|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-356 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 577.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 3 SSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVF 82
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 QSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPL 162
Cdd:COG3839 82 QSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 163 SNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGSPSMNF 242
Cdd:COG3839 162 SNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMNL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 243 FSGEIASRSgkpvFHIGEAAVQLDGyDGALEQGRKVTLGVRPEHIRL--DVADGFEATVDLDEPMGADSLVWLKLNGHAL 320
Cdd:COG3839 242 LPGTVEGGG----VRLGGVRLPLPA-ALAAAAGGEVTLGIRPEHLRLadEGDGGLEATVEVVEPLGSETLVHVRLGGQEL 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 1693059733 321 SARVEAGKRYRAGDKVRIGFKADALSLFDSQSEERL 356
Cdd:COG3839 317 VARVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
15-356 |
2.86e-170 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 478.18 E-value: 2.86e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 15 GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQSYALYPQMTVE 94
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQNYALYPHMSVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 95 KNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELR 174
Cdd:PRK11650 95 ENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 175 VEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGSPSMNFFSGEIasRSGKP 254
Cdd:PRK11650 175 LEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAMNLLDGRV--SADGA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 255 VFHIGEAAVQLDGYDGALEQGRKVTLGVRPEHIRL-DVADGFEATVDLDEPMGADSLVWLKLNGHALSARVEAGKRYRAG 333
Cdd:PRK11650 253 AFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIALsSAEGGVPLTVDTVELLGADNLAHGRWGGQPLVVRLPHQERPAAG 332
|
330 340
....*....|....*....|...
gi 1693059733 334 DKVRIGFKADALSLFDSQSEERL 356
Cdd:PRK11650 333 STLWLHLPANQLHLFDADTGRRI 355
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-350 |
5.15e-155 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 439.15 E-value: 5.15e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGM 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 161 PLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGspSM 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--EA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 241 NFFSGEIASRSGKPVfHIGEAAVQLDGyDGALEQGRKVTLGVRPEHIRL---DVADGFEATVDLDEPMGADSLVWLKL-N 316
Cdd:COG3842 240 NLLPGTVLGDEGGGV-RTGGRTLEVPA-DAGLAAGGPVTVAIRPEDIRLspeGPENGLPGTVEDVVFLGSHVRYRVRLgD 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 1693059733 317 GHALSARV--EAGKRYRAGDKVRIGFKADALSLFDS 350
Cdd:COG3842 318 GQELVVRVpnRAALPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-356 |
1.42e-143 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 410.96 E-value: 1.42e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 3 SSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVF 82
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 QSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPL 162
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 163 SNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGSPSMNF 242
Cdd:PRK11000 162 SNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMNF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 243 FSGEIASrsgkpvfhIGEAAVQL---DGY------DGA-LEQGRKVTLGVRPEH-IRLDVAD-GFEATVDLDEPMGADSL 310
Cdd:PRK11000 242 LPVKVTA--------TAIEQVQVelpNRQqvwlpvEGRgVQVGANMSLGIRPEHlLPSDIADvTLEGEVQVVEQLGNETQ 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1693059733 311 VWLKLNG--HALSARVEAGKRYRAGDKVRIGFKADALSLF--DSQSEERL 356
Cdd:PRK11000 314 IHIQIPAirQNLVYRQNDVVLVEEGATFAIGLPPERCHLFreDGTACRRL 363
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-217 |
5.10e-121 |
|
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: 347.71 E-value: 5.10e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQS 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 YALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSN 164
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 165 LDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLA 217
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-347 |
3.29e-117 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 343.28 E-value: 3.29e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNV-TWQEPKDRGIGMVF 82
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 QSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPL 162
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 163 SNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGspSMNF 242
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 243 FSGEIASrsgkPVFHIGEAAVQldgYDGALEQGrKVTLGVRPEHIRL----DVADGFEATVDLDEPMGADSLVWLKLNGH 318
Cdd:COG1118 240 LRGRVIG----GQLEADGLTLP---VAEPLPDG-PAVAGVRPHDIEVsrepEGENTFPATVARVSELGPEVRVELKLEDG 311
|
330 340 350
....*....|....*....|....*....|....*.
gi 1693059733 319 A-------LSARVEAGKRYRAGDKVRIGFKADALSL 347
Cdd:COG1118 312 EgqpleaeVTKEAWAELGLAPGDPVYLRPRPARVFL 347
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-215 |
1.08e-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: 319.08 E-value: 1.08e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQS 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 YALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSN 164
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1693059733 165 LDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQ 215
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-236 |
9.59e-106 |
|
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: 309.55 E-value: 9.59e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQS 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 YALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSN 164
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 165 LDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLG 236
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-348 |
9.29e-105 |
|
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: 311.59 E-value: 9.29e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQSY 85
Cdd:TIGR03265 6 SIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 86 ALYPQMTVEKNLSFGLRVAGLPKAEIDKRIkraAEILQIEPLL--QRK-PSALSGGQRQRVAIGRALVRDVDVFLFDEPL 162
Cdd:TIGR03265 86 ALFPNLTVADNIAYGLKNRGMGRAEVAERV---AELLDLVGLPgsERKyPGQLSGGQQQRVALARALATSPGLLLLDEPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 163 SNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGspSMNF 242
Cdd:TIGR03265 163 SALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG--EVNW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 243 FSGEiasRSGKPVFHIGEAAVQLDGydGALEQGRKVTLGVRPEHIRLDVADGFEATVDLD----EPMGA---DSLVWLKL 315
Cdd:TIGR03265 241 LPGT---RGGGSRARVGGLTLACAP--GLAQPGASVRLAVRPEDIRVSPAGNAANLLLARvedmEFLGAfyrLRLRLEGL 315
|
330 340 350
....*....|....*....|....*....|....*..
gi 1693059733 316 NGHALSARV--EAGKRY--RAGDKVRIGFKADALSLF 348
Cdd:TIGR03265 316 PGQALVADVsaSEVERLgiRAGQPIWIELPAERLRAF 352
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-293 |
6.21e-102 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 305.33 E-value: 6.21e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQS 84
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 YALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSN 164
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 165 LDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGspSMNFFS 244
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINIFD 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1693059733 245 GEIASRSGKPVFHIGEAAVQLDGY-DGALEQGRKVTLGVRPEHIRLDVAD 293
Cdd:PRK09452 253 ATVIERLDEQRVRANVEGRECNIYvNFAVEPGQKLHVLLRPEDLRVEEIN 302
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-343 |
1.31e-92 |
|
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: 279.76 E-value: 1.31e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 35 LLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKR 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 115 IKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHD 194
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 195 QIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGSPSMnFFSGEIASRSGKPVFHIGEAAVQLDGYDGALEQ 274
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINV-FEATVIERKSEQVVLAGVEGRRCDIYTDVPVEK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 275 GRKVTLGVRPEHIRL---DVADGFEATVDLDEP-----MGADSLVWLKLNGHALSARV----EAGKRYRAGDKVRIGFKA 342
Cdd:TIGR01187 240 DQPLHVVLRPEKIVIeeeDEANSSNAIIGHVIDitylgMTLEVHVRLETGQKVLVSEFfnedDPHMSPSIGDRVGLTWHP 319
|
.
gi 1693059733 343 D 343
Cdd:TIGR01187 320 G 320
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-289 |
5.15e-90 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 273.90 E-value: 5.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 2 NSSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMV 81
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 FQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEP 161
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 162 LSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGSPSMn 241
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANI- 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1693059733 242 fFSGEIASRSgkpvFHIGEAAVQL-DGYDGALEQGrKVTLGVRPEHIRL 289
Cdd:PRK11432 243 -FPATLSGDY----VDIYGYRLPRpAAFAFNLPDG-ECTVGVRPEAITL 285
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
7-348 |
4.32e-89 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 271.56 E-value: 4.32e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDFGSVNvLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQSYA 86
Cdd:NF040840 4 IENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 87 LYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLD 166
Cdd:NF040840 83 LFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 167 AKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGSPsmNFFSGE 246
Cdd:NF040840 163 VQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NIIEGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 247 IASRSGKPVFHIGEAAVQLdgydgALEQGRKVTLGVRPEHIRLDVA-------DGFEATVDLDEPMGAdsLVWLKLN-GH 318
Cdd:NF040840 241 AEKGGEGTILDTGNIKIEL-----PEEKKGKVRIGIRPEDITISTEkvktsarNEFKGKVEEIEDLGP--LVKLTLDvGI 313
|
330 340 350
....*....|....*....|....*....|....*.
gi 1693059733 319 AL------SARVEAGkrYRAGDKVRIGFKADALSLF 348
Cdd:NF040840 314 ILvafitrSSFLDLE--INEGKEVYASFKASAVHVF 347
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-231 |
1.03e-87 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 264.64 E-value: 1.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSS---VSIQDLSLDF----GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwqeP 73
Cdd:COG1116 1 MSAAapaLELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT---G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 74 KDRGIGMVFQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDV 153
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 154 DVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMK---GGVVQQLADPLTiynRPRNRF 230
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSarpGRIVEEIDVDLP---RPRDRE 234
|
.
gi 1693059733 231 V 231
Cdd:COG1116 235 L 235
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-237 |
1.10e-86 |
|
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: 261.50 E-value: 1.10e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQ 83
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 SYALYPQMTVEKNLSFGLRV----AGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFD 159
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1693059733 160 EPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGS 237
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-236 |
8.87e-86 |
|
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: 258.80 E-value: 8.87e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDFGSVnVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQSYA 86
Cdd:cd03299 3 VENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 87 LYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLD 166
Cdd:cd03299 82 LFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 167 AKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLG 236
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
5-236 |
4.16e-81 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 247.02 E-value: 4.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQS 84
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 YALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSN 164
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 165 LDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLG 236
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-344 |
1.72e-78 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 245.13 E-value: 1.72e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQSYA 86
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 87 LYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLD 166
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 167 AKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGspSMNFFSGE 246
Cdd:PRK11607 182 KKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG--SVNVFEGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 247 IASRSGKPVFHIGEAAV---QLDGyDGALEQGRKVTLGVRPEHIRL--DV-ADGFEATVDLDEP---MGADSLVWLKL-N 316
Cdd:PRK11607 260 LKERQEDGLVIDSPGLVhplKVDA-DASVVDNVPVHVALRPEKIMLceEPpADGCNFAVGEVIHiayLGDLSIYHVRLkS 338
|
330 340 350
....*....|....*....|....*....|...
gi 1693059733 317 GHALSARVEAGKRYRAG-----DKVRIGFKADA 344
Cdd:PRK11607 339 GQMISAQLQNAHRYRKGlptwgDEVRLCWEADS 371
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-284 |
1.72e-77 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 241.91 E-value: 1.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQ 83
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 SYALYPQMTVEKNLSFGLRVagLPK------AEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFL 157
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTV--LPRrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 158 FDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGs 237
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG- 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1693059733 238 pSMNFFSGEIasRSGKpvFHIGEAAVQLdGYDGALeQGrKVTLGVRP 284
Cdd:PRK10851 239 -EVNRLQGTI--RGGQ--FHVGAHRWPL-GYTPAY-QG-PVDLFLRP 277
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-238 |
1.02e-76 |
|
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: 236.04 E-value: 1.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVN-VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMV 81
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 FQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEP--LLQRKPSALSGGQRQRVAIGRALVRDVDVFLFD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 160 EPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGSP 238
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-210 |
1.25e-76 |
|
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: 235.06 E-value: 1.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGS----VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwqePKDRGIGM 80
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT---GPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1693059733 161 PLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKG 210
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
15-237 |
5.23e-76 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 236.53 E-value: 5.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 15 GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQSYALYPQMT 92
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVIQQIGLFPHMT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 93 VEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEP--LLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLR 170
Cdd:COG1125 93 VAENIATVPRLLGWDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPITR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693059733 171 SELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGS 237
Cdd:COG1125 173 EQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-234 |
1.78e-71 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 223.67 E-value: 1.78e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 8 QDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD------RGIGMV 81
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 FQSYALYPQMTVEKNLSFGLRVAGLPKAEidkRIKRAAEILQ---IEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLF 158
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAE---REERAAEALElvgLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 159 DEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGF 234
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-213 |
5.88e-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: 5.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDFGS----VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDR 76
Cdd:COG1136 1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 77 G------IGMVFQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALV 150
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 151 RDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQiEALTLADRIAVMKGGVV 213
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-211 |
1.52e-67 |
|
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: 210.12 E-value: 1.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQE----PKDRGIGMVF 82
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 QSYALYPQMTVEKNLSFGlrvaglpkaeidkrikraaeilqiepllqrkpsaLSGGQRQRVAIGRALVRDVDVFLFDEPL 162
Cdd:cd03229 83 QDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1693059733 163 SNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-227 |
2.51e-67 |
|
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: 211.42 E-value: 2.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF-GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMV 81
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 FQsyalYP--QM---TVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVF 156
Cdd:COG1122 81 FQ----NPddQLfapTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1693059733 157 LFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPR 227
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-211 |
3.17e-66 |
|
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: 208.09 E-value: 3.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVN--VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG--IGMV 81
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 FQsyalYPQ-----MTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVF 156
Cdd:cd03225 81 FQ----NPDdqffgPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 157 LFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-213 |
2.10e-65 |
|
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: 206.19 E-value: 2.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGS----VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG--- 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 ---IGMVFQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVD 154
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 155 VFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQiEALTLADRIAVMKGGVV 213
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-236 |
1.31e-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: 202.15 E-value: 1.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwQEPKD-----RGIG 79
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDinklrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQSYALYPQMTVEKNLSFGLR-VAGLPKAEIdkrIKRAAEILQ---IEPLLQRKPSALSGGQRQRVAIGRALVRDVDV 155
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIkVKKMSKAEA---EERAMELLErvgLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 156 FLFDEPLSNLDAKLRSE-LRVeIKRLhQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGF 234
Cdd:COG1126 158 MLFDEPTSALDPELVGEvLDV-MRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAF 235
|
..
gi 1693059733 235 LG 236
Cdd:COG1126 236 LS 237
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-213 |
1.13e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 199.90 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG-IGMVFQ 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 SYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1693059733 164 NLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
9-324 |
1.77e-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: 1.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 9 DLSLDFGSVNVlqNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRnvTWQE--------PKDRGIGM 80
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE--VLQDsargiflpPHRRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYPQMTVEKNLSFGLRVAGLPKAEIDkrIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDE 160
Cdd:COG4148 82 VFQEARLFPHLSVRGNLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 161 PLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGflGSPSM 240
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 241 NFFSGEIASRSGkpvfHIGEAAVQLDGY-----DGALEQGRKVTLGVRPEHIRL--DVADG------FEATV-DLDEPMG 306
Cdd:COG4148 238 SVLEATVAAHDP----DYGLTRLALGGGrlwvpRLDLPPGTRVRVRIRARDVSLalEPPEGssilniLPGRVvEIEPADG 313
|
330
....*....|....*...
gi 1693059733 307 ADSLVWLKLNGHALSARV 324
Cdd:COG4148 314 GQVLVRLDLGGQTLLARI 331
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-215 |
2.03e-62 |
|
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: 198.29 E-value: 2.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIG---EGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRnvTWQE--------PKDRGIGMVFQSYALY 88
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT--VLFDsrkkinlpPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 89 PQMTVEKNLSFGLRvaGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK 168
Cdd:cd03297 88 PHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1693059733 169 LRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQ 215
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-228 |
2.28e-62 |
|
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: 199.64 E-value: 2.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVN----VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGI 78
Cdd:COG1124 2 LEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 79 GMVFQSY--ALYPQMTVEKNLSFGLRVAGLPkaEIDKRIKRAAEILQIEP-LLQRKPSALSGGQRQRVAIGRALVRDVDV 155
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1693059733 156 FLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDqIEALT-LADRIAVMKGGVVQQLADPLTIYNRPRN 228
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
22-236 |
2.39e-62 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 198.83 E-value: 2.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 22 NLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQSYALYPQMTVEKNLSFGL 101
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 102 RVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLH 181
Cdd:COG3840 97 RPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELC 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 182 QKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLG 236
Cdd:COG3840 177 RERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-236 |
1.48e-61 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 201.23 E-value: 1.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 15 GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEP------KDRGIGMVFQSYALY 88
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 89 PQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK 168
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1693059733 169 LRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLG 236
Cdd:TIGR01186 164 IRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-227 |
8.89e-61 |
|
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: 203.21 E-value: 8.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDF--GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIS---EGSIFIKGRNVTWQEPKD 75
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 RG--IGMVFQS--YALYPqMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVR 151
Cdd:COG1123 81 RGrrIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 152 DVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPR 227
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-214 |
1.75e-60 |
|
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: 194.43 E-value: 1.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-----RGIG 79
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQSYALYPQMTVEKNLSFGLRV-AGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLF 158
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 159 DEPLSNLD---AKLRSELrveIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQ 214
Cdd:COG1127 166 DEPTAGLDpitSAVIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-213 |
6.79e-60 |
|
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: 191.97 E-value: 6.79e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPK----DRGIGM 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYPQMTVEKNLSFGLR-VAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFD 159
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 160 EPLSNLDAKLRSE-LRVeIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:cd03262 161 EPTSALDPELVGEvLDV-MKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-233 |
1.42e-59 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 192.77 E-value: 1.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 3 SSVSIQDLSLDFGSVN----VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPkDRGI 78
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 79 gmVFQSYALYPQMTVEKNLSFGLRVAGLPKAEidkRIKRAAEILQIEPLL---QRKPSALSGGQRQRVAIGRALVRDVDV 155
Cdd:COG4525 81 --VFQKDALLPWLNVLDNVAFGLRLRGVPKAE---RRARAEELLALVGLAdfaRRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 156 FLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMK---GGVVQQLADPltiYNRprnRFVA 232
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSpgpGRIVERLELD---FSR---RFLA 229
|
.
gi 1693059733 233 G 233
Cdd:COG4525 230 G 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-211 |
2.96e-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: 190.79 E-value: 2.96e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF----GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVT-----WQEPKD 75
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsrrLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 RGIGMVFQSY--ALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEP---LLQRKPSALSGGQRQRVAIGRALV 150
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLpeeVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 151 RDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDqIEAL-TLADRIAVMKGG 211
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHD-LGVVaKIADRVAVMYAG 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-227 |
1.20e-57 |
|
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: 195.12 E-value: 1.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF-----GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD---- 75
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 -RGIGMVFQ--SYALYPQMTVEKNLSFGLRVAG-LPKAEIDKRIKRAAEILQIEP-LLQRKPSALSGGQRQRVAIGRALV 150
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693059733 151 RDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPR 227
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-211 |
4.61e-56 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 182.70 E-value: 4.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-----RGIG 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQSYALYPQMTVEKNLSFGLRVAG-LPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLF 158
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 159 DEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-213 |
2.28e-54 |
|
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: 179.08 E-value: 2.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG--IGMVF 82
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELArrIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 QSYALYPQMTVEKNLSFG----LRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLF 158
Cdd:COG1120 82 QEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1693059733 159 DEPLSNLDakLRSELRV--EIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:COG1120 162 DEPTSHLD--LAHQLEVleLLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-227 |
1.43e-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: 1.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGS----VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD----- 75
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 RGIGMVFQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDV 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 156 FLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHdQIEAL-TLADRIAVMKGGVVQQLADPLTIYNRPR 227
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-235 |
6.23e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 174.90 E-value: 6.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGI----GM 80
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYPQMTVEKNLSFG-LRVAGLPKAEIDkriKRAAEILQIEPLLQRK---PSALSGGQRQRVAIGRALVRDVDVF 156
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAE---KQARELLAKVGLAERAhhyPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 157 LFDEPLSNLDAKLRSE-LRVeIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFL 235
Cdd:PRK09493 159 LFDEPTSALDPELRHEvLKV-MQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-213 |
7.51e-53 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 174.66 E-value: 7.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG-IGMVFQSY 85
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRqIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 86 ALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNL 165
Cdd:COG4555 84 GLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1693059733 166 DAKLRSELRVEIKRLHqKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:COG4555 164 DVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-213 |
9.35e-53 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 174.86 E-value: 9.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 3 SSVSIQDLSLDF-GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-----R 76
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 77 GIGMVFQSYALYPQMTVEKN--------LSFGLRVAGL-PKAEIDkrikRAAEILQ---IEPLLQRKPSALSGGQRQRVA 144
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNvlagrlgrTSTWRSLLGLfPPEDRE----RALEALErvgLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1693059733 145 IGRALVRDVDVFLFDEPLSNLDAKL-RSELRVeIKRLHQKLGNTMIYVTHdQIE-ALTLADRIAVMKGGVV 213
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDGRV 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-238 |
2.26e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 176.42 E-value: 2.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF----GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD----- 75
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 RGIGMVFQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIkraAEILQ---IEPLLQRKPSALSGGQRQRVAIGRALVRD 152
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRV---AELLElvgLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 153 VDVFLFDEPLSNLDAK-LRSELRVeIKRLHQKLGNTMIYVTHD-----QIealtlADRIAVMKGGVVQQLADPLTIYNRP 226
Cdd:COG1135 159 PKVLLCDEATSALDPEtTRSILDL-LKDINRELGLTIVLITHEmdvvrRI-----CDRVAVLENGRIVEQGPVLDVFANP 232
|
250
....*....|..
