193
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-212 |
9.57e-46 |
|
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: 155.26 E-value: 9.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 8 NARKDYGA-FKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD-----RDIAMVF 81
Cdd:cd03292 5 NVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 82 QNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:cd03292 85 QDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 655334176 162 SNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-218 |
2.61e-45 |
|
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: 154.65 E-value: 2.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGI-----TSGQIQI-GKHI------VNELA 71
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLdGKDIydldvdVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 72 pkdRDIAMVFQNYALYPhMTVAKNMGFSLRLKRM-PRTEIDQRVGNAAKILGL--ESLLERYPKQLSGGQRQRVAMGRAI 148
Cdd:cd03260 81 ---RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 149 VRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRlqTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSP 218
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-223 |
2.69e-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: 155.15 E-value: 2.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 6 VNNARKDYG-AFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKDRD----IAM 79
Cdd:TIGR02315 4 VENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLeGTDITKLRGKKLRKlrrrIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 80 VFQNYALYPHMTVAKN--MGF-----SLR--LKRMPRTEIdQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVR 150
Cdd:TIGR02315 84 IFQHYNLIERLTVLENvlHGRlgykpTWRslLGRFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655334176 151 DPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYD 223
Cdd:TIGR02315 163 QPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
5.62e-45 |
|
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: 152.20 E-value: 5.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 5 SVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRdiamvfqny 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 85 alyphmtvAKNMGFslrlkrmprteidqrVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:cd03214 72 --------ARKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 655334176 165 DAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSG 216
Cdd:cd03214 129 DIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-210 |
2.09e-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: 150.09 E-value: 2.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 5 SVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 83 nyalyphmtvaknmgfslrlkrmprteidqrvgnaakilglesllerypkqLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 655334176 163 NLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-205 |
3.06e-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: 151.23 E-value: 3.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 8 NARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKDRD-----IAMVF 81
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLnGQETPPLNSKKASKfrrekLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 82 QNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:TIGR03608 83 QNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 655334176 162 SNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQiEAMTMADKIV 205
Cdd:TIGR03608 163 GSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVI 204
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-236 |
3.95e-44 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 152.65 E-value: 3.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIV-------NELAPKDRD 76
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdGELVPADRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 77 --------IAMVFQNYALYPHMTVAKN-MGFSLRLKRMPRTEIDQRvgnAAKIL---GLESLLERYPKQLSGGQRQRVAM 144
Cdd:COG4598 89 qlqrirtrLGMVFQSFNLWSHMTVLENvIEAPVHVLGRPKAEAIER---AEALLakvGLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 145 GRAIVRDPAVFLFDEPLSNLDAK-----LRVqMRSEIKElhQRlqtTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPL 219
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPElvgevLKV-MRDLAEE--GR---TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA 239
|
250
....*....|....*..
gi 655334176 220 ELYDRPNNLFVAGFIGS 236
Cdd:COG4598 240 EVFGNPKSERLRQFLSS 256
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-225 |
4.70e-44 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 154.50 E-value: 4.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDY----GAF-------KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVN--- 68
Cdd:COG4608 8 LEVRDLKKHFpvrgGLFgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFdGQDITGlsg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 69 -ELAPKDRDIAMVFQN-YA-LYPHMTVAKNMGFSLRLKRM-PRTEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVA 143
Cdd:COG4608 88 rELRPLRRRMQMVFQDpYAsLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 144 MGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHD-----QIeamtmADKIVVMKDGLIEQSGSP 218
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDlsvvrHI-----SDRVAVMYLGKIVEIAPR 242
|
....*..
gi 655334176 219 LELYDRP 225
Cdd:COG4608 243 DELYARP 249
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-224 |
6.98e-44 |
|
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: 160.77 E-value: 6.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYpHMTVAKN 95
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGTIREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MgfslrlkRMPRTEI-DQRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:COG2274 569 I-------TLGDPDAtDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 164 LDAKLRVQMRSEIKELHQrlQTTTIYVTHDqIEAMTMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:COG2274 642 LDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-236 |
1.22e-43 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 151.14 E-value: 1.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIV-------NELAPKD-- 74
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLyhmpgrnGPLVPADek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 75 ------RDIAMVFQNYALYPHMTVAKNMGFS-LRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRA 147
Cdd:TIGR03005 81 hlrqmrNKIGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 148 IVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNN 227
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
....*....
gi 655334176 228 LFVAGFIGS 236
Cdd:TIGR03005 241 ERTREFLSK 249
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-233 |
2.66e-43 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 154.42 E-value: 2.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD------RDIAMVFQNYALYPHMT 91
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 92 VAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ 171
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 172 MRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGF 233
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
17-210 |
6.45e-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: 146.37 E-value: 6.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYpHMTVAK 94
Cdd:cd03228 16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAYVPQDPFLF-SGTIRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 95 NMgfslrlkrmprteidqrvgnaakilglesllerypkqLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRS 174
Cdd:cd03228 95 NI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 655334176 175 EIKELHQRlqTTTIYVTHDqIEAMTMADKIVVMKDG 210
Cdd:cd03228 138 ALRALAKG--KTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-210 |
7.90e-43 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 149.08 E-value: 7.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 12 DYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKdrdiAMVFQNYALYPHM 90
Cdd:PRK11248 10 DYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdGKPVEGPGAER----GVVFQNEGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRV 170
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 655334176 171 QMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:PRK11248 166 QMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
20-214 |
8.76e-43 |
|
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: 148.35 E-value: 8.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 20 KGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHivnELAPKDRD---------IAMVFQNYALYPHM 90
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDEDararlrarhVGFVFQSFQLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAKNMGFSLRLKRMPRTEidQRvgnAAKIL---GLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 167
Cdd:COG4181 106 TALENVMLPLELAGRRDAR--AR---ARALLervGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 655334176 168 LRVQMRSEIKELHQRLQTTTIYVTHDQIEAmTMADKIVVMKDGLIEQ 214
Cdd:COG4181 181 TGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-262 |
1.50e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 149.11 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNE--LAPKDRDIAMVFQNyalyPH-----MT 91
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenVWDIRHKIGMVFQN----PDnqfvgAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 92 VAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ 171
Cdd:PRK13650 99 VEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 172 MRSEIKELHQRLQTTTIYVTHDqIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGfIGSPAMNFISGSMTEDGF 251
Cdd:PRK13650 179 LIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQLG-LDIPFTTSLVQSLRQNGY 256
|
250
....*....|.
gi 655334176 252 RTADGLLLPSE 262
Cdd:PRK13650 257 DLPEGYLTEKE 267
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-222 |
1.71e-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: 155.30 E-value: 1.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALyPHMTVAKN 95
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWVPQNPYL-FAGTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 mgfsLRLKRMPRTeiDQRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:COG4988 431 ----LRLGRPDAS--DEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHL 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 165 DAKLRVQMRSEIKELHQrlQTTTIYVTHDqIEAMTMADKIVVMKDGLIEQSGSPLELY 222
Cdd:COG4988 505 DAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-162 |
1.76e-42 |
|
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: 144.71 E-value: 1.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKDRD-IAMVFQNYALYPHMTVAKNM 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdGQDLTDDERKSLRKeIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 GFSLRLKRMPRTEIDQRVGNAAKILGLESLLER----YPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-221 |
3.42e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.83 E-value: 3.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKDRD-IAMVFQNyalyPH-----M 90
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKENLKEIRKkIGIIFQN----PDnqfigA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRV 170
Cdd:PRK13632 100 TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 655334176 171 QMRSEIKELHQRLQTTTIYVTHDQIEAmTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:PRK13632 180 EIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-221 |
4.17e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 154.17 E-value: 4.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYpHMTVAK 94
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGTIRE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 95 NmgfsLRLKRMPRTeiDQRVGNAAKILGLESLLERYPKQ-----------LSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:COG1132 433 N----IRYGRPDAT--DEEVEEAAKAAQAHEFIEALPDGydtvvgergvnLSGGQRQRIAIARALLKDPPILILDEATSA 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 164 LDAKLRVQMRSEIKELHQrlQTTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:COG1132 507 LDTETEALIQEALERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-225 |
4.75e-42 |
|
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: 153.30 E-value: 4.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 10 RKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGiTSGQIQI-GKHIV----NELAPKDRDIAMVFQN- 83
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFdGQDLDglsrRALRPLRRRMQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YA-LYPHMTVAKNMGFSLRLKR--MPRTEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDE 159
Cdd:COG4172 372 FGsLSPRMTVGQIIAEGLRVHGpgLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 160 PLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQ--IEAmtMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLavVRA--LAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-197 |
5.64e-42 |
|
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: 145.31 E-value: 5.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 2 AHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKDRDIAMV 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPHMTVAKNMGFSLRLKRMPRTeiDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEP 160
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 655334176 161 LSNLDAKLRVQMRSEIKElHQRLQTTTIYVTHDQIEA 197
Cdd:COG4133 159 FTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLEL 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-226 |
1.41e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.62 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHivnELAPKDRDIAMV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPH--MTVAK--NMGF--SLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAV 154
Cdd:COG1121 81 PQRAEVDWDfpITVRDvvLMGRygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 155 FLFDEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEqSGSPLELYDRPN 226
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEEVLTPEN 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-258 |
1.81e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 146.35 E-value: 1.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDI----AMVFQ--NYALYPHm 90
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGL--ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL 168
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 169 RVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGfIGSPAMNFISGSMTE 248
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESIG-LAVPQVTYLVRKLRK 258
|
250
....*....|
gi 655334176 249 DGFRTADGLL 258
Cdd:PRK13637 259 KGFNIPDDIF 268
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-228 |
4.17e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 145.55 E-value: 4.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKH-IVNELAPKD-----RDIAMVFQnyalYP-H 89
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvITAGKKNKKlkplrKKVGIVFQ----FPeH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 90 M----TVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:PRK13634 97 QlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 165 DAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNL 228
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
5.25e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 144.12 E-value: 5.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD------ 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 75 ----RDIAMVFQNYALYPHMTVAKN-MGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIV 149
Cdd:PRK11264 81 rqlrQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655334176 150 RDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIyVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
10-216 |
1.66e-40 |
|
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: 141.74 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 10 RKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKDRDIAMVFQNYALYP 88
Cdd:cd03266 12 RDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVVKEPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 89 HMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL 168
Cdd:cd03266 92 RLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 655334176 169 RVQMRSEIKELhQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSG 216
Cdd:cd03266 172 TRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
7.52e-40 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 140.99 E-value: 7.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVF 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 82 QNYALYPHMTVAKNMGFSlrlkRMP----R-TEIDQR-VGNAAKILGLESLLERYPKQLSGGQRQR--VAMgrAIVRDPA 153
Cdd:COG4604 82 QENHINSRLTVRELVAFG----RFPyskgRlTAEDREiIDEAIAYLDLEDLADRYLDELSGGQRQRafIAM--VLAQDTD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 154 VFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-222 |
2.52e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 140.54 E-value: 2.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNyalyPH-----M 90
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGMVFQN----PDnqfvgA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRV 170
Cdd:PRK13635 98 TVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 655334176 171 QMRSEIKELHQRLQTTTIYVTHDQIEAMTmADKIVVMKDGLIEQSGSPLELY 222
Cdd:PRK13635 178 EVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-225 |
6.89e-39 |
|
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: 145.29 E-value: 6.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYpHMTVAKN 95
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQRPHLF-DTTLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 mgfsLRLKRMPRTeiDQRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:COG4987 429 ----LRLARPDAT--DEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 165 DAKLRVQMRSEIKE-LHQRlqtTTIYVTHDQiEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:COG4987 503 DAATEQALLADLLEaLAGR---TVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-236 |
8.12e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 141.09 E-value: 8.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 14 GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD-----RDIAMVFQNYALYP 88
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 89 HMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL 168
Cdd:PRK11153 96 SRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 169 RVQMRSEIKELHQRLQTTTIYVTHD-----QIeamtmADKIVVMKDG-LIEQsGSPLELYDRPNNLFVAGFIGS 236
Cdd:PRK11153 176 TRSILELLKDINRELGLTIVLITHEmdvvkRI-----CDRVAVIDAGrLVEQ-GTVSEVFSHPKHPLTREFIQS 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-218 |
1.14e-38 |
|
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: 137.57 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 5 SVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDR---DIAMVF 81
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 82 QNYALYPHMTVAKNM----------GFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRD 151
Cdd:cd03219 82 QIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 152 PAVFLFDEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSP 218
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-214 |
1.57e-38 |
|
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: 138.01 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 21 GVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD-----RDIAMVFQNY--ALYPHMTVA 93
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQDSpsAVNPRMTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 94 KNMGFSLR-LKRMPRTEIDQRVGNAAKILGLES-LLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ 171
Cdd:TIGR02769 109 QIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 655334176 172 MRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDG-LIEQ 214
Cdd:TIGR02769 189 ILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGqIVEE 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
1.63e-38 |
|
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: 136.73 E-value: 1.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKH-IVNELAPKDRDIAMVFQ 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 83 NYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 163 NLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-207 |
5.69e-38 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 136.32 E-value: 5.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDR---DI 77
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 AMVFQNYALYPHMTVAKNM-------------GFSLRLKRMPRTE--IDQRVGNAAKILGLESLLERYPKQLSGGQRQRV 142
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVlvaaharlgrgllAALLRLPRARREEreARERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655334176 143 AMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDqIEA-MTMADKIVVM 207
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD-MDLvMGLADRIVVL 226
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
19-212 |
1.20e-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: 134.40 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHI----VNELAP-KDRDIAMVFQNYALYPHMTV 92
Cdd:TIGR02211 21 LKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFnGQSLsklsSNERAKlRNKKLGFIYQFHHLLPDFTA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 93 AKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQM 172
Cdd:TIGR02211 101 LENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKII 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 655334176 173 RSEIKELHQRLQTTTIYVTHDqIEAMTMADKIVVMKDGLI 212
Cdd:TIGR02211 181 FDLMLELNRELNTSFLVVTHD-LELAKKLDRVLEMKDGQL 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
15-225 |
1.70e-37 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 137.14 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 15 AFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQ-IGKHIVN----ELAPKDRDIAMVFQN--YALY 87
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGmkddEWRAVRSDIQMIFQDplASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 88 PHMTVAKNMGFSLRL--KRMPRTEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:PRK15079 113 PRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 165 DAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-216 |
6.38e-37 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 132.32 E-value: 6.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVvLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRD-IAMVFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 83 NYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 655334176 163 NLDAKLRVQMRSEIKELHQrlQTTTIYVTH--DQIEAmtMADKIVVMKDGLIEQSG 216
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHivEDVES--LCNQVAVLNKGKLVFEG 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-210 |
7.21e-37 |
|
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: 132.02 E-value: 7.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNElAPKDRdIAMVFQN 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-AARNR-IGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 655334176 164 LDAKLRVQMRSEIKELhQRLQTTTIYVTH--DQIEAmtMADKIVVMKDG 210
Cdd:cd03269 159 LDPVNVELLKDVIREL-ARAGKTVILSTHqmELVEE--LCDRVLLLNKG 204
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-212 |
1.06e-36 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 133.27 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDY---------GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELA 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 72 PKD-----RDIAMVFQNY--ALYPHMTVAKNMGFSLR-LKRMPRTEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRV 142
Cdd:PRK10419 81 RAQrkafrRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 143 AMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-220 |
1.93e-36 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 134.62 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 36 GPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNE------LAPKDRDIAMVFQNYALYPHMTVAKNMGFSLRLKRmpRTE 109
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKSM--VAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 110 IDQRVgnaaKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIY 189
Cdd:PRK11144 109 FDKIV----ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170 180 190
....*....|....*....|....*....|.
