|
Name |
Accession |
Description |
Interval |
E-value |
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-356 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 722.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAM 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGSPAM 240
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 241 NLLPGTLSADGGQLLLADGMALPLPAAKPQWAGRQLTLGIRPEHIQLVAQGQGVPLQLQTLELLGADNLAHGQWGGHGVI 320
Cdd:PRK11650 241 NLLDGRVSADGAAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIALSSAEGGVPLTVDTVELLGADNLAHGRWGGQPLV 320
|
330 340 350
....*....|....*....|....*....|....*.
gi 742395038 321 ARLSHETLPAAGSTLYLQLPAQALHFFDTHSGLRMD 356
Cdd:PRK11650 321 VRLPHQERPAAGSTLWLHLPANQLHLFDADTGRRIE 356
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-355 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 605.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAM 80
Cdd:COG3839 1 MASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGSPAM 240
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 241 NLLPGTLSADGgqlLLADGMALPLPAAKPQWAGRQLTLGIRPEHIQLVAQGQ-GVPLQLQTLELLGADNLAHGQWGGHGV 319
Cdd:COG3839 240 NLLPGTVEGGG---VRLGGVRLPLPAALAAAAGGEVTLGIRPEHLRLADEGDgGLEATVEVVEPLGSETLVHVRLGGQEL 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 742395038 320 IARLSHETLPAAGSTLYLQLPAQALHFFDTHSGLRM 355
Cdd:COG3839 317 VARVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-347 |
4.79e-159 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 449.55 E-value: 4.79e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAM 80
Cdd:COG3842 3 MPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGSpaM 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGE--A 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 241 NLLPGTLSADGGQLLLADGMALPLPAAKPQWAGRQLTLGIRPEHIQLVAQGQ--GVPLQLQTLELLGADNLAHGQWG-GH 317
Cdd:COG3842 240 NLLPGTVLGDEGGGVRTGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPenGLPGTVEDVVFLGSHVRYRVRLGdGQ 319
|
330 340 350
....*....|....*....|....*....|..
gi 742395038 318 GVIARLSHETL--PAAGSTLYLQLPAQALHFF 347
Cdd:COG3842 320 ELVVRVPNRAAlpLEPGDRVGLSWDPEDVVVL 351
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-347 |
8.97e-153 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 434.46 E-value: 8.97e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAM 80
Cdd:PRK11000 1 MASVTLRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGSPAM 240
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 241 NLLPGTLSA---DGGQLLLADGMALPLPAAKPQW-AGRQLTLGIRPEHIQLVAQGQgVPL--QLQTLELLGADNLAHGQW 314
Cdd:PRK11000 240 NFLPVKVTAtaiEQVQVELPNRQQVWLPVEGRGVqVGANMSLGIRPEHLLPSDIAD-VTLegEVQVVEQLGNETQIHIQI 318
|
330 340 350
....*....|....*....|....*....|....*
gi 742395038 315 GG--HGVIARLSHETLPAAGSTLYLQLPAQALHFF 347
Cdd:PRK11000 319 PAirQNLVYRQNDVVLVEEGATFAIGLPPERCHLF 353
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-217 |
2.62e-133 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 378.91 E-value: 2.62e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQ 83
Cdd:cd03301 1 VELENVTKRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 742395038 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIG 217
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-346 |
3.69e-123 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 358.30 E-value: 3.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 3 GLKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRV-TDLEPKDRGIAMV 81
Cdd:COG1118 2 SIEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 162 LSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGspAMN 241
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 242 LLPGTlsADGGQlLLADGMALPLPAAKPQWAGrqlTLGIRPEHIQLVAQGQG---VPLQLQTLELLGAD---NLAHGQWG 315
Cdd:COG1118 239 VLRGR--VIGGQ-LEADGLTLPVAEPLPDGPA---VAGVRPHDIEVSREPEGentFPATVARVSELGPEvrvELKLEDGE 312
|
330 340 350
....*....|....*....|....*....|....*
gi 742395038 316 GHGVIARLSHET----LPAAGSTLYLQLPAQALHF 346
Cdd:COG1118 313 GQPLEAEVTKEAwaelGLAPGDPVYLRPRPARVFL 347
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-287 |
2.66e-117 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 344.24 E-value: 2.66e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQ 83
Cdd:PRK09452 15 VELRGISKSFDGKE-VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGSpaMNLL 243
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE--INIF 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 742395038 244 PGT-LSADGGQLLLAD--GMALPLPAAKPQWAGRQLTLGIRPEHIQL 287
Cdd:PRK09452 252 DATvIERLDEQRVRANveGRECNIYVNFAVEPGQKLHVLLRPEDLRV 298
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-236 |
1.39e-113 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 329.58 E-value: 1.39e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQ 83
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIG 236
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-347 |
4.36e-112 |
|
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: 330.46 E-value: 4.36e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAM 80
Cdd:TIGR03265 2 SPYLSIDNIRKRF-GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEaarILELEPLL--KRK-PRELSGGQRQRVAMGRAIVREPAVFL 157
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAE---LLDLVGLPgsERKyPGQLSGGQQQRVALARALATSPGLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 158 FDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGS 237
Cdd:TIGR03265 158 LDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 238 paMNLLPGTLSADGGQLLLADGMALPLPAAKPQWAGRqltLGIRPEHIQLVAQG---QGVPLQLQTLELLGA-------- 306
Cdd:TIGR03265 238 --VNWLPGTRGGGSRARVGGLTLACAPGLAQPGASVR---LAVRPEDIRVSPAGnaaNLLLARVEDMEFLGAfyrlrlrl 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 742395038 307 DNLahgqwGGHGVIARLSHETLP----AAGSTLYLQLPAQALHFF 347
Cdd:TIGR03265 313 EGL-----PGQALVADVSASEVErlgiRAGQPIWIELPAERLRAF 352
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-217 |
5.62e-112 |
|
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: 324.86 E-value: 5.62e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQ 83
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 742395038 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIG 217
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-339 |
2.92e-111 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 328.22 E-value: 2.92e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQ 83
Cdd:PRK11432 7 VVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGSPamNLL 243
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 244 PGTLSADGGQLllaDGMALPLP-AAKPQWAGRQLTLGIRPEHIQLVAQGQgvPLQLQTLE---LLGADNLAHGQWGGHGV 319
Cdd:PRK11432 244 PATLSGDYVDI---YGYRLPRPaAFAFNLPDGECTVGVRPEAITLSEQGE--ESQRCTIKhvaYMGPQYEVTVDWHGQEL 318
|
330 340
....*....|....*....|.