gi 1693059733 227 RNRFVAGFLGSP 238
Cdd:COG1135 233 QSELTRRFLPTV 244
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-213 |
2.12e-51 |
|
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: 171.84 E-value: 2.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF--GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTL---LNcvaGLLDISEGSIFIKGRNV----TWQEPKD 75
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLN---GLLLPTSGKVTVDGLDTldeeNLWEIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 RgIGMVFQSyalyP--QM---TVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALV 150
Cdd:TIGR04520 78 K-VGMVFQN----PdnQFvgaTVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 151 RDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDqIEALTLADRIAVMKGGVV 213
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHD-MEEAVLADRVIVMNKGKI 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-213 |
2.25e-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 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: 169.55 E-value: 2.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-----RGIGMVFQsyalYP----- 89
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrKKVGLVFQ----FPehqlf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 90 QMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQI-EPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK 168
Cdd:TIGR04521 97 EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1693059733 169 LRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:TIGR04521 177 GRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKI 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-213 |
3.59e-50 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 165.26 E-value: 3.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG-IGMVFQ 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 SYALYPQMTVEKNLSfglrvaglpkaeidkrikraaeilqiepllqrkpsaLSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:cd03230 81 EPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1693059733 164 NLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-195 |
7.00e-50 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 166.38 E-value: 7.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF-GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-----RGI 78
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 79 GMVFQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLF 158
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1693059733 159 DEPLSNLDAKLRSELrVEI-KRLHQkLGNTMIYVTHDQ 195
Cdd:COG2884 162 DEPTGNLDPETSWEI-MELlEEINR-RGTTVLIATHDL 197
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-219 |
1.26e-49 |
|
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: 165.82 E-value: 1.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDI-----SEGSIFIKGRNVtWQEPKD---- 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDI-YDLDVDvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 -RGIGMVFQSYALYPqMTVEKNLSFGLRVAG-LPKAEIDKRIKRAAEILQIEPLLQRKPSA--LSGGQRQRVAIGRALVR 151
Cdd:cd03260 80 rRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 152 DVDVFLFDEPLSNLDAklRSELRVE--IKRLHQKLgnTMIYVTHDQIEALTLADRIAVMKGGVVQQLADP 219
Cdd:cd03260 159 EPEVLLLDEPTSALDP--ISTAKIEelIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-213 |
2.23e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 164.60 E-value: 2.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQ 83
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 SYALYPqMTVEKNLSFGLRVAGLPKAEidKRIKRAAEILQIEP-LLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPL 162
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 163 SNLDAKLRSelRVE--IKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:COG4619 159 SALDPENTR--RVEelLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-226 |
3.55e-49 |
|
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: 168.75 E-value: 3.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 23 LNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRnvTWQE--------PKDRGIGMVFQSYALYPQMTVE 94
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR--TLFDsrkgiflpPEKRRIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 95 KNLSFGLRVAGLPKAEIdkRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELR 174
Cdd:TIGR02142 94 GNLRYGMKRARPSERRI--SFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 175 VEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRP 226
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-229 |
8.41e-49 |
|
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: 163.79 E-value: 8.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPkDRGIgmVFQSYALYPQMTVEKNLSF 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 100 GLR--VAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEI 177
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 178 KRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTI-YNRPRNR 229
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDR 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-213 |
1.93e-48 |
|
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: 162.28 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVlqNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQS 84
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 YALYPQMTVEKNLSFGlRVAGLPKAEID-KRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:cd03298 79 NNLFAHLTVEQNVGLG-LSPGLKLTAEDrQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1693059733 164 NLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-214 |
3.31e-48 |
|
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: 161.90 E-value: 3.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGS--VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwQEPKD--RGIGM 80
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAarQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDE 160
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1693059733 161 PLSNLDAKLRSELRVEIKRLhqKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQ 214
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-213 |
3.75e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 162.57 E-value: 3.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVtwqEPKDRGIGM 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP---RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYPQ--MTVEKNLSFGL----RVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVD 154
Cdd:COG1121 80 VPQRAEVDWDfpITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 155 VFLFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-235 |
1.01e-47 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 161.33 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNcVAGLLDI-SEGSIFIKGRNVTWQEPKD------- 75
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLETpDSGQLNIAGHQFDFSQKPSekairll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 -RGIGMVFQSYALYPQMTVEKNLSFG-LRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDV 153
Cdd:COG4161 81 rQKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 154 DVFLFDEPLSNLDAKLRSELrVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVM-KGGVVQQlaDPLTIYNRPRNRFVA 232
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQV-VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMeKGRIIEQ--GDASHFTQPQTEAFA 237
|
...
gi 1693059733 233 GFL 235
Cdd:COG4161 238 HYL 240
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-227 |
6.97e-47 |
|
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: 161.76 E-value: 6.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF----GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLD---ISEGSIFIKGRNVTWQEPKD-- 75
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 ----RGIGMVFQ-SY-ALYPQMTVEKNLSFGLRV-AGLPKAEIDKRIKRAAEILQIEP---LLQRKPSALSGGQRQRVAI 145
Cdd:COG0444 82 kirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 146 GRALVRDVDVFLFDEPLSNLDAKLRSE-LRVeIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYN 224
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQiLNL-LKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
...
gi 1693059733 225 RPR 227
Cdd:COG0444 241 NPR 243
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-218 |
1.05e-46 |
|
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: 158.10 E-value: 1.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 24 NLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQSYALYPQMTVEKNLSFGLRV 103
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 104 AGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQK 183
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1693059733 184 LGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLAD 218
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-224 |
2.44e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 159.44 E-value: 2.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGI----GMVFQ--SYALYPQmTV 93
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvGLVFQypEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 94 EKNLSFGLRVAGLPKAEIDKRIKRAAEI--LQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRS 171
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 172 ELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYN 224
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-211 |
3.55e-46 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 154.71 E-value: 3.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQ 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 syalypqmtveknlsfglrvaglpkaeidkrikraaeilqiepllqrkpsaLSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1693059733 164 NLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-213 |
3.57e-46 |
|
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: 157.34 E-value: 3.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 15 GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-----RGIGMVFQSYALYP 89
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 90 QMTVEKNLSFGlRVAGLPK--------AEIDKRIKRAA-EILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDE 160
Cdd:cd03256 92 RLSVLENVLSG-RLGRRSTwrslfglfPKEEKQRALAAlERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 161 PLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:cd03256 171 PVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-213 |
1.36e-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: 153.75 E-value: 1.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGigmvfQSY 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA-----RKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 86 ALYPQmtveknlsfglrvaglpkaeidkrikrAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNL 165
Cdd:cd03214 76 AYVPQ---------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1693059733 166 DAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:cd03214 129 DIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-205 |
2.55e-45 |
|
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: 153.93 E-value: 2.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVtwQEPKDR--------GI 78
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQET--PPLNSKkaskfrreKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 79 GMVFQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLF 158
Cdd:TIGR03608 79 GYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1693059733 159 DEPLSNLDAKLRSELrVEIKRLHQKLGNTMIYVTHDQiEALTLADRI 205
Cdd:TIGR03608 159 DEPTGSLDPKNRDEV-LDLLLELNDEGKTIIIVTHDP-EVAKQADRV 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-215 |
3.78e-45 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 154.79 E-value: 3.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNcVAGLLDI-SEGSIFIKGRNVTW-QEPKD------ 75
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEMpRSGTLNIAGNHFDFsKTPSDkairel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 -RGIGMVFQSYALYPQMTVEKNL-SFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDV 153
Cdd:PRK11124 81 rRNVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 154 DVFLFDEPLSNLDAKLRSELrVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVM-KGGVVQQ 215
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQI-VSIIRELAETGITQVIVTHEVEVARKTASRVVYMeNGHIVEQ 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-213 |
4.32e-45 |
|
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: 153.84 E-value: 4.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVtwqEPKDRGIGMVFQSY 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL---EKERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 86 AL---YPqMTVEKNLSFGL----RVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLF 158
Cdd:cd03235 78 SIdrdFP-ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 159 DEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
15-206 |
6.49e-45 |
|
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: 153.17 E-value: 6.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 15 GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-----RGIGMVFQSYALYP 89
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRIGVVFQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 90 QMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKL 169
Cdd:TIGR02673 93 DRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 1693059733 170 RSELRVEIKRLHQkLGNTMIYVTHDqieaLTLADRIA 206
Cdd:TIGR02673 173 SERILDLLKRLNK-RGTTVIVATHD----LSLVDRVA 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-213 |
7.59e-45 |
|
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: 153.36 E-value: 7.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDR---GIGMVF 82
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 QSYALYPQMTVEKNLSFGLRVagLPKAEIDKRIkraAEILQIEPLLQ----RKPSALSGGQRQRVAIGRALVRDVDVFLF 158
Cdd:cd03224 82 EGRRIFPELTVEENLLLGAYA--RRRAKRKARL---ERVYELFPRLKerrkQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 159 DEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-204 |
1.18e-44 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 152.25 E-value: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG-IGMVFQ 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 SYALYPQMTVEKNLSFGLRVAGLPKAEIDkrIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1693059733 164 NLDAKLRSELRVEIKRlHQKLGNTMIYVTHDQIEA-----LTLADR 204
Cdd:COG4133 161 ALDAAGVALLAELIAA-HLARGGAVLLTTHQPLELaaarvLDLGDF 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-224 |
5.21e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 152.84 E-value: 5.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 2 NSSVSIQDLSLDFG--SVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RG 77
Cdd:PRK13632 5 SVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 IGMVFQSyalyPQ-----MTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRD 152
Cdd:PRK13632 85 IGIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 153 VDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALtLADRIAVMKGGVVQQLADPLTIYN 224
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILN 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-233 |
7.19e-44 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 151.78 E-value: 7.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwQEPKDRGIgmVFQSYA 86
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-GPGAERGV--VFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 87 LYPQMTVEKNLSFGLRVAGLPKAEidkRIKRAAEILQ---IEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQ---RLEIAHQMLKkvgLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 164 NLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMK---GGVVQQLADPLTiynrprNRFVAG 233
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgpGRVVERLPLNFA------RRFVAG 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-163 |
1.79e-43 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 147.41 E-value: 1.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQSYALYPQMTVEKNL 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 98 SFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRK----PSALSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
7-213 |
5.71e-43 |
|
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: 148.99 E-value: 5.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDFGS-VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-----RGIGM 80
Cdd:TIGR02315 4 VENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYPQMTVEKNLSFGlRVAG----------LPKAEIdKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALV 150
Cdd:TIGR02315 84 IFQHYNLIERLTVLENVLHG-RLGYkptwrsllgrFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 151 RDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
1.75e-42 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 148.26 E-value: 1.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDI-----SEGSIFIKGRNVtwQEPK- 74
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDI--YDPDv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 75 D-----RGIGMVFQSYALYPqMTVEKNLSFGLRVAGL-PKAEIDKRI----KRAAeilqiepL-------LQRKPSALSG 137
Cdd:COG1117 86 DvvelrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVeeslRKAA-------LwdevkdrLKKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 138 GQRQRVAIGRALVRDVDVFLFDEPLSNLDAKlrSELRVE--IKRLHQKLgnTMIYVTHDQIEALTLADRIAVMKGGVVQQ 215
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPI--STAKIEelILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVE 233
|
250
....*....|....
gi 1693059733 216 LADPLTIYNRPRNR 229
Cdd:COG1117 234 FGPTEQIFTNPKDK 247
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-211 |
2.32e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 147.04 E-value: 2.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 24 NLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQSYALYPQMTVEKNLSFGLRv 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLN- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 104 AGLP-KAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQ 182
Cdd:PRK10771 98 PGLKlNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQ 177
|
170 180
....*....|....*....|....*....
gi 1693059733 183 KLGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:PRK10771 178 ERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-251 |
3.46e-42 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 151.34 E-value: 3.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVT------WQEPKDRGIGMVFQSYALYPQMTV 93
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdaeLREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 94 EKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSEL 173
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 174 RVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGSPSMN--FFSGEIASRS 251
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISqvFSAKDIARRT 283
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-215 |
5.13e-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: 5.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 15 GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQSYALYpQMT 92
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 93 VEKNLSFglrvaGLPKAEiDKRIKRAAEILQIEPLLQRKP-----------SALSGGQRQRVAIGRALVRDVDVFLFDEP 161
Cdd:COG1132 430 IRENIRY-----GRPDAT-DEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1693059733 162 LSNLDAklRSELRVE--IKRLHQklGNTMIYVTHdQIEALTLADRIAVMKGG-VVQQ 215
Cdd:COG1132 504 TSALDT--ETEALIQeaLERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGrIVEQ 555
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-237 |
8.01e-42 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 146.48 E-value: 8.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTW-------QEPKDR- 76
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpdrdgeLVPADRr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 77 -------GIGMVFQSYALYPQMTVEKNLSFG-LRVAGLPKAEIdkrIKRAAEILQIEPLLQRK---PSALSGGQRQRVAI 145
Cdd:COG4598 89 qlqrirtRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEA---IERAEALLAKVGLADKRdayPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 146 GRALVRDVDVFLFDEPLSNLDAKLRSE-LRVeIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYN 224
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPELVGEvLKV-MRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG 243
|
250
....*....|...
gi 1693059733 225 RPRNRFVAGFLGS 237
Cdd:COG4598 244 NPKSERLRQFLSS 256
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-215 |
1.35e-41 |
|
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: 154.22 E-value: 1.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDFG--SVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIG 79
Cdd:COG2274 473 DIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQSYALYpQMTVEKNLSFglrvaGLPKAEiDKRIKRAAEILQIEPLLQRKP-----------SALSGGQRQRVAIGRA 148
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITL-----GDPDAT-DEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 149 LVRDVDVFLFDEPLSNLDAklRSELRVeIKRLHQKLGN-TMIYVTHDqIEALTLADRIAVMKGG-VVQQ 215
Cdd:COG2274 626 LLRNPRILILDEATSALDA--ETEAII-LENLRRLLKGrTVIIIAHR-LSTIRLADRIIVLDKGrIVED 690
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-219 |
2.91e-41 |
|
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: 151.83 E-value: 2.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 2 NSSVSIQDLSLDF-GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGI 78
Cdd:COG4988 334 PPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 79 GMVFQSYALyPQMTVEKNLSFGLRVAGlpkaeiDKRIKRAAEILQIEPLLQRKP-----------SALSGGQRQRVAIGR 147
Cdd:COG4988 414 AWVPQNPYL-FAGTIRENLRLGRPDAS------DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 148 ALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQklGNTMIYVTHDqIEALTLADRIAVMKGGVVQQLADP 219
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTH 555
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
15-213 |
3.51e-41 |
|
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: 143.66 E-value: 3.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 15 GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwQEPKD--RGIGMVFQSYALYPQMT 92
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEPAEarRRLGFVSDSTGLYDRLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 93 VEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSE 172
Cdd:cd03266 95 ARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1693059733 173 LRVEIKRLhQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:cd03266 175 LREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-208 |
5.76e-41 |
|
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: 143.73 E-value: 5.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDR---GIGMVF 82
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 QSYALYPQMTVEKNL----------SFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRD 152
Cdd:cd03219 82 QIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1693059733 153 VDVFLFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDqIEALT-LADRIAVM 208
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHD-MDVVMsLADRVTVL 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-218 |
5.90e-41 |
|
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: 144.41 E-value: 5.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDR---GIGMVF 82
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlGIARTF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 QSYALYPQMTVEKNL----------SFGLRVAGLPK-----AEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGR 147
Cdd:COG0411 86 QNPRLFPELTVLENVlvaaharlgrGLLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 148 ALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDqIEALT-LADRIAVMKGGVVqqLAD 218
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD-MDLVMgLADRIVVLDFGRV--IAE 234
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-194 |
6.71e-41 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 142.62 E-value: 6.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLD---ISEGSIFIKGRNVTWQEPKDRGIGM 80
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYPQMTVEKNLSFGLRvAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDE 160
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190
....*....|....*....|....*....|....
gi 1693059733 161 PLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHD 194
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-211 |
7.15e-41 |
|
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: 141.37 E-value: 7.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGS--VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGM 80
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYpQMTVEKNLsfglrvaglpkaeidkrikraaeilqiepllqrkpsaLSGGQRQRVAIGRALVRDVDVFLFDE 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1693059733 161 PLSNLDAKLRSELRVEIKRLHQklGNTMIYVTHDqIEALTLADRIAVMKGG 211
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-213 |
7.35e-41 |
|
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: 141.03 E-value: 7.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD---RGIGMV 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 FQsyalypqmtveknlsfglrvaglpkaeidkrikraaeilqiepllqrkpsaLSGGQRQRVAIGRALVRDVDVFLFDEP 161
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 162 LSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-213 |
1.50e-40 |
|
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: 142.43 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDR---GIGMVF 82
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 QSYALYPQMTVEKNLSFGLRVAGlPKAEIDKRIKRAAEILQI-EPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEP 161
Cdd:COG0410 85 EGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELFPRlKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 162 LSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:COG0410 164 SLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRI 214
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-227 |
4.00e-40 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 144.10 E-value: 4.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF-----------GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEP 73
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 74 KD-----RGIGMVFQ-SYA-LYPQMTVEKNLSFGLRVAGL-PKAEidkRIKRAAEILQIEPL----LQRKPSALSGGQRQ 141
Cdd:COG4608 88 RElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGLaSKAE---RRERVAELLELVGLrpehADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 142 RVAIGRALVRDVDVFLFDEPLSNLDaklrselrVEI--------KRLHQKLGNTMIYVTHDqieaLT----LADRIAVMK 209
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALD--------VSIqaqvlnllEDLQDELGLTYLFISHD----LSvvrhISDRVAVMY 232
|
250
....*....|....*...
gi 1693059733 210 GGVVQQLADPLTIYNRPR 227
Cdd:COG4608 233 LGKIVEIAPRDELYARPL 250
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-215 |
7.20e-40 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 143.79 E-value: 7.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 15 GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-----RGIGMVFQSYALYP 89
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 90 QMTVEKNLSFGLRVAGLPKAEIDKRIkraAEILQIEPLLQRK---PSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLD 166
Cdd:PRK11153 96 SRTVFDNVALPLELAGTPKAEIKARV---TELLELVGLSDKAdryPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 167 -AKLRSELRVeIKRLHQKLGNTMIYVTHdQIEAL-TLADRIAVMKGG-VVQQ 215
Cdd:PRK11153 173 pATTRSILEL-LKDINRELGLTIVLITH-EMDVVkRICDRVAVIDAGrLVEQ 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-213 |
8.38e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 147.10 E-value: 8.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 14 FGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD---RGIGMVFQSYALYPQ 90
Cdd:COG3845 15 FGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIGMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 91 MTVEKNLSFGLRVAGLPKAEIDKRIKRAAEI-----LQIEPllQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNL 165
Cdd:COG3845 95 LTVAENIVLGLEPTKGGRLDRKAARARIRELserygLDVDP--DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1693059733 166 DAKLRSELRVEIKRLhQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:COG3845 173 TPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-211 |
1.93e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 145.93 E-value: 1.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD---RGIGMV 81
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 FQSYALYPQMTVEKNLSFG--LRVAGLpkaeIDKR--IKRAAEILQ-----IEPllQRKPSALSGGQRQRVAIGRALVRD 152
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGrePRRGGL----IDWRamRRRARELLArlgldIDP--DTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693059733 153 VDVFLFDEPLSNLDAKlrselrvEIKRLH------QKLGNTMIYVTH--DQIEAltLADRIAVMKGG 211
Cdd:COG1129 159 ARVLILDEPTASLTER-------EVERLFriirrlKAQGVAIIYISHrlDEVFE--IADRVTVLRDG 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-236 |
3.90e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 136.90 E-value: 3.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIS-----EGSIFIKGRNVtWQEPKD 75
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNI-YSPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 -----RGIGMVFQSYALYPQMTVEKNLSFGLRVAGL--PKAEIDKRI----KRAAEILQIEPLLQRKPSALSGGQRQRVA 144
Cdd:PRK14267 80 pievrREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVewalKKAALWDEVKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 145 IGRALVRDVDVFLFDEPLSNLD---AKLRSELRVEIKRLHqklgnTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLT 221
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKKEY-----TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
250
....*....|....*....