gi 655334176 190 VTHDQIEAMTMADKIVVMKDGLIEQSGsPLE 220
Cdd:PRK11144 185 VSHSLDEILRLADRVVVLEQGKVKAFG-PLE 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-210 |
3.45e-35 |
|
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: 126.00 E-value: 3.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD---RDIAMV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FqnyalyphmtvaknmgfslrlkrmprteidqrvgnaakilglesllerypkQLSGGQRQRVAMGRAIVRDPAVFLFDEP 160
Cdd:cd03216 81 Y---------------------------------------------------QLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 655334176 161 LSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-212 |
3.47e-35 |
|
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: 127.65 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 5 SVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNElapkDRDIAMVFQN 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLEKE----RKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 Y----------------ALYPHMtvaknmGFSLRLKRMPRTEIDQrvgnAAKILGLESLLERYPKQLSGGQRQRVAMGRA 147
Cdd:cd03235 77 RsidrdfpisvrdvvlmGLYGHK------GLFRRLSKADKAKVDE----ALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 148 IVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-221 |
4.08e-35 |
|
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: 127.94 E-value: 4.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 13 YGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNeLAPKDR---DIAMVFQNYALYP 88
Cdd:cd03224 10 YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDITG-LPPHERaraGIGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 89 HMTVAKN--MGFSLRLKRMPRTEIDqrvgnaaKILG----LESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:cd03224 89 ELTVEENllLGAYARRRAKRKARLE-------RVYElfprLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 163 NLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-246 |
4.15e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 128.93 E-value: 4.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDI------ 77
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 ---------AMVFQNYALYPHMTVAKN-MGFSLRLKRMPRTEIDQR-VGNAAKILGLESLLERYPKQLSGGQRQRVAMGR 146
Cdd:PRK10619 86 qlrllrtrlTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERaVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 147 AIVRDPAVFLFDEPLSNLDAKLrvqmRSEIKELHQRLQ---TTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYD 223
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPEL----VGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
250 260
....*....|....*....|....
gi 655334176 224 RPNnlfvagfigSPAM-NFISGSM 246
Cdd:PRK10619 242 NPQ---------SPRLqQFLKGSL 256
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-225 |
6.96e-35 |
|
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: 133.66 E-value: 6.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 10 RKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKS----TLLRMIAGLEGITSGQIQI-GKHIVNeLAPKD------RDIA 78
Cdd:COG4172 17 GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFdGQDLLG-LSERElrrirgNRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 79 MVFQN--YALYPHMTVAKNMGFSLRLKR-MPRTEIDQRvgnAAKILGL------ESLLERYPKQLSGGQRQRV--AMgrA 147
Cdd:COG4172 96 MIFQEpmTSLNPLHTIGKQIAEVLRLHRgLSGAAARAR---ALELLERvgipdpERRLDAYPHQLSGGQRQRVmiAM--A 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 148 IVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDqieaMT----MADKIVVMKDGLIEQSGSPLELYD 223
Cdd:COG4172 171 LANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQGPTAELFA 246
|
..
gi 655334176 224 RP 225
Cdd:COG4172 247 AP 248
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-212 |
1.20e-34 |
|
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: 126.55 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYpHMTVAK 94
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQDVTLF-YGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 95 NMGFSLRLKRmprteiDQRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:cd03245 97 NITLGAPLAD------DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 655334176 164 LDaklrvqMRSEiKELHQRLQT-----TTIYVTHdQIEAMTMADKIVVMKDGLI 212
Cdd:cd03245 171 MD------MNSE-ERLKERLRQllgdkTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
17-212 |
5.13e-34 |
|
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: 132.68 E-value: 5.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYpHMTVAK 94
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTLRD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 95 NMGFslrlkRMPRTEiDQRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:TIGR03375 558 NIAL-----GAPYAD-DEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEPTSA 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 655334176 164 LDaklrvqMRSEiKELHQRLQ-----TTTIYVTHdQIEAMTMADKIVVMKDGLI 212
Cdd:TIGR03375 632 MD------NRSE-ERFKDRLKrwlagKTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-224 |
1.67e-33 |
|
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: 123.88 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYpHMTVAK 94
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGLVSQDVFLF-NDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 95 NMGFSLRlkrmprTEIDQRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:cd03251 95 NIAYGRP------GATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 164 LDAklrvqmRSE--IKELHQRLQT--TTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:cd03251 169 LDT------ESErlVQAALERLMKnrTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-214 |
1.67e-33 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 123.10 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQN 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHMTVAKNMGFSLRLKRMPRTEIDQrvgnAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 655334176 164 LDAKLRVQMRSEIKELhqRLQTTTIYVTHDQIEAM-TMADKIVVMKDG-LIEQ 214
Cdd:cd03268 157 LDPDGIKELRELILSL--RDQGITVLISSHLLSEIqKVADRIGIINKGkLIEE 207
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-224 |
4.68e-33 |
|
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: 122.72 E-value: 4.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 16 FKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNE--LAPKDRDIAMVFQNYALYpHMTVA 93
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtLDSLRRAIGVVPQDTVLF-NDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 94 KNMGFSlrlkRMPRTEIDQRvgNAAKILGLESLLERYPKQ-----------LSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:cd03253 93 YNIRYG----RPDATDEEVI--EAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 163 NLDAKLRVQMRSEIKELHQRlqTTTIYVTHDQIEAMTmADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:cd03253 167 ALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-229 |
5.99e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.22 E-value: 5.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 13 YGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLL----RMIAGLEGI-TSGQIQI-GKHI------VNELApkdRDIAMV 80
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMNDLIPGArVEGEILLdGEDIydpdvdVVELR---RRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPhMTVAKNMGFSLRLKRM-PRTEIDQRVGNAAKILGL----ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVF 155
Cdd:COG1117 98 FQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 156 LFDEPLSNLD--AKLRVqmrsE--IKELHQRLqtTTIYVTHDQIEAMTMADKIVVMKDG-LIEqsgsplelYDRPNNLF 229
Cdd:COG1117 177 LMDEPTSALDpiSTAKI----EelILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGeLVE--------FGPTEQIF 241
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-222 |
6.07e-33 |
|
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: 122.65 E-value: 6.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYPhMTVAK 94
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 95 NmgfsLRLKRMPRT--EIDQ--RVGNAAKIL-----GLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:cd03249 96 N----IRYGKPDATdeEVEEaaKKANIHDFImslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 166 AKlrvqmrSEiKELHQRLQ-----TTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLELY 222
Cdd:cd03249 172 AE------SE-KLVQEALDramkgRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-214 |
8.90e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 121.85 E-value: 8.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAP------KDRDIAMVFQNYALYPHMTV 92
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 93 AKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQM 172
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 655334176 173 RSEIKELHQRLQTTTIYVTHDQIEAMTMaDKIVVMKDGLIEQ 214
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-216 |
1.10e-32 |
|
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: 122.12 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNnarkdYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQ-IQI-----GKHIVNELAPKd 74
Cdd:COG1119 6 LRNVTVR-----RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLfgerrGGEDVWELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 75 rdIAMV---FQNYaLYPHMTVaKNM---GF--SLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGR 146
Cdd:COG1119 80 --IGLVspaLQLR-FPRDETV-LDVvlsGFfdSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655334176 147 AIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTH---DQIEAMTmadKIVVMKDGLIEQSG 216
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhveEIPPGIT---HVLLLKDGRVVAAG 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-207 |
1.93e-32 |
|
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: 127.02 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 14 GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYPHmT 91
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 92 VAKNMGfsLRLKRMPRTEIDQ---RVG----NAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:TIGR02857 412 IAENIR--LARPDASDAEIREaleRAGldefVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 655334176 165 DAKLRVQMRSEIKELHQRlqTTTIYVTHDqIEAMTMADKIVVM 207
Cdd:TIGR02857 490 DAETEAEVLEALRALAQG--RTVLLVTHR-LALAALADRIVVL 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-221 |
2.39e-32 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 126.46 E-value: 2.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 12 DYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQ--IQIGKHIVN--ELAPKDRD-----IAMVFQ 82
Cdd:TIGR03269 293 DRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDmtKPGPDGRGrakryIGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 83 NYALYPHMTVAKNMGFSLRLKrMPRTEIDQRVGNAAKILGL-----ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLF 157
Cdd:TIGR03269 373 EYDLYPHRTVLDNLTEAIGLE-LPDELARMKAVITLKMVGFdeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 158 DEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
18-227 |
6.61e-32 |
|
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: 119.40 E-value: 6.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEG----ITSGQIQIGKHIVNELAPKDRDIAMVFQN--YALYPHMT 91
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 92 VAKNMGFSLRLKRMPRTEIDQRVGNAAKILGL---ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL 168
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 169 RVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNN 227
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-227 |
2.82e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 118.41 E-value: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 8 NARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL-----EGITSGQIQI-GKHIVNE-LAPKD--RDIA 78
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLfGRNIYSPdVDPIEvrREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 79 MVFQNYALYPHMTVAKNMGFSLRLKRM--PRTEIDQRVGNAAKILGL----ESLLERYPKQLSGGQRQRVAMGRAIVRDP 152
Cdd:PRK14267 89 MVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 153 AVFLFDEPLSNLDAKLRVQMRSEIKELHQRLqtTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNN 227
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-225 |
3.26e-31 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 117.78 E-value: 3.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 13 YGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDR---DIAMVFQNYALYPH 89
Cdd:COG0410 13 YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 90 MTVAKNmgfsLRL---KRMPRTEIDQRvgnaakilgLESLLERYPK----------QLSGGQRQRVAMGRAIVRDPAVFL 156
Cdd:COG0410 93 LTVEEN----LLLgayARRDRAEVRAD---------LERVYELFPRlkerrrqragTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 157 FDEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-212 |
6.73e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 117.88 E-value: 6.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDR--DIAMVFQNYAL--YPHMTV 92
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakYIGRVFQDPMMgtAPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 93 AKNM----------GFSLRLKRMPRTEIDQRVgnaAKI-LGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:COG1101 100 EENLalayrrgkrrGLRRGLTKKRRELFRELL---ATLgLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 655334176 162 SNLDAKlrvqmRSEI-----KELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:COG1101 177 AALDPK-----TAALvleltEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-224 |
9.35e-31 |
|
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: 116.56 E-value: 9.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYPHmTVAKN 95
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MgfslrlkRMPRTEI-DQRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:cd03254 97 I-------RLGRPNAtDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 164 LDAKLRVQMRSEIKELHQrlQTTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:cd03254 170 IDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-193 |
9.60e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 116.13 E-value: 9.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 14 GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD-----RDIAMVFQNYALYP 88
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 89 HMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL 168
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180
....*....|....*....|....*
gi 655334176 169 RVQMRSEIKELHqRLQTTTIYVTHD 193
Cdd:PRK10908 173 SEGILRLFEEFN-RVGVTVLMATHD 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-210 |
1.19e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.28 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD-RD--IAMV 80
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAagIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPHMTVAKNMGFSLRLKRMPRteIDQRVGN--AAKIL---GLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVF 155
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGREPRRGGL--IDWRAMRrrARELLarlGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 156 LFDEPLSNLDAKlrvqmrsEIKELHQ---RLQ---TTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:COG1129 163 ILDEPTASLTER-------EVERLFRiirRLKaqgVAIIYISHRLDEVFEIADRVTVLRDG 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
17-212 |
1.59e-30 |
|
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: 115.05 E-value: 1.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKhivNELAPKDR--DIAMVFQN--YALYPHmTV 92
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERrkSIGYVMQDvdYQLFTD-SV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 93 AKNMGFSLRLKRMPRTEIDQrvgnAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQM 172
Cdd:cd03226 90 REELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 655334176 173 RSEIKELhQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:cd03226 166 GELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-230 |
2.39e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 117.13 E-value: 2.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKhivnELAPKDRD-IAmvf 81
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGE----PLDPEDRRrIG--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 82 qnY-----ALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFL 156
Cdd:COG4152 75 --YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 157 FDEPLSNLD---AKLrvqMRSEIKELHQRlQTTTIYVTH--DQIEAmtMADKIVVMKDGLIEQSGSPLELYDR--PNNLF 229
Cdd:COG4152 153 LDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHqmELVEE--LCDRIVIINKGRKVLSGSVDEIRRQfgRNTLR 226
|
.
gi 655334176 230 V 230
Cdd:COG4152 227 L 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-225 |
2.67e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 117.76 E-value: 2.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVN----ELAPKDRDIAMVFQN-YA-LYPH 89
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLKadpeAQKLLRQKIQIVFQNpYGsLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 90 MTVAKNMGFSLRLK-RMPRTEIDQRVGNAAKILGLES-LLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 167
Cdd:PRK11308 109 KKVGQILEEPLLINtSLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 168 LRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:PRK11308 189 VQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-223 |
1.33e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.46 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNyalyPH-----M 90
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQN----PDnqfvgS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRV 170
Cdd:PRK13648 100 IVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 655334176 171 QMRSEIKELHQRLQTTTIYVTHDQIEAMTmADKIVVMKDGLIEQSGSPLELYD 223
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-210 |
1.91e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 111.15 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYPHmTVAKNM 96
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLPQDDELFSG-SIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 gfslrlkrmprteidqrvgnaakilglesllerypkqLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEI 176
Cdd:cd03246 97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....
gi 655334176 177 KELHQRlQTTTIYVTHdQIEAMTMADKIVVMKDG 210
Cdd:cd03246 140 AALKAA-GATRIVIAH-RPETLASADRILVLEDG 171
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-216 |
3.79e-29 |
|
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: 117.83 E-value: 3.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYPHmTVAKNM 96
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 GfslrlkRMPRTEIDQRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:TIGR01842 413 A------RFGENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 655334176 166 AKLRVQMRSEIKELHQRlQTTTIYVTHdQIEAMTMADKIVVMKDGLIEQSG 216
Cdd:TIGR01842 487 EEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFG 535
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-216 |
6.04e-29 |
|
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: 117.16 E-value: 6.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHivnELAPKDRD-----IAMVFQNYALYPHmTVA 93
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGA---DLSQWDREelgrhIGYLPQDVELFDG-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 94 KNMGfslrlkRMPrtEID-QRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:COG4618 424 ENIA------RFG--DADpEKVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 162 SNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQiEAMTMADKIVVMKDGLIEQSG 216
Cdd:COG4618 496 SNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFG 548
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-210 |
2.00e-28 |
|
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: 109.18 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL--EGITSGQIQIGKHIVNELAPKDRdIAMVFQNYALYPHMTVAKNM 96
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 GFSLRLKrmprteidqrvgnaakilglesllerypkQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEI 176
Cdd:cd03213 104 MFAAKLR-----------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 655334176 177 KELHQrLQTTTIYVTHD-QIEAMTMADKIVVMKDG 210
Cdd:cd03213 155 RRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-224 |
3.18e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.98 E-value: 3.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNyalyPH----- 89
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGLVFQD----PDdqvfs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 90 MTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLR 169
Cdd:PRK13647 95 STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 170 VQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:PRK13647 175 ETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-225 |
3.43e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.39 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL-----EGITSGQI-----QIGKHIVNEL 70
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVyldgqDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 71 ApkdRDIAMVFQNYALYPHMTVAKNMGFSLRLKRM--PRTEIDQRVGNAAKILGL----ESLLERYPKQLSGGQRQRVAM 144
Cdd:PRK14247 81 R---RRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 145 GRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLqtTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
.