gi 742395038 320 IARLSHETL-PAAGSTLYLQL 339
Cdd:PRK11432 319 LLQVNATQLqPDLGEHYYLEI 339
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
5-287 |
3.72e-110 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 325.41 E-value: 3.72e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 5 KLQAVTKSY-DGKTPV--IKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTD-----LEPKDR 76
Cdd:NF040933 4 RVENVTKIFkKGKKEVvaLDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPPEDR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 77 GIAMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVF 156
Cdd:NF040933 84 NIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 157 LFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIG 236
Cdd:NF040933 164 LLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLIG 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 742395038 237 SpaMNLLPGTLSADGgqLLLADGMALPLPAAKPQwaGRQLTLGIRPEHIQL 287
Cdd:NF040933 244 D--INLLEGKVEEEG--LVDGNDLKIPLPNPKLE--AGEVIIGIRPEDIDI 288
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-237 |
1.53e-95 |
|
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: 283.85 E-value: 1.53e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 3 GLKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVF 82
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYPHMSVYDNMAYGLKIR----GFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 159 DEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGS 237
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-287 |
6.01e-93 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 281.19 E-value: 6.01e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdgKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQ 83
Cdd:NF040840 2 IRIENLSKDW--KEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:NF040840 80 NYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGspAMNLL 243
Cdd:NF040840 160 ALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG--FENII 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 742395038 244 PGTLSADG-GQLLLADGMALPLPAAKpqwAGRqLTLGIRPEHIQL 287
Cdd:NF040840 238 EGVAEKGGeGTILDTGNIKIELPEEK---KGK-VRIGIRPEDITI 278
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-287 |
1.69e-91 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 276.68 E-value: 1.69e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 35 MVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQR 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 115 VEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHD 194
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 195 QVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGSpaMNLLPGT-LSADGGQLLLADGMALPLPAAK--PQW 271
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE--INVFEATvIERKSEQVVLAGVEGRRCDIYTdvPVE 238
|
250
....*....|....*.
gi 742395038 272 AGRQLTLGIRPEHIQL 287
Cdd:TIGR01187 239 KDQPLHVVLRPEKIVI 254
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
9-236 |
1.85e-88 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 265.90 E-value: 1.85e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQNYALY 88
Cdd:TIGR00968 6 ISKRF-GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 89 PHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
Cdd:TIGR00968 85 KHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742395038 169 LRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIG 236
Cdd:TIGR00968 165 VRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
3.58e-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: 263.49 E-value: 3.58e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSY---DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKdrg 77
Cdd:COG1116 5 APALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 IAMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFL 157
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 742395038 158 FDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-236 |
7.47e-84 |
|
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: 254.18 E-value: 7.47e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKsyDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQ 83
Cdd:cd03299 1 LKVENLSK--DWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIG 236
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-303 |
1.68e-83 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 257.32 E-value: 1.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQNYALY 88
Cdd:PRK10851 8 IKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 89 PHMSVYDNMAYGLKI----RGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
Cdd:PRK10851 87 RHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 165 LDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGSpaMNLLP 244
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE--VNRLQ 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 245 GTLSadGGQLLLAdGMALPLPAAkPQWAGRqLTLGIRPEHIQLVAQGQ-GVPLQLQTLEL 303
Cdd:PRK10851 245 GTIR--GGQFHVG-AHRWPLGYT-PAYQGP-VDLFLRPWEVDISRRTSlDSPLPVQVLEV 299
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-296 |
8.33e-83 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 253.86 E-value: 8.33e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 5 KLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMVF 82
Cdd:COG1125 3 EFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEP--LLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGSPAM 240
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGADRG 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 241 NLLPGTLSADGgqllLADGMALPLPAAKPQWAGRQLTLGIRPEHIqLVAQGQGVPL 296
Cdd:COG1125 243 LRRLSLLRVED----LMLPEPPTVSPDASLREALSLMLERGVDWL-LVVDEDGRPL 293
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-287 |
1.03e-82 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 256.30 E-value: 1.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQ 83
Cdd:PRK11607 20 LEIRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGSpaMNLL 243
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVF 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 742395038 244 PGTLSA--DGGQLLLADGMALPLP--AAKPQWAGRQLTLGIRPEHIQL 287
Cdd:PRK11607 257 EGVLKErqEDGLVIDSPGLVHPLKvdADASVVDNVPVHVALRPEKIML 304
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-210 |
2.56e-82 |
|
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: 249.70 E-value: 2.56e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGK---TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKdrgIAM 80
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 742395038 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNK 210
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-238 |
5.62e-75 |
|
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: 231.81 E-value: 5.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMV 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEP--LLKRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 160 EPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIGSP 238
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-217 |
6.25e-71 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 220.24 E-value: 6.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 22 QIDLDVaDGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI------DTRRVTDLEPKDRGIAMVFQNYALYPHMSVYD 95
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfDSRKKINLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 96 NMAYGLKIRGFGKDhiRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRL 175
Cdd:cd03297 95 NLAFGLKRKRNRED--RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 742395038 176 ELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIG 217
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-211 |
2.00e-70 |
|
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: 217.83 E-value: 2.00e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLE----PKDRGIA 79
Cdd:cd03229 1 LELKNVSKRYGQKT-VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNYALYPHMSVYDNMAYGlkirgfgkdhirqrveeaarilelepllkrkpreLSGGQRQRVAMGRAIVREPAVFLFD 159
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 742395038 160 EPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-235 |
6.60e-70 |
|
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: 219.44 E-value: 6.60e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD------RGIAMVFQNYALY 88
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 89 PHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
Cdd:cd03294 115 PHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 169 LRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFI 235
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-211 |
4.72e-68 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 213.12 E-value: 4.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY---DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG--- 77
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 ---IAMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPA 154
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 155 VFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMtLAQRVIVMNKG 211
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDG 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-212 |
7.56e-68 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 212.60 E-value: 7.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY---DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG--- 77
Cdd:COG1136 5 LELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 ---IAMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPA 154
Cdd:COG1136 85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 155 VFLFDEPLSNLDAKLRVQ-MRLeLQQLHRRLKTTSLYVTHDQvEAMTLAQRVIVMNKGV 212
Cdd:COG1136 165 LILADEPTGNLDSKTGEEvLEL-LRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-290 |
9.80e-67 |
|
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: 214.19 E-value: 9.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 22 QIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI------DTRRVTDLEPKDRGIAMVFQNYALYPHMSVYD 95
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqDSARGIFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 96 NMAYGLKIRGFGKDHIRqrVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRL 175
Cdd:COG4148 97 NLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 176 ELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGfiGSPAMNLLPGT--------- 246
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAGSVLEATvaahdpdyg 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 742395038 247 ---LSADGGQLLLAdgmALPLPaakpqwAGRQLTLGIRPEHIQLVAQ 290
Cdd:COG4148 253 ltrLALGGGRLWVP---RLDLP------PGTRVRVRIRARDVSLALE 290
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-229 |
1.72e-66 |
|
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: 209.50 E-value: 1.72e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMV 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNyalyP-----HMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVF 156
Cdd:COG1122 81 FQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 157 LFDEPLSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHDQVEAMTLAQRVIVMNKG--VAEqiGTPSEVYQRPASL 229
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTV-IIVTHDLDLVAELADRVIVLDDGriVAD--GTPREVFSDYELL 228
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-236 |
5.83e-66 |
|
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: 212.40 E-value: 5.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEP------KDRGIAMVFQNYALY 88
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 89 PHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742395038 169 LRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIG 236
Cdd:TIGR01186 164 IRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-211 |
6.41e-65 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 205.29 E-value: 6.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-----RGI 78
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 159 DEPLSNLDAKLRVQ-MRLeLQQLHRRlKTTSLYVTHDQ--VEAMtlAQRVIVMNKG 211
Cdd:COG2884 162 DEPTGNLDPETSWEiMEL-LEEINRR-GTTVLIATHDLelVDRM--PKRVLELEDG 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-236 |