gi 1693059733 222 IYNRPRN----RFVAGFLG 236
Cdd:PRK14267 235 VFENPEHelteKYVTGALG 253
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-213 |
4.49e-38 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 139.24 E-value: 4.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 35 LLGPSGCGKSTLLNCVAGLLDISEGSIFIKGR------NVTWQEPKDRGIGMVFQSYALYPQMTVEKNLSFGlrVAGLPK 108
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaeKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYG--MAKSMV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 109 AEIDKRIkraaEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTM 188
Cdd:PRK11144 107 AQFDKIV----ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPI 182
|
170 180
....*....|....*....|....*
gi 1693059733 189 IYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:PRK11144 183 LYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-211 |
1.55e-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: 133.86 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGeFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG-IGMVFQ 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 SYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1693059733 164 NLDAklrsELRVEIKRLHQKLGNTMIYV--THDQIEALTLADRIAVMKGG 211
Cdd:cd03264 160 GLDP----EERIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAVLNKG 205
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-225 |
2.56e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 135.24 E-value: 2.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVT----WQepKDRGIGMVFQSyalyPQ----- 90
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeenvWD--IRHKIGMVFQN----PDnqfvg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 91 MTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLR 170
Cdd:PRK13650 97 ATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 171 SELRVEIKRLHQKLGNTMIYVTHDqIEALTLADRIAVMKGGVVQQLADPLTIYNR 225
Cdd:PRK13650 177 LELIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-223 |
3.84e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 134.76 E-value: 3.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDF--GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--R 76
Cdd:PRK13635 2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 77 GIGMVFQSyalyPQ-----MTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVR 151
Cdd:PRK13635 82 QVGMVFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 152 DVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTlADRIAVMKGGVVQQLADPLTIY 223
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-229 |
4.71e-37 |
|
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: 133.44 E-value: 4.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDR---GIGMV 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 FQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEP 161
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 162 LSNLDAKLRSELRVEIKRLHQKlgNTMIYVT-HDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNR 229
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDR--GIGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-215 |
4.76e-37 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 133.99 E-value: 4.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 3 SSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGigmvf 82
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 QSYALYPQ-------MTVEKNLSFG----LRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVR 151
Cdd:PRK11231 76 RRLALLPQhhltpegITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 152 DVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGG-VVQQ 215
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGhVMAQ 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-211 |
4.99e-37 |
|
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: 132.71 E-value: 4.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 17 VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQSYALYpQMTVE 94
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQDVTLF-YGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 95 KNLSFGLRVAGlpkaeiDKRIKRAAEILQIEPLLQRKP-----------SALSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:cd03245 96 DNITLGAPLAD------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1693059733 164 NLDakLRSELRVeIKRLHQKLGN-TMIYVTHdQIEALTLADRIAVMKGG 211
Cdd:cd03245 170 AMD--MNSEERL-KERLRQLLGDkTLIIITH-RPSLLDLVDRIIVMDSG 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-213 |
5.22e-37 |
|
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: 132.34 E-value: 5.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQS 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 YALYPQMTVEKNLSFGLRVAGLPKaeidKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSN 164
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1693059733 165 LDAKLRSELRvEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:cd03268 157 LDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-229 |
6.23e-37 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 133.65 E-value: 6.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFikGRNVTWQEPKDRgIGMVFQSYA 86
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL--AGTAPLAEARED-TRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 87 LYPQMTVEKNLSFGLRVAGLPKAEidkrikRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLD 166
Cdd:PRK11247 92 LLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1693059733 167 AKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGvvqQLADPLTI-YNRPRNR 229
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIGLDLTVdLPRPRRR 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-213 |
7.70e-37 |
|
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: 132.49 E-value: 7.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwQEPKD--RGIGMVF 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV-REPREvrRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 QSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPL 162
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1693059733 163 SNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-213 |
1.08e-36 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 132.90 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVF 82
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 QSYALYPQMTVEKNLSFGlRVA---GLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFD 159
Cdd:COG4604 82 QENHINSRLTVRELVAFG-RFPyskGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1693059733 160 EPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-215 |
2.73e-36 |
|
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: 131.40 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 2 NSSVSIQDLSLDF----GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwqePKD-- 75
Cdd:COG4181 6 APIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF---ALDed 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 -------RGIGMVFQSYALYPQMTVEKNLSFGLRVAGLPKAEidkriKRAAEILQ---IEPLLQRKPSALSGGQRQRVAI 145
Cdd:COG4181 83 ararlraRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR-----ARARALLErvgLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 146 GRALVRDVDVFLFDEPLSNLDAKLRS---ELrveIKRLHQKLGNTMIYVTHDQiealTLA---DRIAVMKGGVVQQ 215
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEqiiDL---LFELNRERGTTLVLVTHDP----ALAarcDRVLRLRAGRLVE 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-235 |
2.87e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 132.01 E-value: 2.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 2 NSSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD------ 75
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 ---------RGIGMVFQSYALYPQMTVEKN-LSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRK-PSALSGGQRQRVA 144
Cdd:PRK10619 83 dknqlrllrTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 145 IGRALVRDVDVFLFDEPLSNLDaklrSELRVEIKRLHQKL---GNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLT 221
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALD----PELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQ 238
|
250
....*....|....
gi 1693059733 222 IYNRPRNRFVAGFL 235
Cdd:PRK10619 239 LFGNPQSPRLQQFL 252
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-210 |
3.83e-36 |
|
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: 130.22 E-value: 3.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 15 GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVT----WQEPK-DRGIGMVFQSYALYP 89
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYlRRKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 90 QMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKL 169
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1693059733 170 RSELRVEIKRLHQKlGNTMIYVTHD-QIEALTLADRIAVMKG 210
Cdd:cd03292 172 TWEIMNLLKKINKA-GTTVVVATHAkELVDTTRHRVIALERG 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-265 |
9.57e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 131.68 E-value: 9.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQ-EPKD-----RGIGMVFQ--SYALYPQm 91
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkKNKKlkplrKKVGIVFQfpEHQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 92 TVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQI-EPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLR 170
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 171 SELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPrNRFVAGFLGSPSMNFFSGEIASR 250
Cdd:PRK13634 182 KEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP-DELEAIGLDLPETVKFKRALEEK 260
|
250
....*....|....*....
gi 1693059733 251 SG----KPVFHIGEAAVQL 265
Cdd:PRK13634 261 FGisfpKPCLTLEELAHEV 279
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
17-211 |
1.05e-35 |
|
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: 129.39 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 17 VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG------IGMVFQSYALYPQ 90
Cdd:TIGR02211 18 TRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnkkLGFIYQFHHLLPD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 91 MTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLR 170
Cdd:TIGR02211 98 FTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1693059733 171 SELRVEIKRLHQKLGNTMIYVTHDqieaLTLA---DRIAVMKGG 211
Cdd:TIGR02211 178 KIIFDLMLELNRELNTSFLVVTHD----LELAkklDRVLEMKDG 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-215 |
1.31e-35 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 136.05 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDF--GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNV-TWQEPKDRG-IG 79
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLrDLDEDDLRRrIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQSYALYpQMTVEKNlsfgLRVAgLPKAEiDKRIKRAAEILQIEPLLQRKP-----------SALSGGQRQRVAIGRA 148
Cdd:COG4987 413 VVPQRPHLF-DTTLREN----LRLA-RPDAT-DEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1693059733 149 LVRDVDVFLFDEPLSNLDAKLRSELrveIKRLHQKLGN-TMIYVTHDQiEALTLADRIAVMKGGVVQQ 215
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQAL---LADLLEALAGrTVLLITHRL-AGLERMDRILVLEDGRIVE 549
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-236 |
2.02e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 129.48 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 3 SSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVaGLLDISE------GSIFIKG-RNVTWQEPKD 75
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEagtirvGDITIDTaRSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 RG----IGMVFQSYALYPQMTVEKNLSFG-LRVAGLPKAEIdkrIKRAAEILQIEPLLQRK---PSALSGGQRQRVAIGR 147
Cdd:PRK11264 81 RQlrqhVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEA---TARARELLAKVGLAGKEtsyPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 148 ALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRP- 226
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPq 236
|
250
....*....|...
gi 1693059733 227 --RNR-FVAGFLG 236
Cdd:PRK11264 237 qpRTRqFLEKFLL 249
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-227 |
2.40e-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: 135.20 E-value: 2.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF-----------GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDiSEGSIFIKGRNVTWQEP 73
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 74 KD-----RGIGMVFQS-YA-LYPQMTVEKNLSFGLRV--AGLPKAEIDKRIKRAAEILQIEP-LLQRKPSALSGGQRQRV 143
Cdd:COG4172 355 RAlrplrRRMQVVFQDpFGsLSPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 144 AIGRALVRDVDVFLFDEPLSNLDaklRSeLRVEI----KRLHQKLGNTMIYVTHDQ--IEAltLADRIAVMKGGVVQQLA 217
Cdd:COG4172 435 AIARALILEPKLLVLDEPTSALD---VS-VQAQIldllRDLQREHGLAYLFISHDLavVRA--LAHRVMVMKDGKVVEQG 508
|
250
....*....|
gi 1693059733 218 DPLTIYNRPR 227
Cdd:COG4172 509 PTEQVFDAPQ 518
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-240 |
4.62e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 129.34 E-value: 4.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNvTWQEPKDRGI----GMVFQS-YALYPQMTVE 94
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSKLQGIrklvGIVFQNpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 95 KNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELR 174
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 175 VEIKRLHQKlGNTMIYVTHDqIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAgfLGSPSM 240
Cdd:PRK13644 177 ERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG--LTPPSL 238
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-211 |
9.67e-35 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 126.22 E-value: 9.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFG-SVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEpKDRGIGMVFQS 84
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-RRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 --YALYPQmTVEKNLSFGLRVAGLPKAEIDKRIKRaaeiLQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPL 162
Cdd:cd03226 80 vdYQLFTD-SVREELLLGLKELDAGNEQAETVLKD----LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1693059733 163 SNLDAKLRSELRVEIKRLhQKLGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:cd03226 155 SGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-211 |
1.24e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 127.89 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF--GSVN---VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVT-WQEPK-DRG 77
Cdd:COG1101 2 LELKNLSKTFnpGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTkLPEYKrAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 IGMVFQSYAL--YPQMTVEKNLS--------FGLRvAGLPKAEIDKRIKRAAEI-LQIEPLLQRKPSALSGGQRQRVAIG 146
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLR-RGLTKKRRELFRELLATLgLGLENRLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 147 RALVRDVDVFLFDEPLSNLDAKlRSELRVEI-KRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-219 |
3.60e-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: 133.07 E-value: 3.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQSYALYpQMTVEKN 96
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTLRDN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 97 LSFGLRVAGlpkaeiDKRIKRAAEILQIEPLLQRKPS-----------ALSGGQRQRVAIGRALVRDVDVFLFDEPLSNL 165
Cdd:TIGR03375 559 IALGAPYAD------DEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEPTSAM 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 166 DAklRSELRVeIKRLHQKL-GNTMIYVTHdQIEALTLADRIAVMKGG----------VVQQLADP 219
Cdd:TIGR03375 633 DN--RSEERF-KDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGrivadgpkdqVLEALRKG 693
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-208 |
3.79e-34 |
|
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: 131.64 E-value: 3.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 3 SSVSIQDLSLDF-GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIG 79
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQSYALYPQmTVEKNLSFGLRVAglPKAEIDKRIKRA--AEILQ-----IEPLLQRKPSALSGGQRQRVAIGRALVRD 152
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDA--SDAEIREALERAglDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 153 VDVFLFDEPLSNLDAKLRSELRVEIKRLHQklGNTMIYVTHDqIEALTLADRIAVM 208
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-215 |
7.61e-34 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 124.56 E-value: 7.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDR---GIGMVF 82
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 QSYALYPQMTVEKNLSFGLRVAGLPKAEIDkrikraAEILQIEPLLQ----RKPSALSGGQRQRVAIGRALVRDVDVFLF 158
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIP------DEIYELFPVLKemlgRRGGDLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1693059733 159 DEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVM-KGGVVQQ 215
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMeRGRVVAS 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-213 |
8.62e-34 |
|
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: 123.93 E-value: 8.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwQEPKDRgIGMVFQS 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-IAARNR-IGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 YALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSN 164
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1693059733 165 LDAKLRSELRVEIKRLHQKlGNTMIYVTH--DQIEAltLADRIAVMKGGVV 213
Cdd:cd03269 159 LDPVNVELLKDVIRELARA-GKTVILSTHqmELVEE--LCDRVLLLNKGRA 206
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-215 |
5.03e-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: 5.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 17 VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQSYALYPqMTVE 94
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 95 KNLSFGLRVAglpKAEIDKRIKRAAEIL--------QIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLD 166
Cdd:cd03249 95 ENIRYGKPDA---TDEEVEEAAKKANIHdfimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1693059733 167 AKlrSELRVEiKRLHQ-KLGNTMIYVTHdQIEALTLADRIAVMKGGVVQQ 215
Cdd:cd03249 172 AE--SEKLVQ-EALDRaMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVE 217
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-229 |
9.91e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 122.58 E-value: 9.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIS-----EGSIFIKGRNV------TWQEP 73
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysprtdTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 74 KDrgIGMVFQSYALYPqMTVEKNLSFGLRVAGLPKAEI-----DKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRA 148
Cdd:PRK14239 86 KE--IGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVldeavEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 149 LVRDVDVFLFDEPLSNLDAKlrSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRN 228
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPI--SAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
.
gi 1693059733 229 R 229
Cdd:PRK14239 241 K 241
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-235 |
1.25e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 122.33 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 3 SSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIS-----EGSIFIKGRNVTWQEPKD-- 75
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 RGIGMVFQSYALYPQMTVEKNLSFGLRVAGL--PKAEIDKRIKRAAEILQ----IEPLLQRKPSALSGGQRQRVAIGRAL 149
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 150 VRDVDVFLFDEPLSNLD----AKLRSeLRVEIKRlhqklGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNR 225
Cdd:PRK14247 162 AFQPEVLLADEPTANLDpentAKIES-LFLELKK-----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
250
....*....|....
gi 1693059733 226 PRN----RFVAGFL 235
Cdd:PRK14247 236 PRHelteKYVTGRL 249
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-211 |
1.63e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.91 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwqePKDR-GIGmvf 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRrRIG--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 qsY-----ALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFL 157
Cdd:COG4152 75 --YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 158 FDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTH--DQIEAltLADRIAVMKGG 211
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHqmELVEE--LCDRIVIINKG 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-211 |
2.00e-32 |
|
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: 122.22 E-value: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-----RGIGMVFQ-SY-ALYPQM 91
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQdSPsAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 92 TVEKNLSFGLR-VAGLPKAEidkRIKRAAEILQIEPL----LQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLD 166
Cdd:TIGR02769 106 TVRQIIGEPLRhLTSLDESE---QKARIAELLDMVGLrsedADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1693059733 167 AKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
2.72e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 121.77 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDFGSVN-VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-RG- 77
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 IGMVFQSyalyPQ-----MTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRD 152
Cdd:PRK13647 81 VGLVFQD----PDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 153 VDVFLFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNR 225
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-215 |
2.80e-32 |
|
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: 120.80 E-value: 2.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGS--VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGM 80
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYPQmTVEKNLSFGLRVAGlpkaeiDKRIKRAAEILQIEPLLQRKP-----------SALSGGQRQRVAIGRAL 149
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGRPGAT------REEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 150 VRDVDVFLFDEPLSNLDakLRSELRVE--IKRLHQklGNTMIYVTHdQIEALTLADRIAVM-KGGVVQQ 215
Cdd:cd03251 154 LKDPPILILDEATSALD--TESERLVQaaLERLMK--NRTTFVIAH-RLSTIENADRIVVLeDGKIVER 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-224 |
2.88e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 122.50 E-value: 2.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 18 NVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRN----------------VTWQEPKDRGI--- 78
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvlekLVIQKTRFKKIkki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 79 -------GMVFQ--SYALYPQmTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQI-EPLLQRKPSALSGGQRQRVAIGRA 148
Cdd:PRK13651 101 keirrrvGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 149 LVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYN 224
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-223 |
6.18e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 120.96 E-value: 6.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKG-----RNVTWqEPKDRGiGMVFQSyalyP--QM 91
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdEENLW-DIRNKA-GMVFQN----PdnQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 92 T---VEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK 168
Cdd:PRK13633 99 VatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 169 LRSELRVEIKRLHQKLGNTMIYVTHDQIEALTlADRIAVMKGGVVQQLADPLTIY 223
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-213 |
1.61e-31 |
|
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: 119.03 E-value: 1.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEG-SIFIKGR---NVTWQEPKDRgIGM 80
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrgGEDVWELRKR-IGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VfqSYAL----YPQMTVEKNL------SFGLRVAglPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALV 150
Cdd:COG1119 83 V--SPALqlrfPRDETVLDVVlsgffdSIGLYRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 151 RDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-236 |
2.42e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 119.12 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 8 QDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDI-----SEGSIFIKGRNVTWQE--PKD--RGI 78
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDvdPVEvrRRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 79 GMVFQSYALYPQmTVEKNLSFGLRVAGLpKAEID----KRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVD 154
Cdd:PRK14243 94 GMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDelveRSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 155 VFLFDEPLSNLDAKlrSELRVE--IKRLHQKLgnTMIYVTHDQIEALTLADRIA------VMKGGVVQQLA--DPL-TIY 223
Cdd:PRK14243 172 VILMDEPCSALDPI--STLRIEelMHELKEQY--TIIIVTHNMQQAARVSDMTAffnvelTEGGGRYGYLVefDRTeKIF 247
|
250
....*....|....*..
gi 1693059733 224 NRPRNR----FVAGFLG 236
Cdd:PRK14243 248 NSPQQQatrdYVSGRFG 264
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-213 |
3.95e-31 |
|
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: 116.50 E-value: 3.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLD--ISEGSIFIKGRNVTWQEPKDRgIGMVFQSYALYPQMTVEKN 96
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 97 LSFglrvaglpkaeidkrikrAAEIlqiepllqrkpSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVE 176
Cdd:cd03213 103 LMF------------------AAKL-----------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1693059733 177 IKRLHQkLGNTMIYVTHD-QIEALTLADRIAVMKGGVV 213
Cdd:cd03213 154 LRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-227 |
4.85e-31 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 122.87 E-value: 4.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGS----VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLD----ISEGSIFIKGRNVTWQEPKD-- 75
Cdd:COG4172 8 SVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSERElr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 --RG--IGMVFQ--SYALYPQMTVEKNLSFGLRV-AGLPKAEIDKRikrAAEILQ---I---EPLLQRKPSALSGGQRQR 142
Cdd:COG4172 88 riRGnrIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARAR---ALELLErvgIpdpERRLDAYPHQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 143 VAIGRALVRDVDVFLFDEPLSNLDAKLRS---ELrveIKRLHQKLGNTMIYVTHDqieaLTL----ADRIAVMKGGVVQQ 215
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAqilDL---LKDLQRELGMALLLITHD----LGVvrrfADRVAVMRQGEIVE 237
|
250
....*....|..
gi 1693059733 216 LADPLTIYNRPR 227
Cdd:COG4172 238 QGPTAELFAAPQ 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-215 |
7.07e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 116.84 E-value: 7.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 16 SVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTW------QEPKDRGIGMVFQSYALYP 89
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakAELRNQKLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 90 QMTVEKNLSFGLRVAGLPKAEIDKRikrAAEILQIEPLLQR---KPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLD 166
Cdd:PRK11629 101 DFTALENVAMPLLIGKKKPAEINSR---ALEMLAAVGLEHRanhRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 167 AKLRSELRVEIKRLHQKLGNTMIYVTHDqieaLTLADRIA---VMKGGVVQQ 215
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRMSrqlEMRDGRLTA 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-229 |
1.04e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 116.67 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 2 NSSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwQEPKDR----G 77
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-HLPMHKrarlG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 IGmvfqsyalY-PQ-------MTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRAL 149
Cdd:COG1137 80 IG--------YlPQeasifrkLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 150 VRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQK-LGntmIYVT-HDQIEALTLADRIAVMKGGVVqqLA--DPLTIYNR 225
Cdd:COG1137 152 ATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERgIG---VLITdHNVRETLGICDRAYIISEGKV--LAegTPEEILNN 226
|
....