gi 655334176 225 P 225
Cdd:PRK14247 236 P 236
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-228 |
6.71e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 110.25 E-value: 6.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 16 FKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIG------KHIVNELAPKDRDIAMVFQnyalYPH 89
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDditithKTKDKYIRPVRKRIGMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 90 M-----TVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLE-SLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:PRK13646 96 SqlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 164 LDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNL 228
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-233 |
7.90e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.80 E-value: 7.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNE-LAPKDRDIAMVFQNY-ALYPHMTVAKN 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAEnVWNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSE 175
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 176 IKELHQRLQTTTIYVTHDQIEAMTmADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGF 233
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGL 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-252 |
8.99e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.92 E-value: 8.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKD-----RDIAMVFQ-------- 82
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHITPETGNKNlkklrKKVSLVFQfpeaqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 83 NYALYPHMTVAKNMGFSlrlkrmprteiDQRVGNAA----KILGL-ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLF 157
Cdd:PRK13641 101 NTVLKDVEFGPKNFGFS-----------EDEAKEKAlkwlKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 158 DEPLSNLDAKLRVQMRSEIKElHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLfVAGFIGSP 237
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKD-YQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWL-KKHYLDEP 247
|
250
....*....|....*
gi 655334176 238 AMNFISGSMTEDGFR 252
Cdd:PRK13641 248 ATSRFASKLEKGGFK 262
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-210 |
9.53e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.20 E-value: 9.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKhivnELAPKD-RD----- 76
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGK----PVRIRSpRDaialg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 77 IAMVFQNYALYPHMTVAKN--MGF-SLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPA 153
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENivLGLePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655334176 154 VFLFDEPLSNLDAKlrvqmrsEIKELHQRLQ------TTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:COG3845 162 ILILDEPTAVLTPQ-------EADELFEILRrlaaegKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-207 |
1.10e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 107.32 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 13 YGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHivnelapkdRDIAMVFQNYALYPHM-- 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------ARVAYVPQRSEVPDSLpl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAK--NMGF--SLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDA 166
Cdd:NF040873 73 TVRDlvAMGRwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 655334176 167 KLRVQMRSEIKELHQRlQTTTIYVTHDqIEAMTMADKIVVM 207
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHD-LELVRRADPCVLL 191
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-232 |
1.52e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.12 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL--------EGITSGQIQIGKHIVNELAPKdrdIAMVFQNY-ALYP 88
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWDIREK---VGIVFQNPdNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 89 HMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL 168
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 169 RVQMRSEIKELHQRLQTTTIYVTHDqIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAG 232
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHD-IDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIG 241
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-222 |
1.68e-27 |
|
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: 108.01 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDR---DIAMV 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEP 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 161 LSNLDAKlRVQmrsEIKELHQRLQTTTIYV---THDQIEAMTMADKIVVMKDGLIEQSGSPLELY 222
Cdd:cd03218 161 FAGVDPI-AVQ---DIQKIIKILKDRGIGVlitDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-224 |
1.91e-27 |
|
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: 112.89 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYPHmTVAK 94
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVALVSQDVVLFND-TIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 95 NMGFSlrlkrMPRTEIDQRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:TIGR02203 425 NIAYG-----RTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEATSA 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 164 LDAKLRVQMRSEIKELHQrlQTTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:TIGR02203 500 LDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-222 |
2.30e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.64 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIqigkhIVNELAPKDR----DI----AMVFQN-----Y 84
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-----YVDGLDTSDEenlwDIrnkaGMVFQNpdnqiV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 85 ALYPHMTVA---KNMGfslrlkrMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:PRK13633 100 ATIVEEDVAfgpENLG-------IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 162 SNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTmADKIVVMKDGLIEQSGSPLELY 222
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-212 |
4.10e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 112.12 E-value: 4.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 2 AHVSVNNARKDY----GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIV----NELAP 72
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVaGQDVAtldaDALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 73 KDRD-IAMVFQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRD 151
Cdd:PRK10535 83 LRREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 152 PAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIyVTHD-QIEAmtMADKIVVMKDGLI 212
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHDpQVAA--QAERVIEIRDGEI 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
7-216 |
7.03e-27 |
|
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: 106.08 E-value: 7.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 7 NNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKhivnelapkdRDIAMVFQNYAL 86
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------RVSSLLGLGGGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 87 YPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDA 166
Cdd:cd03220 96 NPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 655334176 167 KLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSG 216
Cdd:cd03220 176 AFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-221 |
1.30e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 105.92 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 3 HVSVNNarkdygafKAI-KGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEG--ITSGQIQI-GKHIvNELAPKDR--- 75
Cdd:COG0396 7 HVSVEG--------KEIlKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLdGEDI-LELSPDERara 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 76 DIAMVFQNYALYPHMTV------AKNmgfSLRLKRMPRTEIDQRVGNAAKILGL-ESLLERYPKQ-LSGGQRQRVAMGRA 147
Cdd:COG0396 78 GIFLAFQYPVEIPGVSVsnflrtALN---ARRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 148 IVRDPAVFLFDEPLSNLDA-KLRVqMRSEIKELHQRlQTTTIYVTH-----DQIEamtmADKIVVMKDGLIEQSGSPlEL 221
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHyqrilDYIK----PDFVHVLVDGRIVKSGGK-EL 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-257 |
1.34e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 106.74 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 15 AFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVN------ELAPKDRDIAMVFQnyalYP 88
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQ----FP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 89 HM-----TVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:PRK13643 94 ESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 163 NLDAKLRVQMRSEIKELHQRLQtTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPnNLFVAGFIGSPAMNFI 242
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEV-DFLKAHELGVPKATHF 251
|
250
....*....|....*
gi 655334176 243 SGSMTEDGFRTADGL 257
Cdd:PRK13643 252 ADQLQKTGAVTFEKL 266
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
19-193 |
2.55e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 104.48 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQ-IGK--HIVNE---LAPKDRDIAMVFQNYALYPHMTV 92
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlVGQplHQMDEearAKLRAKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 93 AKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQM 172
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180
....*....|....*....|.
gi 655334176 173 RSEIKELHQRLQTTTIYVTHD 193
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHD 206
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
15-220 |
2.72e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 106.32 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 15 AFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQ-IGKHIVNELAPKD------------------- 74
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwIFKDEKNKKKTKEkekvleklviqktrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 75 ------RDIAMVFQ--NYALYpHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMG 145
Cdd:PRK13651 99 kikeirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 146 RAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLE 220
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-220 |
2.75e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.10 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 13 YGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYPHM 90
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAKNMGFSlrlkRMP--------RTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:PRK11231 92 TVRELVAYG----RSPwlslwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 163 NLDAKLRVQMRSEIKELHQRLQtTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLE 220
Cdd:PRK11231 168 YLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-222 |
3.51e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.86 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 3 HVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIV-------NELAPKDR 75
Cdd:PRK13645 11 NVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkiKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 76 DIAMVFQ--NYALYPHmTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMGRAIVRDP 152
Cdd:PRK13645 91 EIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 153 AVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELY 222
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-228 |
3.97e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 105.27 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 14 GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNE-LAPKDRDIAMVFQN---YALYP 88
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKEnIREVRKFVGLVFQNpddQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 89 hmTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL 168
Cdd:PRK13652 95 --TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 169 RVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNL 228
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-226 |
6.01e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.68 E-value: 6.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEgitsgQIQIGKHIVNELAPKD--------RDIAMVFQN-YALYP 88
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLL-----RPQKGKVLVSGIDTGDfsklqgirKLVGIVFQNpETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 89 HMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL 168
Cdd:PRK13644 92 GRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 169 RVQMRSEIKELHQRLQtTTIYVTHDqIEAMTMADKIVVMKDGLIEQSGSPLELYDRPN 226
Cdd:PRK13644 172 GIAVLERIKKLHEKGK-TIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-224 |
7.01e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.62 E-value: 7.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 6 VNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELapkdrDIAMVFQnya 85
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL-----ELGAGFH--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 86 lyPHMTVAKNMGFSLRLKRMPRTEIDQRVgnaAKIL---GLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:COG1134 101 --PELTGRENIYLNGRLLGLSRKEIDEKF---DEIVefaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 163 NLDAKLRVQMRSEIKELHQRlQTTTIYVTHD--QIEamTMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:COG1134 176 VGDAAFQKKCLARIRELRES-GRTVIFVSHSmgAVR--RLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-202 |
1.17e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.58 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITS-----GQIQI-GKHI------VNELA 71
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFfNQNIyerrvnLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 72 pkdRDIAMVFQNYALYPhMTVAKNMGFSLRL-KRMPRTEIDQRVGNAAKILGL----ESLLERYPKQLSGGQRQRVAMGR 146
Cdd:PRK14258 88 ---RQVSMVHPKPNLFP-MSVYDNVAYGVKIvGWRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 655334176 147 AIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMAD 202
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
20-225 |
1.18e-25 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 108.12 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 20 KGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKhivnELAPKD-----RDIAMVFQNYALYP----- 88
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYdGQ----DLAGLDvqavrRQLGVVLQNGRLMSgsife 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 89 ------------HMTVAKNMGFSLRLKRMP---RTEIDQRVGNaakilglesllerypkqLSGGQRQRVAMGRAIVRDPA 153
Cdd:TIGR03797 546 niaggapltldeAWEAARMAGLAEDIRAMPmgmHTVISEGGGT-----------------LSGGQRQRLLIARALVRKPR 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 154 VFLFDEPLSNLDAKlrvqMRSEIKELHQRLQTTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:TIGR03797 609 ILLFDEATSALDNR----TQAIVSESLERLKVTRIVIAH-RLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-212 |
1.23e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 104.78 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 10 RKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIV----NELApkdRDIAMVF-QNY 84
Cdd:COG4586 29 RREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPfkrrKEFA---RRIGVVFgQRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 85 ALYPHMTVAKnmgfSLRLKR----MPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQR--VAMgrAIVRDPAVFLFD 158
Cdd:COG4586 106 QLWWDLPAID----SFRLLKaiyrIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRceLAA--ALLHRPKILFLD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 655334176 159 EPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHD--QIEAmtMADKIVVMKDGLI 212
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHGRI 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-218 |
1.79e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.93 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 5 SVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQ 82
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 83 nyalypHMTVAknmgFSL------RLKRMPRTEIDQRVGNAA----KILGLESLLERYPKQLSGGQRQRVAMGRAIVR-- 150
Cdd:PRK13548 84 ------HSSLS----FPFtveevvAMGRAPHGLSRAEDDALVaaalAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlw 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 151 ----DPAVFLFDEPLSNLDakLRVQ---MRSeIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSP 218
Cdd:PRK13548 154 epdgPPRWLLLDEPTSALD--LAHQhhvLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-221 |
1.85e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 103.14 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 13 YGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNyALYPHM 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQN-ATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAKNMGFSLRLKRMP-----RTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:PRK10253 96 ITVQELVARGRYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 655334176 166 AKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-228 |
2.08e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 103.23 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHI---VNELAPKDRDIAMVFQN-----YAlyP 88
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIkydKKSLLEVRKTVGIVFQNpddqlFA--P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 89 hmTVAKNMGFS-LRLKrMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 167
Cdd:PRK13639 95 --TVEEDVAFGpLNLG-LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 168 LRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNL 228
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-214 |
2.39e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.71 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKST----LLRMIAGLEGITSGQIQIGKHIVNELAPKDRDIAMVFQ--NYALYPHMT 91
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQdpNSSLNPRLN 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 92 VAKNMGFSLRL--KRMPRTEIDQRVGNAAKILGLE-SLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL 168
Cdd:PRK15134 381 VLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTV 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 655334176 169 RVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDG-LIEQ 214
Cdd:PRK15134 461 QAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGeVVEQ 507
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-210 |
2.83e-25 |
|
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: 101.01 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNA-----RKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIvnelapkdrdiA 78
Cdd:cd03250 1 ISVEDAsftwdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI-----------A 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 79 MVFQNyALYPHMTVAKNMGFSLR------------------LKRMP---RTEIDQRVGNaakilglesllerypkqLSGG 137
Cdd:cd03250 70 YVSQE-PWIQNGTIRENILFGKPfdeeryekvikacalepdLEILPdgdLTEIGEKGIN-----------------LSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 138 QRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ-MRSEIKElHQRLQTTTIYVTHdQIEAMTMADKIVVMKDG 210
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHiFENCILG-LLLNNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-221 |
3.42e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 106.47 E-value: 3.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 22 VSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITsGQIQIGKHIVNELAPKD--RDIAMVFQNYALyPHMTVAKNMgfS 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNV--L 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 100 LRLKRMPRTEIDQRVGNA-------AKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQM 172
Cdd:PRK11174 445 LGNPDASDEQLQQALENAwvseflpLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 655334176 173 RSEIKELHQrlQTTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:PRK11174 525 MQALNAASR--RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-226 |
6.13e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 101.77 E-value: 6.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 22 VSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIV----NELAPKDRDIAMVFQNYALYPHMTVAKNM 96
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIPamsrSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 GFSLRL-KRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSE 175
Cdd:PRK11831 106 AYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 655334176 176 IKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPN 226
Cdd:PRK11831 186 ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
29-223 |
6.72e-25 |
|
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: 100.70 E-value: 6.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 29 GEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKhivNELAPKDRDIAMVFQNYAL---YP---HMTVAKNMGFSLRL 102
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG---ASPGKGWRHIGYVPQRHEFawdFPisvAHTVMSGRTGHIGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 103 KRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQR 182
Cdd:TIGR03771 83 LRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELAGA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 655334176 183 lQTTTIYVTHDQIEAMTMADKIVVMkDGLIEQSGSPLELYD 223
Cdd:TIGR03771 163 -GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQD 201
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-213 |
6.90e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.39 E-value: 6.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 13 YGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL-----EGITSGQIQIGKHivNELAPKD------RDIAMVF 81
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGH--NIYSPRTdtvdlrKEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 82 QNYALYPhMTVAKNMGFSLRLKRMPRTEI-DQRVGNAAKILGL----ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFL 156
Cdd:PRK14239 93 QQPNPFP-MSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 157 FDEPLSNLDAKLRVQMRSEIKELHQrlQTTTIYVTHDQIEAMTMADKIVVMKDG-LIE 213
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGdLIE 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-225 |
9.63e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 101.40 E-value: 9.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVN--ELAPKDRDIAMVFQN--YALYPHMTV 92
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 93 AKNMGFSLRLK-RMPRTEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRV 170
Cdd:PRK15112 107 SQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 171 QMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:PRK15112 187 QLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-222 |
1.19e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.24 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 16 FKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIG----------KHIVNELAPKD--------RDI 77
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSKKiknfkelrRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 AMVFQ--NYALYPHmTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMGRAIVRDPAV 154
Cdd:PRK13631 119 SMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 155 FLFDEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELY 222
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-311 |
1.41e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.38 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIA 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 79 MVFQNYALYPHMTVAK--NMGFSLRLKRM-PRTEIDQR-VGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAV 154
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQvvEMGRTPHRSRFdTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 155 FLFDEPLSNLDAKLRVQMRseikELHQRL---QTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNnlFVA 231
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTL----ELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADT--LRA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 232 GFIGSPAM--NFISGSMTEDGFRTADGLLLPSERR--------PADAAIYgirpehiRLDPGGIEVTTVVVePTGSETLV 301
Cdd:PRK09536 235 AFDARTAVgtDPATGAPTVTPLPDPDRTEAAADTRvhvvgggqPAARAVS-------RLVAAGASVSVGPV-PEGDTAAE 306
|
330
....*....|.