3.53e-62 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 198.44 E-value: 3.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpviKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQ 83
Cdd:COG3840 2 LRLDDLTYRYGDFP---LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFIG 236
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-228 |
5.02e-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: 198.49 E-value: 5.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGK---TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGI 78
Cdd:COG1124 2 LEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNY--ALYPHMSVYDNMAYGLKIRGFgkDHIRQRVEEAARILELEP-LLKRKPRELSGGQRQRVAMGRAIVREPAV 155
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742395038 156 FLFDEPLSNLDAKLRVQ-MRLeLQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPAS 228
Cdd:COG1124 160 LLLDEPTSALDVSVQAEiLNL-LKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-211 |
7.56e-62 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 196.92 E-value: 7.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 5 KLQAVTKSY-DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG--IAMV 81
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNyalyP-HM----SVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVF 156
Cdd:cd03225 81 FQN----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 157 LFDEPLSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTI-IIVTHDLDLLLELADRVIVLEDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
8.99e-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: 8.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYD----GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD---- 75
Cdd:COG1123 261 LEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 76 -RGIAMVFQN--YALYPHMSVYDNMAYGLKIRGFG-KDHIRQRVEEAARILELEP-LLKRKPRELSGGQRQRVAMGRAIV 150
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 151 REPAVFLFDEPLSNLDAKLRVQ-MRLeLQQLHRRLKTTSLYVTHD--QVEAMtlAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQiLNL-LRDLQRELGLTYLFISHDlaVVRYI--ADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-224 |
1.04e-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: 194.81 E-value: 1.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-----RGI 78
Cdd:COG1127 6 IEVRNLTKSFGDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYPHMSVYDNMAYGLKIR-GFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFL 157
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742395038 158 FDEPLSNLDAK-LRVQMRLeLQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQ 224
Cdd:COG1127 165 YDEPTAGLDPItSAVIDEL-IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-225 |
2.45e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 191.43 E-value: 2.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG-IAMVF 82
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 163 SNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVIVMNKG--VAEqiGTPSEVYQR 225
Cdd:COG1131 160 SGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGriVAD--GTPDELKAR 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-228 |
3.18e-59 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 190.98 E-value: 3.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDlEPKD-----RGI 78
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDinklrRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYPHMSVYDNMAYGL-KIRGFGKDHIRQRveeAARILE---LEPLLKRKPRELSGGQRQRVAMGRAIVREPA 154
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEER---AMELLErvgLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 155 VFLFDEPLSNLDAK-----LRVqMRlELqqlhRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPAS 228
Cdd:COG1126 157 VMLFDEPTSALDPElvgevLDV-MR-DL----AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-208 |
2.90e-57 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 186.99 E-value: 2.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYDGK---TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDleP-KDR 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PgADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 77 GIamVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVF 156
Cdd:COG4525 79 GV--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 742395038 157 LFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVM 208
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-224 |
1.02e-56 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 184.63 E-value: 1.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 6 LQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-----RGIAM 80
Cdd:cd03261 3 LRGLTKSFGGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSVYDNMAYGLKIRG-FGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
Cdd:cd03261 82 LFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 160 EPLSNLDAK-LRVQMRLeLQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQ 224
Cdd:cd03261 162 EPTAGLDPIaSGVIDDL-IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-226 |
3.14e-56 |
|
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: 183.17 E-value: 3.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYD---GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD----- 75
Cdd:cd03258 2 IELKNVSKVFGdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 76 RGIAMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAV 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 156 FLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHdQVEAM-TLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-249 |
4.21e-56 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 186.05 E-value: 4.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY---DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD----- 75
Cdd:COG1135 2 IELENLSKTFptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 76 RGIAMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAV 155
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 156 FLFDEPLSNLDAK-----LRVqmrleLQQLHRRLKTTSLYVTHDqveaM----TLAQRVIVMNKG-VAEQiGTPSEVYQR 225
Cdd:COG1135 162 LLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGrIVEQ-GPVLDVFAN 231
|
250 260
....*....|....*....|....
gi 742395038 226 PASLFVAGFIGSPAMNLLPGTLSA 249
Cdd:COG1135 232 PQSELTRRFLPTVLNDELPEELLA 255
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-222 |
3.62e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 181.02 E-value: 3.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-----RGI 78
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYPHMSVYDN-----MAY--GLK--IRGFGKDHIrqrvEEAARILE---LEPLLKRKPRELSGGQRQRVAMG 146
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNvlagrLGRtsTWRslLGLFPPEDR----ERALEALErvgLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 147 RAIVREPAVFLFDEPLSNLDAKL-RVQMRLeLQQLHRRLKTTSLYVTHdQVE-AMTLAQRVIVMNKGvaeQI---GTPSE 221
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDG---RVvfdGPPAE 233
|
.
gi 742395038 222 V 222
Cdd:COG3638 234 L 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-212 |
1.23e-53 |
|
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: 175.80 E-value: 1.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPK----DRGIA 79
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNYALYPHMSVYDNMAYGL-KIRGFGKDhirQRVEEAARILELEPLLKRK---PRELSGGQRQRVAMGRAIVREPAV 155
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPiKVKGMSKA---EAEERALELLEKVGLADKAdayPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 156 FLFDEPLSNLDAklrvQMRLELQQLHRRL---KTTSLYVTHDQVEAMTLAQRVIVMNKGV 212
Cdd:cd03262 157 MLFDEPTSALDP----ELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-222 |
1.35e-53 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 177.16 E-value: 1.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG--IAMV 81
Cdd:COG1120 2 LEAENLSVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELArrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNYALYPHMSVYDNMAYG----LKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFL 157
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 158 FDEPLSNLDAKLRVQ-MRLeLQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEV 222
Cdd:COG1120 161 LDEPTSHLDLAHQLEvLEL-LRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-229 |
4.42e-53 |
|
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: 176.08 E-value: 4.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY-DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDtrrvtDLEPKD------- 75
Cdd:TIGR04520 1 IEVENVSFSYpESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-----GLDTLDeenlwei 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 76 -RGIAMVFQNyalyPH-----MSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAI 149
Cdd:TIGR04520 76 rKKVGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 150 VREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAmTLAQRVIVMNKGVAEQIGTPSEVYQRPASL 229
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQVELL 230
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-211 |
1.80e-52 |
|
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: 173.46 E-value: 1.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY---DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG--- 77
Cdd:cd03257 2 LEVKNLSVSFptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 --IAMVFQNY--ALYPHMSVYDNMAYGLKIRGFGKDH--IRQRVEEAARILELEP-LLKRKPRELSGGQRQRVAMGRAIV 150
Cdd:cd03257 82 keIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742395038 151 REPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-229 |
7.18e-52 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 179.71 E-value: 7.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY-DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLER---TTSGDIYIDTRRVTDLEPKDRG-- 77
Cdd:COG1123 5 LEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEALRGrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 IAMVFQN--YALYPhMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAV 155
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742395038 156 FLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASL 229
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-228 |
9.37e-52 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 171.81 E-value: 9.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 6 LQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGI----AMV 81
Cdd:PRK09493 4 FKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNYALYPHMSVYDNMAYG-LKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:PRK09493 83 FQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742395038 161 PLSNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPAS 228
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-211 |
1.23e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.38 E-value: 1.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMV 81
Cdd:COG4619 1 LELEGLSFRVGGK-PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNYALYPhMSVYDNMAYGLKIRGFGKDhiRQRVEEAARILELEP-LLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:COG4619 80 PQEPALWG-GTVRDNLPFPFQLRERKFD--RERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 742395038 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-211 |
1.34e-51 |
|
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: 170.37 E-value: 1.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVikQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQ 83
Cdd:cd03298 1 VRLDKIRFSY-GEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:cd03298 78 ENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 742395038 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-229 |
1.87e-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 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: 172.25 E-value: 1.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTP----VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD---- 75
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 76 -RGIAMVFQnyalYPHM-----SVYDNMAYGLKIRGFGKDHIRQRVEEAARILEL-EPLLKRKPRELSGGQRQRVAMGRA 148
Cdd:TIGR04521 81 rKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 149 IVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPAS 228
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDE 236
|
.