gi 1693059733 226 PRNR 229
Cdd:COG1137 227 PLVR 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
15-211 |
1.98e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 116.71 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 15 GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-----RGIGMVFQSY--AL 87
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSisAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 88 YPQMTVEKNLSFGLR-VAGLPKAEidkRIKRAAEILQI----EPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPL 162
Cdd:PRK10419 103 NPRKTVREIIREPLRhLLSLDKAE---RLARASEMLRAvdldDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1693059733 163 SNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-211 |
2.00e-30 |
|
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: 114.87 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVN-----VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGrnvtwqepkdrgig 79
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 mvfqSYALYPQ------MTVEKNLSFGlrvaglpkAEIDK-RIKRAAEILQIEPLLQRKP-----------SALSGGQRQ 141
Cdd:cd03250 67 ----SIAYVSQepwiqnGTIRENILFG--------KPFDEeRYEKVIKACALEPDLEILPdgdlteigekgINLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 142 RVAIGRALVRDVDVFLFDEPLSNLDAKLRSEL--RVEIKRLhqKLGNTMIYVTHdQIEALTLADRIAVMKGG 211
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLL--LNNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-213 |
4.29e-30 |
|
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: 115.02 E-value: 4.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKG---RNVTwQEPKDRGIGMVfqsyalyPQMTVEK 95
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVT-LDSLRRAIGVV-------PQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 96 NLSFGLRVA-GLPKAEiDKRIKRAAEILQIEPLLQRKPSA-----------LSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:cd03253 88 NDTIGYNIRyGRPDAT-DEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1693059733 164 NLDAKLRSELRVEIKRLHQklGNTMIYVTHdQIEALTLADRIAVMKGGVV 213
Cdd:cd03253 167 ALDTHTEREIQAALRDVSK--GRTTIVIAH-RLSTIVNADKIIVLKDGRI 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-213 |
6.87e-30 |
|
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: 112.69 E-value: 6.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG--IGMVFQSYALYPQmTVEKN 96
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 97 LsfglrvaglpkaeidkrikraaeilqiepllqrkpsaLSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVE 176
Cdd:cd03246 96 I-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 1693059733 177 IKRLhQKLGNTMIYVTHdQIEALTLADRIAVMKGGVV 213
Cdd:cd03246 139 IAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
15-211 |
8.43e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 120.21 E-value: 8.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 15 GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGI------GMVFQSYALY 88
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrrehfGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 89 PQMTVEKNLSFGLRVAGLPKAEidkRIKRAAEILQIEPLLQR---KPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNL 165
Cdd:PRK10535 99 SHLTAAQNVEVPAVYAGLERKQ---RLLRAQELLQRLGLEDRveyQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1693059733 166 DAKLRSELRVEIKRLHQKlGNTMIYVTHD-QIEAltLADRIAVMKGG 211
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDR-GHTVIIVTHDpQVAA--QAERVIEIRDG 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-223 |
9.89e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 115.19 E-value: 9.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDF---GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-- 75
Cdd:PRK13642 1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 RGIGMVFQSY-ALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVD 154
Cdd:PRK13642 81 RKIGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 155 VFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTlADRIAVMKGGVVQQLADPLTIY 223
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-208 |
1.08e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 112.71 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 14 FGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGrnvtwqepkDRGIGMVFQSYALYPQM-- 91
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVPDSLpl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 92 TVEKNLSFGL-RVAGL---PKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDA 167
Cdd:NF040873 73 TVRDLVAMGRwARRGLwrrLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1693059733 168 KLRSELRVEIKRLHQKlGNTMIYVTHDqIEALTLADRIAVM 208
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHD-LELVRRADPCVLL 191
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-213 |
1.81e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.56 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPK----DRGIGMVFQS--YALYpQMTV 93
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklRESVGMVFQDpdNQLF-SASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 94 EKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSEL 173
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1693059733 174 RVEIKRLHQKLGNTMIYVTHDqIEALTL-ADRIAVMKGGVV 213
Cdd:PRK13636 181 MKLLVEMQKELGLTIIIATHD-IDIVPLyCDNVFVMKEGRV 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-226 |
2.31e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.13 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 8 QDLSLDF-GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQS 84
Cdd:PRK13652 7 RDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 ---YALYPqmTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEP 161
Cdd:PRK13652 87 pddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 162 LSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRP 226
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-211 |
6.76e-29 |
|
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: 111.66 E-value: 6.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 13 DFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGrNVTWQEPKD--RGIGMVF-QSYALYP 89
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKflRRIGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 90 QMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKL 169
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1693059733 170 RSELRVEIKRLHQKLGNTMIYVTHD--QIEAltLADRIAVMKGG 211
Cdd:cd03267 189 QENIRNFLKEYNRERGTTVLLTSHYmkDIEA--LARRVLVIDKG 230
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-228 |
1.28e-28 |
|
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: 110.92 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 21 QNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLD----ISEGSIFIKGRNVTWQEPKDRGIGMVFQS--YALYPQMTVE 94
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 95 KNLSFGLRVAGLPKAEIDKRIK---RAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRS 171
Cdd:TIGR02770 83 NHAIETLRSLGKLSKQARALILealEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1693059733 172 ELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRN 228
Cdd:TIGR02770 163 RVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-227 |
1.47e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 113.26 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 24 NLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDR-----GIGMVFQS--YALYPQMTVEKN 96
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 97 LSFGLRV--AGLPKAEIDKRIKRAAEILQIEP-LLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSEL 173
Cdd:PRK15079 121 IAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1693059733 174 RVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPR 227
Cdd:PRK15079 201 VNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-211 |
1.72e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 115.65 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDR---GIGMV 81
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 FQSYALYPQMTVEKNLSFGL----RVAGLPKAEIDKRIKRAAEILQIEPL---LQRKPSALSGGQRQRVAIGRALVRDVD 154
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRhltkKVCGVNIIDWREMRVRAAMMLLRVGLkvdLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1693059733 155 VFLFDEPLSNLDAKLRSELRVEIKRLhQKLGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-222 |
1.77e-28 |
|
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: 115.67 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIK-GR---NVTWQEPKDRG--- 77
Cdd:TIGR03269 285 VSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDewvDMTKPGPDGRGrak 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 --IGMVFQSYALYPQMTVEKNL--SFGLRvagLPKaEIDKRikRAAEILQI--------EPLLQRKPSALSGGQRQRVAI 145
Cdd:TIGR03269 365 ryIGILHQEYDLYPHRTVLDNLteAIGLE---LPD-ELARM--KAVITLKMvgfdeekaEEILDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693059733 146 GRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTI 222
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-226 |
2.99e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 110.90 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIsEGSIFIKGR----NVTWQEPK----- 74
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRveffNQNIYERRvnlnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 75 -DRGIGMVFQSYALYPqMTVEKNLSFGLRVAGL-PKAEIDKRIK---RAAEIL-QIEPLLQRKPSALSGGQRQRVAIGRA 148
Cdd:PRK14258 86 lRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVEsalKDADLWdEIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 149 LVRDVDVFLFDEPLSNLD--AKLRSELRVEIKRLHQKLgnTMIYVTHDQIEALTLADRIAVMKGG---VVQQLADPLT-- 221
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDpiASMKVESLIQSLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFKGNenrIGQLVEFGLTkk 242
|
....*
gi 1693059733 222 IYNRP 226
Cdd:PRK14258 243 IFNSP 247
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
4.10e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 111.87 E-value: 4.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDFGS-----VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIK----------GRNV 68
Cdd:PRK13631 21 ILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 69 TWQEPKD--------RGIGMVFQ--SYALYpQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQI-EPLLQRKPSALSG 137
Cdd:PRK13631 101 TNPYSKKiknfkelrRRVSMVFQfpEYQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 138 GQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELrVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLA 217
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
....*.
gi 1693059733 218 DPLTIY 223
Cdd:PRK13631 259 TPYEIF 264
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-211 |
7.09e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.17 E-value: 7.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPK----DRGIGMVFQSyalyP--QM- 91
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevRKTVGIVFQN----PddQLf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 92 --TVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKL 169
Cdd:PRK13639 93 apTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1693059733 170 RSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:PRK13639 173 ASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDG 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-224 |
7.75e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.84 E-value: 7.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQSyalyPQ-----MT 92
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQN----PDnqfvgSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 93 VEKNLSFGLRVAGLPKAEIDKRIKRAAEilQIEPLLQR--KPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLR 170
Cdd:PRK13648 101 VKYDVAFGLENHAVPYDEMHRRVSEALK--QVDMLERAdyEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1693059733 171 SELRVEIKRLHQKLGNTMIYVTHDQIEALTlADRIAVMKGGVVQQLADPLTIYN 224
Cdd:PRK13648 179 QNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-211 |
8.55e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 109.43 E-value: 8.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVT----WQEPKDRGigmV 81
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawspWELARRRA---V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 F-QSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRAL------VRDVD 154
Cdd:COG4559 80 LpQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1693059733 155 VFLF-DEPLSNLDakLRSELRV-EI-KRLHQKlGNTMIYVTHDqieaLTL----ADRIAVMKGG 211
Cdd:COG4559 160 RWLFlDEPTSALD--LAHQHAVlRLaRQLARR-GGGVVAVLHD----LNLaaqyADRILLLHQG 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-224 |
1.06e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 110.10 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLdISE------GSIFIKGRNVTWQEPKD--RGIGMVFQ--SYALYp 89
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-ISEtgqtivGDYAIPANLKKIKEVKRlrKEIGLVFQfpEYQLF- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 90 QMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQI-EPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK 168
Cdd:PRK13645 105 QETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 169 LRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYN 224
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-219 |
3.30e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 107.47 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDF----------------------GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISE 58
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 59 GSIFIKGRnVTWqePKDRGIGMVfqsyalyPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGG 138
Cdd:COG1134 81 GRVEVNGR-VSA--LLELGAGFH-------PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 139 QRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHD--QIEalTLADRIAVMKGGVVQQL 216
Cdd:COG1134 151 MRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSmgAVR--RLCDRAIWLEKGRLVMD 227
|
...
gi 1693059733 217 ADP 219
Cdd:COG1134 228 GDP 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-233 |
4.59e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 106.89 E-value: 4.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVT-WQEPK--DRG 77
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdWQTAKimREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 IGMVFQSYALYPQMTVEKNLSFGLRVAglPKAEIDKRIKRAAEILqiePLLQ----RKPSALSGGQRQRVAIGRALVRDV 153
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYELF---PRLHerriQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 154 DVFLFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGG--VVQQLADPLTIYNRPRNRFV 231
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGhvVLEDTGDALLANEAVRSAYL 235
|
..
gi 1693059733 232 AG 233
Cdd:PRK11614 236 GG 237
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-215 |
7.10e-27 |
|
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: 106.16 E-value: 7.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQSYALYPQmTVEKN 96
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 97 LSFglrvaGLPKAEiDKRIKRAAEILQIEPLLQRKP-----------SALSGGQRQRVAIGRALVRDVDVFLFDEPLSNL 165
Cdd:cd03254 97 IRL-----GRPNAT-DEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 166 DAKlrSELRVE--IKRLHQklGNTMIYVTHdQIEALTLADRIAVMKGG-VVQQ 215
Cdd:cd03254 171 DTE--TEKLIQeaLEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGkIIEE 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-215 |
2.40e-26 |
|
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: 109.84 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG--IGMVFQSYALYPQmTVEKN 96
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhIGYLPQDVELFDG-TIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 97 lsfglrVAGLPKAEIDKrIKRAAEILQIEPLLQRKP-----------SALSGGQRQRVAIGRALVRDVDVFLFDEPLSNL 165
Cdd:COG4618 426 ------IARFGDADPEK-VVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1693059733 166 DAKLRSELRVEIKRLHQKlGNTMIYVTHDQiEALTLADRIAVMKGGVVQQ 215
Cdd:COG4618 499 DDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQA 546
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-217 |
2.51e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 105.84 E-value: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 8 QDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQSY 85
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 86 ALYPQMTVEKNLSFGlRVAGLP-----KAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDE 160
Cdd:PRK10253 91 TTPGDITVQELVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1693059733 161 PLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADR-IAVMKGGVVQQLA 217
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHlIALREGKIVAQGA 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-225 |
3.60e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 105.47 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEpkdRGIGMVFQS 84
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK---RGLLALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 YALYPQ--------MTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVF 156
Cdd:PRK13638 79 VATVFQdpeqqifyTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 157 LFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNR 225
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-225 |
3.96e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.60 E-value: 3.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQ-EPKD-----RGIGMVFQsyalYPQM-- 91
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsKNKDikqirKKVGLVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 92 ---TVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQI-EPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDA 167
Cdd:PRK13649 99 feeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1693059733 168 KLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNR 225
Cdd:PRK13649 179 KGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-219 |
4.76e-26 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 103.78 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 25 LEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNvtwQEPKDRGIGMVFQSYAL---YPQMTVEKNLSFGL 101
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS---PGKGWRHIGYVPQRHEFawdFPISVAHTVMSGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 102 RVAGL---PKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKlRSELRVEIK 178
Cdd:TIGR03771 78 GHIGWlrrPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMP-TQELLTELF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1693059733 179 RLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV-----QQLADP 219
Cdd:TIGR03771 157 IELAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIadgtpQQLQDP 202
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-238 |
4.82e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 104.85 E-value: 4.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNV------TWQEPKDRgI 78
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrsRLYTVRKR-M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 79 GMVFQSYALYPQMTVEKNLSFGLRV-AGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFL 157
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 158 FDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGG--VVQQLADPLTIYNRPRNR-FVAGF 234
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKkiVAHGSAQALQANPDPRVRqFLDGI 246
|
....
gi 1693059733 235 LGSP 238
Cdd:PRK11831 247 ADGP 250
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-210 |
4.98e-26 |
|
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: 104.41 E-value: 4.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 26 EIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQ----EPKDrgigmvfqsyalypQMTVEKNLSFGL 101
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKpqyiKADY--------------EGTVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 102 RVAGLP---KAEIdkrikraAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIK 178
Cdd:cd03237 87 KDFYTHpyfKTEI-------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170 180 190
....*....|....*....|....*....|..
gi 1693059733 179 RLHQKLGNTMIYVTHDQIEALTLADRIAVMKG 210
Cdd:cd03237 160 RFAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-241 |
5.08e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 106.20 E-value: 5.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 15 GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-----RGIGMVFQS-YA-L 87
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 88 YPQMTVEKNLSFGLRV-AGLPKAEidkRIKRAAEILQIEPL----LQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPL 162
Cdd:PRK11308 106 NPRKKVGQILEEPLLInTSLSAAE---RREKALAMMAKVGLrpehYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 163 SNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRFVAGFLGS-PSMN 241
Cdd:PRK11308 183 SALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSAtPRLN 262
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-211 |
6.17e-26 |
|
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: 102.13 E-value: 6.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDfgsvNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDR---GIGMV 81
Cdd:cd03215 5 LEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 ---FQSYALYPQMTVEKNLSFglrvaglpkaeidkrikraaeilqiepllqrkPSALSGGQRQRVAIGRALVRDVDVFLF 158
Cdd:cd03215 81 pedRKREGLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 159 DEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-211 |
8.87e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 107.69 E-value: 8.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 14 FGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD---RGIGMVFQSYALYPQ 90
Cdd:PRK11288 14 FPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaAGVAIIYQELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 91 MTVEKNLSFGlrvaGLPKAE--IDKR--IKRAAEILQ-----IEPllQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEP 161
Cdd:PRK11288 94 MTVAENLYLG----QLPHKGgiVNRRllNYEAREQLEhlgvdIDP--DTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1693059733 162 LSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-247 |
1.16e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.53 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEP----KD--RGIGMVFQsyalYPQM-- 91
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKlrKKVSLVFQ----FPEAql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 92 ---TVEKNLSFGLRVAGLPKAEI-DKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDA 167
Cdd:PRK13641 99 fenTVLKDVEFGPKNFGFSEDEAkEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 168 KLRSELrVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPrNRFVAGFLGSPSMNFFSGEI 247
Cdd:PRK13641 179 EGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK-EWLKKHYLDEPATSRFASKL 256
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-213 |
2.20e-25 |
|
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: 101.96 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 16 SVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLD---ISEGSIFIKGRNVTWQEPKDRgIGMVFQSYALYPQMT 92
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 93 VEKNLSFGLRVAgLPKAEIDKRIKRAAEI-----LQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDA 167
Cdd:cd03234 98 VRETLTYTAILR-LPRKSSDAIRKKRVEDvllrdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1693059733 168 KLRSELRVEIKRLHQklGNTMIYVTHDQ--IEALTLADRIAVMKGGVV 213
Cdd:cd03234 177 FTALNLVSTLSQLAR--RNRIVILTIHQprSDLFRLFDRILLLSSGEI 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-211 |
2.80e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.73 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG-IGMVFQ 83
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 SYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1693059733 164 NLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-224 |
5.20e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.55 E-value: 5.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwQEPKDR-------GIGMVFQsyalYPQM- 91
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIT-HKTKDKyirpvrkRIGMVFQ----FPESq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 92 ----TVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIE-PLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLD 166
Cdd:PRK13646 98 lfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1693059733 167 AKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYN 224
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-226 |
5.21e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.57 E-value: 5.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 2 NSSVSIQDLSLDF--GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLL---DISEGSIFIKGRNVT----WqE 72
Cdd:PRK13640 3 DNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTaktvW-D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 73 PKDRgIGMVFQSyalyPQ-----MTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGR 147
Cdd:PRK13640 82 IREK-VGIVFQN----PDnqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 148 ALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDqIEALTLADRIAVMKGGVVQQLADPLTIYNRP 226
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHD-IDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-211 |
6.55e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 101.30 E-value: 6.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLD--ISEGSIFIKGRNVTWQEPKDR---GIGM 80
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQsyalYPqmtVE----KNLSFgLRVA-------GLPKAEIDKRIKRAAEILQIEP-LLQRkpSA---LSGGQRQRVAI 145
Cdd:COG0396 82 AFQ----YP---VEipgvSVSNF-LRTAlnarrgeELSAREFLKLLKEKMKELGLDEdFLDR--YVnegFSGGEKKRNEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1693059733 146 GRALVRDVDVFLFDEPLSNLDA---KLRSELrveIKRLHQKlGNTMIYVTH-----DQIEaltlADRIAVMKGG 211
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIdalRIVAEG---VNKLRSP-DRGILIITHyqrilDYIK----PDFVHVLVDG 217
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-214 |
6.75e-25 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 105.51 E-value: 6.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG--IGMVFQSYALYPQmTVEKN 96
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIGYLPQDVELFPG-TVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 97 LSfglRVAGLPKAEidkRIKRAAEILQIEPLLQRKP-----------SALSGGQRQRVAIGRALVRDVDVFLFDEPLSNL 165
Cdd:TIGR01842 412 IA---RFGENADPE---KIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1693059733 166 DAKLRSELRVEIKRLhQKLGNTMIYVTHdQIEALTLADRIAVMKGGVVQ 214
Cdd:TIGR01842 486 DEEGEQALANAIKAL-KARGITVVVITH-RPSLLGCVDKILVLQDGRIA 532
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-230 |
7.69e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.17 E-value: 7.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKST----LLNCVAglldiSEGSIFIKGRNV-TWQE----PKDRGIGMVFQ--SYAL 87
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLhNLNRrqllPVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 88 YPQMTVEKNLSFGLRV--AGLPKAEIDKRIKRAAEILQIEPLL-QRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSN 164
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 165 LDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRF 230
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-247 |
7.90e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.12 E-value: 7.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQ------EPKDRGIGMVFQsyalYPQM-- 91
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkeiKPVRKKVGVVFQ----FPESql 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 92 ---TVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQI-EPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDA 167
Cdd:PRK13643 98 feeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 168 KLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPrNRFVAGFLGSPSMNFFSGEI 247
Cdd:PRK13643 178 KARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEV-DFLKAHELGVPKATHFADQL 255
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-194 |
1.04e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 100.24 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 17 VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG------IGMVFQSYALYPQ 90
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 91 MTVEKNlsfgLRVAGLPKAEIDKRIK-RAAEILQIEPLLQR---KPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLD 166
Cdd:PRK10584 103 LNALEN----VELPALLRGESSRQSRnGAKALLEQLGLGKRldhLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180
....*....|....*....|....*...
gi 1693059733 167 AKLRSELRVEIKRLHQKLGNTMIYVTHD 194
Cdd:PRK10584 179 RQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-215 |
1.06e-24 |
|
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: 105.21 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDFG-SVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVtwqepKDRGIG 79
Cdd:TIGR01193 470 LNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL-----KDIDRH 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQSYALYPQM------TVEKNLSFGLRvaglPKAEIDKrIKRAAEILQIEPLLQRKP-----------SALSGGQRQR 142
Cdd:TIGR01193 545 TLRQFINYLPQEpyifsgSILENLLLGAK----ENVSQDE-IWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1693059733 143 VAIGRALVRDVDVFLFDEPLSNLDakLRSELRVeIKRLHQKLGNTMIYVTHdQIEALTLADRIAVM-KGGVVQQ 215
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLD--TITEKKI-VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLdHGKIIEQ 689
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-300 |
1.27e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.38 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGigmvfQS 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS-----RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 YALYPQmtvEKNLSFGLRVAGL-------------PKAEIDKR-IKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALV 150
Cdd:PRK09536 79 VASVPQ---DTSLSFEFDVRQVvemgrtphrsrfdTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 151 RDVDVFLFDEPLSNLDakLRSELR-VEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNR 229
Cdd:PRK09536 156 QATPVLLLDEPTASLD--INHQVRtLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 230 fvAGF-----------LGSPSMNFFSG-EIASRSGKPVFHI---GEAAVQLDGydGALEQGRKVTLGVRPEHirlDVADG 294
Cdd:PRK09536 234 --AAFdartavgtdpaTGAPTVTPLPDpDRTEAAADTRVHVvggGQPAARAVS--RLVAAGASVSVGPVPEG---DTAAE 306
|
....*.
gi 1693059733 295 FEATVD 300
Cdd:PRK09536 307 TAARVG 312
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-211 |
2.01e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.23 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGigmvfQSY 85
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA-----RRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 86 ALYPQMTvekNLSFGLRVA----------GLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVR---- 151
Cdd:PRK13548 79 AVLPQHS---SLSFPFTVEevvamgraphGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwep 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1693059733 152 --DVDVFLFDEPLSNLDakLRSELRV-EI-KRLHQKLGNTMIYVTHDqieaLTLA----DRIAVMKGG 211
Cdd:PRK13548 156 dgPPRWLLLDEPTSALD--LAHQHHVlRLaRQLAHERGLAVIVVLHD----LNLAaryaDRIVLLHQG 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-213 |
3.30e-24 |
|
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: 98.76 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRnVTWqePKDRGIGMVfqsyalyPQMTVEKNLS 98
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSS--LLGLGGGFN-------PELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 99 FGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIK 178
Cdd:cd03220 107 LNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLR 186
|
170 180 190
....*....|....*....|....*....|....*
gi 1693059733 179 RLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:cd03220 187 ELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-194 |
3.51e-24 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 98.79 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 14 FGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD-----RGIGMVFQSYALY 88
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 89 PQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK 168
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180
....*....|....*....|....*.