gi 655334176 302 IV-RLGTQTLT 311
Cdd:PRK09536 307 TAaRVGCEAVT 317
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-193 |
2.17e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 6 VNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIgkhivnelaPKDRDIAMVFQNYA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 86 LYPHMTVAKN--MGFSLR---LKRMPRTE---------------------------IDQRVGNAAKILGL-ESLLERYPK 132
Cdd:COG0488 72 LDDDLTVLDTvlDGDAELralEAELEELEaklaepdedlerlaelqeefealggweAEARAEEILSGLGFpEEDLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 133 QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAklrvqmrsE-IKELHQRLQT---TTIYVTHD 193
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL--------EsIEWLEEFLKNypgTVLVVSHD 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-222 |
3.46e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.20 E-value: 3.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELApKDRDI-------AMVFQnyalYPH 89
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTS-KNKDIkqirkkvGLVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 90 M-----TVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:PRK13649 96 SqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 164 LDAKLRVQMRSEIKELHQrLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELY 222
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-217 |
4.52e-24 |
|
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: 98.37 E-value: 4.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 5 SVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDR---DIAMVF 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 82 QNYALYPHMTVAKN--MGFSLRLKRmpRTEIDQRVGNAAKILglESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDE 159
Cdd:TIGR03410 82 QGREIFPRLTVEENllTGLAALPRR--SRKIPDEIYELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 160 PLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGS 217
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-220 |
7.02e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 98.65 E-value: 7.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALyphmtvakNM 96
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSL--------AF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 GFS----LRLKRMP----RTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAI------VRDPAVFLF-DEPL 161
Cdd:COG4559 89 PFTveevVALGRAPhgssAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPRWLFlDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 162 SNLDakLRVQ---MRSeIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLE 220
Cdd:COG4559 169 SALD--LAHQhavLRL-ARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-210 |
8.06e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.91 E-value: 8.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIG---KHIVNELAPKDRDI 77
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqeMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 AMVFQNYALYPHMTVAKNmgfsLRLKRMP-------RTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVR 150
Cdd:PRK11288 82 AIIYQELHLVPEMTVAEN----LYLGQLPhkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 151 DPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-225 |
9.06e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.49 E-value: 9.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPK--DRDIAMVFQNYALYPHmTVAKNM 96
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 GFSLRlkrmpRTEIDQrVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:TIGR00958 576 AYGLT-----DTPDEE-IMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 166 AKLRvQMRSEIKELHQRlqtTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:TIGR00958 650 AECE-QLLQESRSRASR---TVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-212 |
9.09e-24 |
|
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: 97.79 E-value: 9.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 10 RKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD-RDIAMVF-QNYALY 87
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlRRIGVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 88 PHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 167
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 655334176 168 LRVQMRSEIKELHQRLQTTTIYVTHD--QIEAmtMADKIVVMKDGLI 212
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYmkDIEA--LARRVLVIDKGRL 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-225 |
9.94e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 102.24 E-value: 9.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 10 RKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKS-TLLRMIAGLEGiTSGQIQIGKHI-------VNELAPKDR------ 75
Cdd:PRK10261 23 MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMLlrrrsrqVIELSEQSAaqmrhv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 76 ---DIAMVFQN--YALYPHMTVAKNMGFSLRLKR-MPRTEI---DQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGR 146
Cdd:PRK10261 102 rgaDMAMIFQEpmTSLNPVFTVGEQIAESIRLHQgASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAM 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 147 AIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
1.17e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.11 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 2 AHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRD-IAMV 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEP 160
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 161 LSNLDAKLRVQMRSEIKELHQRLQTTTIyVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGKTILL-TTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-210 |
1.77e-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: 96.73 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI--GKHIVNELAPKDRDIAMVFQNYALY-------- 87
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREILALRRRTIGYvsqflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 88 PHMT----VAKnmgfSLRLKRMPRTEIDQRVGNAAKILGL-ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:COG4778 106 PRVSaldvVAE----PLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 655334176 163 NLDAKLRVQMRSEIKELHQRlQTTTIYVTHDqIEAM-TMADKIVVMKDG 210
Cdd:COG4778 182 SLDAANRAVVVELIEEAKAR-GTAIIGIFHD-EEVReAVADRVVDVTPF 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-216 |
1.87e-23 |
|
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: 96.57 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 9 ARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL---EGITSGQIQI-GKHIVNELAPKDrdIAMVFQNY 84
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFnGQPRKPDQFQKC--VAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 85 ALYPHMTVAKNMGFSLRLkRMPRT----EIDQRVGNAA-KILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDE 159
Cdd:cd03234 91 ILLPGLTVRETLTYTAIL-RLPRKssdaIRKKRVEDVLlRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 160 PLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSG 216
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
19-221 |
2.23e-23 |
|
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: 101.36 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPK--DRDIAMVFQNYALYPHmTVAKNM 96
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIRDNI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 gfSLRLKRMPrteiDQRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:TIGR01846 552 --ALCNPGAP----FEHVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEATSALD 625
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 655334176 166 AKLRVQMRSEIKELHQrlQTTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:TIGR01846 626 YESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-226 |
2.37e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.64 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGkhivnelapkDRDI--- 77
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLD----------GEDIthl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 ----------------AMVFQNyalyphMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQR 141
Cdd:COG1137 71 pmhkrarlgigylpqeASIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 142 VAMGRAIVRDPAVFLFDEPLSNLDAkLRVqmrSEIKELHQRLQTTTIYV--T-HDQIEAMTMADKIVVMKDGLIEQSGSP 218
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDP-IAV---ADIQKIIRHLKERGIGVliTdHNVRETLGICDRAYIISEGKVLAEGTP 220
|
....*...
gi 655334176 219 LELYDRPN 226
Cdd:COG1137 221 EEILNNPL 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-206 |
3.11e-23 |
|
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: 96.71 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 11 KDYGAFK--AIKGvsvDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIgkhIVNELAPKDRDIAMVFQNYALYP 88
Cdd:cd03237 8 KTLGEFTleVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI---ELDTVSYKPQYIKADYEGTVRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 89 HMTVAKNMGFSLRLKrmprTEIdqrvgnaAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL 168
Cdd:cd03237 82 LSSITKDFYTHPYFK----TEI-------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 655334176 169 RVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVV 206
Cdd:cd03237 151 RLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-229 |
3.78e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.77 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 13 YGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGK---HIVNELAPK------DRDIAMVFQN 83
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKvtfHGKNLYAPDvdpvevRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHmTVAKNMGFSLRLKRMpRTEIDQRVGNAAKILGLESLLERYPKQ----LSGGQRQRVAMGRAIVRDPAVFLFDE 159
Cdd:PRK14243 100 PNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 160 PLSNLDAKLRVQMRSEIKELHQrlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLEL--YDRPNNLF 229
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLveFDRTEKIF 247
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-234 |
5.92e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 96.27 E-value: 5.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-------GKHIVNELAPKDR-DIAMVFQNYALYPHM 90
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkvlyfGKDIFQIDAIKLRkEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAKNMGFSLRLKRMP-RTEIDQRVGNAAKILGL----ESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 166 AKLRVQMRSEIKELHQRLqtTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFI 234
Cdd:PRK14246 186 IVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-221 |
1.17e-22 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 99.12 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 20 KGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYpHMTVAKNMG 97
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAYNIA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 98 FSlrlkrmpRTEIDQR-VGNAAKILGLESLLERYPKQ-----------LSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:COG5265 454 YG-------RPDASEEeVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 166 AKLRVQMRSEIKELHQRlqTTTIYVTH------DqieamtmADKIVVMKDGLIEQSGSPLEL 221
Cdd:COG5265 527 SRTERAIQAALREVARG--RTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAEL 579
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-216 |
1.63e-22 |
|
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: 92.76 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPkdrdiamvfqnyalyphmTVAKNM 96
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK------------------ALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 GFslrlkrmprteIDQRVgnaakILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEI 176
Cdd:cd03247 78 SV-----------LNQRP-----YLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 655334176 177 -KELHQRlqtTTIYVTHdQIEAMTMADKIVVMKDGLIEQSG 216
Cdd:cd03247 142 fEVLKDK---TLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-166 |
1.86e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.40 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 20 KGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIqigkhivnELAPKDRDIAMVF--------QNyALYPHMT 91
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI--------KLDGGDIDDPDVAeachylghRN-AMKPALT 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 92 VAKNMGFSLRLKRMPRTEIDQrvgnAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDA 166
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
18-222 |
1.99e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNE----LAPKDRDIAMVFQ--NYALYPhMT 91
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkgLMKLRESVGMVFQdpDNQLFS-AS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 92 VAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ 171
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 655334176 172 MRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELY 222
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-192 |
2.05e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 98.34 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIgkhivnelaPKDRDIAMVFQN-Y--------AL-YP 88
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQRpYlplgtlreALlYP 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 89 HmtvaknmgfslrlkrmPRTEI-DQRVGNAAKILGLESLLERY------PKQLSGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:COG4178 450 A----------------TAEAFsDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|..
gi 655334176 162 SNLDAKLRVQMrseIKELHQRLQTTT-IYVTH 192
Cdd:COG4178 514 SALDEENEAAL---YQLLREELPGTTvISVGH 542
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-224 |
2.23e-22 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 94.09 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPK--DRDIAMVFQNYALYpHMTVAKN 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MgfSLRLKRMPRteidQRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:cd03252 96 I--ALADPGMSM----ERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 165 DAKlrvQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:cd03252 170 DYE---SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-207 |
2.36e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 14 GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYPHmT 91
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 92 VAKNMGFSLRLkRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ 171
Cdd:PRK10247 97 VYDNLIFPWQI-RNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHN 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 655334176 172 MRSEIKELHQRLQTTTIYVTHDQIEaMTMADKIVVM 207
Cdd:PRK10247 176 VNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-225 |
2.50e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 95.96 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYG----AFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL----EGITSGQIQIGKHIVNELAP 72
Cdd:PRK11022 1 MALLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 73 KDR------DIAMVFQN--YALYPHMTVAKNMGFSLRLKRM-PRTEIDQRVGNAAKILGL---ESLLERYPKQLSGGQRQ 140
Cdd:PRK11022 81 KERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 141 RVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLE 220
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
....*
gi 655334176 221 LYDRP 225
Cdd:PRK11022 241 IFRAP 245
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-221 |
3.93e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.40 E-value: 3.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNE--LAPKDRDIAMVFQNYALYpHMTVAKN 95
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVALVSQNVHLF-NDTIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MGFSlRLKRMPRTEIDQrvgnAAKIL-----------GLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:PRK11176 437 IAYA-RTEQYSREQIEE----AARMAyamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 165 DAKLRVQMRSEIKELHQrlQTTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:PRK11176 512 DTESERAIQAALDELQK--NRTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
4.40e-22 |
|
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: 97.18 E-value: 4.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGI--TSGQI-----------------QIG- 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpsKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 64 --KHIVNELAPKDRD---------------IAMVFQ-NYALYPHMTVAKNMgfslrLKRMPRT--EIDQRVGNAAKILGL 123
Cdd:TIGR03269 81 pcPVCGGTLEPEEVDfwnlsdklrrrirkrIAIMLQrTFALYGDDTVLDNV-----LEALEEIgyEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 124 ESLLERY---PKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTH--DQIEam 198
Cdd:TIGR03269 156 VQLSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpEVIE-- 233
|
250 260
....*....|....*....|....*.
gi 655334176 199 TMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-225 |
4.47e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.23 E-value: 4.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKST----LLRMIAGLEG-ITSGQIQIGKHIVNELAPKDRDIAMVFQN-YA-LYPHM 90
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVESQGGeIIFNGQRIDTLSPGKLQALRRDIQFIFQDpYAsLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAKNMGFSLRLKRMPRTEIDQ-RVGNAAKILGLE-SLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL 168
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKAAAaRVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 169 RVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-212 |
4.64e-22 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 92.92 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPK--DRDIAMVFQNYALYPHmTVAKNM 96
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 GFSLRLKRMPR-TEIDQRVGNAAKILGLES-----LLERyPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRV 170
Cdd:cd03248 109 AYGLQSCSFECvKEAAQKAHAHSFISELASgydteVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 655334176 171 QMRSEIKELHQRlqTTTIYVTHdQIEAMTMADKIVVMKDGLI 212
Cdd:cd03248 188 QVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-217 |
5.24e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.54 E-value: 5.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL---EGITSGQIQIGKHIVNELAPKDRDI--- 77
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIrks 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 ----AMVFQNYALYPHMTVAKNMGFSlRLKRMP--RT-------EIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAM 144
Cdd:PRK09984 85 rantGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwRTcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 145 GRAIVRDPAVFLFDEPLSNLDAK-LRVQMRSeIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGS 217
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPEsARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-223 |
6.06e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.90 E-value: 6.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKDRDIAMVFQ 82
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 83 NYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 163 NLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYD 223
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-213 |
1.31e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIvnELA--PKDRDiamvf 81
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV--KIGyfDQHQE----- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 82 qnyALYPHMTVAKNMG--------FSLR--LKRM--PRTEIDQRVGNaakilglesllerypkqLSGGQRQRVAMGRAIV 149
Cdd:COG0488 389 ---ELDPDKTVLDELRdgapggteQEVRgyLGRFlfSGDDAFKPVGV-----------------LSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 150 RDPAVFLFDEPLSNLDaklrVQMRSEIKELhqrLQT---TTIYVTHDQ--IEamTMADKIVVMKDGLIE 213
Cdd:COG0488 449 SPPNVLLLDEPTNHLD----IETLEALEEA---LDDfpgTVLLVSHDRyfLD--RVATRILEFEDGGVR 508
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
19-225 |
1.52e-21 |
|
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: 95.78 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELaPKDR---DIAMVFQNYALYpHMTVAKN 95
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVAMVDQDIFLF-EGTVRDN 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MgfSLRLKRMPRTEIDQRVGNAA---KIL----GLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAkl 168
Cdd:TIGR03796 573 L--TLWDPTIPDADLVRACKDAAihdVITsrpgGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDP-- 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 169 rvQMRSEIKELHQRLQTTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:TIGR03796 649 --ETEKIIDDNLRRRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-224 |
1.89e-21 |
|
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: 95.58 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNArkdYGAfKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELapkDRDIAMV 80
Cdd:TIGR01193 476 INDVSYSYG---YGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNY-ALYPHM---TVAKNmgfsLRLKRMPRTEIDQ--RVGNAAKI--------LGLESLLERYPKQLSGGQRQRVAMGR 146
Cdd:TIGR01193 549 FINYlPQEPYIfsgSILEN----LLLGAKENVSQDEiwAACEIAEIkddienmpLGYQTELSEEGSSISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 147 AIVRDPAVFLFDEPLSNLDAKLRvqmRSEIKELHQRLQTTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITE---KKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-192 |
2.08e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 90.50 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 21 GVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPK-DRDIAMVFQNYALYPHMTVAKNMGFS 99
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 100 LRLKRMPRTEIDqrvgNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKlRVQMRSEIKEL 179
Cdd:TIGR01189 98 AAIHGGAQRTIE----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAGLLRA 172
|
170
....*....|...
gi 655334176 180 HQRLQTTTIYVTH 192
Cdd:TIGR01189 173 HLARGGIVLLTTH 185
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-221 |
3.77e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.73 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIA-----GLEGitSGQIQIGKHIVNelAPKDRDI-AMVFQNYALYPHMTV 92
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkGVKG--SGSVLLNGMPID--AKEMRAIsAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 93 AKNMGFS--LRLKR-MPRTEIDQRVGNAAKILGLESL------LERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:TIGR00955 117 REHLMFQahLRMPRrVTKKEKRERVDEVLQALGLRKCantrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 164 LDAKLRVQMRSEIKELHQRlqTTTIYVTHDQ--IEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQK--GKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-193 |
7.01e-21 |
|
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: 93.58 E-value: 7.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 14 GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYpHMT 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 92 VAKNmgfsLRLKRMPRTeiDQRVGNAAKILGLESLLERYP-----------KQLSGGQRQRVAMGRAIVRDPAVFLFDEP 160
Cdd:TIGR02868 425 VREN----LRLARPDAT--DEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|...
gi 655334176 161 LSNLDAKLRVQMRSEIKELHQRLqtTTIYVTHD 193
Cdd:TIGR02868 499 TEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-218 |
7.33e-21 |
|
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: 89.48 E-value: 7.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKST----LLRMIAglegITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYPHmT 91
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVE----LSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 92 VAKNMGFslrLKRMPRTEIDQ---RVGN----AAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:cd03244 94 IRSNLDP---FGEYSDEELWQaleRVGLkefvESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 655334176 165 DAKLRVQMRSEIKElhQRLQTTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSP 218
Cdd:cd03244 171 DPETDALIQKTIRE--AFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-225 |
1.17e-20 |
|
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: 89.89 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-----GKHIVNELAPKDR--- 75
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERrrl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 76 ---DIAMVFQNYALYPHMTVAKNMGFSLRL----------------KRMPRTEIDQrvgnaakilgleSLLERYPKQLSG 136
Cdd:TIGR02323 84 mrtEWGFVHQNPRDGLRMRVSAGANIGERLmaigarhygnirataqDWLEEVEIDP------------TRIDDLPRAFSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 137 GQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSG 216
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
....*....