gi 742395038 229 L 229
Cdd:TIGR04521 237 L 237
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
9-211 |
7.89e-51 |
|
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: 168.58 E-value: 7.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-----RGIAMVFQ 83
Cdd:TIGR02673 7 VSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:TIGR02673 87 DFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 742395038 164 NLDAKLRVQ-MRLeLQQLHRRlKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:TIGR02673 167 NLDPDLSERiLDL-LKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-222 |
8.83e-51 |
|
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: 168.90 E-value: 8.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGL-----ERTTSGDIYIDTRRVTDLEPKD--- 75
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 76 -RGIAMVFQNYALYPhMSVYDNMAYGLKIRGF-GKDHIRQRVEEAARILELEPLLKRK--PRELSGGQRQRVAMGRAIVR 151
Cdd:cd03260 80 rRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 152 EPAVFLFDEPLSNLD--AKLRVqmrlelQQLHRRLK--TTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEV 222
Cdd:cd03260 159 EPEVLLLDEPTSALDpiSTAKI------EELIAELKkeYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-225 |
1.99e-50 |
|
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: 168.50 E-value: 1.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG-IAMVF 82
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRqIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 163 SNLDAKLRVQMRLELQQLhRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQR 225
Cdd:COG4555 161 NGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-344 |
6.00e-50 |
|
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: 170.68 E-value: 6.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 23 IDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI------DTRRVTDLEPKDRGIAMVFQNYALYPHMSVYDN 96
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 97 MAYGLKiRGFGKDHiRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLE 176
Cdd:TIGR02142 96 LRYGMK-RARPSER-RISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 177 LQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAgfiGSPAMNLLPGTLSAdggqLLL 256
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA---REDQGSLIEGVVAE----HDQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 257 ADGM-ALPLPAA------KPQWAGRQLTLGIRPEHIQLVAQGqgvPLQLQTLELLGAD--NLAHGQWGGHGV-------- 319
Cdd:TIGR02142 247 HYGLtALRLGGGhlwvpeNLGPTGARLRLRVPARDVSLALQK---PEATSIRNILPARvvEIEDSDIGRVGVvlesggkt 323
|
330 340 350
....*....|....*....|....*....|
gi 742395038 320 ----IARLSHETLP-AAGSTLYLQLPAQAL 344
Cdd:TIGR02142 324 lwarITRWARDELGiAPGTPVFAQIKAVAL 353
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-224 |
7.04e-49 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 165.99 E-value: 7.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTP----VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGI- 78
Cdd:PRK13637 3 IKIENLTHIYMEGTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 ---AMVFQ--NYALYPHmSVYDNMAYGLKIRGFGKDHIRQRVEEAARI--LELEPLLKRKPRELSGGQRQRVAMGRAIVR 151
Cdd:PRK13637 83 kkvGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 152 EPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQ 224
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-226 |
1.58e-48 |
|
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: 163.41 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 20 IKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPkDRGIamVFQNYALYPHMSVYDNMAY 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 100 GLK--IRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEL 177
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 742395038 178 QQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEV-YQRP 226
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-208 |
4.12e-48 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 161.50 E-value: 4.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 3 GLKLQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAG-LER--TTSGDIYIDTRRVTDLEPKDRGIA 79
Cdd:COG4136 1 MLSLENLTITLGGR-PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPafSASGEVLLNGRRLTALPAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNYALYPHMSVYDNMAYGLKiRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 742395038 160 EPLSNLDAKLRVQMR-LELQQLHRRlKTTSLYVTHDqVEAMTLAQRVIVM 208
Cdd:COG4136 159 EPFSKLDAALRAQFReFVFEQIRQR-GIPALLVTHD-EEDAPAAGRVLDL 206
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-227 |
2.10e-45 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 155.29 E-value: 2.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDR---GIAM 80
Cdd:cd03219 1 LEVRGLTKRFGGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSVYDNMAYGLKIRGFGKDH----------IRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIV 150
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSGLLlararreereARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 151 REPAVFLFDEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG--VAEqiGTPSEVYQRPA 227
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGrvIAE--GTPDEVRNNPR 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-211 |
2.45e-45 |
|
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: 154.49 E-value: 2.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-----RGI 78
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 742395038 159 DEPLSNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
2.58e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 155.25 E-value: 2.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRrvtDLEPKDRGIAM 80
Cdd:COG1121 4 MPAIELENLTVSYGGR-PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPH--MSVYDNMAYGLK-----IRGFGKDHiRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREP 153
Cdd:COG1121 80 VPQRAEVDWDfpITVRDVVLMGRYgrrglFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 154 AVFLFDEPLSNLDAKLRVQ-MRLeLQQLHRRlKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQiGTPSEV 222
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEAlYEL-LRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEV 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-217 |
5.03e-45 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 154.84 E-value: 5.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRgiaMVFQ 83
Cdd:PRK11247 13 LLLNAVSKRYGERT-VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKirgfgkDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:PRK11247 89 DARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 742395038 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGvaeQIG 217
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIG 213
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-217 |
5.38e-45 |
|
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: 153.48 E-value: 5.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 24 DLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQNYALYPHMSVYDNMAYGLKI 103
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 104 RGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRR 183
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 742395038 184 LKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIG 217
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-224 |
5.63e-45 |
|
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: 154.26 E-value: 5.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-----RGI 78
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYPHMSVYDNMAYGL-----KIRGFGKDHIRQRVEEAARILE---LEPLLKRKPRELSGGQRQRVAMGRAIV 150
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrsTWRSLFGLFPKEEKQRALAALErvgLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 151 REPAVFLFDEPLSNLDAKLRVQ-MRLeLQQLHRRLKTTSLYVTHdQVE-AMTLAQRVIVMNKGvaeQI---GTPSEVYQ 224
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLH-QVDlAREYADRIVGLKDG---RIvfdGPPAELTD 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-211 |
2.30e-44 |
|
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: 150.24 E-value: 2.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG-IAMVF 82
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYPHMSVYDNMayglkirgfgkdhirqrveeaarilelepllkrkprELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 742395038 163 SNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd03230 124 SGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-225 |
5.96e-44 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 160.77 E-value: 5.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDG-KTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAM 80
Cdd:COG2274 474 IELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYpHMSVYDNMAyglkirgFGKDHI-RQRVEEAARILELEPLLKRKP-----------RELSGGQRQRVAMGRA 148
Cdd:COG2274 554 VLQDVFLF-SGTIRENIT-------LGDPDAtDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742395038 149 IVREPAVFLFDEPLSNLDAKLrvQMRLeLQQLHRRLK-TTSLYVTHDqVEAMTLAQRVIVMNKGVAEQIGTPSEVYQR 225
Cdd:COG2274 626 LLRNPRILILDEATSALDAET--EAII-LENLRRLLKgRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-222 |
1.53e-43 |
|
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: 150.96 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDR---G 77
Cdd:COG0411 2 DPLLEVRGLTKRFGGLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 IAMVFQNYALYPHMSVYDNMAYGLKIR----------GFGKDH-----IRQRVEEAARILELEPLLKRKPRELSGGQRQR 142
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARlgrgllaallRLPRARreereARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 143 VAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDqVEA-MTLAQRVIVMNKG--VAEqiGTP 219
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD-MDLvMGLADRIVVLDFGrvIAE--GTP 237
|
...