gi 1693059733 169 LrSELRVEIKRLHQKLGNTMIYVTHD 194
Cdd:PRK10908 172 L-SEGILRLFEEFNRVGVTVLMATHD 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-194 |
3.65e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIkgrnvtwqePKDRGIGMVFQSYA 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 87 LYPQMTVEKNLSFGLRVAGLPKAEIDK--------------------------------RIKRAAEILQI-EPLLQRKPS 133
Cdd:COG0488 72 LDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedlerlaelqeefealggweaeaRAEEILSGLGFpEEDLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 134 ALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK----LRSELRveikrlhqKLGNTMIYVTHD 194
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLEsiewLEEFLK--------NYPGTVLVVSHD 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-205 |
4.78e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.25 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 15 GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQSYALYPQmT 92
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 93 VEKNLSFGLRVAGlPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSE 172
Cdd:PRK10247 97 VYDNLIFPWQIRN-QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHN 175
|
170 180 190
....*....|....*....|....*....|...
gi 1693059733 173 LRVEIKRLHQKLGNTMIYVTHDQIEaLTLADRI 205
Cdd:PRK10247 176 VNEIIHRYVREQNIAVLWVTHDKDE-INHADKV 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-211 |
4.97e-24 |
|
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: 97.00 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVN--VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNV-TWQEPKDRGIGMV 81
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVsDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 FQSYALYpQMTVEKNLsfGLRvaglpkaeidkrikraaeilqiepllqrkpsaLSGGQRQRVAIGRALVRDVDVFLFDEP 161
Cdd:cd03247 81 NQRPYLF-DTTLRNNL--GRR--------------------------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1693059733 162 LSNLDAKLRSE-LRVEIKRLHQKlgnTMIYVTHdQIEALTLADRIAVMKGG 211
Cdd:cd03247 126 TVGLDPITERQlLSLIFEVLKDK---TLIWITH-HLTGIEHMDKILFLENG 172
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-213 |
6.92e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 98.93 E-value: 6.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLL---DISEGSIFIKGRNVTWQEPKDRG 77
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 I-------GMVFQSYALYPQMTVEKNLSFGlRVAGLP---------KAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQ 141
Cdd:PRK09984 81 IrksrantGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 142 RVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-215 |
9.62e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 102.23 E-value: 9.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDL---SLDfGSVnVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIsEGSIFIKGRNVTWQEPKD--RGI 78
Cdd:PRK11174 349 TIEAEDLeilSPD-GKT-LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESwrKHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 79 GMVFQSYALyPQMTVEKNLSFGlrVAGLPKAEIDKRIKRA--AEILQIEPL-----LQRKPSALSGGQRQRVAIGRALVR 151
Cdd:PRK11174 426 SWVGQNPQL-PHGTLRDNVLLG--NPDASDEQLQQALENAwvSEFLPLLPQgldtpIGDQAAGLSVGQAQRLALARALLQ 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 152 DVDVFLFDEPLSNLDAklRSELRVeIKRLHQ-KLGNTMIYVTHdQIEALTLADRIAVMKGG-VVQQ 215
Cdd:PRK11174 503 PCQLLLLDEPTASLDA--HSEQLV-MQALNAaSRRQTTLMVTH-QLEDLAQWDQIWVMQDGqIVQQ 564
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-212 |
1.87e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.13 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 3 SSVSIQ--DLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDR-GIG 79
Cdd:PRK13536 38 STVAIDlaGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFD 159
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 160 EPLSNLDAKLRsELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGV 212
Cdd:PRK13536 198 EPTTGLDPHAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-211 |
4.49e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.85 E-value: 4.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 17 VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRnVTWQEPKD--RGIGMVF-QSYALYPQMTV 93
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY-VPFKRRKEfaRRIGVVFgQRSQLWWDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 94 EKnlSFGL--RVAGLPKAEIDKRIKRAAEILQIEPLLQ---RKpsaLSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK 168
Cdd:COG4586 114 ID--SFRLlkAIYRIPDAEYKKRLDELVELLDLGELLDtpvRQ---LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVV 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1693059733 169 LRSELRVEIKRLHQKLGNTMIYVTHD--QIEAltLADRIAVMKGG 211
Cdd:COG4586 189 SKEAIREFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHG 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-213 |
4.66e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.71 E-value: 4.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDfgsvNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD---RGIGMV- 81
Cdd:COG1129 258 EVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVp 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 --FQSYALYPQMTVEKNLSFG----LRVAG-LPKAEIDKRIKRAAEILQIE-PLLQRKPSALSGGQRQRVAIGRALVRDV 153
Cdd:COG1129 334 edRKGEGLVLDLSIRENITLAsldrLSRGGlLDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 154 DVFLFDEPLSNLD--AKlrselrVEIKRLHQKL---GNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:COG1129 414 KVLILDEPTRGIDvgAK------AEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-193 |
4.67e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 95.33 E-value: 4.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRgIGMVFQSYALYPQMTVEKNLS 98
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 99 FGLRVAGLPKAEIDkrikRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKlRSELRVEIK 178
Cdd:PRK13539 96 FWAAFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAELI 170
|
170
....*....|....*
gi 1693059733 179 RLHQKLGNTMIYVTH 193
Cdd:PRK13539 171 RAHLAQGGIVIAATH 185
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-227 |
7.17e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.83 E-value: 7.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTW---QEPKDRGIGMVF 82
Cdd:PRK11300 7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlpgHQIARMGVVRTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 QSYALYPQMTVEKNL--------SFGLrVAGLPK------AEIDKrIKRAAEILQIEPLLQ---RKPSALSGGQRQRVAI 145
Cdd:PRK11300 87 QHVRLFREMTVIENLlvaqhqqlKTGL-FSGLLKtpafrrAESEA-LDRAATWLERVGLLEhanRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 146 GRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNR 225
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 244
|
..
gi 1693059733 226 PR 227
Cdd:PRK11300 245 PD 246
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-215 |
8.72e-23 |
|
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: 95.25 E-value: 8.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPK--DRGIGMVFQSYALYPQmTVEKN 96
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLFNR-SIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 97 LSFGLRVAGLPKAEIDKRIKRAAE-ILQI----EPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKlrS 171
Cdd:cd03252 96 IALADPGMSMERVIEAAKLAGAHDfISELpegyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE--S 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1693059733 172 ElRVEIKRLHQKL-GNTMIYVTHdQIEALTLADRIAVMKGG-VVQQ 215
Cdd:cd03252 174 E-HAIMRNMHDICaGRTVIIIAH-RLSTVKNADRIIVMEKGrIVEQ 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-211 |
2.61e-22 |
|
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: 93.65 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDF-----GSV--NVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGR----NVT 69
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 70 WQEPKD------RGIGMVFQSYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQI-EPLLQRKPSALSGGQRQR 142
Cdd:COG4778 81 QASPREilalrrRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 143 VAIGRALVRDVDVFLFDEPLSNLDAKLRselRVEIKRLHQKL--GNTMIYVTHDQ--IEAltLADRIAVMKGG 211
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANR---AVVVELIEEAKarGTAIIGIFHDEevREA--VADRVVDVTPF 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-213 |
2.86e-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: 93.69 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGS---VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPK--DRGIG 79
Cdd:cd03248 12 VKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQSYALYPQmTVEKNLSFGLR-------VAGLPKAEIDKRIKRAAEILQIEplLQRKPSALSGGQRQRVAIGRALVRD 152
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYGLQscsfecvKEAAQKAHAHSFISELASGYDTE--VGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1693059733 153 VDVFLFDEPLSNLDAKlrSELRVEiKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:cd03248 169 PQVLILDEATSALDAE--SEQQVQ-QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-219 |
3.65e-22 |
|
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: 94.13 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRN------VTWQEPKDRGI 78
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelYQLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 79 -----GMVFQSYALYPQMTV-------EKNLSFGLRVAGLPKAEIDKRIKRaaeiLQIEP-LLQRKPSALSGGQRQRVAI 145
Cdd:TIGR02323 84 mrtewGFVHQNPRDGLRMRVsaganigERLMAIGARHYGNIRATAQDWLEE----VEIDPtRIDDLPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 146 GRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV-------QQLAD 218
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVvesgltdQVLDD 239
|
.
gi 1693059733 219 P 219
Cdd:TIGR02323 240 P 240
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-235 |
4.06e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.96 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQepKD---------- 75
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFG--KDifqidaiklr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 RGIGMVFQSYALYPQMTVEKNLSFGLRVAGLP-KAEIDKRIKRAAEIL----QIEPLLQRKPSALSGGQRQRVAIGRALV 150
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 151 RDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLgnTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRF 230
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
....*
gi 1693059733 231 VAGFL 235
Cdd:PRK14246 248 TEKYV 252
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-238 |
5.38e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 93.70 E-value: 5.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 17 VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRG--IGMVFQ--SYALYPQMT 92
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrIRMIFQdpSTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 93 VEKNLSFGLRV-AGLPKAEIDKRIKRAAEILQIEP-LLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLR 170
Cdd:PRK15112 106 ISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 171 SELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGG-VVQQ------LADPLTIYNRprnRFVAGFLGSP 238
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGeVVERgstadvLASPLHELTK---RLIAGHFGEA 257
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
19-213 |
6.03e-22 |
|
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: 97.12 E-value: 6.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPK--DRGIGMVFQSYALYPQmTVEKN 96
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIRDN 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 97 LSFGlrVAGLPKAEIDKRIKRAAEILQIEPLLQ-------RKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK- 168
Cdd:TIGR01846 551 IALC--NPGAPFEHVIHAAKLAGAHDFISELPQgyntevgEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYEs 628
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1693059733 169 ---LRSELRvEIKRlhqklGNTMIYVTHdQIEALTLADRIAVMKGGVV 213
Cdd:TIGR01846 629 ealIMRNMR-EICR-----GRTVIIIAH-RLSTVRACDRIIVLEKGQI 669
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-213 |
1.02e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.60 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDiSEGSIFIKGRNVTWQEPKD--RGIGMVFQSYALYPQMTVEKNL 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 98 SFGLRvAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRdVD--------VFLFDEPLSNLDAKL 169
Cdd:COG4138 91 ALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQ-VWptinpegqLLLLDEPMNSLDVAQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1693059733 170 RSELRVEIKRLHQkLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:COG4138 169 QAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-194 |
1.06e-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: 95.89 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDF-GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVT--WQEPKDRGIGMVFQ 83
Cdd:TIGR02868 337 LRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSslDQDEVRRRVSVCAQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 SYALYpQMTVEKNLSFGLrvaglPKAEiDKRIKRAAEILQIEPLLQRKP-----------SALSGGQRQRVAIGRALVRD 152
Cdd:TIGR02868 417 DAHLF-DTTVRENLRLAR-----PDAT-DEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1693059733 153 VDVFLFDEPLSNLDAKLRSELrveIKRLHQKL-GNTMIYVTHD 194
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADEL---LEDLLAALsGRTVVLITHH 529
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-225 |
1.07e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.89 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEP---KDRGIGMV 81
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 FQSYALYPQMTVEKNLSFglrvaGLPKAEID-KRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDE 160
Cdd:PRK15439 92 PQEPLLFPNLSVKENILF-----GLPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 161 PLSNLDAKLRSELRVEIKRLhQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVqQLADPLTIYNR 225
Cdd:PRK15439 167 PTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTI-ALSGKTADLST 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-228 |
1.09e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.08 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 17 VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNV-----TWQEPKDRGIGMVFQS-YA-LYP 89
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspGKLQALRRDIQFIFQDpYAsLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 90 QMTVEKNLSFGLRVAGLPKAEIDKriKRAAEILQIEPLLQ----RKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNL 165
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLLPGKAAA--ARVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 166 DAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRN 228
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQH 557
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-219 |
1.23e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 92.68 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQ------EPKDRGI- 78
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRdlyalsEAERRRLl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 79 ----GMVFQSYALYPQMTV-------EKNLSFGLRVAG---------LPKAEID-KRIKRAaeilqiepllqrkPSALSG 137
Cdd:PRK11701 88 rtewGFVHQHPRDGLRMQVsaggnigERLMAVGARHYGdiratagdwLERVEIDaARIDDL-------------PTTFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 138 GQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV---- 213
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVvesg 234
|
....*....
gi 1693059733 214 ---QQLADP 219
Cdd:PRK11701 235 ltdQVLDDP 243
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-211 |
1.25e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.05 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSldFG----SVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVT-WQEPKDR-G 77
Cdd:PRK11160 338 SLTLNNVS--FTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdYSEAALRqA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 IGMVFQSYALYPQmTVEKNLSFglrvaGLPKAeIDKRIkraAEILQ---IEPLLQRKPS----------ALSGGQRQRVA 144
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNLLL-----AAPNA-SDEAL---IEVLQqvgLEKLLEDDKGlnawlgeggrQLSGGEQRRLG 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 145 IGRALVRDVDVFLFDEPLSNLDAKLRSelrvEIKRLHQKL--GNTMIYVTHdQIEALTLADRIAVMKGG 211
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETER----QILELLAEHaqNKTVLMITH-RLTGLEQFDRICVMDNG 549
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-213 |
2.22e-21 |
|
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: 90.28 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLD--ISEGSIFIKGRNVTWQEPKDR---GIGM 80
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYPQMtveKNLSFgLRvaglpkaEIDKrikraaeilqiepllqrkpsALSGGQRQRVAIGRALVRDVDVFLFDE 160
Cdd:cd03217 82 AFQYPPEIPGV---KNADF-LR-------YVNE--------------------GFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1693059733 161 PLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTH-DQIEALTLADRIAVMKGGVV 213
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREE-GKSVLIITHyQRLLDYIKPDRVHVLYDGRI 183
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-225 |
6.93e-21 |
|
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: 93.71 E-value: 6.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDI--SEGSIFIK----------------GR 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHvalcekcgyverpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 67 N------------VTWQEPKD-------RGIGMVFQ-SYALYPQMTVEKNLSFGLRVAGLPKaeiDKRIKRAAEILQIEP 126
Cdd:TIGR03269 81 PcpvcggtlepeeVDFWNLSDklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEG---KEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 127 LLQRK---PSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTH--DQIEalTL 201
Cdd:TIGR03269 158 LSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpEVIE--DL 235
|
250 260
....*....|....*....|....
gi 1693059733 202 ADRIAVMKGGVVQQLADPLTIYNR 225
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-213 |
6.97e-21 |
|
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: 93.63 E-value: 6.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 16 SVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKG---RNVTWQEPKdRGIGMVFQSYALYPQmT 92
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdlADYTLASLR-RQVALVSQDVVLFND-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 93 VEKNLSFGlRVAGLPKAeidkRIKRAAEILQIEPLLQRKP-----------SALSGGQRQRVAIGRALVRDVDVFLFDEP 161
Cdd:TIGR02203 422 IANNIAYG-RTEQADRA----EIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 162 LSNLDAKLRSELRVEIKRLHQklGNTMIYVTHdQIEALTLADRIAVMKGGVV 213
Cdd:TIGR02203 497 TSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRI 545
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-213 |
7.10e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 93.73 E-value: 7.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKG---RNVTwQEPKDRGIGMVfqsyalyPQMTVEK 95
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVT-QASLRAAIGIV-------PQDTVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 96 NLSFGLRVA-GLPKAEiDKRIKRAAEILQIEPLLQRKPSA-----------LSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:COG5265 445 NDTIAYNIAyGRPDAS-EEEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 164 NLDAKLRSELRVEIKRLHQklGNTMIYVTH------DqiealtlADRIAVMKGGVV 213
Cdd:COG5265 524 ALDSRTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRI 570
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-194 |
8.87e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 90.17 E-value: 8.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFikgrnvtwQEPKDRgIGM 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLR-IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYPQM--TVEKnlsFGLRVAGLPKAEIDKRIKRaaeiLQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLF 158
Cdd:PRK09544 72 VPQKLYLDTTLplTVNR---FLRLRPGTKKEDILPALKR----VQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 1693059733 159 DEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHD 194
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-226 |
1.10e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 93.25 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDFGS---VNVLQNLNLEIGEGEFLVLLGPSGCGKSTllnCVAGLLDI---SEGSIFIKGRNVTWQEPK 74
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNLyqpTGGQVLLDGVPLVQYDHH 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 75 --DRGIGMVFQSYALYPQmTVEKNLSFGLRVAglPKAEIDKRIKRAAEILQIEPLLQ-------RKPSALSGGQRQRVAI 145
Cdd:TIGR00958 552 ylHRQVALVGQEPVLFSG-SVRENIAYGLTDT--PDEEIMAAAKAANAHDFIMEFPNgydtevgEKGSQLSGGQKQRIAI 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 146 GRALVRDVDVFLFDEPLSNLDAklrselrvEIKRLHQKL----GNTMIYVTHdQIEALTLADRIAVMKGGVVQQLADPLT 221
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDA--------ECEQLLQESrsraSRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQ 699
|
....*
gi 1693059733 222 IYNRP 226
Cdd:TIGR00958 700 LMEDQ 704
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-237 |
1.42e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDF---GSVN-VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIS-----EGSIFIKGRNVTW-QEPKD 75
Cdd:PRK15134 7 AIENLSVAFrqqQTVRtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHaSEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 RG-----IGMVFQS--YALYPQMTVEKNLS------FGLRVAGlPKAEIDKRIKRAAeILQIEPLLQRKPSALSGGQRQR 142
Cdd:PRK15134 87 RGvrgnkIAMIFQEpmVSLNPLHTLEKQLYevlslhRGMRREA-ARGEILNCLDRVG-IRQAAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 143 VAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGG--VVQQLADPL 220
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGrcVEQNRAATL 244
|
250
....*....|....*..
gi 1693059733 221 tiYNRPRNRFVAGFLGS 237
Cdd:PRK15134 245 --FSAPTHPYTQKLLNS 259
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-216 |
1.53e-20 |
|
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: 93.47 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGrnvtwqepkdrgigmvfqSYALYPQM------TV 93
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------------SVAYVPQQawiqndSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 94 EKNLSFGlrvaglpKAEIDKRIKRAAEILQIEPLLQRKPSA-----------LSGGQRQRVAIGRALVRDVDVFLFDEPL 162
Cdd:TIGR00957 716 RENILFG-------KALNEKYYQQVLEACALLPDLEILPSGdrteigekgvnLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 163 SNLDAKLRSELRVEIKRLHQKLGN-TMIYVTHDqIEALTLADRIAVMKGGVVQQL 216
Cdd:TIGR00957 789 SAVDAHVGKHIFEHVIGPEGVLKNkTRILVTHG-ISYLPQVDVIIVMSGGKISEM 842
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-227 |
1.57e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 89.37 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDFGSVNVlQNLNLEIGEGEFLVLLGPSGCGKStlLNCvAGLLDI-------SEGSIFIKGRNVTWQEP 73
Cdd:PRK10418 1 MPQQIELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKS--LTC-AAALGIlpagvrqTAGRVLLDGKPVAPCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 74 KDRGIGMVFQS--YALYPQMTVEKNLSFGLRVAGLPKAeiDKRIKRAAEILQIEP---LLQRKPSALSGGQRQRVAIGRA 148
Cdd:PRK10418 77 RGRKIATIMQNprSAFNPLHTMHTHARETCLALGKPAD--DATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 149 LVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPR 227
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-210 |
1.89e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 92.56 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 26 EIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKgrnvtwqepkdrgigmVFQSYAlyPQ-------MTVEKNLS 98
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----------------LKISYK--PQyikpdydGTVEDLLR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 99 FGLRVAGLP--KAEIDKRikraaeiLQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVE 176
Cdd:PRK13409 423 SITDDLGSSyyKSEIIKP-------LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 495
|
170 180 190
....*....|....*....|....*....|....