gi 655334176 217 SPLELYDRP 225
Cdd:TIGR02323 232 LTDQVLDDP 240
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
1.87e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.78 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPK--DRDI 77
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFdGKDITDWQTAKimREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 AMVFQNYALYPHMTVAKNM---GFSLRlkrmpRTEIDQRVgnaAKILGL-ESLLERYPKQ---LSGGQRQRVAMGRAIVR 150
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLamgGFFAE-----RDQFQERI---KWVYELfPRLHERRIQRagtMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 151 DPAVFLFDEPLSNLDAKLRVQMRSEIKELhqRLQTTTIY-VTHDQIEAMTMADKIVVMKDG--LIEQSGSPL 219
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQL--REQGMTIFlVEQNANQALKLADRGYVLENGhvVLEDTGDAL 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-216 |
2.05e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.21 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 5 SVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-----GKHIVNELAPKDR---- 75
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgQLRDLYALSEAERrrll 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 76 --DIAMVFQNYA--LYPHMTVAKNMGFSL---------RLKR-----MPRTEIDqrvgnAAKILGLeslleryPKQLSGG 137
Cdd:PRK11701 88 rtEWGFVHQHPRdgLRMQVSAGGNIGERLmavgarhygDIRAtagdwLERVEID-----AARIDDL-------PTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 138 QRQRVAMGRAIVRDPAVFLFDEPLSNLDakLRVQMR--SEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQS 215
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLD--VSVQARllDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
.
gi 655334176 216 G 216
Cdd:PRK11701 234 G 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-210 |
2.87e-20 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 86.72 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRD---IAMV---FQNYALYPHM 90
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVpedRKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAKNMGFSLrlkrmprteidqrvgnaakilglesllerypkQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD--AKl 168
Cdd:cd03215 94 SVAENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDvgAK- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 655334176 169 rvqmrseiKELHQRLQ------TTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:cd03215 141 --------AEIYRLIReladagKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-221 |
3.23e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.81 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD-RD-IAMVFQNYALYPHmtvak 94
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaISVVSQRVHLFSA----- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 95 nmgfSLR--LKRMPRTEIDQRVGNAAKILGLESLLERYP----------KQLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:PRK11160 429 ----TLRdnLLLAAPNASDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 163 NLDAKLRVQMRSEIKELHQrlQTTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:PRK11160 505 GLDAETERQILELLAEHAQ--NKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-225 |
5.76e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 5.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKS----TLLRMIAGLEGI-TSGQIQI-GKHIVNELAPKDR-----DIAMVFQN--YA 85
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFhGESLLHASEQTLRgvrgnKIAMIFQEpmVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 86 LYPHMTVAKNMGFSLRLKR-----MPRTEIDQ---RVG--NAAKILGleslleRYPKQLSGGQRQRVAMGRAIVRDPAVF 155
Cdd:PRK15134 105 LNPLHTLEKQLYEVLSLHRgmrreAARGEILNcldRVGirQAAKRLT------DYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 156 LFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-236 |
8.16e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 88.63 E-value: 8.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 14 GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL---EGITSGQIQI-GKHIVNeLAPKD------RDIAMVFQN 83
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFnGREILN-LPEKElnklraEQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 --YALYPHMTVAKNMGFSLRL-KRMPRTEIDQ---RVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLF 157
Cdd:PRK09473 106 pmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEesvRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 158 DEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGFIGS 236
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNA 264
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-233 |
2.63e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.21 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL----EGITSGQIQIGKHIVNELAPKDRDIAMVFQNYALYPHMT-VA 93
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLlrpqKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPEQQIFYTdID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 94 KNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMR 173
Cdd:PRK13638 97 SDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 174 SEIKELHQRLQTTTIyVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLFVAGF 233
Cdd:PRK13638 177 AIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-210 |
3.17e-19 |
|
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: 84.62 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 8 NARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGIT---SGQIQIGKHIVNELAPK-DRDIAMVFQN 83
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKyPGEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHMTVAKNMGFSLRLKrmprteidqrvGNAakilglesllerYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:cd03233 92 DVHFPTLTVRETLDFALRCK-----------GNE------------FVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 655334176 164 LDAKLRVQMRSEIKELHQRLQTTTI---YVTHDQIEAMTmaDKIVVMKDG 210
Cdd:cd03233 149 LDSSTALEILKCIRTMADVLKTTTFvslYQASDEIYDLF--DKVLVLYEG 196
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-192 |
3.32e-19 |
|
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: 83.36 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIgkhivnelaPKDRDIAMVFQNyalyPHMTVAknmgf 98
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR----PYLPLG----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 99 SLRlkrmprteidqrvgnaakilglESLLerYP--KQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEI 176
Cdd:cd03223 79 TLR----------------------EQLI--YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170
....*....|....*.
gi 655334176 177 KELHqrlqTTTIYVTH 192
Cdd:cd03223 135 KELG----ITVISVGH 146
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-210 |
3.33e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.69 E-value: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDR---DIAMV 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPHMTVAKNM--GFSLRLKRMPRTEID-----QRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPA 153
Cdd:PRK09700 86 YQELSVIDELTVLENLyiGRHLTKKVCGVNIIDwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 154 VFLFDEPLSNLDAK-------LRVQMRSEIKELhqrlqtttIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:PRK09700 166 VIIMDEPTSSLTNKevdylflIMNQLRKEGTAI--------VYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-210 |
4.48e-19 |
|
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: 82.50 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIvnelapkdrdiamvfqn 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 yalyphmtvaknmgfslrlkrmprteidqRVGnaakilglesllerYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:cd03221 64 -----------------------------KIG--------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 655334176 164 LDAKLRVQMRSEIKELHQrlqtTTIYVTHDQ--IEAmtMADKIVVMKDG 210
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDRyfLDQ--VATKIIELEDG 143
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-224 |
5.29e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 88.09 E-value: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHI--VNeLAPKDRDIAMVFQNYALYpHMTVAK 94
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIrtVT-RASLRRNIAVVFQDAGLF-NRSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 95 NmgfsLRLKRMPRTEIDQRvgNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:PRK13657 428 N----IRVGRPDATDEEMR--AAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 164 LDAKLRVQMRSEIKEL-HQRlqtTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:PRK13657 502 LDVETEAKVKAALDELmKGR---TTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-235 |
1.01e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.76 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 34 LVGPSGCGKSTLLRMIAGLEGITSGQ------IQIGKHIVN--ELAPKDRDIAMVFQNYALYPhMTVAKNMGFSLRLKRM 105
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGYrysgdvLLGGRSIFNyrDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 106 -PRTEI----DQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELH 180
Cdd:PRK14271 131 vPRKEFrgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 181 QRLqtTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNL----FVAGFIG 235
Cdd:PRK14271 211 DRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetarYVAGLSG 267
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-223 |
1.22e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.64 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAP---KDRDIAMV 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPHMTVAKNMGFslrlkRMPRTEID-QRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDE 159
Cdd:PRK15439 92 PQEPLLFPNLSVKENILF-----GLPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 160 PLSNLDAKLRVQMRSEIKELhQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYD 223
Cdd:PRK15439 167 PTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST 229
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-192 |
1.59e-18 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 82.97 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 26 IGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHivNELAPKDRDIAMVFQNYALYPHMTVAKNMGF-----S 99
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKT--ATRGDRSRFMAYLGHLPGLKADLSTLENLHFlcglhG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 100 LRLKRMPrteidqrvGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKlRVQMRSEIKEL 179
Cdd:PRK13543 112 RRAKQMP--------GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLVNRMISA 182
|
170
....*....|...
gi 655334176 180 HQRLQTTTIYVTH 192
Cdd:PRK13543 183 HLRGGGAALVTTH 195
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-225 |
4.50e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.35 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 13 YGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKDRDIAMV--FQNYALYPH 89
Cdd:PRK11300 15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLrGQHIEGLPGHQIARMGVVrtFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 90 MTVAKNM----------GFSLRLKRMP---RTEiDQRVGNAAKIL---GLESLLERYPKQLSGGQRQRVAMGRAIVRDPA 153
Cdd:PRK11300 95 MTVIENLlvaqhqqlktGLFSGLLKTPafrRAE-SEALDRAATWLervGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 154 VFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-233 |
4.65e-18 |
|
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: 85.84 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIG-KHIVNELAPKDRDIAMVFQNYALYPHMTVAKNM 96
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGgKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 GFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEI 176
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 177 keLHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELydrpNNLFVAGF 233
Cdd:TIGR01257 1105 --LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-228 |
8.60e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.43 E-value: 8.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 21 GVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLegiTSGQIQI---GKHI----VNELApkdRDIAMVFQNYALYPHMTVA 93
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGL---LPGQGEIllnGRPLsdwsAAELA---RHRAYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 94 KNMGFSLRLKrMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVR-DPAV------FLFDEPLSNLDA 166
Cdd:COG4138 88 QYLALHQPAG-ASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvWPTInpegqlLLLDEPMNSLDV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 167 KLRVQMRSEIKELHQrLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDrPNNL 228
Cdd:COG4138 167 AQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT-PENL 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-210 |
2.24e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 82.95 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL--EGITSGQIQIGKHIVNELAPKDRD---IA 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTEragIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 79 MVFQNYALYPHMTVAKN--MGFSLRLK--RMPRTEIDQRVGNAAKILGLESL-LERYPKQLSGGQRQRVAMGRAIVRDPA 153
Cdd:TIGR02633 82 IIHQELTLVPELSVAENifLGNEITLPggRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 154 VFLFDEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-210 |
2.89e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.67 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 7 NNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL--------EGITSGQIQIGKHIvnelapkdRD-- 76
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyegEIIFEGEELQASNI--------RDte 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 77 ---IAMVFQNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKIL---GLESLLERYPKQLSGGQRQRVAMGRAIVR 150
Cdd:PRK13549 81 ragIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLaqlKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 151 DPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
29-221 |
3.93e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.22 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 29 GEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPK--DRDIAMVFQNYALYPHMTVAKNMGfslrLKRMP 106
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMTVRELVA----IGRYP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 107 --------RTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKE 178
Cdd:PRK10575 113 whgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHR 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 655334176 179 LHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:PRK10575 193 LSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-225 |
6.99e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.97 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKS----TLLRMI-AGLEgITSGQIQIGKHIVNELAPKDRDIAMVFQN--YALYPHMT 91
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVR-QTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 92 VAKNMGFSLRLKRMPRTeiDQRVGNAAKILGLES---LLERYPKQLSGGQRQRVAMGRAIVRDpAVFLF-DEPLSNLDAK 167
Cdd:PRK10418 98 MHTHARETCLALGKPAD--DATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCE-APFIIaDEPTTDLDVV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 168 LRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:PRK10418 175 AQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-210 |
9.55e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.46 E-value: 9.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLegiTSGQIQIGKHIVNELAPKD---RDIAMVFQNYALYPHMTVAKN 95
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGR---IQGNNFTGTILANNRKPTKqilKRTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MGFsLRLKRMPRTEIDQrvgnaAKILGLESLLER--------------YPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:PLN03211 161 LVF-CSLLRLPKSLTKQ-----EKILVAESVISElgltkcentiignsFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 655334176 162 SNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-212 |
9.74e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.83 E-value: 9.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD---RDIAMVFQN---YALYPHM 90
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVPEDrkgEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAKNMGFSL-----RLKRMPRTEIDQRVGNAAKILGLeslleRYP------KQLSGGQRQRVAMGRAIVRDPAVFLFDE 159
Cdd:COG1129 346 SIRENITLASldrlsRGGLLDRRRERALAEEYIKRLRI-----KTPspeqpvGNLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 160 PLSNLD--AKlrvqmrSEIKELHQRL---QTTTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:COG1129 421 PTRGIDvgAK------AEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-224 |
1.17e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 77.18 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 3 HVSVNNarkdygafKAI-KGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEG--ITSGQIQIGKHIVNELAPKDR---D 76
Cdd:cd03217 7 HVSVGG--------KEIlKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 77 IAMVFQNYALYPHMTVAK-----NMGFslrlkrmprteidqrvgnaakilglesllerypkqlSGGQRQRVAMGRAIVRD 151
Cdd:cd03217 79 IFLAFQYPPEIPGVKNADflryvNEGF------------------------------------SGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 152 PAVFLFDEPLSNLDAK-LRVQMRsEIKELHQRlQTTTIYVTH-DQIEAMTMADKIVVMKDGLIEQSGsPLELYDR 224
Cdd:cd03217 123 PDLAILDEPDSGLDIDaLRLVAE-VINKLREE-GKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-221 |
1.22e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNEL---APKDRDI 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 AMVFQNYALYPHMTVAKNMGFSLRLKRMPRTEidQRVGNAAKIL---GLESLLERYPKQLSGGQRQRVAMGRAIVRDPAV 154
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAE--QREDRANELMeefHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 155 FLFDEPLSNLDAKLRVQMRSEIKelHQRLQTTTIYVT-HDQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIE--HLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
10-206 |
1.90e-16 |
|
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: 80.21 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 10 RKDYGAFKaikgVSVDIGD---GEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIqigkhivnelaPKDRDIAMVFQnyal 86
Cdd:COG1245 348 TKSYGGFS----LEVEGGEireGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLKISYKPQ---- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 87 YP----HMTVAKNMgFSLRLKRMP----RTEIdqrvgnaAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFD 158
Cdd:COG1245 409 YIspdyDGTVEEFL-RSANTDDFGssyyKTEI-------IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 655334176 159 EPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDqIEAMTM-ADKIVV 206
Cdd:COG1245 481 EPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD-IYLIDYiSDRLMV 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-206 |
4.24e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKaikgVSVDIGD---GEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQigkhivnelapKDRDIAMV 80
Cdd:PRK13409 341 VEYPDLTKKLGDFS----LEVEGGEiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-----------PELKISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 FQNYALYPHMTVAKNmgfslrLKRMP--------RTEIdqrvgnaAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDP 152
Cdd:PRK13409 406 PQYIKPDYDGTVEDL------LRSITddlgssyyKSEI-------IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 655334176 153 AVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVV 206
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
4-210 |
8.48e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 75.45 E-value: 8.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGA-FKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRD------ 76
Cdd:cd03290 1 VQVTNGYFSWGSgLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrys 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 77 IAMVFQNYALYpHMTVAKNMGFSLRLKRmprteidQRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMG 145
Cdd:cd03290 81 VAYAAQKPWLL-NATVEENITFGSPFNK-------QRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655334176 146 RAIVRDPAVFLFDEPLSNLDAKLRVQ-MRSEIKELHQRLQTTTIYVTHdQIEAMTMADKIVVMKDG 210
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-224 |
9.08e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 78.83 E-value: 9.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIgkhivnelapkDRDIAMVFQNyALYPHMTVAKNMGF 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----------KGSVAYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 99 SLRLKRmPRTeidQRVGNAAKILgleSLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 167
Cdd:TIGR00957 722 GKALNE-KYY---QQVLEACALL---PDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 168 LRVQMRSEIKELHQRLQTTT-IYVTHDqIEAMTMADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:TIGR00957 795 VGKHIFEHVIGPEGVLKNKTrILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-165 |
1.50e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.86 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 13 YGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKhivnELAPKDRDIAM----VFQNYALY 87
Cdd:NF033858 276 FGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfGQ----PVDAGDIATRRrvgyMSQAFSLY 351
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 88 PHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:NF033858 352 GELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-225 |
1.95e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 76.10 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 14 GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEG----ITSGQIQIGKHIVNELAPKDR------DIAMVFQN 83
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 --YALYPHMTVAKNMGFSL---------------RLKRMprTEIDQRVGnaakILGLESLLERYPKQLSGGQRQRVAMGR 146
Cdd:COG4170 98 psSCLDPSAKIGDQLIEAIpswtfkgkwwqrfkwRKKRA--IELLHRVG----IKDHKDIMNSYPHELTEGECQKVMIAM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 147 AIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQrLQTTTI-YVTHDqIEAMT-MADKIVVMKDGLIEQSGSPLELYDR 224
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQ-LQGTSIlLISHD-LESISqWADTITVLYCGQTVESGPTEQILKS 249
|
.