gi 742395038 220 SEV 222
Cdd:COG0411 238 AEV 240
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-211 |
3.68e-43 |
|
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: 149.04 E-value: 3.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY-DGK--TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG--- 77
Cdd:TIGR02211 2 LKCENLGKRYqEGKldTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 ---IAMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPA 154
Cdd:TIGR02211 82 nkkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 155 VFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDqveaMTLA---QRVIVMNKG 211
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHD----LELAkklDRVLEMKDG 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
5.14e-43 |
|
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: 148.42 E-value: 5.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY-DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI-DTRRVTDLEPKDRGIAMV 81
Cdd:cd03263 1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYInGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742395038 162 LSNLDAKLRVQM-RLELQQLHRRlktTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSE 221
Cdd:cd03263 161 TSGLDPASRRAIwDLILEVRKGR---SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-234 |
6.01e-43 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 153.65 E-value: 6.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 20 IKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYID---TRRVTDLEPKD---RGIAMVFQNYALYPHMSV 93
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdIAKISDAELREvrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 94 YDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQM 173
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742395038 174 RLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGF 234
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-211 |
6.19e-43 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 149.46 E-value: 6.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDlEPKDRGIamVFQ 83
Cdd:PRK11248 2 LQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 742395038 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-237 |
6.72e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 151.88 E-value: 6.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 5 KLQAVTKSYDGKTPVI---KQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-----R 76
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 77 GIAMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVF 156
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 157 LFDEPLSNLDAKLRVQMrLEL-QQLHRRLKTTSLYVTH--DQVEAmtLAQRVIVMNKG-VAEQiGTPSEVYQRPASLFVA 232
Cdd:PRK11153 163 LCDEATSALDPATTRSI-LELlKDINRELGLTIVLITHemDVVKR--ICDRVAVIDAGrLVEQ-GTVSEVFSHPKHPLTR 238
|
....*
gi 742395038 233 GFIGS 237
Cdd:PRK11153 239 EFIQS 243
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-163 |
8.97e-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: 145.48 E-value: 8.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 20 IKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMVFQNYALYPHMSVYDNM 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 98 AYGLKIRGFGKDHIRQRVEEAARILELEPLLKRK----PRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-211 |
3.70e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 146.65 E-value: 3.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpviKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQ 83
Cdd:PRK10771 2 LKLTDITWLYHHLP---MRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKiRGFGKDHI-RQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGLN-PGLKLNAAqREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 742395038 163 SNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-215 |
4.47e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 146.70 E-value: 4.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 3 GLKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRV---TDLEPKD---- 75
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAirll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 76 -RGIAMVFQNYALYPHMSVYDNM-AYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREP 153
Cdd:COG4161 81 rQKVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 154 AVFLFDEPLSNLDAKLRVQMR---LELQQlhrrLKTTSLYVTHDQVEAMTLAQRVIVMNKG-VAEQ 215
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVeiiRELSQ----TGITQVIVTHEVEFARKVASQVVYMEKGrIIEQ 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-221 |
4.74e-42 |
|
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: 146.42 E-value: 4.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY---DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRrvtDLEPKD----- 75
Cdd:COG4181 9 IELRGLTKTVgtgAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDedara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 76 ----RGIAMVFQNYALYPHMSVYDNMAYGLKIRgfGKDHIRQRveeAARILE---LEPLLKRKPRELSGGQRQRVAMGRA 148
Cdd:COG4181 86 rlraRHVGFVFQSFQLLPTLTALENVMLPLELA--GRRDARAR---ARALLErvgLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 149 IVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQveamTLA---QRVIVMNKGVAEQIGTPSE 221
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP----ALAarcDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-224 |
6.69e-42 |
|
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: 146.29 E-value: 6.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-----RGI 78
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYPHMSVYDNMAYGL--------KIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIV 150
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742395038 151 REPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQ 224
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-221 |
7.37e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 153.78 E-value: 7.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 3 GLKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAM 80
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYpHMSVYDNMAYGLkirgfgKDHIRQRVEEAARILELEPLLKRKP-----------RELSGGQRQRVAMGRAI 149
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYGR------PDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742395038 150 VREPAVFLFDEPLSNLDAK--LRVQmrlelQQLHRRLK-TTSLYVTH--DQVEAmtlAQRVIVMNKG-VAEQiGTPSE 221
Cdd:COG1132 492 LKDPPILILDEATSALDTEteALIQ-----EALERLMKgRTTIVIAHrlSTIRN---ADRILVLDDGrIVEQ-GTHEE 560
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-222 |
9.86e-42 |
|
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: 145.27 E-value: 9.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDR---GIAM 80
Cdd:cd03224 1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSVYDNMAYGLKIRgfGKDHIRQRVEeaaRILELEPLLK----RKPRELSGGQRQRVAMGRAIVREPAVF 156
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYAR--RRAKRKARLE---RVYELFPRLKerrkQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742395038 157 LFDEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG--VAEqiGTPSEV 222
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGrvVLE--GTAAEL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
9.88e-42 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 147.89 E-value: 9.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIK---QIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLER---TTSGDIYIDTRRVTDLEPKD-- 75
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 76 ----RGIAMVFQN-Y-ALYPHMSVYDNMAYGLKI-RGFGKDHIRQRVEEAARILELEP---LLKRKPRELSGGQRQRVAM 145
Cdd:COG0444 82 kirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 146 GRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLeLQQLHRRLKTTSLYVTHD--QVEAMtlAQRVIVMNKG-VAEqIGTPSE 221
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQiLNL-LKDLQRELGLAILFITHDlgVVAEI--ADRVAVMYAGrIVE-EGPVEE 237
|
....*.