gi 1693059733 177 IKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKG 210
Cdd:PRK13409 496 IRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-210 |
3.58e-20 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 91.77 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 26 EIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRnvtwqepkdrgIgmvfqSYAlyPQ-------MTVEKNLS 98
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-----------I-----SYK--PQyispdydGTVEEFLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 99 fGLRVAGLP----KAEIDKRikraaeiLQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELR 174
Cdd:COG1245 424 -SANTDDFGssyyKTEIIKP-------LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 1693059733 175 VEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKG 210
Cdd:COG1245 496 KAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-211 |
6.59e-20 |
|
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: 87.00 E-value: 6.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGMVFQ-SYALYP----QMTVE 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSvAYAAQKpwllNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 95 KNLSFGlrvaglpkAEIDK-RIKRAAEILQIEPLLQRKPSA-----------LSGGQRQRVAIGRALVRDVDVFLFDEPL 162
Cdd:cd03290 97 ENITFG--------SPFNKqRYKAVTDACSLQPDIDLLPFGdqteigerginLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1693059733 163 SNLDAKLRSELRVE-IKRLHQKLGNTMIYVTHdQIEALTLADRIAVMKGG 211
Cdd:cd03290 169 SALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-211 |
7.26e-20 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 90.56 E-value: 7.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 9 DLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPK---DRGIGMVFQSY 85
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 86 ALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEI---LQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPL 162
Cdd:PRK10982 83 NLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIfdeLDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1693059733 163 SNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-211 |
7.71e-20 |
|
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: 84.42 E-value: 7.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIfIKGRNVTwqepkdrgigmvfqs 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-TWGSTVK--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 YALYPQmtveknlsfglrvaglpkaeidkrikraaeilqiepllqrkpsaLSGGQRQRVAIGRALVRDVDVFLFDEPLSN 164
Cdd:cd03221 65 IGYFEQ--------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1693059733 165 LDAKLRSELRVEIKRLHQklgnTMIYVTHDQ--IEAltLADRIAVMKGG 211
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDRyfLDQ--VATKIIELEDG 143
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-213 |
1.45e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 90.18 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 8 QDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVtwqEPKD----RGIGMVFQ 83
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDiatrRRVGYMSQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 SYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:NF033858 347 AFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1693059733 164 NLDAKLRS---ELRVEIKRlhqKLGNTmIYV-THDQIEALtLADRIAVMKGGVV 213
Cdd:NF033858 427 GVDPVARDmfwRLLIELSR---EDGVT-IFIsTHFMNEAE-RCDRISLMHAGRV 475
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-214 |
2.77e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 89.45 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIfikgrnvtWQEpkdRGIGMVFQSyALYPQMTVEKNLS 98
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------WAE---RSIAYVPQQ-AWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 99 FGlrvaglpKAEIDKRIKRAAEILQIEPLLQRKPSA-----------LSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDA 167
Cdd:PTZ00243 743 FF-------DEEDAARLADAVRVSQLEADLAQLGGGleteigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1693059733 168 KLrSELRVEIKRLHQKLGNTMIYVTHdQIEALTLADRIAVMKGGVVQ 214
Cdd:PTZ00243 816 HV-GERVVEECFLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVE 860
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-242 |
4.16e-19 |
|
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: 85.50 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 29 EGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIfikGRNVTWQEPKDRGIGMVFQSYalypqmtVEKNLSFGLRVAG--- 105
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF---DDPPDWDEILDEFRGSELQNY-------FTKLLEGDVKVIVkpq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 106 ----LPKAE-------IDKRIKRAA-----EILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKL 169
Cdd:cd03236 95 yvdlIPKAVkgkvgelLKKKDERGKldelvDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1693059733 170 RSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKG-----GVVQQladPLTIYNRPrNRFVAGFLGSPSMNF 242
Cdd:cd03236 175 RLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLYGepgayGVVTL---PKSVREGI-NEFLDGYLPTENMRF 247
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-236 |
6.79e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.53 E-value: 6.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 9 DLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLD-IS----EGSIFIKGRNV-TWQEPKD--RGIGM 80
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkVSgyrySGDVLLGGRSIfNYRDVLEfrRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYPqMTVEKNLSFGLRVAGL-PKAEI----DKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDV 155
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAHKLvPRKEFrgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 156 FLFDEPLSNLDAKLRSELRVEIKRLHQKLgnTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRN----RFV 231
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHaetaRYV 262
|
....*
gi 1693059733 232 AGFLG 236
Cdd:PRK14271 263 AGLSG 267
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
19-215 |
1.08e-18 |
|
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: 87.31 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwQEPKDR---GIGMVFQSYALYpQMTVEK 95
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPRE-EIPREVlanSVAMVDQDIFLF-EGTVRD 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 96 NLSfgLRVAGLPkaeiDKRIKRAAEILQIEPLLQRKP-----------SALSGGQRQRVAIGRALVRDVDVFLFDEPLSN 164
Cdd:TIGR03796 572 NLT--LWDPTIP----DADLVRACKDAAIHDVITSRPggydaelaeggANLSGGQRQRLEIARALVRNPSILILDEATSA 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 165 LDAKlrSELRVeIKRLHQKlGNTMIYVTHdQIEALTLADRIAVM-KGGVVQQ 215
Cdd:TIGR03796 646 LDPE--TEKII-DDNLRRR-GCTCIIVAH-RLSTIRDCDEIIVLeRGKVVQR 692
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-213 |
1.11e-18 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 87.15 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 29 EGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIfikGRNVTWQEPKDRGIGMVFQSY-----------ALYPQMtVEKnl 97
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSWDEVLKRFRGTELQDYfkklangeikvAHKPQY-VDL-- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 98 sfglrvagLPKA----------EIDKR--IKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNL 165
Cdd:COG1245 172 --------IPKVfkgtvrelleKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 166 DAKLRseLRVE--IKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKG-----GVV 213
Cdd:COG1245 244 DIYQR--LNVArlIRELAEE-GKYVLVVEHDLAILDYLADYVHILYGepgvyGVV 295
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-215 |
1.17e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.94 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF-GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKG---RNVTWQEPKdRGIGM 80
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASLR-RNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQSYALYPQmTVEKNLsfglRVaGLPKAEiDKRIKRAAEILQIEPLLQRKP-----------SALSGGQRQRVAIGRAL 149
Cdd:PRK13657 414 VFQDAGLFNR-SIEDNI----RV-GRPDAT-DEEMRAAAERAQAHDFIERKPdgydtvvgergRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693059733 150 VRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQklGNTMIYVTHdQIEALTLADRIAVM-KGGVVQQ 215
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFdNGRVVES 550
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-211 |
1.70e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.52 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 13 DFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIS--EGSIFIKGRNVTWQEPKD---RGIGMVFQSYAL 87
Cdd:PRK13549 14 TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDterAGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 88 YPQMTVEKNLSFGlrvaglpkAEI--------DKRIKRAAEILQ-----IEPLLqrKPSALSGGQRQRVAIGRALVRDVD 154
Cdd:PRK13549 94 VKELSVLENIFLG--------NEItpggimdyDAMYLRAQKLLAqlkldINPAT--PVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 155 VFLFDEPLSNLDAklrSELRV--EIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:PRK13549 164 LLILDEPTASLTE---SETAVllDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-219 |
1.74e-18 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 82.93 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDF--GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIG 79
Cdd:cd03244 2 DIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQSYALYpQMTVEKNLSfglrvaglPKAEI-DKRIKRAAEILQIEPLLQRKPSAL-----------SGGQRQRVAIGR 147
Cdd:cd03244 82 IIPQDPVLF-SGTIRSNLD--------PFGEYsDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 148 ALVRDVDVFLFDEPLSNLD----AKLRSELRVEIKrlhqklGNTMIYVTHdQIEALTLADRIAVMKGGVVQQLADP 219
Cdd:cd03244 153 ALLRKSKILVLDEATASVDpetdALIQKTIREAFK------DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-237 |
2.02e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.45 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF----GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLD-----ISEGSIFIKGRN---VTWQE 72
Cdd:PRK10261 13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEqagglVQCDKMLLRRRSrqvIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 73 PKD------RG--IGMVFQS--YALYPQMTVEKNLSFGLRV-AGLPKAEIDKRIKRAAEILQI---EPLLQRKPSALSGG 138
Cdd:PRK10261 93 QSAaqmrhvRGadMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 139 QRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLAD 218
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
250
....*....|....*....
gi 1693059733 219 PLTIYNRPRNRFVAGFLGS 237
Cdd:PRK10261 253 VEQIFHAPQHPYTRALLAA 271
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-216 |
3.49e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.61 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 11 SLDFGSVnvlQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD---RGIGMVFQSY-- 85
Cdd:PRK09700 273 SRDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrd 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 86 -ALYPQMTVEKNLSF-------GLRVA-GLPKAEIDKRIKRAA-EILQIE-PLLQRKPSALSGGQRQRVAIGRALVRDVD 154
Cdd:PRK09700 350 nGFFPNFSIAQNMAIsrslkdgGYKGAmGLFHEVDEQRTAENQrELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 155 VFLFDEPLSNLDAKLRSelrvEIKRLHQKL---GNTMIYVTHDQIEALTLADRIAVMKGGVVQQL 216
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKA----EIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-211 |
4.41e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 85.26 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 13 DFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIS--EGSIFIKGRNVTWQEPKD---RGIGMVFQSYAL 87
Cdd:TIGR02633 10 TFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDterAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 88 YPQMTVEKNLSFGLRVAgLPKAeidkRIKRAAEILQIEPLLQ----------RKPSALSGGQRQRVAIGRALVRDVDVFL 157
Cdd:TIGR02633 90 VPELSVAENIFLGNEIT-LPGG----RMAYNAMYLRAKNLLRelqldadnvtRPVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1693059733 158 FDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-193 |
5.60e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 85.32 E-value: 5.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIS--EGSIFIKGRNVTwqEPKDRGIGMVFQ 83
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT--KQILKRTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 SYALYPQMTVEKNLSFgLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPS---------ALSGGQRQRVAIGRALVRDVD 154
Cdd:PLN03211 148 DDILYPHLTVRETLVF-CSLLRLPKSLTKQEKILVAESVISELGLTKCENtiignsfirGISGGERKRVSIAHEMLINPS 226
|
170 180 190
....*....|....*....|....*....|....*....
gi 1693059733 155 VFLFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTH 193
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMH 264
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
4-215 |
7.33e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 84.76 E-value: 7.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVT------WqepkdRG 77
Cdd:PRK10789 315 DVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklqldsW-----RS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 -IGMVFQSYALYPQmTVEKNLSFglrvaGLPKAEiDKRIKRAAEILQIEPLLQRKPSA-----------LSGGQRQRVAI 145
Cdd:PRK10789 390 rLAVVSQTPFLFSD-TVANNIAL-----GRPDAT-QQEIEHVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISI 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1693059733 146 GRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQklGNTMIYVTHdQIEALTLADRIAVMK-GGVVQQ 215
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAH-RLSALTEASEILVMQhGHIAQR 530
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
7-213 |
9.28e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.52 E-value: 9.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDfgsvNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDiSEGSIFIKGRNV-TWQEPK---DRG----- 77
Cdd:PRK03695 3 LNDVAVS----TRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLeAWSAAElarHRAylsqq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 ----IGM-VFQSYALYpqmtveknlsfglRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRV-------AI 145
Cdd:PRK03695 78 qtppFAMpVFQYLTLH-------------QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1693059733 146 GRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQkLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:PRK03695 145 WPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-247 |
1.07e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.09 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 29 EGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIfikGRNVTWQEPKDRGIGMVFQSY-----------ALYPQMtVEKnl 97
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDY---EEEPSWDEVLKRFRGTELQNYfkklyngeikvVHKPQY-VDL-- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 98 sfglrvagLPKA----------EIDKR--IKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNL 165
Cdd:PRK13409 172 --------IPKVfkgkvrellkKVDERgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 166 DAKLRseLRVE--IKRLHQklGNTMIYVTHDQIEALTLADRIAVMKG-----GVVQQladpltiynrPR------NRFVA 232
Cdd:PRK13409 244 DIRQR--LNVArlIRELAE--GKYVLVVEHDLAVLDYLADNVHIAYGepgayGVVSK----------PKgvrvgiNEYLK 309
|
250
....*....|....*
gi 1693059733 233 GFLGSPSMNFFSGEI 247
Cdd:PRK13409 310 GYLPEENMRIRPEPI 324
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-214 |
1.25e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIkGRNVTwqepkdrgIGMVFQS 84
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--------IGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 YA-LYPQMTVEKNLSfglrvaglpkaeidkRIKRAAEILQIEPLL---------QRKP-SALSGGQRQRVAIGRALVRDV 153
Cdd:COG0488 387 QEeLDPDKTVLDELR---------------DGAPGGTEQEVRGYLgrflfsgddAFKPvGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 154 DVFLFDEPLSNLDAKLRSELrvEikrlhQKLGN---TMIYVTHDQiEAL-TLADRIAVMKGGVVQ 214
Cdd:COG0488 452 NVLLLDEPTNHLDIETLEAL--E-----EALDDfpgTVLLVSHDR-YFLdRVATRILEFEDGGVR 508
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-193 |
1.54e-17 |
|
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: 79.71 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPK-DRGIGMVFQS 84
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 YALYPQMTVEKNLSFGLRVAGlpkaEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSN 164
Cdd:TIGR01189 82 PGLKPELSALENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*....
gi 1693059733 165 LDAKlRSELRVEIKRLHQKLGNTMIYVTH 193
Cdd:TIGR01189 158 LDKA-GVALLAGLLRAHLARGGIVLLTTH 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-234 |
1.71e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 84.29 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 23 LNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNV-TWQEPKDRGIGMVFQSYALYPQMTVEKNLSFGL 101
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 102 RVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIkrLH 181
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LK 1106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 182 QKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIynrpRNRFVAGF 234
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-246 |
2.38e-17 |
|
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: 83.81 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGR-----NVTWQEPKdrgigmvfqsyalypqmTV 93
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRisfspQTSWIMPG-----------------TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 94 EKNLSFGL-----RVAGLPKA-EIDKRIKRAAEILQIepLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDA 167
Cdd:TIGR01271 504 KDNIIFGLsydeyRYTSVIKAcQLEEDIALFPEKDKT--VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 168 KLRSEL--RVEIKRLHQKlgnTMIYVThDQIEALTLADRIAVMKGGVVQQLADPLTIYNRpRNRFVAGFLGSPSMNFFSG 245
Cdd:TIGR01271 582 VTEKEIfeSCLCKLMSNK---TRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSELQAK-RPDFSSLLLGLEAFDNFSA 656
|
.
gi 1693059733 246 E 246
Cdd:TIGR01271 657 E 657
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-211 |
2.61e-17 |
|
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: 81.06 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGR-----NVTWQEPKdrgigmvfqsyalypqmTV 93
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRisfssQFSWIMPG-----------------TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 94 EKNLSFGL-----RVAGLPKA-EIDKRIKRAAEilQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDa 167
Cdd:cd03291 115 KENIIFGVsydeyRYKSVVKAcQLEEDITKFPE--KDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD- 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1693059733 168 kLRSELRVEIKRLHQKLGN-TMIYVThDQIEALTLADRIAVMKGG 211
Cdd:cd03291 192 -VFTEKEIFESCVCKLMANkTRILVT-SKMEHLKKADKILILHEG 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-211 |
3.96e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 6 SIQDLSL-DFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDR---GIGMV 81
Cdd:COG3845 259 EVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 ---FQSYALYPQMTVEKNLSFG------LRVAGLpkaeID-KRIKRAAEILqIE------PLLQRKPSALSGGQRQRVAI 145
Cdd:COG3845 339 pedRLGRGLVPDMSVAENLILGryrrppFSRGGF----LDrKAIRAFAEEL-IEefdvrtPGPDTPARSLSGGNQQKVIL 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 146 GRALVRDVDVFLFDEPLSNLDAKlrselrvEIKRLHQKL------GNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVG-------AIEFIHQRLlelrdaGAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
19-215 |
4.56e-17 |
|
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: 82.31 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTW--QEPKDRGIGMVFQSYALYP------- 89
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGldVQAVRRQLGVVLQNGRLMSgsifeni 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 90 ----QMTVEKNLSfGLRVAGLpkaeiDKRIKRAAeiLQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNL 165
Cdd:TIGR03797 548 aggaPLTLDEAWE-AARMAGL-----AEDIRAMP--MGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSAL 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1693059733 166 DAKLRSELRVEIKRlhqkLGNTMIYVTHdQIEALTLADRIAVMKGG-VVQQ 215
Cdd:TIGR03797 620 DNRTQAIVSESLER----LKVTRIVIAH-RLSTIRNADRIYVLDAGrVVQQ 665
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-211 |
5.31e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.17 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 8 QDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVT---WQEPKDRGIGMVFQS 84
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllpLHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 YALYPQMTVEKNLSFGLRVAGLPKAEidKRIKRAAEILQ---IEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEP 161
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRDDLSAE--QREDRANELMEefhIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 162 LSNLDAKlrseLRVEIKRLHQKL---GNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:PRK10895 165 FAGVDPI----SVIDIKRIIEHLrdsGLGVLITDHNVRETLAVCERAYIVSQG 213
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-166 |
5.51e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.99 E-value: 5.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVtwQEPK----DRGIGMVFQSYALYPQmTVEK 95
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--RDYTlaslRNQVALVSQNVHLFND-TIAN 435
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1693059733 96 NLSFGlRVAGLPKAEIDKRIKRAAEILQIEPLLQ-------RKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLD 166
Cdd:PRK11176 436 NIAYA-RTEQYSREQIEEAARMAYAMDFINKMDNgldtvigENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-244 |
7.69e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.63 E-value: 7.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGL----LDISeGSIFIKGRNVTWQEPKDRGiGMVFQSYALYPQMTVEK 95
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRspkgVKGS-GSVLLNGMPIDAKEMRAIS-AYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 96 NLSFGLRV---AGLPKaeiDKRIKRAAEILQIEPLLQ---------RKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:TIGR00955 119 HLMFQAHLrmpRRVTK---KEKRERVDEVLQALGLRKcantrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 164 NLDAKLRSELRVEIKRLHQKlGNTMIYVTHD-QIEALTLADRIAVMKGGVVqqladpltiynrprnrfvaGFLGSP--SM 240
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRV-------------------AYLGSPdqAV 255
|
....
gi 1693059733 241 NFFS 244
Cdd:TIGR00955 256 PFFS 259
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-193 |
1.02e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.01 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 2 NSSVSIQDLSLDFGSVNVL-QNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIkgrnvtwqePkdRGIGM 80
Cdd:COG4178 360 DGALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------P--AGARV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VF---QSY--------AL-YPQmtveknlsfglrvagLPKAEIDKRIKRAAEILQIEPLLQR------KPSALSGGQRQR 142
Cdd:COG4178 429 LFlpqRPYlplgtlreALlYPA---------------TAEAFSDAELREALEAVGLGHLAERldeeadWDQVLSLGEQQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 143 VAIGRALVRDVDVFLFDEPLSNLDAKLRSELrveIKRLHQKLGN-TMIYVTH 193
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAAL---YQLLREELPGtTVISVGH 542
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
7-195 |
3.43e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 77.37 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAG--LLDISEGSIFIKGRNVTWQEPKDR---GIGMV 81
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERahlGIFLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 FQsyalYPqmtVE----KNLSFgLRVA--------GLPkaEID-----KRIKRAAEILQIEP-LLQRKPS-ALSGGQRQR 142
Cdd:CHL00131 90 FQ----YP---IEipgvSNADF-LRLAynskrkfqGLP--ELDpleflEIINEKLKLVGMDPsFLSRNVNeGFSGGEKKR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 143 VAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQ 195
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQ 211
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
9-196 |
4.51e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.76 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 9 DLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwqepKDRG-----IGMVFQ 83
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCtyqkqLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 SYALYPQMTVEKNLSFGLRVAGlPKAEIDKRIKraaeILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHFSP-GAVGITELCR----LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|...
gi 1693059733 164 NLDAKLRSELRVEIKRlHQKLGNTMIYVTHDQI 196
Cdd:PRK13540 157 ALDELSLLTIITKIQE-HRAKGGAVLLTSHQDL 188
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-215 |
5.38e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 79.40 E-value: 5.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDFGSVN---VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAG-LLDISEGSIFIKGR-----NVTWqepk 74
Cdd:PLN03130 614 AISIKNGYFSWDSKAerpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTvayvpQVSW---- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 75 drgigmVFQSyalypqmTVEKNLSFGlrvaglpkAEIDK-RIKRAAEILQIEPLLQRKPSA-----------LSGGQRQR 142
Cdd:PLN03130 690 ------IFNA-------TVRDNILFG--------SPFDPeRYERAIDVTALQHDLDLLPGGdlteigergvnISGGQKQR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 143 VAIGRALVRDVDVFLFDEPLSNLDAK---------LRSELRveikrlhqklGNTMIYVThDQIEALTLADRIAVMKGGVV 213
Cdd:PLN03130 749 VSMARAVYSNSDVYIFDDPLSALDAHvgrqvfdkcIKDELR----------GKTRVLVT-NQLHFLSQVDRIILVHEGMI 817
|
..
gi 1693059733 214 QQ 215
Cdd:PLN03130 818 KE 819
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
9-235 |
6.74e-16 |
|
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: 74.53 E-value: 6.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 9 DLSLDFGSVNVLQNLNlEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGsifikgrNVTWQepkdrgigmvfqsyaly 88
Cdd:cd03222 5 DCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD-------NDEWD----------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 89 pqmtveknlsfGLRVAGLPKaEIDkrikraaeilqiepllqrkpsaLSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK 168
Cdd:cd03222 60 -----------GITPVYKPQ-YID----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 169 LRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKG--GVVQQLADPLTIYNrPRNRFVAGFL 235
Cdd:cd03222 106 QRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGepGVYGIASQPKGTRE-GINRFLRGYL 173
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-222 |
7.74e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.36 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 2 NSSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNV-TWQEPK-DRGIG 79
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeSWSSKAfARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQSYALYPQMTVEKNLSFGLR----VAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDV 155
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAIGRYpwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693059733 156 FLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTI 222
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-254 |
1.02e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.07 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDF----GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLL---DISEGSIFIKGRNV----T 69
Cdd:PRK09473 9 ADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLaanGRIGGSATFNGREIlnlpE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 70 WQEPKDRG--IGMVFQS--YALYPQMTVEKNLSFGLRV-AGLPKAEIDKRIKRAAEILQIEPLLQRK---PSALSGGQRQ 141
Cdd:PRK09473 89 KELNKLRAeqISMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 142 RVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLT 221
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
250 260 270
....*....|....*....|....*....|....