gi 655334176 225 P 225
Cdd:COG4170 250 P 250
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-174 |
1.99e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.07 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 21 GVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPK-DRDIAMVFQNYALYPHMTVAKNMGFS 99
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 100 LRLKRmprteiDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD----AKLRVQMRS 174
Cdd:cd03231 98 HADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARFAEAMAG 170
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-217 |
2.28e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.51 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 22 VSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQigkhivnelapKDRDIAMVFQNyALYPHMTVAKNMGF--- 98
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILFfde 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 99 --SLRLK---RMPRTEID-QRVGNaakilGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL--RV 170
Cdd:PTZ00243 747 edAARLAdavRVSQLEADlAQLGG-----GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeRV 821
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 655334176 171 QMRSEIKELHQRlqtTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGS 217
Cdd:PTZ00243 822 VEECFLGALAGK---TRVLATH-QVHVVPRADYVVALGDGRVEFSGS 864
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-218 |
2.83e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIqigkhivnELAPKDRdIAMVFQN 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR-IGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHM--TVAKNMgfslRLKrmPRTEiDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:PRK09544 76 LYLDTTLplTVNRFL----RLR--PGTK-KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 162 SNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMkDGLIEQSGSP 218
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTP 204
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-207 |
2.88e-15 |
|
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: 74.71 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 28 DGEFVVLVGPSGCGKSTLLRMIAGlegitSGQIQIGKHivnELAPKDRDIAMVFQNYALYPHMTVAKNMGFSLRLK---- 103
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAG-----KLKPNLGKF---DDPPDWDEILDEFRGSELQNYFTKLLEGDVKVIVKpqyv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 104 -RMPRTeIDQRVGN-------------AAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLR 169
Cdd:cd03236 97 dLIPKA-VKGKVGEllkkkdergkldeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 655334176 170 VQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVM 207
Cdd:cd03236 176 LNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
12-202 |
3.71e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.06 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 12 DYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKDRDIAMVFQNYALYPHM 90
Cdd:PRK13540 10 DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKKDLCTYQKQLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAKNMGFSLRLKRMpRTEIDQRVgnaaKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRV 170
Cdd:PRK13540 90 TLRENCLYDIHFSPG-AVGITELC----RLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180 190
....*....|....*....|....*....|..
gi 655334176 171 QMRSEIKElhQRLQTTTIYVTHDQIEAMTMAD 202
Cdd:PRK13540 165 TIITKIQE--HRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-167 |
3.99e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 21 GVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIqigkHIVNELAPKDRDiamVFQNYALY--------PHMTV 92
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV----LWQGEPIRRQRD---EYHQDLLYlghqpgikTELTA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 93 AKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERypkQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 167
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVR---QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-225 |
4.16e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.29 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYPHmTVAKN 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MGfslrLKRMPRTEidQRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:PRK10789 409 IA----LGRPDATQ--QEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 165 DAKLRVQMrseIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRP 225
Cdd:PRK10789 483 DGRTEHQI---LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-224 |
5.03e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.32 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVN-----ELAPKdrdI 77
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlGGDMADarhrrAVCPR---I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 AMVFQ----NyaLYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPA 153
Cdd:NF033858 79 AYMPQglgkN--LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 154 VFLFDEPLSNLDAKLRVQMRSEIKEL-HQRLQTTTIYVTHDQIEAMTMaDKIVVMKDGLIEQSGSPLELYDR 224
Cdd:NF033858 157 LLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLAR 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-216 |
1.33e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNElAPKDRDIAMVFQNYAL---YP------ 88
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNLVAYVPQSEEVdwsFPvlvedv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 89 -HMTVAKNMGFslrlKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 167
Cdd:PRK15056 101 vMMGRYGHMGW----LRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 655334176 168 LRVQMRSEIKELhqRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSG 216
Cdd:PRK15056 177 TEARIISLLREL--RDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-205 |
1.45e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.60 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIA 78
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDppRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 79 -MVF---------QNYAL--YPHMT--VAKNMGFSLrLKRMPRTE----------IDQRVGNAAKILGL--ESLLerypK 132
Cdd:PRK11147 81 gTVYdfvaegieeQAEYLkrYHDIShlVETDPSEKN-LNELAKLQeqldhhnlwqLENRINEVLAQLGLdpDAAL----S 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655334176 133 QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAklrvqmrSEIKELHQRLQT---TTIYVTHDQIEAMTMADKIV 205
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI-------ETIEWLEGFLKTfqgSIIFISHDRSFIRNMATRIV 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-222 |
1.48e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.01 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 22 VSVDIGDGEFVVLVGPSGCGKSTLLRMIAGlegitsgqiqigkhivnELAPKDRDIAMVFQNYALYPHM------TVAKN 95
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVVIRGSVAYVPQVswifnaTVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MGFSLRLKrmprteiDQRVGNAAKILGLESLLERYPKQ-----------LSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:PLN03232 699 ILFGSDFE-------SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 165 DAKLRVQM-RSEIKElhqRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELY 222
Cdd:PLN03232 772 DAHVAHQVfDSCMKD---ELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-214 |
2.69e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 7 NNARKDygaFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIV--NELAPKDRDIAMVFQN 83
Cdd:PRK09700 270 NVTSRD---RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKDISprSPLDAVKKGMAYITES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 Y---ALYPHMTVAKNMGFSLRLKRM----------PRTEidQRVGNAA-KILGLE-SLLERYPKQLSGGQRQRVAMGRAI 148
Cdd:PRK09700 347 RrdnGFFPNFSIAQNMAISRSLKDGgykgamglfhEVDE--QRTAENQrELLALKcHSVNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 149 VRDPAVFLFDEPLSNLDaklrVQMRSEIKELHQRLQ---TTTIYVTHDQIEAMTMADKIVVMKDGLIEQ 214
Cdd:PRK09700 425 CCCPEVIIFDEPTRGID----VGAKAEIYKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-217 |
5.38e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.83 E-value: 5.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 3 HVSVNNarkdygaFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEG--ITSGQIQIGKHIVNELAPKDRD---I 77
Cdd:CHL00131 14 HASVNE-------NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEERAhlgI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 AMVFQnyalYP-HMTVAKNMGFsLRL------KRMPRTEID-----QRVGNAAKILGL-ESLLERYPKQ-LSGGQRQRVA 143
Cdd:CHL00131 87 FLAFQ----YPiEIPGVSNADF-LRLaynskrKFQGLPELDpleflEIINEKLKLVGMdPSFLSRNVNEgFSGGEKKRNE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 144 MGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELhQRLQTTTIYVTHDQ-IEAMTMADKIVVMKDGLIEQSGS 217
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQrLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-228 |
8.13e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.35 E-value: 8.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 22 VSVDIGDGEFVVLVGPSGCGKSTLLRMIAG-LEGitSGQIQIG-----KHIVNELApKDRD---------IAM-VFQNYA 85
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGlLPG--SGSIQFAgqpleAWSAAELA-RHRAylsqqqtppFAMpVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 86 LYPHmtvaknmgfSLRLKRMPRTEIDQrvgnAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVR-DPAV------FLFD 158
Cdd:PRK03695 92 LHQP---------DKTRTEAVASALNE----VAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 159 EPLSNLDAKLRVQMRSEIKELHQrLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYdRPNNL 228
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL-TPENL 226
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
22-212 |
9.35e-14 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 72.30 E-value: 9.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 22 VSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKDRDI-AMVFQNYALYPHMtVAKNMGFS 99
Cdd:TIGR01194 361 IDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLdGAAVSADSRDDYRDLfSAIFADFHLFDDL-IGPDEGEH 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 100 LRLKRMprTEIDQRVGNAAKIlGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKEL 179
Cdd:TIGR01194 440 ASLDNA--QQYLQRLEIADKV-KIEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKRFFYEELLPD 516
|
170 180 190
....*....|....*....|....*....|...
gi 655334176 180 HQRLQTTTIYVTHDQiEAMTMADKIVVMKDGLI 212
Cdd:TIGR01194 517 LKRQGKTIIIISHDD-QYFELADQIIKLAAGCI 548
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-221 |
1.89e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.69 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 22 VSVDIGDGEFVVLVGPSGCGKSTLLRMIAGlegitsgqiqigkhivnELAPKDRDIAMVFQNYALYPHM------TVAKN 95
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLG-----------------ELPPRSDASVVIRGTVAYVPQVswifnaTVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MGFSLRLKRmprteidQRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:PLN03130 699 ILFGSPFDP-------ERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 165 DAKLRVQMRSE-IK-ELHQRlqtTTIYVThDQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:PLN03130 772 DAHVGRQVFDKcIKdELRGK---TRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
11-206 |
2.09e-13 |
|
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: 67.60 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 11 KDYGAFKAIKGVSvDIGDGEFVVLVGPSGCGKSTLLRMIAGlegitsgqiqigkhivnELAPKDRDIAmvfqnyalYPHM 90
Cdd:cd03222 8 KRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAG-----------------QLIPNGDNDE--------WDGI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 91 TVAKNmgfslrlkrmprteiDQRVgnaakilglesllerypkQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRV 170
Cdd:cd03222 62 TPVYK---------------PQYI------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRL 108
|
170 180 190
....*....|....*....|....*....|....*.
gi 655334176 171 QMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVV 206
Cdd:cd03222 109 NAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-212 |
2.97e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 22 VSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVN------------ELAPKDRdiamvfQNYALYPH 89
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdairagiMLCPEDR------KAEGIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 90 MTVAKNMGFSLRLKRMP-RTEIDQR--VGNAAKILGLESLLERYPKQ----LSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:PRK11288 346 HSVADNINISARRHHLRaGCLINNRweAENADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 655334176 163 NLDaklrVQMRSEIKELHQRLQT---TTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:PRK11288 426 GID----VGAKHEIYNVIYELAAqgvAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-207 |
3.31e-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: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 29 GEFVVLVGPSGCGKSTLLRmiaglegITSGQIQIGKHIVNELAPKDrDIAMVFQNYALYPHMTVAKNMGFSLRLK----- 103
Cdd:COG1245 99 GKVTGILGPNGIGKSTALK-------ILSGELKPNLGDYDEEPSWD-EVLKRFRGTELQDYFKKLANGEIKVAHKpqyvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 104 RMPR----------TEIDQR--VGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ 171
Cdd:COG1245 171 LIPKvfkgtvrellEKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLN 250
|
170 180 190
....*....|....*....|....*....|....*.
gi 655334176 172 MRSEIKELhQRLQTTTIYVTHDQIEAMTMADKIVVM 207
Cdd:COG1245 251 VARLIREL-AEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-234 |
3.40e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.45 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 14 GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEG----ITSGQIQIGKHIVNELAPKDR------DIAMVFQ- 82
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 83 -NYALYPHMTVAKNM---------------GFSLRLKRMprTEIDQRVGnaakILGLESLLERYPKQLSGGQRQRVAMGR 146
Cdd:PRK15093 98 pQSCLDPSERVGRQLmqnipgwtykgrwwqRFGWRKRRA--IELLHRVG----IKDHKDAMRSFPYELTEGECQKVMIAI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 147 AIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPN 226
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPH 251
|
....*...
gi 655334176 227 NLFVAGFI 234
Cdd:PRK15093 252 HPYTQALI 259
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-229 |
4.56e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.58 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLL----RMI--AGLEGITSGQiQIGKHIVNELApkdRDIAMVFQNYALYPHmTV 92
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMVevCGGEIRVNGR-EIGAYGLRELR---RQFSMIPQDPVLFDG-TV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 93 AKNMG-FS----------LRLKRMprteiDQRVgnAAKILGLESLLERYPKQLSGGQRQRVAMGRAIV-RDPAVFLFDEP 160
Cdd:PTZ00243 1401 RQNVDpFLeassaevwaaLELVGL-----RERV--ASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEA 1473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 161 LSNLDAKLRVQMRSEIKELHQrlQTTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLF 229
Cdd:PTZ00243 1474 TANIDPALDRQIQATVMSAFS--AYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-217 |
4.98e-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: 70.43 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNELAPKDRDIAMVFQNYALYPHMTVAKNM 96
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 GFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEI 176
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 655334176 177 KELhQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGS 217
Cdd:TIGR01257 2114 VSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-194 |
5.35e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.29 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 16 FKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIgkhivnelapkdrdiamVFQNYALYPHMTVAKN 95
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-----------------DVPDNQFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MGfslrlkrmPRTEIDQrvgnAAKIL---GLES--LLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRV 170
Cdd:COG2401 106 IG--------RKGDFKD----AVELLnavGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180
....*....|....*....|....
gi 655334176 171 QMRSEIKELHQRLQTTTIYVTHDQ 194
Cdd:COG2401 174 RVARNLQKLARRAGITLVVATHHY 197
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-210 |
1.33e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.98 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 9 ARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIA----GLEGITSGQIQIGKHIVNELAPKDR-DIAMVFQN 83
Cdd:TIGR00956 67 KFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRgDVVYNAET 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 YALYPHMTVAKNMGFSLRLkRMPRTEID---------QRVGNAAKILGLE-----SLLERYPKQLSGGQRQRVAMGRAIV 149
Cdd:TIGR00956 147 DVHFPHLTVGETLDFAARC-KTPQNRPDgvsreeyakHIADVYMATYGLShtrntKVGNDFVRGVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 150 RDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTT---TIYVTHDqiEAMTMADKIVVMKDG 210
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTplvAIYQCSQ--DAYELFDKVIVLYEG 287
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-218 |
2.06e-12 |
|
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: 65.51 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAF--KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVN-ELAPKDRDIAM 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 80 VFQNYALYphmtvaknMGfSLRLKRMPRTEIDQRvgnaaKILGLESLLERyPKQLSGGQRQRVAMGRAIVRDPAVFLFDE 159
Cdd:cd03369 87 IPQDPTLF--------SG-TIRSNLDPFDEYSDE-----EIYGALRVSEG-GLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 160 PLSNLDaklrVQMRSEIKE-LHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSP 218
Cdd:cd03369 152 ATASID----YATDALIQKtIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-209 |
2.11e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 8 NARKDYGAFKAIkgvSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIG-KHIVNELAPK--DRDIAMVFQN- 83
Cdd:PTZ00265 393 DTRKDVEIYKDL---NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKwwRSKIGVVSQDp 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 ------------YALYP-------------------------HMTVAKNMG-FSLRLKRMPRTEI-----------DQRV 114
Cdd:PTZ00265 470 llfsnsiknnikYSLYSlkdlealsnyynedgndsqenknkrNSCRAKCAGdLNDMSNTTDSNELiemrknyqtikDSEV 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 115 GNAAKILGLESLLERYP-----------KQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRL 183
Cdd:PTZ00265 550 VDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNE 629
|
250 260
....*....|....*....|....*.
gi 655334176 184 QTTTIYVTHdQIEAMTMADKIVVMKD 209
Cdd:PTZ00265 630 NRITIIIAH-RLSTIRYANTIFVLSN 654
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-217 |
7.21e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.28 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPK--DRDIAMVFQNYALyphmtVAKNM 96
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPVV-----LADTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 GFSLRLKRmprtEID-QRVGNAAKILGLESLLERYPK-----------QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 164
Cdd:PRK10790 432 LANVTLGR----DISeEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANI 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 655334176 165 DAKLRVQMRSEIKELhqRLQTTTIYVTHdQIEAMTMADKIVVMKDGLIEQSGS 217
Cdd:PRK10790 508 DSGTEQAIQQALAAV--REHTTLVVIAH-RLSTIVEADTILVLHRGQAVEQGT 557
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-243 |
9.40e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.47 E-value: 9.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIqigKHivnelapkDRDIAMVFQNYALYPHmTVAKNMGF 98
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---KH--------SGRISFSPQTSWIMPG-TIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 99 SLrlkrmprTEIDQRVGNAAKILGLESLLERYPKQ-----------LSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDak 167
Cdd:TIGR01271 510 GL-------SYDEYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD-- 580
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 168 lrVQMRSEIKE--LHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELY-DRPNnlFVAGFIGSPAMNFIS 243
Cdd:TIGR01271 581 --VVTEKEIFEscLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQaKRPD--FSSLLLGLEAFDNFS 655
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-165 |
1.22e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.73 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIvnelapkdrDIAMVFQN 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------KLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 Y-ALYPHMTVAKNMGFSLRLKRMPRTEIDQRV---------GNAAKILGlesllerypkQLSGGQRQRVAMGRAIVRDPA 153
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLDIIKLGKREIPSRAyvgrfnfkgSDQQKKVG----------QLSGGERNRVHLAKTLKSGGN 463
|
170
....*....|..