gi 742395038 222 VYQRPA 227
Cdd:COG0444 238 LFENPR 243
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-215 |
1.75e-41 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 145.16 E-value: 1.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI-----DTRRVTDlePKD--- 75
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfDFSKTPS--DKAire 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 76 --RGIAMVFQNYALYPHMSVYDNMAYG-LKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVRE 152
Cdd:PRK11124 80 lrRNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 153 PAVFLFDEPLSNLDAKLRVQMR---LELQQLHrrlkTTSLYVTHDQVEAMTLAQRVIVMNKG-VAEQ 215
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVsiiRELAETG----ITQVIVTHEVEVARKTASRVVYMENGhIVEQ 222
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
23-227 |
2.94e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 147.19 E-value: 2.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 23 IDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-----RGIAMVFQN-YA-LYPHMSVYD 95
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYAsLNPRMTVGD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 96 NMAYGLKIRGFG-KDHIRQRVEEAARILELEP-LLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ- 172
Cdd:COG4608 117 IIAEPLRIHGLAsKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQv 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 173 MRLeLQQLHRRLKTTSLYVTHD--QVEAMtlAQRVIVMNKGVAEQIGTPSEVYQRPA 227
Cdd:COG4608 197 LNL-LEDLQDELGLTYLFISHDlsVVRHI--SDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-206 |
1.62e-40 |
|
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: 141.60 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 6 LQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYID---TRRVTDLEP----KDRgI 78
Cdd:TIGR03608 1 LKNISKKFGDKV-ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNgqeTPPLNSKKAskfrREK-L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:TIGR03608 79 GYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 742395038 159 DEPLSNLDAKLR-VQMRLeLQQLHRRLKTTsLYVTHDQvEAMTLAQRVI 206
Cdd:TIGR03608 159 DEPTGSLDPKNRdEVLDL-LLELNDEGKTI-IIVTHDP-EVAKQADRVI 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
1.73e-40 |
|
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: 140.21 E-value: 1.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGK-TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAM 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYpHMSVYDNMayglkirgfgkdhirqrveeaarilelepllkrkpreLSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 742395038 161 PLSNLDAKLRVQMRLELQQLHRrlKTTSLYVTHDqVEAMTLAQRVIVMNKG 211
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-237 |
1.76e-40 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 143.02 E-value: 1.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYID-------TRRVTDLEPKDR 76
Cdd:COG4598 9 LEVRDLHKSF-GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGgeeirlkPDRDGELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 77 --------GIAMVFQNYALYPHMSVYDN-MAYGLKIRGFGKDhirQRVEEAARILELEPLLKRK---PRELSGGQRQRVA 144
Cdd:COG4598 88 rqlqrirtRLGMVFQSFNLWSHMTVLENvIEAPVHVLGRPKA---EAIERAEALLAKVGLADKRdayPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 145 MGRAIVREPAVFLFDEPLSNLDAK-----LRVqMRlELQQLHRrlktTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTP 219
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPElvgevLKV-MR-DLAEEGR----TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPP 238
|
250
....*....|....*...
gi 742395038 220 SEVYQRPASLFVAGFIGS 237
Cdd:COG4598 239 AEVFGNPKSERLRQFLSS 256
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-225 |
4.06e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.85 E-value: 4.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY-DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAM 80
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNyalyPH-----MSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAV 155
Cdd:PRK13635 86 VFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 156 FLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTlAQRVIVMNKGVAEQIGTPSEVYQR 225
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-222 |
4.58e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 142.44 E-value: 4.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 5 KLQAVTKSYDG-KTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMV 81
Cdd:PRK13632 9 KVENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNyalyPH-----MSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVF 156
Cdd:PRK13632 89 FQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 157 LFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAmTLAQRVIVMNKGVAEQIGTPSEV 222
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-225 |
2.06e-39 |
|
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: 146.83 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMV 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNYALyPHMSVYDNmayglkIRGFGKDHIRQRVEEAARILELEPLLKRKP-----------RELSGGQRQRVAMGRAIV 150
Cdd:COG4988 417 PQNPYL-FAGTIREN------LRLGRPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 151 REPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRlkTTSLYVTHDQvEAMTLAQRVIVMNKGVAEQIGTPSEVYQR 225
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-211 |
2.85e-39 |
|
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: 136.61 E-value: 2.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 5 KLQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMVF 82
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QnyalyphmsvydnmayglkirgfgkdhirqrveeaarilelepllkrkpreLSGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 742395038 163 SNLDAKLRVQMRLELQQLHRRLKTTsLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTV-IIVTHDPELAELAADRVIVLKDG 156
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-226 |
3.23e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 139.50 E-value: 3.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSG-----DIYIDTRRvtDLEPKD 75
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTAR--SLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 76 RGI-------AMVFQNYALYPHMSVYDNMAYGLKIRgfgKDHIRQRVEEAARILELEPLLKRK----PRELSGGQRQRVA 144
Cdd:PRK11264 78 GLIrqlrqhvGFVFQNFNLFPHRTVLENIIEGPVIV---KGEPKEEATARARELLAKVGLAGKetsyPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 145 MGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQ 224
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
..
gi 742395038 225 RP 226
Cdd:PRK11264 234 DP 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-212 |
3.24e-39 |
|
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: 138.65 E-value: 3.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQID---LDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDlEPKD--RGI 78
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDgvsFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEarRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 742395038 159 DEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGV 212
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-251 |
3.80e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 140.25 E-value: 3.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 14 DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVT--DLEPKDRGIAMVFQNyalyPH- 90
Cdd:PRK13650 17 DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeeNVWDIRHKIGMVFQN----PDn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 91 ----MSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
Cdd:PRK13650 93 qfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 167 AKLRVQMRLELQQLHRRLKTTSLYVTHDqVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGfIGSPAMNLLPGT 246
Cdd:PRK13650 173 PEGRLELIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQLG-LDIPFTTSLVQS 250
|
....*
gi 742395038 247 LSADG 251
Cdd:PRK13650 251 LRQNG 255
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-198 |
4.32e-39 |
|
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: 137.61 E-value: 4.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG-IAMVF 82
Cdd:COG4133 3 LEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYPHMSVYDNMAYGLKIRGFGKDhiRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 742395038 163 SNLDAklrvQMRLELQQL---HRRLKTTSLYVTHDQVEA 198
Cdd:COG4133 160 TALDA----AGVALLAELiaaHLARGGAVLLTTHQPLEL 194
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-212 |
9.18e-38 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 134.58 E-value: 9.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDlepKDRGIAMVFQNYAL- 87
Cdd:cd03235 5 LTVSYGGH-PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKRIGYVPQRRSId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 88 --YPhMSVYDNMAYGL-----KIRGFGKDHiRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:cd03235 81 rdFP-ISVRDVVLMGLyghkgLFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 742395038 161 PLSNLDAKLRVQ-MRLeLQQLHRRLKTTsLYVTHDQVEAMTLAQRVIVMNKGV 212
Cdd:cd03235 159 PFAGVDPKTQEDiYEL-LRELRREGMTI-LVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-208 |
1.28e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.92 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGkTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD---RGIAM 80