gi 1693059733 222 IYNRPRNRFVAGFLGS-PSMNFFSGEIASRSGKP 254
Cdd:PRK09473 249 VFYQPSHPYSIGLLNAvPRLDAEGESLLTIPGNP 282
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-213 |
6.12e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 6.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 24 NLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDrGI--GMVF-----QSYALYPQMTVEKN 96
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD-AIraGIMLcpedrKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 97 LSFGLRVAGLPKAEI--DKRIKRAAEiLQIEPLLQRKPSA------LSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK 168
Cdd:PRK11288 352 INISARRHHLRAGCLinNRWEAENAD-RFIRSLNIKTPSReqlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVG 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1693059733 169 LRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:PRK11288 431 AKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-211 |
8.12e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 1 MNSSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDR---G 77
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 IGMVFQSYALYPQMTVEKNL--------SFGLRVAGLPKAEIDKRIKRaaeiLQIEPLLQRKPSALSGGQRQRVAIGRAL 149
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIflgrefvnRFGRIDWKKMYAEADKLLAR----LNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 150 VRDVDVFLFDEPLSNL-DAKLRSELRVeIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTETESLFRV-IRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-211 |
1.14e-14 |
|
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: 71.91 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIS---EGSIFIKGrnVTWQEPKDRgigmvFQSYALY-------- 88
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG--IPYKEFAEK-----YPGEIIYvseedvhf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 89 PQMTVEKNLSFGLRVaglpkaeidkrikRAAEILqiepllqrkpSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK 168
Cdd:cd03233 96 PTLTVRETLDFALRC-------------KGNEFV----------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1693059733 169 LRSELRVEIKRLHQKLGNT-MIYVTHDQIEALTLADRIAVMKGG 211
Cdd:cd03233 153 TALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-168 |
1.23e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 21 QNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKdrgigmvFQSYALY--------PQMT 92
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 93 VEKNLSFGLRVAGLPKAEidkrikRAAEILQIEPLLQRK--P-SALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK 168
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDE------ALWEALAQVGLAGFEdvPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-161 |
2.49e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.39 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwqEPKDR-------- 76
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRravcpria 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 77 ----GIGMvfqsyALYPQMTVEKNLSFGLRVAGLPKAEIDKRIkraAEILQ---IEPLLQRKPSALSGGQRQRVAIGRAL 149
Cdd:NF033858 80 ympqGLGK-----NLYPTLSVFENLDFFGRLFGQDAAERRRRI---DELLRatgLAPFADRPAGKLSGGMKQKLGLCCAL 151
|
170
....*....|..
gi 1693059733 150 VRDVDVFLFDEP 161
Cdd:NF033858 152 IHDPDLLILDEP 163
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
7-235 |
3.89e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.47 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDFGSVNV----LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLD----ISEGSIFIKGRNVTWQEPKDR-- 76
Cdd:PRK11022 6 VDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 77 ----GIGMVFQS--YALYPQMTVEKNLSFGLRV-AGLPKAEidkRIKRAAEILQI------EPLLQRKPSALSGGQRQRV 143
Cdd:PRK11022 86 lvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKT---RRQRAIDLLNQvgipdpASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 144 AIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLADPLTIY 223
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250
....*....|..
gi 1693059733 224 NRPRNRFVAGFL 235
Cdd:PRK11022 243 RAPRHPYTQALL 254
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-210 |
4.52e-14 |
|
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: 69.10 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSL--DFGSVnVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIkgrnvtwqePKDRGIGMVF 82
Cdd:cd03223 1 IELENLSLatPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 83 Q-SYalYPQMTveknlsfgLRvaglpkaeidkrikraaEILqIEPLLQrkpsALSGGQRQRVAIGRALVRDVDVFLFDEP 161
Cdd:cd03223 71 QrPY--LPLGT--------LR-----------------EQL-IYPWDD----VLSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1693059733 162 LSNLDAKlrSELRveIKRLHQKLGNTMIYVTHdQIEALTLADRIAVMKG 210
Cdd:cd03223 119 TSALDEE--SEDR--LYQLLKELGITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-193 |
4.80e-14 |
|
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: 70.21 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPK-DRGIGMVFQSYALYPQMTVEKNL 97
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 98 SFGLRVAGlpkaeiDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDaKLRSELRVEI 177
Cdd:cd03231 95 RFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD-KAGVARFAEA 167
|
170
....*....|....*.
gi 1693059733 178 KRLHQKLGNTMIYVTH 193
Cdd:cd03231 168 MAGHCARGGMVVLTTH 183
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-215 |
5.73e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.47 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQD--LSLDFGSVN-VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISE-GSIFIKGrnvtwqepkdrgig 79
Cdd:PLN03232 614 AISIKNgyFSWDSKTSKpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRG-------------- 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 mvfqSYALYPQM------TVEKNLSFGLRVAglpkaeiDKRIKRAAEILQIEPLLQRKPSA-----------LSGGQRQR 142
Cdd:PLN03232 680 ----SVAYVPQVswifnaTVRENILFGSDFE-------SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQR 748
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 143 VAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRlHQKLGNTMIYVThDQIEALTLADRIAVMKGGVVQQ 215
Cdd:PLN03232 749 VSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKE 819
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
23-213 |
6.36e-14 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 72.68 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 23 LNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQSYALYP---QMTVEKNL 97
Cdd:TIGR01194 361 IDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDyrDLFSAIFADFHLFDdliGPDEGEHA 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 98 SFGLRVAGLPKAEIDKRIKraaeilqIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLR----SEL 173
Cdd:TIGR01194 441 SLDNAQQYLQRLEIADKVK-------IEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKrffyEEL 513
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1693059733 174 RVEIKRlhqkLGNTMIYVTHDQiEALTLADRIAVMKGGVV 213
Cdd:TIGR01194 514 LPDLKR----QGKTIIIISHDD-QYFELADQIIKLAAGCI 548
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-205 |
1.11e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.91 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 3 SSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAG--LLDisEGSIFIKGRNVT---WQEPKDRG 77
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevLLD--DGRIIYEQDLIVarlQQDPPRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 IGMVF---------QSYAL--YPQMTV-------EKNLSfglRVAGLPKA-------EIDKRIKRAAEILQIEPllQRKP 132
Cdd:PRK11147 80 EGTVYdfvaegieeQAEYLkrYHDISHlvetdpsEKNLN---ELAKLQEQldhhnlwQLENRINEVLAQLGLDP--DAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693059733 133 SALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDaklrselrVE-IKRLHQKLGN---TMIYVTHDQIEALTLADRI 205
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD--------IEtIEWLEGFLKTfqgSIIFISHDRSFIRNMATRI 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-213 |
1.96e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.53 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwQEPKDRGIGMVFQSYAL---YPQMtVEKN 96
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-QALQKNLVAYVPQSEEVdwsFPVL-VEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 97 LSFG-------LRVaglPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKL 169
Cdd:PRK15056 101 VMMGryghmgwLRR---AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1693059733 170 RSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:PRK15056 178 EARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-214 |
3.65e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.06 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 18 NVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWqepkdrgigmvfqsyalYPQMTVEKNL 97
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQF-----------------GREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 98 SfglrvaglpkaeIDKRIKRAAEILQI-----EPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSE 172
Cdd:COG2401 107 G------------RKGDFKDAVELLNAvglsdAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1693059733 173 LRVEIKRLHQKLGNTMIYVTH--DQIEALTLADRIAVMKGGVVQ 214
Cdd:COG2401 175 VARNLQKLARRAGITLVVATHhyDVIDDLQPDLLIFVGYGGVPE 218
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-211 |
4.93e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.52 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 30 GEFLVLLGPSGCGKSTLLNCVAGLLD---ISEGSIFIKGRNVtwQEPKDRGIGMVFQSYALYPQMTVEKNLSFGLRV--- 103
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPL--DSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLrqp 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 104 AGLPKAEIDKRIKRAAEILQIE----PLLQRKPSALSGGQRQRVAIGRALVRDVDVFLF-DEPLSNLDaklrSELRVEIK 178
Cdd:TIGR00956 867 KSVSKSEKMEYVEEVIKLLEMEsyadAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLD----SQTAWSIC 942
|
170 180 190
....*....|....*....|....*....|....*...
gi 1693059733 179 RLHQKLGNT--MIYVTHDQIEALTLA--DRIAVM-KGG 211
Cdd:TIGR00956 943 KLMRKLADHgqAILCTIHQPSAILFEefDRLLLLqKGG 980
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-216 |
5.85e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.62 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 23 LNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIGMVFQSYALYPQMtveknlsfg 100
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAVFTDFHLFDQL--------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 101 LRVAGLPKAeiDKRIKRAAEILQIEPLLQRKPS-----ALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRV 175
Cdd:PRK10522 413 LGPEGKPAN--PALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQ 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1693059733 176 EIKRLHQKLGNTMIYVTHDQiEALTLADRIAVMKGGVVQQL 216
Cdd:PRK10522 491 VLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLSEL 530
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-211 |
6.07e-13 |
|
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: 66.50 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 2 NSSVSIQDLSLDFGSVNV----LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIS--EGSIFIKGRnvtwqePKD 75
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGkrqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGR------PLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 ----RGIGMVFQSYALYPQMTVEKNLSFG--LRvaglpkaeidkrikraaeilqiepllqrkpsALSGGQRQRVAIGRAL 149
Cdd:cd03232 75 knfqRSTGYVEQQDVHSPNLTVREALRFSalLR-------------------------------GLSVEQRKRLTIGVEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 150 VRDVDVFLFDEPLSNLDaklrSELRVEIKRLHQKLGNT--MIYVTHDQIEALTLA--DRIAVMKGG 211
Cdd:cd03232 124 AAKPSILFLDEPTSGLD----SQAAYNIVRFLKKLADSgqAILCTIHQPSASIFEkfDRLLLLKRG 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-214 |
6.59e-13 |
|
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: 69.47 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 22 NLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIS-EGSIFIKGRNVTWQEPKD---RGIGMVFQS---YALYPQMTVE 94
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 95 KNLSfglrVAGLPKAEIDKRIKRAAEILQIEPLLQR------KP----SALSGGQRQRVAIGRALVRDVDVFLFDEPLSN 164
Cdd:TIGR02633 358 KNIT----LSVLKSFCFKMRIDAAAELQIIGSAIQRlkvktaSPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1693059733 165 LDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVVQ 214
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-215 |
6.99e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 69.75 E-value: 6.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDFGSVN-VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTW--QEPKDRGIGM 80
Cdd:PRK10790 340 RIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlsHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 81 VFQ-----SYALYPQMTVEKNLSfglrvaglpkaeiDKRIKRAAEILQIEPLLQRKP-----------SALSGGQRQRVA 144
Cdd:PRK10790 420 VQQdpvvlADTFLANVTLGRDIS-------------EEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693059733 145 IGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKlgNTMIYVTHdQIEALTLADRIAVM-KGGVVQQ 215
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH-RLSTIVEADTILVLhRGQAVEQ 555
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-208 |
8.27e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.67 E-value: 8.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 17 VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFI------KGRNVTWQEPKdrgIGMVFQ------- 83
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndshnlKDINLKWWRSK---IGVVSQdpllfsn 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 ------SYALYPQMTVE----------------KNLSFGLRVA---------------GLPKAEIDKRIKRAAEILQI-- 124
Cdd:PTZ00265 475 siknniKYSLYSLKDLEalsnyynedgndsqenKNKRNSCRAKcagdlndmsnttdsnELIEMRKNYQTIKDSEVVDVsk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 125 ---------------EPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMI 189
Cdd:PTZ00265 555 kvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
250
....*....|....*....
gi 1693059733 190 YVTHdQIEALTLADRIAVM 208
Cdd:PTZ00265 635 IIAH-RLSTIRYANTIFVL 652
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-219 |
8.73e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 66.67 E-value: 8.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDFGS--VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVtwqepKDRGIGMV 81
Cdd:cd03369 6 EIEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI-----STIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 82 FQSYALYPQ------MTVEKNLSfglrvaglPKAEI-DKRIKRAAEIlqiepllQRKPSALSGGQRQRVAIGRALVRDVD 154
Cdd:cd03369 81 RSSLTIIPQdptlfsGTIRSNLD--------PFDEYsDEEIYGALRV-------SEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 155 VFLFDEPLSNL----DAKLRSELRVEIKrlhqklGNTMIYVTHdQIEALTLADRIAVMKGGVVQQLADP 219
Cdd:cd03369 146 VLVLDEATASIdyatDALIQKTIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-211 |
1.77e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 22 NLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDrGI--GMVFQSY-----ALYPQMTVE 94
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD-GLanGIVYISEdrkrdGLVLGMSVK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 95 KNLSF-GLRVagLPKAEIdkRIKRAAEILQIEPLLQ----RKPSA------LSGGQRQRVAIGRALVRDVDVFLFDEPLS 163
Cdd:PRK10762 349 ENMSLtALRY--FSRAGG--SLKHADEQQAVSDFIRlfniKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1693059733 164 NLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
9-166 |
2.14e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 9 DLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEpKDRGIGMVFQSYALY 88
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLGHLPGLK 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1693059733 89 PQMTVEKNLSFglrVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLD 166
Cdd:PRK13543 95 ADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-211 |
3.97e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 22 NLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLD-ISEGSIFIKGRNVTWQEPKD---RGIGMVFQS---YALYPQMTVE 94
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 95 KNLSfglrVAGLPKAEIDKRIKRAAEILQIEPLLQR----KPSA------LSGGQRQRVAIGRALVRDVDVFLFDEPLSN 164
Cdd:PRK13549 360 KNIT----LAALDRFTGGSRIDDAAELKTILESIQRlkvkTASPelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1693059733 165 LDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:PRK13549 436 IDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-215 |
1.11e-11 |
|
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: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF--GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDiSEGSIFIKG---RNVTWQEPKdRGIG 79
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvswNSVTLQTWR-KAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQSYALYPQmTVEKNLSfglrvaglPKAEI-DKRIKRAAEILQIEPLLQRKPS-----------ALSGGQRQRVAIGR 147
Cdd:TIGR01271 1296 VIPQKVFIFSG-TFRKNLD--------PYEQWsDEEIWKVAEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLAR 1366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1693059733 148 ALVRDVDVFLFDEPLSNLDAKLRSELRveiKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQ 215
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIR---KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-207 |
1.32e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 57 SEGSIFIKGRNVTWQEPKD-RGIGMVFQSYALYPQMTVEKNLSFGLRVAGLpkaeidKRIKRAAEILQIEPLLQRKPS-- 133
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFGKEDATR------EDVKRACKFAAIDEFIESLPNky 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 134 ---------ALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDA---KLRSELRVEIKrlhQKLGNTMIYVTHdQIEALTL 201
Cdd:PTZ00265 1349 dtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIK---DKADKTIITIAH-RIASIKR 1424
|
....*.
gi 1693059733 202 ADRIAV 207
Cdd:PTZ00265 1425 SDKIVV 1430
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-211 |
1.76e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 22 NLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDR-GIGMVF-----QSYALYPQMTVEK 95
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 96 N--------LSFGLRvaglPKAE--IDKRIKRAAEILQIEPllQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNL 165
Cdd:PRK15439 361 NvcalthnrRGFWIK----PAREnaVLERYRRALNIKFNHA--EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1693059733 166 DAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-230 |
1.96e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.38 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 4 SVSIQDLSLDF--GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKD--RGIG 79
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQSYALYPQmTVEKNLSfglrvaglPKAE-IDKRIKRAAEILQIEPLLQRKPSAL-----------SGGQRQRVAIGR 147
Cdd:PLN03232 1314 IIPQSPVLFSG-TVRFNID--------PFSEhNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLAR 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 148 ALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLgnTMIYVTHdQIEALTLADRIAVMKGGVVQQLADPLTIYNRPR 227
Cdd:PLN03232 1385 ALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSC--TMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
...
gi 1693059733 228 NRF 230
Cdd:PLN03232 1462 SAF 1464
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-166 |
2.48e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.89 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLD--ISEGSIFIKGRNVTWQEPKDR---GIG 79
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQsyalYPQMTVEKNLSFGLRVA-----------GLPKAEIDKRIKRAAEILQIEP-LLQRKPS-ALSGGQRQRVAIG 146
Cdd:PRK09580 82 MAFQ----YPVEIPGVSNQFFLQTAlnavrsyrgqePLDRFDFQDLMEEKIALLKMPEdLLTRSVNvGFSGGEKKRNDIL 157
|
170 180
....*....|....*....|
gi 1693059733 147 RALVRDVDVFLFDEPLSNLD 166
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLD 177
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
280-348 |
2.96e-11 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 58.79 E-value: 2.96e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 280 LGVRPEHIRLDVA-DGFEATVDLDEPMGADSLVWLKL-NGHALSARVEAG--KRYRAGDKVRIGFKADALSLF 348
Cdd:pfam08402 1 LAIRPEKIRLAAAaNGLSGTVTDVEYLGDHTRYHVELaGGEELVVRVPNAhaRPPAPGDRVGLGWDPEDAHVL 73
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
5-173 |
3.30e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.81 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLqNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVT-WQEPKDRGIGmvfQ 83
Cdd:PRK13541 2 LSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINnIAKPYCTYIG---H 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 SYALYPQMTVEKNLSFGlrvaglpkAEI---DKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDE 160
Cdd:PRK13541 78 NLGLKLEMTVFENLKFW--------SEIynsAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
170
....*....|...
gi 1693059733 161 PLSNLDAKLRSEL 173
Cdd:PRK13541 150 VETNLSKENRDLL 162
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-211 |
3.70e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 14 FGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIS--EGSIFIKGRNVTWQEPKD---RGIGMVFQSYALY 88
Cdd:NF040905 11 FPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDseaLGIVIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 89 PQMTVEKNLSFGLRVA--GLpkaeID--KRIKRAAEILQiEPLLQRKPSALSG----GQRQRVAIGRALVRDVDVFLFDE 160
Cdd:NF040905 91 PYLSIAENIFLGNERAkrGV----IDwnETNRRARELLA-KVGLDESPDTLVTdigvGKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 161 PLSNLD----AKLRsELRVEIKrlhqKLGNTMIYVTHDQIEALTLADRIAVMKGG 211
Cdd:NF040905 166 PTAALNeedsAALL-DLLLELK----AQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-194 |
3.88e-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: 64.19 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSifikgrnvTWQEPkDRGIGMVFQSYALYPQMTVEKNLS 98
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------ARPQP-GIKVGYLPQEPQLDPTKTVRENVE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 99 FGLRVA--------------GLPKAEIDKRIKRAAEI-------------LQIE--------PLLQRKPSALSGGQRQRV 143
Cdd:TIGR03719 91 EGVAEIkdaldrfneisakyAEPDADFDKLAAEQAELqeiidaadawdldSQLEiamdalrcPPWDADVTKLSGGERRRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1693059733 144 AIGRALVRDVDVFLFDEPLSNLDAKLRSELRveiKRLHQKLGnTMIYVTHD 194
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDAESVAWLE---RHLQEYPG-TVVAVTHD 217
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
7-208 |
6.82e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 62.62 E-value: 6.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDF----GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLD----ISEGSIFIKGRNVTWQEPKDR-- 76
Cdd:COG4170 6 IRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 77 ----GIGMVFQ--SYALYPQMTVEKNLSFglrvaGLPKAEIDK--------RIKRAAEIL------QIEPLLQRKPSALS 136
Cdd:COG4170 86 iigrEIAMIFQepSSCLDPSAKIGDQLIE-----AIPSWTFKGkwwqrfkwRKKRAIELLhrvgikDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 137 GGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDqIEALT-LADRIAVM 208
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHD-LESISqWADTITVL 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-217 |
1.64e-10 |
|
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: 62.72 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 30 GEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwqepkdRGIGMVFQSYALYPQ-------MTVEKNLSFGLR 102
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL------TNISDVHQNMGYCPQfdaiddlLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 103 VAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQ 182
Cdd:TIGR01257 2039 LRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR 2118
|
170 180 190
....*....|....*....|....*....|....*
gi 1693059733 183 KlGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLA 217
Cdd:TIGR01257 2119 E-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLG 2152
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
236-287 |
2.68e-10 |
|
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK transport protein.