gi 655334176 154 VFLFDEPLSNLD 165
Cdd:TIGR03719 464 VLLLDEPTNDLD 475
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
130-209 |
1.27e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 130 YPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHdQIEAMTMADKIVVMKD 209
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFNN 1433
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-219 |
1.38e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.46 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 22 VSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDR-DIAMVF-----QNYALYPHMTVAKN 95
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MgFSLRLKRMPrteIDQRVGNAAKIlgleslLERYPKQ--------------LSGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:PRK15439 362 V-CALTHNRRG---FWIKPARENAV------LERYRRAlnikfnhaeqaartLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 162 SNLDaklrVQMRSEIKELHQRL---QTTTIYVTHDQIEAMTMADKIVVMKDGLIeqSGSPL 219
Cdd:PRK15439 432 RGVD----VSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI--SGALT 486
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-210 |
1.71e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.52 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 29 GEFVVLVGPSGCGKSTLLRMIAglEGITSGQIQIGKHIVNeLAPKD----RDIAMVFQNYALYPHMTVAKNMGFSLRLKR 104
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVN-GRPLDssfqRSIGYVQQQDLHLPTSTVRESLRFSAYLRQ 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 105 ---MPRTEIDQRVGNAAKILGLESLLERY---PKQ-LSGGQRQRVAMGRAIVRDPAVFLF-DEPLSNLDAklrvQMRSEI 176
Cdd:TIGR00956 866 pksVSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDS----QTAWSI 941
|
170 180 190
....*....|....*....|....*....|....*...
gi 655334176 177 KELHQRLQTT--TIYVTHDQIEAMTMA--DKIVVMKDG 210
Cdd:TIGR00956 942 CKLMRKLADHgqAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-243 |
2.36e-11 |
|
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: 63.72 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIqigKHivnelapkDRDIAMVFQNYALYPHmTVAKNMGF 98
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---KH--------SGRISFSSQFSWIMPG-TIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 99 SLrlkrmprTEIDQRVGNAAKILGLESLLERYPKQ-----------LSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDak 167
Cdd:cd03291 121 GV-------SYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD-- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 168 lrVQMRSEIKE---LHQRLQTTTIYVThDQIEAMTMADKIVVMKDGLIEQSGSPLELYD-RPNnlFVAGFIGSPAMNFIS 243
Cdd:cd03291 192 --VFTEKEIFEscvCKLMANKTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSlRPD--FSSKLMGYDTFDQFS 266
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-207 |
2.44e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 28 DGEFVVLVGPSGCGKSTLLRmiaglegITSGQIQ--IGKHivNELAPKDRDIAMvFQNYALYPHMTVAKNMGFSLRLK-- 103
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVK-------ILSGELIpnLGDY--EEEPSWDEVLKR-FRGTELQNYFKKLYNGEIKVVHKpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 104 ---RMPR----------TEIDQRvGNA---AKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 167
Cdd:PRK13409 168 yvdLIPKvfkgkvrellKKVDER-GKLdevVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 655334176 168 LRVQMRSEIKELHQrlQTTTIYVTHDQIEAMTMADKIVVM 207
Cdd:PRK13409 247 QRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-212 |
5.50e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 3 HVSVNNARKDygafKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKHIVNeLAPKDRDIAMVF 81
Cdd:COG3845 262 NLSVRDDRGV----PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLdGEDITG-LSPRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 82 ------QNYALYPHMTVAKNM------------GFSLRLKRMPRteidqrvgNAakilglESLLERY----------PKQ 133
Cdd:COG3845 337 yipedrLGRGLVPDMSVAENLilgryrrppfsrGGFLDRKAIRA--------FA------EELIEEFdvrtpgpdtpARS 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 134 LSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-166 |
9.42e-11 |
|
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: 60.33 E-value: 9.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLE--GITSGQIQI-GKHIVNELApkdRDIAMVFQNYALYPHMTVAKN 95
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKtaGVITGEILInGRPLDKNFQ---RSTGYVEQQDVHSPNLTVREA 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655334176 96 MGFSlrlkrmprteidqrvgnaAKILGlesllerypkqLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDA 166
Cdd:cd03232 100 LRFS------------------ALLRG-----------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-193 |
1.23e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLR-MIAGLEGiTSGQIQIGKHIvnelapkdrDIAMvFQNY--ALYPHMTVAKN 95
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQA-DSGRIHCGTKL---------EVAY-FDQHraELDPEKTVMDN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MGfslrlkrmprtEIDQRV---GNAAKILG-LESLL-----ERYP-KQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:PRK11147 404 LA-----------EGKQEVmvnGRPRHVLGyLQDFLfhpkrAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
170 180
....*....|....*....|....*...
gi 655334176 166 aklrVQMRSEIKELHQRLQTTTIYVTHD 193
Cdd:PRK11147 473 ----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-218 |
1.83e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.61 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGleGITSGQIQIGKHIVNELAPKDRDIAMV-----FQNYALYPHMTvA 93
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGGGAPRGARVTGDVTLNGEPLAAIdaprlARLRAVLPQAA-Q 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 94 KNMGFSLR----LKRMPRT----EIDQRVGN----AAKILGLESLLERYPKQLSGGQRQRVAMGRAI---------VRDP 152
Cdd:PRK13547 94 PAFAFSAReivlLGRYPHArragALTHRDGEiawqALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655334176 153 AVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSP 218
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-193 |
1.88e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 5 SVNNARKDYGAFKAI-KGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEgitsgqiqigKHIVNELAP-KDRDIAMVFQ 82
Cdd:TIGR03719 6 TMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVD----------KDFNGEARPqPGIKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 83 NYALYPHMTVAKNMGFSLR-----LKRM---------PRTEID---------QRVGNAAKILGLESLLE------RYP-- 131
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEGVAeikdaLDRFneisakyaePDADFDklaaeqaelQEIIDAADAWDLDSQLEiamdalRCPpw 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 132 ----KQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKlrvqmrsEIKELHQRLQT---TTIYVTHD 193
Cdd:TIGR03719 156 dadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-------SVAWLERHLQEypgTVVAVTHD 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-229 |
2.18e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD--RDIAMVFQNYALYPHmTVAKNM 96
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFSG-TVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 G-FSLR-----LKRMPRTEIDQRVGNAAkiLGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRV 170
Cdd:PLN03232 1331 DpFSEHndadlWEALERAHIKDVIDRNP--FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 171 QMRSEIKElhqRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLF 229
Cdd:PLN03232 1409 LIQRTIRE---EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-212 |
7.74e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKD---RDIAMVFQNY---ALYPHMTV 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 93 AKNMG------FSLRLKRMPRTEIDQRVGNAAKILGLES-LLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:PRK10762 348 KENMSltalryFSRAGGSLKHADEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 655334176 166 aklrVQMRSEIKELHQRLQT---TTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:PRK10762 428 ----VGAKKEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-210 |
1.17e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKDRD---IAMVFQNYALYPHMTVA 93
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGIIHQELNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 94 KNMgFSLRLKRMPRTEIDQRVGNAA-----KILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL 168
Cdd:PRK10762 98 ENI-FLGREFVNRFGRIDWKKMYAEadkllARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 655334176 169 RVQMRSEIKELhqRLQTTTI-YVTHDQIEAMTMADKIVVMKDG 210
Cdd:PRK10762 177 TESLFRVIREL--KSQGRGIvYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-216 |
2.05e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.52 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 16 FKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQigkhivnelapKDRDIAMVFQNYALYPHMTVAKN 95
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------RNGEVSVIAISAGLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 96 MGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSE 175
Cdd:PRK13546 106 IEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDK 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 655334176 176 IKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSG 216
Cdd:PRK13546 186 IYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-165 |
2.71e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIvnelapkdrDIAMVFQN 83
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV---------KLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 84 Y-ALYPHMTVAKNMGFSLRLKRMPRTEIDQRV---------GNAAKILGlesllerypkQLSGGQRQRVAMGRAIVRDPA 153
Cdd:PRK11819 396 RdALDPNKTVWEEISGGLDIIKVGNREIPSRAyvgrfnfkgGDQQKKVG----------VLSGGERNRLHLAKTLKQGGN 465
|
170
....*....|..
gi 655334176 154 VFLFDEPLSNLD 165
Cdd:PRK11819 466 VLLLDEPTNDLD 477
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
18-224 |
3.14e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.06 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQI-GKhivnELAPKDRD-----IAMVFQNYALYPHMT 91
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGK----PVTAEQPEdyrklFSAVFTDFHLFDQLL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 92 vaKNMGFSLRlkrmprteiDQRVGNAAKILGLESLLE----RYPK-QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDA 166
Cdd:PRK10522 414 --GPEGKPAN---------PALVEKWLERLKMAHKLEledgRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 167 KLRvqmRSEIKELHQRLQT---TTIYVTHDQiEAMTMADKIVVMKDG-LIEQSGSPLELYDR 224
Cdd:PRK10522 483 HFR---REFYQVLLPLLQEmgkTIFAISHDD-HYFIHADRLLEMRNGqLSELTGEERDAASR 540
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-210 |
3.41e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 8 NARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPK---DRDIAMVFQNY 84
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 85 ALYPHMTVAKNMGfslrLKRMPRTE--IDQ-RVGNAAKILGLESLLERYPKQ----LSGGQRQRVAMGRAIVRDPAVFLF 157
Cdd:PRK10982 83 NLVLQRSVMDNMW----LGRYPTKGmfVDQdKMYRDTKAIFDELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 655334176 158 DEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-210 |
4.08e-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: 57.91 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL-EGITSGQIQIGKHIVNELAPKD---RDIAMVFQN---YALYPH 89
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 90 MTVAKNMGFSLRLKRMPRTEID-----QRVGNAAKILGLESLLERYP-KQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:TIGR02633 354 LGVGKNITLSVLKSFCFKMRIDaaaelQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 655334176 164 LDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-169 |
5.01e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.26 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 36 GPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNELAPKdrDIAMVFQNYALYPHMTVAKNMGFSLRLKRMPRTeidqrVG 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP--YCTYIGHNLGLKLEMTVFENLKFWSEIYNSAET-----LY 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 655334176 116 NAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLR 169
Cdd:PRK13541 106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-214 |
6.56e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.61 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 3 HVSVNNARKDY--GAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGiTSGQIQIGKHIVNELAPKDRDIAmv 80
Cdd:TIGR01271 1217 QMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA-- 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 fqnYALYPHMTVAKNMGFSLRLKRMPRTEiDQRVGNAAKILGLESLLERYPKQL-----------SGGQRQRVAMGRAIV 149
Cdd:TIGR01271 1294 ---FGVIPQKVFIFSGTFRKNLDPYEQWS-DEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSIL 1369
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 150 RDPAVFLFDEPLSNLDAKLRVQMRseiKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQ 214
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDPVTLQIIR---KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-192 |
1.23e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 56.30 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIgkhivnelaPKDRDIAMVFQNyalyPHMTVAknmgf 98
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQR----PYMTLG----- 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 99 SLR--------LKRMPRTEI-DQRVGNAAKILGLESLLER---------YPKQLSGGQRQRVAMGRAIVRDPAVFLFDEP 160
Cdd:TIGR00954 530 TLRdqiiypdsSEDMKRRGLsDKDLEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 655334176 161 LSnldaKLRVQMRSEIKELHQRLQTTTIYVTH 192
Cdd:TIGR00954 610 TS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-216 |
2.52e-08 |
|
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: 53.10 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLrmiagLEGITSGqiqiGKHIVNELAPKdrdiamvfqnyaLYPHMTVaknmg 97
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLV-----NEGLYAS----GKARLISFLPK------------FSRNKLI----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 98 FSLRLKRMprteIDqrvgnaakiLGLESL-LERYPKQLSGGQRQRVAMGRAIVRDP--AVFLFDEPLSNLDAKLRVQMRS 174
Cdd:cd03238 64 FIDQLQFL----ID---------VGLGYLtLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 655334176 175 EIKELHQrLQTTTIYVTHDQiEAMTMADKIVVMKDGLIEQSG 216
Cdd:cd03238 131 VIKGLID-LGNTVILIEHNL-DVLSSADWIIDFGPGSGKSGG 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-193 |
2.79e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 5 SVNNARKDYGAFKAI-KGVS------VDIGdgefvvLVGPSGCGKSTLLRMIAGLEGITSGQ------IQIG-------- 63
Cdd:PRK11819 8 TMNRVSKVVPPKKQIlKDISlsffpgAKIG------VLGLNGAGKSTLLRIMAGVDKEFEGEarpapgIKVGylpqepql 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 64 ------KHIVNE-LAPKDRDIAMVFQNYALYphmtvAKNMG-FSLRLKRMPR--TEIDqrvgnAAKILGLESLLE----- 128
Cdd:PRK11819 82 dpektvRENVEEgVAEVKAALDRFNEIYAAY-----AEPDAdFDALAAEQGElqEIID-----AADAWDLDSQLEiamda 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 129 -RYP------KQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKlrvqmrsEIKELHQRLQT---TTIYVTHD 193
Cdd:PRK11819 152 lRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE-------SVAWLEQFLHDypgTVVAVTHD 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-217 |
3.39e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQ------IGKHivnelapkDRDI 77
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsenanIGYY--------AQDH 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 AMVFQNyalypHMTVAKNMGfslrLKRMPRTEiDQRV-GNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFL 156
Cdd:PRK15064 392 AYDFEN-----DLTLFDWMS----QWRQEGDD-EQAVrGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 157 FDEPLSNLDaklrvqMRSeIKELHQRL---QTTTIYVTHDQIEAMTMADKIVVMK-DGLIEQSGS 217
Cdd:PRK15064 462 MDEPTNHMD------MES-IESLNMALekyEGTLIFVSHDREFVSSLATRIIEITpDGVVDFSGT 519
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
19-229 |
3.67e-08 |
|
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: 53.76 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTL----LRMIAGLEG-ITSGQIQIGKHIVNELAPKdrdIAMVFQNYALYPHmtva 93
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFDGkIVIDGIDISKLPLHTLRSR---LSIILQDPILFSG---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 94 knmgfSLRLKRMP-RTEIDQRVGNAAKILGLESLLERYPKQL-----------SGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:cd03288 110 -----SIRFNLDPeCKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655334176 162 SNLDaklrvqMRSEikELHQRLQTT-----TIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYDRPNNLF 229
Cdd:cd03288 185 ASID------MATE--NILQKVVMTafadrTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
235-278 |
4.47e-08 |
|
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: 49.12 E-value: 4.47e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 655334176 235 GSPAMNFISGSMTEDGFRTADG---LLLPSERRPADAA------IYGIRPEHI 278
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLLVLGGgvtLPLPEGQVLALKLyvgkevILGIRPEHI 53
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-216 |
1.37e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAG-----LEgiTSGQIQIGKHIVNELAPKdRDIAMVFQNYALYPHMTVA 93
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGkldpsLK--VSGEITYNGYRLNEFVPR-KTSAYISQNDVHVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 94 KNMGFSLR-------------LKR-------MPRTEIDQRVGNAA--------------KILGLE-----SLLERYPKQL 134
Cdd:PLN03140 258 ETLDFSARcqgvgtrydllseLARrekdagiFPEAEVDLFMKATAmegvksslitdytlKILGLDickdtIVGDEMIRGI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 135 SGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMrseIKELHQ--RLQTTTIYVTHDQ--IEAMTMADKIVVMKDG 210
Cdd:PLN03140 338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQI---VKCLQQivHLTEATVLMSLLQpaPETFDLFDDIILLSEG 414
|
....*.