Cdd:COG1129 5 LEMRGISKSFGG-VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILE-----LEPllKRKPRELSGGQRQRVAMGRAIVREPAV 155
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLArlgldIDP--DTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 156 FLFDEPLSNLDAKlrvqmrlELQQLH---RRLK---TTSLYVTHDQVEAMTLAQRVIVM 208
Cdd:COG1129 162 LILDEPTASLTER-------EVERLFriiRRLKaqgVAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-211 |
2.52e-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: 133.11 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGIAMVFQ 83
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGFGKdhirQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 742395038 164 NLDAKLRVQMRlELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd03268 156 GLDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-211 |
4.10e-37 |
|
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: 131.79 E-value: 4.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 5 KLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRgiamvfqn 84
Cdd:cd03214 1 EVENLSVGYGGRT-VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 85 yalyphmsvydnmaygLKIRGFgkdhirqrVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
Cdd:cd03214 72 ----------------ARKIAY--------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 742395038 165 LDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd03214 128 LDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDG 174
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-213 |
5.22e-37 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 132.40 E-value: 5.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLE-------PKDR 76
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 77 GiamvfqnyaLYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVF 156
Cdd:cd03269 80 G---------LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 157 LFDEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTH--DQVEAMtlAQRVIVMNKGVA 213
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHqmELVEEL--CDRVLLLNKGRA 206
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-226 |
6.74e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 133.62 E-value: 6.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLR-------MVAGLerTTSGDIYIDTRRV----TDLEPKDRGIAMVFQ 83
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGA--RVEGEILLDGEDIydpdVDVVELRRRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPhMSVYDNMAYGLKIRGF-GKDHIRQRVEEAARIL----ELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:COG1117 100 KPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAalwdEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 159 DEPLSNLD--AKLRVqmrlelQQLHRRLKT--TSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:COG1117 179 DEPTSALDpiSTAKI------EELILELKKdyTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-227 |
8.84e-37 |
|
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: 132.80 E-value: 8.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDR---G 77
Cdd:COG0410 1 MPMLEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 IAMVFQNYALYPHMSVYDNMAYGLKIRGfGKDHIRQRVEeaaRILELEPLLKRKPR----ELSGGQRQRVAMGRAIVREP 153
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLE---RVYELFPRLKERRRqragTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 154 AVFLFDEPLSNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVIVMNKG--VAEqiGTPSEVYQRPA 227
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGriVLE--GTAAELLADPE 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-227 |
1.13e-36 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 135.39 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 37 GPSGCGKSTLLRMVAGLERTTSGDIYI------DTRRVTDLEPKDRGIAMVFQNYALYPHMSVYDNMAYGLKirGFGKDH 110
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLngrvlfDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA--KSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 111 IRQRVEeaarILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLY 190
Cdd:PRK11144 109 FDKIVA----LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 742395038 191 VTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPA 227
Cdd:PRK11144 185 VSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-221 |
3.86e-36 |
|
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: 130.57 E-value: 3.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDGKTPViKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI---DTRRvtdlEPKD--RGIAMVFQ 83
Cdd:cd03265 6 LVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghDVVR----EPREvrRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 742395038 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSE 221
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-226 |
4.35e-36 |
|
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: 137.12 E-value: 4.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 21 KQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTtSGDIYIDTRRVTDLEPKD-----RGIAMVFQN-YA-LYPHMSV 93
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 94 YDNMAYGLKIRGFGKDHiRQRVEEAARILE---LEP-LLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKL 169
Cdd:COG4172 382 GQIIAEGLRVHGPGLSA-AERRARVAEALEevgLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742395038 170 RVQMrLEL-QQLHRRLKTTSLYVTHDQ--VEAMtlAQRVIVMNKG-VAEQiGTPSEVYQRP 226
Cdd:COG4172 461 QAQI-LDLlRDLQREHGLAYLFISHDLavVRAL--AHRVMVMKDGkVVEQ-GPTEQVFDAP 517
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
9-211 |
1.77e-35 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 128.86 E-value: 1.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDG-KTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMVFQNY 85
Cdd:cd03245 8 VSFSYPNqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 86 ALYpHMSVYDNMAYGlkiRGFGKDhirQRVEEAARILELEPLLKRKP-----------RELSGGQRQRVAMGRAIVREPA 154
Cdd:cd03245 88 TLF-YGTLRDNITLG---APLADD---ERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 155 VFLFDEPLSNLDAKLRVQMRLELQQLHRrlKTTSLYVTHDQVeAMTLAQRVIVMNKG 211
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSG 214
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-237 |
2.58e-35 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 129.18 E-value: 2.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-------- 75
Cdd:TIGR03005 1 VRFSDVTKRF-GILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpade 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 76 ------RG-IAMVFQNYALYPHMSVYDNMAYG-LKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGR 147
Cdd:TIGR03005 80 khlrqmRNkIGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 148 AIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPA 227
Cdd:TIGR03005 160 ALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPK 239
|
250
....*....|
gi 742395038 228 SLFVAGFIGS 237
Cdd:TIGR03005 240 EERTREFLSK 249
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-211 |
5.83e-35 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 127.68 E-value: 5.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-----RGI 78
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 742395038 159 DEPLSNLDAKLRVQMrLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:PRK10908 162 DEPTGNLDDALSEGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-225 |
6.96e-35 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 127.73 E-value: 6.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVT--DLEPKDRGIAMVFQNYA 86
Cdd:cd03253 6 VTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevTLDSLRRAIGVVPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 87 LYpHMSVYDNMAYGlkirgfGKDHIRQRVEEAARILELEPLLKRKPR-----------ELSGGQRQRVAMGRAIVREPAV 155
Cdd:cd03253 86 LF-NDTIGYNIRYG------RPDATDEEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 156 FLFDEPLSNLDaklrVQMRLELQQLHRRLKT--TSLYVTHDQVEAMTlAQRVIVMNKG-VAEQiGTPSEVYQR 225
Cdd:cd03253 159 LLLDEATSALD----THTEREIQAALRDVSKgrTTIVIAHRLSTIVN-ADKIIVLKDGrIVER-GTHEELLAK 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-229 |
4.29e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.06 E-value: 4.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTP----VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVT------DLEP 73
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 74 KDRGIAMVFQnyalYPHM-----SVYDNMAYGLKIRGFGKDHIRQRVEEAARILEL-EPLLKRKPRELSGGQRQRVAMGR 147
Cdd:PRK13634 83 LRKKVGIVFQ----FPEHqlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 148 AIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPA 227
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
..
gi 742395038 228 SL 229
Cdd:PRK13634 239 EL 240
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-228 |
4.90e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 126.34 E-value: 4.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSY-----DGKTP---VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLE 72
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglSGKHQhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 73 PKD-----RGIAMVFQNY--ALYPHMSVYDNMAYGLK-IRGFGKDHIRQRVEEAARILELEP-LLKRKPRELSGGQRQRV 143
Cdd:PRK10419 81 RAQrkafrRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 144 AMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG--VAEQIGTPSE 221
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGqiVETQPVGDKL 240
|
....*..