Pssm-ID: 465563 [Multi-domain] Cd Length: 53 Bit Score: 55.28 E-value: 2.68e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 236 GSPSMNFFSGEIasRSGKPVFHIGEAAVQLDGYDGALEQ---GRKVTLGVRPEHI 287
Cdd:pfam17912 1 GSPPMNFLPATV--VEDGLLVLGGGVTLPLPEGQVLALKlyvGKEVILGIRPEHI 53
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-215 |
3.80e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 59.87 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF--GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIsEGSIFIKGrnVTWQ----EPKDRGI 78
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDG--VSWNsvplQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 79 GMVFQSYALYPQmTVEKNLSfglrvaglPKAE-IDKRIKRAAEILQIEPLLQRKPS-----------ALSGGQRQRVAIG 146
Cdd:cd03289 80 GVIPQKVFIFSG-TFRKNLD--------PYGKwSDEEIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 147 RALVRDVDVFLFDEPLSNLDAKLRSELRveiKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQQ 215
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIR---KTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-213 |
5.78e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.46 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIS--------EGSIFIKGRNVTWQEPKdrgigMVFQSYALYPQ 90
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAP-----RLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 91 -------MTVEKNLSFG----LRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRAL---------V 150
Cdd:PRK13547 91 aaqpafaFSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 151 RDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-219 |
1.15e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.96 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 12 LDFgsvnVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwqepkDRGIGMVFQSYALYPQM 91
Cdd:TIGR00957 1298 LDL----VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA-----KIGLHDLRFKITIIPQD 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 92 TVEknLSFGLRVAGLPKAEI-DKRIKRAAEILQIEPLLQRKPSA-----------LSGGQRQRVAIGRALVRDVDVFLFD 159
Cdd:TIGR00957 1369 PVL--FSGSLRMNLDPFSQYsDEEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 160 EPLSNLDAKLRSELRVEIKRlhQKLGNTMIYVTHdQIEALTLADRIAVMKGGVVQQLADP 219
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRT--QFEDCTVLTIAH-RLNTIMDYTRVIVLDKGEVAEFGAP 1503
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-213 |
2.52e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSI------------------FIKGR 66
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyyaqdhaydFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 67 NVT-----WQEPKD-----RGI-G-MVFQSyalypqmtveknlsfglrvaglpkAEIDKRIKraaeilqiepllqrkpsA 134
Cdd:PRK15064 400 TLFdwmsqWRQEGDdeqavRGTlGrLLFSQ------------------------DDIKKSVK-----------------V 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 135 LSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKlrselrvEIKRLHQKLGN---TMIYVTHDQIEALTLADRIAVMK-G 210
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME-------SIESLNMALEKyegTLIFVSHDREFVSSLATRIIEITpD 511
|
...
gi 1693059733 211 GVV 213
Cdd:PRK15064 512 GVV 514
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-194 |
4.18e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNL------EIGegeflvLLGPSGCGKSTLLNCVAGLLDISEGSIFI-KGRNVTW--QEPKdrgigmvfqsyaLYP 89
Cdd:PRK11819 22 ILKDISLsffpgaKIG------VLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKVGYlpQEPQ------------LDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 90 QMTVEKNLSFGLR-----------VA---GLPKAEIDKRIKRAAEiLQ----------IEPLLQ------RKPSA----- 134
Cdd:PRK11819 84 EKTVRENVEEGVAevkaaldrfneIYaayAEPDADFDALAAEQGE-LQeiidaadawdLDSQLEiamdalRCPPWdakvt 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1693059733 135 -LSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKlrSELRVEiKRLHQKLGnTMIYVTHD 194
Cdd:PRK11819 163 kLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE--SVAWLE-QFLHDYPG-TVVAVTHD 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-213 |
5.50e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNV---TWQEPKDRGIGMVFQ---SYALYPQMTV 93
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnhNANEAINHGFALVTEerrSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 94 EKNL----------SFGLrvagLPKAEIDKRIKRAAEILQIE-PLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPL 162
Cdd:PRK10982 344 GFNSlisnirnyknKVGL----LDNSRMKSDTQWVIDSMRVKtPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1693059733 163 SNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-193 |
6.02e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGrnvtwqepkdrGIGMVFQSYALYPQMTVEKNLSF 99
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------SAALIAISSGLNGQLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 100 GLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKR 179
Cdd:PRK13545 109 KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNE 188
|
170
....*....|....
gi 1693059733 180 LHQKlGNTMIYVTH 193
Cdd:PRK13545 189 FKEQ-GKTIFFISH 201
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
16-205 |
1.13e-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: 53.87 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 16 SVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVaglLDISEGSIFIKGRnvtwQEPKDRGIGMVFQSYALypqmtVEK 95
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG---LYASGKARLISFL----PKFSRNKLIFIDQLQFL-----IDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 96 NLSFglrvagLPkaeidkrikraaeilqieplLQRKPSALSGGQRQRVAIGRALVRDVD--VFLFDEPLSNLDAKLRSEL 173
Cdd:cd03238 75 GLGY------LT--------------------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL 128
|
170 180 190
....*....|....*....|....*....|..
gi 1693059733 174 RVEIKRLHQkLGNTMIYVTHDqIEALTLADRI 205
Cdd:cd03238 129 LEVIKGLID-LGNTVILIEHN-LDVLSSADWI 158
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-219 |
1.16e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 56.34 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 23 LNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQepkDRG-----IGMVFQSYALYPqmtveknl 97
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD---NREayrqlFSAVFSDFHLFD-------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 98 sfglRVAGLPKAEIDKRIKRAAEILQieplLQRKPS---------ALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK 168
Cdd:COG4615 420 ----RLLGLDGEADPARARELLERLE----LDHKVSvedgrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPE 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1693059733 169 LR----SELRVEIKRlhqkLGNTMIYVTHDQiEALTLADRIAVMKGGVVQQLADP 219
Cdd:COG4615 492 FRrvfyTELLPELKA----RGKTVIAISHDD-RYFDLADRVLKMDYGKLVELTGP 541
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-166 |
1.20e-08 |
|
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: 56.48 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIkGRNVTwqepkdrgIGMVFQS 84
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK--------LAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 85 Y-ALYPQMTVEKNLSFGLRVAGLPKAEIDKR-------IKRAAEilqiepllQRKPSALSGGQRQRVAIGRALVRDVDVF 156
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLDIIKLGKREIPSRayvgrfnFKGSDQ--------QKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170
....*....|
gi 1693059733 157 LFDEPLSNLD 166
Cdd:TIGR03719 466 LLDEPTNDLD 475
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-207 |
1.53e-08 |
|
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: 53.15 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 30 GEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIkgrnvtwqepkdrgigmvfqsyalypqmtveknlsfglrvaglpka 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 110 eIDKRIKRAAEILQIEPLLQ-RKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEI-----KRLHQK 183
Cdd:smart00382 36 -IDGEDILEEVLDQLLLIIVgGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSE 114
|
170 180
....*....|....*....|....
gi 1693059733 184 LGNTMIYVTHDQIEALTLADRIAV 207
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-194 |
2.05e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIF---------------------- 62
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSldpnerlgklrqdqfafeeftv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 63 ----IKGRNVTWQ--EPKDRgIgmvfqsYALyPQMTVEKnlsfGLRVAGLPK--AEIDKRI--KRAAEIL---QIEPLLQ 129
Cdd:PRK15064 82 ldtvIMGHTELWEvkQERDR-I------YAL-PEMSEED----GMKVADLEVkfAEMDGYTaeARAGELLlgvGIPEEQH 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 130 RKP-SALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKlrselrvEIKRLHQKLGN---TMIYVTHD 194
Cdd:PRK15064 150 YGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIN-------TIRWLEDVLNErnsTMIIISHD 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-194 |
2.48e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGR-NVTWqepkdrgigmvFQSY 85
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAY-----------FDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 86 --ALYPQMTVEKNLSFGlrvaglpKAE--IDKRIKRAAEILQ---IEPLLQRKP-SALSGGQRQRVAIGRALVRDVDVFL 157
Cdd:PRK11147 391 raELDPEKTVMDNLAEG-------KQEvmVNGRPRHVLGYLQdflFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLI 463
|
170 180 190
....*....|....*....|....*....|....*..
gi 1693059733 158 FDEPLSNLDAKLRsELRVEIKRLHQklgNTMIYVTHD 194
Cdd:PRK11147 464 LDEPTNDLDVETL-ELLEELLDSYQ---GTVLLVSHD 496
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-217 |
2.63e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 3 SSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSI-----------FIKGRNVTWQ 71
Cdd:PRK10938 2 SSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqfshitrlsFEQLQKLVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 72 EPKDRGIGMvfqsyalypqmtveknLSFGLRVAGLPKAEI-------DKRIKRAAEILQIEPLLQRKPSALSGGQRQRVA 144
Cdd:PRK10938 82 EWQRNNTDM----------------LSPGEDDTGRTTAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 145 IGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTH------DQIE-ALTLAD--------RIAVMK 209
Cdd:PRK10938 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNrfdeipDFVQfAGVLADctlaetgeREEILQ 224
|
....*...
gi 1693059733 210 GGVVQQLA 217
Cdd:PRK10938 225 QALVAQLA 232
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
7-226 |
3.00e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.42 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 7 IQDLSLDF----GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGlldISEGSIFIKGRNVTWQE-------PKD 75
Cdd:PRK15093 6 IRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG---VTKDNWRVTADRMRFDDidllrlsPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 R------GIGMVFQSyalyPQMTVEKNLSFGLR-VAGLPK--------AEIDKRIKRAAEILQI------EPLLQRKPSA 134
Cdd:PRK15093 83 RrklvghNVSMIFQE----PQSCLDPSERVGRQlMQNIPGwtykgrwwQRFGWRKRRAIELLHRvgikdhKDAMRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 135 LSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVVQ 214
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250
....*....|..
gi 1693059733 215 QLADPLTIYNRP 226
Cdd:PRK15093 239 ETAPSKELVTTP 250
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-218 |
5.19e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.28 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 20 LQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIfikgrnvtwqePKDRGIGMVFQSYALYPQMTVEKNLSF 99
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAISAGLSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 100 GLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKR 179
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 1693059733 180 LHQKlGNTMIYVTHDQIEALTLADRIAVMKGGVVQQLAD 218
Cdd:PRK13546 189 FKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-193 |
8.08e-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: 53.98 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTWQEPKDRGIGM-VFQSYALYPqMTVEKNL 97
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLgTLRDQIIYP-DSSEDMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 98 SFGLRvaglpkaeiDKRIKRAAEILQIEPLLQRKPS---------ALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAk 168
Cdd:TIGR00954 546 RRGLS---------DKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV- 615
|
170 180
....*....|....*....|....*
gi 1693059733 169 lrsELRVEIKRLHQKLGNTMIYVTH 193
Cdd:TIGR00954 616 ---DVEGYMYRLCREFGITLFSVSH 637
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
5-213 |
2.09e-07 |
|
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: 51.45 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDFGSV--NVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVT---WQEPKDRgIG 79
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISklpLHTLRSR-LS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 80 MVFQSYALYPQmTVEKNLSfglrvaglPKAE-IDKRIKRAAEILQIEPLLQRKPSAL-----------SGGQRQRVAIGR 147
Cdd:cd03288 99 IILQDPILFSG-SIRFNLD--------PECKcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLAR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 148 ALVRDVDVFLFDEPLSNLDAKLRSELRveiKRLHQKLGNTMIYVTHDQIEALTLADRIAVMKGGVV 213
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENILQ---KVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
30-168 |
3.65e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 30 GEFLVLLGPSGCGKSTLLNCVAGLLD--ISEGSIFIKGRNVTwQEPKDRGIGMVFQSYALYPQMTVEKNLSFG--LRvag 105
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKK-QETFARISGYCEQNDIHSPQVTVRESLIYSafLR--- 981
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1693059733 106 LPKaEIDKRIK-----RAAEILQIEPL---LQRKP--SALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDAK 168
Cdd:PLN03140 982 LPK-EVSKEEKmmfvdEVMELVELDNLkdaIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-205 |
4.86e-07 |
|
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: 49.91 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 34 VLLGPSGCGKSTLLNCVAGLL--DISEGSIFIKGRNVTWQEPKDRG-IGMVFQSyALYPQMTVEKNLSFGLRVAGLPKAE 110
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYALtgELPPNSKGGAHDPKLIREGEVRAqVKLAFEN-ANGKKYTITRSLAILENVIFCHQGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 111 IDKrikraaeilqiepLLQRKPSALSGGQRQ------RVAIGRALVRDVDVFLFDEPLSNLDAKLRSELRVEIKRLHQKL 184
Cdd:cd03240 105 SNW-------------PLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQ 171
|
170 180
....*....|....*....|..
gi 1693059733 185 GN-TMIYVTHDQiEALTLADRI 205
Cdd:cd03240 172 KNfQLIVITHDE-ELVDAADHI 192
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-205 |
4.96e-07 |
|
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: 49.95 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 17 VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLlncvaglldiSEGSIFIKGR---------------------NVTWQEPKD 75
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSL----------AFDTIYAEGQrryveslsayarqflgqmdkpDVDSIEGLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 76 RGIGMVFQSYALYPQMTV----EKNLSFGLRVAglpKAEIDKRIKRAAEIlQIEPL-LQRKPSALSGGQRQRVA----IG 146
Cdd:cd03270 78 PAIAIDQKTTSRNPRSTVgtvtEIYDYLRLLFA---RVGIRERLGFLVDV-GLGYLtLSRSAPTLSGGEAQRIRlatqIG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1693059733 147 RALVrDVdVFLFDEPLSNLDAKLRSELRVEIKRLhQKLGNTMIYVTHDQiEALTLADRI 205
Cdd:cd03270 154 SGLT-GV-LYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHV 208
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-230 |
8.34e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGRNVTwqepkDRGIGMVFQSYALYPQ------MT 92
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG-----AYGLRELRRQFSMIPQdpvlfdGT 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 93 VEKNLS-F----------GLRVAGLpkaeidkRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALV-RDVDVFLFDE 160
Cdd:PTZ00243 1400 VRQNVDpFleassaevwaALELVGL-------RERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDE 1472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 161 PLSNLDAKLRSELRVEIKRLHQklGNTMIYVTHdQIEALTLADRIAVMKGGVVQQLADPLTIYNRPRNRF 230
Cdd:PTZ00243 1473 ATANIDPALDRQIQATVMSAFS--AYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-167 |
1.48e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 16 SVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDIS----EGSIFIKGrnVTWQEPKDRGIGMVFQSYAL---Y 88
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDG--ITPEEIKKHYRGDVVYNAETdvhF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 89 PQMTVEKNLSF-------GLRVAGLPKAEIDKRIkrAAEILQIEPLLQRKPS--------ALSGGQRQRVAIGRALVRDV 153
Cdd:TIGR00956 151 PHLTVGETLDFaarcktpQNRPDGVSREEYAKHI--ADVYMATYGLSHTRNTkvgndfvrGVSGGERKRVSIAEASLGGA 228
|
170
....*....|....
gi 1693059733 154 DVFLFDEPLSNLDA 167
Cdd:TIGR00956 229 KIQCWDNATRGLDS 242
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-216 |
2.23e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 3 SSVSIQDLSLDFGSVNVLQNLNLEIGEGEFLVLLGPSGCG--KSTLLNCVAGlldisEGSIFIKGRNVTW---QEPKDRG 77
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G-----PDAGRRPWRF*TWcanRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 IGMVFQ-SYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKRAAEILQIEPLLQRKPSALSGGQRQRVAIGRALVRDVDVF 156
Cdd:NF000106 87 IG*HRPvR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1693059733 157 LFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQIEA------LTLADRIAVMKGGVVQQL 216
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDEL 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
128-205 |
3.18e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 128 LQRKPSALSGGQRQRVA----IGRALVrDVdVFLFDEPLSNLDAKLRSELRVEIKRLhQKLGNTMIYVTHDQiEALTLAD 203
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRlatqIGSGLT-GV-LYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDE-DTIRAAD 557
|
..
gi 1693059733 204 RI 205
Cdd:TIGR00630 558 YV 559
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-166 |
3.76e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 5 VSIQDLSLDF-GSVNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFikgrnvtwQEPKDRgIGMVFQ 83
Cdd:PLN03073 509 ISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------RSAKVR-MAVFSQ 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 84 SYALYPQMTVEKNLSFGLRVAGLPKAEIDKRIKR--AAEILQIEPLLqrkpsALSGGQRQRVAIGRALVRDVDVFLFDEP 161
Cdd:PLN03073 580 HHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSfgVTGNLALQPMY-----TLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
....*
gi 1693059733 162 LSNLD 166
Cdd:PLN03073 655 SNHLD 659
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-209 |
6.12e-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: 45.81 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 22 NLNLEIGEGEFLVLLGPSGCGKSTLLNCVAglldisegsifikgrnvtwqepkdrgigmvfqsYALYPQMTVEKNLSFGL 101
Cdd:cd03227 13 PNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSATRRRSGVK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 102 RvaGLPKAEIDkrikraAEILQIepLLQrkpsaLSGGQRQRVAI----GRALVRDVDVFLFDEPLSNLDAKLRSELrVEI 177
Cdd:cd03227 60 A--GCIVAAVS------AELIFT--RLQ-----LSGGEKELSALalilALASLKPRPLYILDEIDRGLDPRDGQAL-AEA 123
|
170 180 190
....*....|....*....|....*....|..
gi 1693059733 178 KRLHQKLGNTMIYVTHDQIEALtLADRIAVMK 209
Cdd:cd03227 124 ILEHLVKGAQVIVITHLPELAE-LADKLIHIK 154
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
109-193 |
1.48e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 109 AEIDKRIK---------RAAEIL---QIEPLLQRKPS-ALSGGQRQRVAIGRALVRDVDVFLFDEPLSNLDakLRSELRV 175
Cdd:PLN03073 306 EEIYKRLElidaytaeaRAASILaglSFTPEMQVKATkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWL 383
|
90
....*....|....*...
gi 1693059733 176 EIKRLhqKLGNTMIYVTH 193
Cdd:PLN03073 384 ETYLL--KWPKTFIVVSH 399
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-195 |
1.68e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 19 VLQNLNLEIGEGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFIKGrnvTWQepkdrgIGMVFQSYALYPQMTVE---- 94
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG---NWQ------LAWVNQETPALPQPALEyvid 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 95 -----KNLSFGLRVA-----GLPKAEIDKRI---------KRAAEILQ----IEPLLQRKPSALSGGQRQRVAIGRALVR 151
Cdd:PRK10636 87 gdreyRQLEAQLHDAnerndGHAIATIHGKLdaidawtirSRAASLLHglgfSNEQLERPVSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1693059733 152 DVDVFLFDEPLSNLDakLRSELRVEiKRLHQKLGnTMIYVTHDQ 195
Cdd:PRK10636 167 RSDLLLLDEPTNHLD--LDAVIWLE-KWLKSYQG-TLILISHDR 206
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
128-205 |
1.65e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 128 LQRKPSALSGGQRQRVAIGRALVRDVD--VFLFDEPLSNLDAKLRSELRVEIKRLHQKlGNTMIYVTHDQiEALTLADRI 205
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDE-QMISLADRI 547
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
241-289 |
1.65e-04 |
|
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common architecture comprising two variable hydrophobic transmembrane domains (TMDs) that form the translocation pathway and two conserved hydrophilic ABC-ATPases that hydrolyze ATP. This is the C-terminal regulatory domain found at the ATPase subunit of CysA, a putative sulfate ABC transporter from Alicyclobacillus acidocaldarius. The regulatory domain of CysA is built up of an elongated beta-barrel composed of two beta-sandwiches that form a common hydrophobic core.
Pssm-ID: 465531 [Multi-domain] Cd Length: 43 Bit Score: 38.58 E-value: 1.65e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1693059733 241 NFFSGEIasRSGKpvFHIGEAAVQLDGYDGAleQGRKVTLGVRPEHIRL 289
Cdd:pfam17850 1 NLFHGRV--EDGR--VRIGGLALPLPELAGA--EGSEVVAYVRPHDLEI 43
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
17-194 |
1.63e-03 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.52 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 17 VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLN-----CVAGLLDISEGSI----FIKG-RNVTW-----QEPKDRG---- 77
Cdd:cd03271 8 ENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypALARRLHLKKEQPgnhdRIEGlEHIDKvividQSPIGRTprsn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1693059733 78 ----------IGMVF--------------------QSYALYPQMTVEKNLSFGLRVAglpkaeidkRIKRAAEILQIEPL 127
Cdd:cd03271 88 patytgvfdeIRELFcevckgkrynretlevrykgKSIADVLDMTVEEALEFFENIP---------KIARKLQTLCDVGL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1693059733 128 ----LQRKPSALSGGQRQRVAIGRALVRDVD---VFLFDEPLSNL---DAKlrsELRVEIKRLHQKlGNTMIYVTHD 194
Cdd:cd03271 159 gyikLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVK---KLLEVLQRLVDK-GNTVVVIEHN 231
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
29-69 |
2.22e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 38.29 E-value: 2.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1693059733 29 EGEFLVLLGPSGCGKSTLLNCVAGLLDISEGSIFI---KGRNVT 69
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEISEklgRGRHTT 148
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
17-48 |
2.57e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 2.57e-03
10 20 30
....*....|....*....|....*....|..
gi 1693059733 17 VNVLQNLNLEIGEGEFLVLLGPSGCGKSTLLN 48
Cdd:TIGR00630 621 ENNLKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
34-61 |
3.61e-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: 3.61e-03
10 20
....*....|....*....|....*...
gi 1693059733 34 VLLGPSGCGKSTLLNCVAGLLDISEGSI 61
Cdd:cd01854 89 VLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
18-48 |
5.89e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.52 E-value: 5.89e-03
10 20 30
....*....|....*....|....*....|.
gi 1693059733 18 NVLQNLNLEIGEGEFLVLLGPSGCGKSTLLN 48
Cdd:PRK00349 623 NNLKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
11-52 |
7.56e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 37.99 E-value: 7.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1693059733 11 SLDFGSVNVLQNLnleIGEGEFLVLLGPSGCGKSTLLNCVAG 52
Cdd:PRK01889 179 ALDGEGLDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLG 217
|
|
| |