gi 655334176 211 LIEQSG 216
Cdd:PLN03140 415 QIVYQG 420
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-185 |
1.84e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 23 SVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIG------------KHIVNE---------LAPKDRD----I 77
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfshitrlsfeqlQKLVSDewqrnntdmLSPGEDDtgrtT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 78 AMVFQNYalyphmtvaknmgfslrlkrmprTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLF 157
Cdd:PRK10938 103 AEIIQDE-----------------------VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLIL 159
|
170 180
....*....|....*....|....*...
gi 655334176 158 DEPLSNLDAKLRVQMRSEIKELHQRLQT 185
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASLHQSGIT 187
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-221 |
2.45e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.64 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKST----LLRMIAGLEG-ITSGQIQIGKHIVNELAPKdrdIAMVFQNYALYPHmtva 93
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINESAEGeIIIDGLNIAKIGLHDLRFK---ITIIPQDPVLFSG---- 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 94 knmgfSLRLKRMPRTEI-DQRVGNAAKILGLESLLERYP-----------KQLSGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:TIGR00957 1375 -----SLRMNLDPFSQYsDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 162 SNLDAKLRVQMRSEIKelhQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIR---TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-211 |
3.69e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.91 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 29 GEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIqigkhivnelapkdrdiamvfqnyalyphmtVAKNMGFSLRLKRMPRT 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-------------------------------IYIDGEDILEEVLDQLL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 109 EIdqrvgnaakilglesLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEI-----KELHQRL 183
Cdd:smart00382 51 LI---------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSEK 115
|
170 180 190
....*....|....*....|....*....|...
gi 655334176 184 QTTTIYVTHDQIEAMTMA-----DKIVVMKDGL 211
Cdd:smart00382 116 NLTVILTTNDEKDLGPALlrrrfDRRIVLLLIL 148
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-221 |
4.34e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.27 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 4 VSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLlRMIAGLEGITSGQ--IQIGKHIVNELAPKDRDIAMVF 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRrpWRF*TWCANRRALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 82 QNYALYPHMTVAKNMGFSLRLKRMPRTEIDQRVGNAAKILGLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPL 161
Cdd:NF000106 93 VR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 162 SNLDAKLRVQMRSEIKELhQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLEL 221
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-159 |
2.50e-06 |
|
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: 49.03 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 22 VSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIGKHIVNelaPKDRD-----IAMVFQNYALYPHMTVAKNM 96
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREayrqlFSAVFSDFHLFDRLLGLDGE 427
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 97 GFSLR----LKRMprtEIDQRV---GNAakilgLESLlerypkQLSGGQRQRVAMGRAIVRDPAVFLFDE 159
Cdd:COG4615 428 ADPARarelLERL---ELDHKVsveDGR-----FSTT------DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-167 |
3.15e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLE--GITSGQIQIGKHivnelaPKDRDI-----AMVFQNYALYPHMT 91
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKtgGYIEGDIRISGF------PKKQETfarisGYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 92 VAKNMGFS--LRL-KRMPRTEIDQRVGNAAKILGLESLLER---YP--KQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 163
Cdd:PLN03140 970 VRESLIYSafLRLpKEVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
....
gi 655334176 164 LDAK 167
Cdd:PLN03140 1050 LDAR 1053
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-208 |
3.49e-06 |
|
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: 46.58 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 14 GAFKAIKGV-SVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQigkhivnelapkdrdiamvfqnyalyphmtv 92
Cdd:cd03227 5 GRFPSYFVPnDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATR------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 93 aknmgfslrlkrmPRTEIDQRVGNAAKILGLESLLerypKQLSGGQRQRVAM-----GRAIVRDPaVFLFDEPLSNLDAK 167
Cdd:cd03227 54 -------------RRSGVKAGCIVAAVSAELIFTR----LQLSGGEKELSALalilaLASLKPRP-LYILDEIDRGLDPR 115
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 655334176 168 LRVQMRSEIKELHQRlQTTTIYVTHDQiEAMTMADKIVVMK 208
Cdd:cd03227 116 DGQALAEAILEHLVK-GAQVIVITHLP-ELAELADKLIHIK 154
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-197 |
5.43e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 2 AHVSVNNARKDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAG-----------LEGIT--SGQI--QIGKHI 66
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRrgSGETiwDIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 67 ------------VNELApKDRDIAMVFQNYALYphmtvaknMGFSLRLKRMPRTEIDqrvgnaakILGLESLLERYP-KQ 133
Cdd:PRK10938 339 gyvssslhldyrVSTSV-RNVILSGFFDSIGIY--------QAVSDRQQKLAQQWLD--------ILGIDKRTADAPfHS 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655334176 134 LSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRLQTTTIYVTHDQIEA 197
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-210 |
5.98e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 32 VVLVGPSGCGKSTLLRMIAGLEGITSGQIQigkhivneLAPKDRdIAMVFQNYALYPHMTVAKNMGFSLRLKRMPRTEID 111
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVF--------RSAKVR-MAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLR 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 112 QRVGNaakiLGLESLLERYPK-QLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAklrvqmrSEIKELHQRL---QTTT 187
Cdd:PLN03073 609 AHLGS----FGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL-------DAVEALIQGLvlfQGGV 677
|
170 180
....*....|....*....|...
gi 655334176 188 IYVTHDQIEAMTMADKIVVMKDG 210
Cdd:PLN03073 678 LMVSHDEHLISGSVDELWVVSEG 700
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-207 |
6.98e-06 |
|
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: 46.48 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTL----------LRMIAGLEGITSGQI-QIGKHIVNE---LAPKdrdIAMVFQNY 84
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYARQFLgQMDKPDVDSiegLSPA---IAIDQKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 85 ALYPHMTVAKNMGFS--LRLkRMPRTEIDQRVGNAAKIlGLESL-LERYPKQLSGGQRQRVAMGRAIVR--DPAVFLFDE 159
Cdd:cd03270 88 SRNPRSTVGTVTEIYdyLRL-LFARVGIRERLGFLVDV-GLGYLtLSRSAPTLSGGEAQRIRLATQIGSglTGVLYVLDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 655334176 160 PLSNLDAKLRVQMRSEIKELhQRLQTTTIYVTHDQiEAMTMADKIVVM 207
Cdd:cd03270 166 PSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHVIDI 211
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
19-216 |
1.06e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.32 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 19 IKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEG--ITSGQIQIGKHIVNELAPKDR---DIAMVFQnyalYP-HMTV 92
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageGIFMAFQ----YPvEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 93 AKNMGF------SLRLKR----MPRTEIDQRVGNAAKILGL-ESLLERYPKQ-LSGGQRQRVAMGRAIVRDPAVFLFDEP 160
Cdd:PRK09580 93 VSNQFFlqtalnAVRSYRgqepLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDES 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 655334176 161 LSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQ-IEAMTMADKIVVMKDGLIEQSG 216
Cdd:PRK09580 173 DSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQrILDYIKPDYVHVLYQGRIVKSG 228
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
28-210 |
1.61e-05 |
|
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: 45.29 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 28 DGEFVVLVGPSGCGKSTLLRMI-AGLEGITSGQIQIGKHIVNELAPKDR--DIAMVFQN-----YALYPHMTVAKNMGFS 99
Cdd:cd03240 21 FSPLTLIVGQNGAGKTTIIEALkYALTGELPPNSKGGAHDPKLIREGEVraQVKLAFENangkkYTITRSLAILENVIFC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 100 lrlkrmPRTEIDqrvgnaakilgleSLLERYPKQLSGGQRQ------RVAMGRAIVRDPAVFLFDEPLSNLDA-KLRVQM 172
Cdd:cd03240 101 ------HQGESN-------------WPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESL 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 655334176 173 RSEIKELHQRLQTTTIYVTHDQiEAMTMADKIV-VMKDG 210
Cdd:cd03240 162 AEIIEERKSQKNFQLIVITHDE-ELVDAADHIYrVEKDG 199
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
272-338 |
1.64e-05 |
|
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: 42.22 E-value: 1.64e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655334176 272 GIRPEHIRLDPG--GIEVTTVVVEPTGSETLVIVRLGTQTLTCVFR---ERIRAAPGEVLRIAPIHDTVHLF 338
Cdd:pfam08402 2 AIRPEKIRLAAAanGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVpnaHARPPAPGDRVGLGWDPEDAHVL 73
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
132-204 |
2.76e-05 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 44.94 E-value: 2.76e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 132 KQLSGGQRQRVAMGR--AIVR-DPAVF-LFDEPLSNLDAKLRVQMRSEIKELHQRLQ--TTTIyvthdQIEAMTMADKI 204
Cdd:cd03272 157 QQLSGGQKSLVALALifAIQKcDPAPFyLFDEIDAALDAQYRTAVANMIKELSDGAQfiTTTF-----RPELLEVADKF 230
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-165 |
3.03e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNNARKDYGAfkAIKGV-----SVDIGDGEFVV-------------LVGPSGCGKSTLLRMIA--GLEGI-TSGQ 59
Cdd:PLN03073 159 MPGVYVNHDGNGGGP--AIKDIhmenfSISVGGRDLIVdasvtlafgrhygLVGRNGTGKTTFLRYMAmhAIDGIpKNCQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 60 IQigkHIVNELAPKD-------------------RDIAMVFQNYALYPHMTVAKNMG----------FSLRL----KRMP 106
Cdd:PLN03073 237 IL---HVEQEVVGDDttalqcvlntdiertqlleEEAQLVAQQRELEFETETGKGKGankdgvdkdaVSQRLeeiyKRLE 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655334176 107 RTEIDQRVGNAAKIL-GLE---SLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 165
Cdd:PLN03073 314 LIDAYTAEARAASILaGLSftpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
134-212 |
7.42e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 7.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655334176 134 LSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-212 |
9.33e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.15 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 17 KAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL-EGITSGQIQIGKHIVNELAPKD---RDIAMVFQN---YALYPH 89
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 90 MTVAKNMGFSLrLKRMPRTeidQRVGNAAKILGLESLLERYP----------KQLSGGQRQRVAMGRAIVRDPAVFLFDE 159
Cdd:PRK13549 356 MGVGKNITLAA-LDRFTGG---SRIDDAAELKTILESIQRLKvktaspelaiARLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 655334176 160 PLSNLDAKLRVQMRSEIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDGLI 212
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-210 |
5.78e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 11 KDYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGL------EG--ITSGQIQIGKHIVnelAPKDRDIAMVFQ 82
Cdd:NF040905 9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyEGeiLFDGEVCRFKDIR---DSEALGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 83 NYALYPHMTVAKNMgFsLRLKRMPRTEIDQRVGN--AAKIL---GLESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLF 157
Cdd:NF040905 86 ELALIPYLSIAENI-F-LGNERAKRGVIDWNETNrrARELLakvGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 158 DEPLSNL-----DAKLRVqmrseIKELHQRlQTTTIYVTHDQIEAMTMADKIVVMKDG 210
Cdd:NF040905 164 DEPTAALneedsAALLDL-----LLELKAQ-GITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
16-61 |
6.37e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.45 E-value: 6.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 655334176 16 FKAIKGVSVDIGDgeFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQ 61
Cdd:COG4637 10 FKSLRDLELPLGP--LTVLIGANGSGKSNLLDALRFLSDAARGGLQ 53
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-328 |
7.62e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 121 LGLESL-LERYPKQLSGGQRQRVAMGRAI------VrdpaVFLFDEPLSNLDAKLRVQMRSEIKELhQRLQTTTIYVTHD 193
Cdd:TIGR00630 475 VGLDYLsLSRAAGTLSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 194 QiEAMTMADKIVVM------KDGLIEQSGSPLELYDRPNNLfvagfigspAMNFISGSMTedgfrtadgLLLPSERRPAD 267
Cdd:TIGR00630 550 E-DTIRAADYVIDIgpgageHGGEVVASGTPEEILANPDSL---------TGQYLSGRKK---------IEVPAERRPGN 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655334176 268 A---AIYGIRPEHIRldpgGIEVT------TVVVEPTGS--ETLVIvrlgtQTLTCVFRERIRAA---PGEVLRI 328
Cdd:TIGR00630 611 GkflTLKGARENNLK----NITVSiplglfTCITGVSGSgkSTLIN-----DTLYPALANRLNGAktvPGRYTSI 676
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-224 |
9.30e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 1 MAHVSVNnarkdYGAFKAIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGlegitsgqiqigkhivnELAPKDRDIAMV 80
Cdd:PRK10636 315 MEKVSAG-----YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG-----------------ELAPVSGEIGLA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 81 -------FQNYAL---------YPHMTvaknmgfslrlkRMPRTEIDQRVGNAAKILGLE-SLLERYPKQLSGGQRQRVA 143
Cdd:PRK10636 373 kgiklgyFAQHQLeflradespLQHLA------------RLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLV 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 144 MGRAIVRDPAVFLFDEPLSNLDaklrVQMRSEIKELHQRLQTTTIYVTHDQIEAMTMADKIVVMKDGLIEQSGSPLELYD 223
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLD----LDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQ 516
|
.
gi 655334176 224 R 224
Cdd:PRK10636 517 Q 517
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
3-47 |
1.48e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.99 E-value: 1.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 655334176 3 HVSVNNarkdygaFKAIKGVSVDIGDGeFVVLVGPSGCGKSTLLR 47
Cdd:COG3593 5 KIKIKN-------FRSIKDLSIELSDD-LTVLVGENNSGKSSILE 41
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
15-179 |
1.52e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.22 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 15 AFKAIKG-VSVDIGDGeFVVLVGPSGCGKSTLLRMIA-GLEGITSGQIQIGKHIVNELAPKDRdIAMVFQ-NYALYphmT 91
Cdd:COG0419 9 NFRSYRDtETIDFDDG-LNLIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLINVGSEEAS-VELEFEhGGKRY---R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 92 VAK---------NMGFSLR---LKRMPRTEIDQRVGNAAKIL------------GLESLLERY---------PKQLSGGQ 138
Cdd:COG0419 84 IERrqgefaeflEAKPSERkeaLKRLLGLEIYEELKERLKELeealesaleelaELQKLKQEIlaqlsgldpIETLSGGE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 655334176 139 RQRVAMGRAIvrdpAVFLfDepLSNLDAKLRVQMRSEIKEL 179
Cdd:COG0419 164 RLRLALADLL----SLIL-D--FGSLDEERLERLLDALEEL 197
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-162 |
3.12e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.49 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655334176 18 AIKGVSVDIGDGEFVVLVGPSGCGKSTLLRMIAGLEGITSGQIQIgkhivnelapkDRDIAMVFQNYALYPHMTVAKNM- 96
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-----------KGSAALIAISSGLNGQLTGIENIe 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655334176 97 --GFSLRLKRMPRTEIDQRVGNAAKIlglESLLERYPKQLSGGQRQRVAMGRAIVRDPAVFLFDEPLS 162
Cdd:PRK13545 108 lkGLMMGLTKEKIKEIIPEIIEFADI---GKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
29-65 |
3.53e-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: 38.15 E-value: 3.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 655334176 29 GEFVVLVGPSGCGKSTLLRMIAGLEGITSGQI----QIGKH 65
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGEIseklGRGRH 125
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
32-49 |
4.50e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 37.13 E-value: 4.50e-03
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
23-50 |
4.88e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 37.48 E-value: 4.88e-03
10 20
....*....|....*....|....*...
gi 655334176 23 SVDIGDGEFVVLVGPSGCGKSTLLRMIA 50
Cdd:pfam13191 18 RVRSGRPPSVLLTGEAGTGKTTLLRELL 45
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
26-50 |
5.79e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.84 E-value: 5.79e-03
10 20
....*....|....*....|....*.
gi 655334176 26 IGDGE-FVVLVGPSGCGKSTLLRMIA 50
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRRLL 64
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
20-45 |
9.17e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 9.17e-03
10 20
....*....|....*....|....*.
gi 655334176 20 KGVSVDIGDGEFVVLVGPSGCGKSTL 45
Cdd:COG0178 17 KNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| |