gi 742395038 222 VYQRPAS 228
Cdd:PRK10419 241 TFSSPAG 247
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
15-228 |
5.33e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 125.85 E-value: 5.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD---------------RGIA 79
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrllrTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNYALYPHMSVYDN-MAYGLKIRGFGKDHIRQR-VEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFL 157
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERaVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742395038 158 FDEPLSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPAS 228
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEGKTM-VVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-227 |
5.43e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 125.35 E-value: 5.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDR---GIAM 80
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 161 PLSNLDAKlRVQmrlELQQLHRRLKTTSLYV---THDQVEAMTLAQRVIVMNKG--VAEqiGTPSEVYQRPA 227
Cdd:cd03218 160 PFAGVDPI-AVQ---DIQKIIKILKDRGIGVlitDHNVRETLSITDRAYIIYEGkvLAE--GTPEEIAANEL 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-225 |
7.06e-34 |
|
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: 125.04 E-value: 7.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGK-TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAM 80
Cdd:cd03251 1 VEFKNVTFRYPGDgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYpHMSVYDNMAYGLkirgfgKDHIRQRVEEAARILELEPLLKRKPR-----------ELSGGQRQRVAMGRAI 149
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGR------PGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742395038 150 VREPAVFLFDEPLSNLD--AKLRVQMRLELQQLHRrlktTSLYVTHdQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQR 225
Cdd:cd03251 154 LKDPPILILDEATSALDteSERLVQAALERLMKNR----TTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-226 |
8.44e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 125.34 E-value: 8.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 13 YDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGL-----ERTTSGDIYIDTRRV--TDLEPKD--RGIAMVFQ 83
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIysPDVDPIEvrREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPHMSVYDNMAYGLKIRGF--GKDHIRQRVE----EAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFL 157
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEwalkKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 158 FDEPLSNLD----AKLRvQMRLELQQlhrrlKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:PRK14267 173 MDEPTANIDpvgtAKIE-ELLFELKK-----EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-227 |
9.02e-34 |
|
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: 131.04 E-value: 9.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 2 AGLKLQAVTKSYDG-KTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGI 78
Cdd:COG4987 332 PSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYpHMSVYDNmaygLKIrgfGKDHI-RQRVEEAARILELEPLLKRKP-----------RELSGGQRQRVAMG 146
Cdd:COG4987 412 AVVPQRPHLF-DTTLREN----LRL---ARPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 147 RAIVREPAVFLFDEPLSNLDAKLRVQMrleLQQLHRRLKT-TSLYVTHDQVeAMTLAQRVIVMNKGVAEQIGTPSEVYQR 225
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALAGrTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
..
gi 742395038 226 PA 227
Cdd:COG4987 560 NG 561
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-211 |
1.28e-33 |
|
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: 123.46 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGeFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG-IAMVF 82
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 742395038 163 SNLDAKLRVQMRLELQQLHRrlKTTSLYVTH--DQVEAMtlAQRVIVMNKG 211
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGE--DRIVILSTHivEDVESL--CNQVAVLNKG 205
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-226 |
1.62e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 126.74 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 20 IKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDR-----GIAMVFQN--YALYPHMS 92
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 93 VYDNMAYGLKIR--GFGKDHIRQRVEE-AARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKL 169
Cdd:PRK15079 117 IGEIIAEPLRTYhpKLSRQEVKDRVKAmMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 170 RVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:PRK15079 197 QAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-211 |
2.37e-33 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 121.38 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD---RGIAM 80
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQnyalyphmsvydnmayglkirgfgkdhirqrveeaarilelepllkrkpreLSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 161 PLSNLDAKlrvqmrlELQQLH---RRLK---TTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd03216 109 PTAALTPA-------EVERLFkviRRLRaqgVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-226 |
4.48e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 123.27 E-value: 4.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 5 KLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMVF 82
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYPHMSVYDNMAYGL----KIRGFGKDHirQRVEEAARILELEPLLKRKPRELSGGQRQR--VAMgrAIVREPAVF 156
Cdd:COG4604 82 QENHINSRLTVRELVAFGRfpysKGRLTAEDR--EIIDEAIAYLDLEDLADRYLDELSGGQRQRafIAM--VLAQDTDYV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742395038 157 LFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG-VAEQiGTPSEVYQRP 226
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGrVVAQ-GTPEEIITPE 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-228 |
8.53e-33 |
|
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: 122.99 E-value: 8.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-----RGIAMVFQNY--AL 87
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQDSpsAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 88 YPHMSVYDNMAYGLK-IRGFGKDHIRQRVEEAARILELEP-LLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
Cdd:TIGR02769 102 NPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 166 DAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG--VAEQIGTPSEVYQRPAS 228
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGqiVEECDVAQLLSFKHPAG 246
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-211 |
1.67e-32 |
|
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: 120.44 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRrvtDLEPKDR--GIAMVFQN-- 84
Cdd:cd03226 5 ISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERrkSIGYVMQDvd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 85 YALYPHmSVYDNMAYGLKIRGFGKdhirQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
Cdd:cd03226 82 YQLFTD-SVREELLLGLKELDAGN----EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 742395038 165 LDAKlrvQMRlELQQLHRRL---KTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd03226 157 LDYK---NME-RVGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-211 |
1.68e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 122.12 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTP----VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG-- 77
Cdd:COG1101 2 LELKNLSKTFNPGTVnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 IAMVFQNYAL--YPHMSVYDNMAYGL---KIRGFGKDHIRQRVEEAARILE-----LEPLLKRKPRELSGGQRQRVAMGR 147
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLALAYrrgKRRGLRRGLTKKRRELFRELLAtlglgLENRLDTKVGLLSGGQRQALSLLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 148 AIVREPAVFLFDEPLSNLDAKlRVQMRLEL-QQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-225 |
2.42e-32 |
|
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: 120.79 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMVFQNYA 86
Cdd:cd03254 8 VNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 87 LYPHmSVYDNMAYGlkirgfGKDHIRQRVEEAARILELEPLLKRKPR-----------ELSGGQRQRVAMGRAIVREPAV 155
Cdd:cd03254 88 LFSG-TIMENIRLG------RPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 156 FLFDEPLSNLDaklrVQMRLELQQLHRRL--KTTSLYVTHdQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQR 225
Cdd:cd03254 161 LILDEATSNID----TETEKLIQEALEKLmkGRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-227 |
7.45e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 120.86 E-value: 7.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIY---IDTRRVTDLEPKDRGIAM 80
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQN-YALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742395038 160 EPLSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHDqVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPA 227
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTI-VYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-211 |
1.13e-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: 119.42 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSG-DIYI-DTRR----VTDLEPKdrg 77
Cdd:COG1119 4 LELRNVTVRRGGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfGERRggedVWELRKR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 IAMV---FQNYaLYPHMSVYDNMAYGLkirgFG--------KDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMG 146
Cdd:COG1119 80 IGLVspaLQLR-FPRDETVLDVVLSGF----FDsiglyrepTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742395038 147 RAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTH---DQVEAMTlaqRVIVMNKG 211
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhveEIPPGIT---HVLLLKDG 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-211 |
1.40e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 124.37 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGktpVI--KQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD---RGI 78
Cdd:COG3845 6 LELRGITKRFGG---VVanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYPHMSVYDNMAYGLKIRGFG---KDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAV 155
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGLEPTKGGrldRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 156 FLFDEPLSNLDAklrvQMRLELQQLHRRLK---TTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:COG3845 163 LILDEPTAVLTP----QEADELFEILRRLAaegKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-211 |
1.98e-31 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 118.59 E-value: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 18 PVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIyidtrRVTDLEPKDRG------IAMVF-QNYALYPH 90
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-----RVAGLVPWKRRkkflrrIGVVFgQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 91 MSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR 170
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 742395038 171 VQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
6-211 |
4.36e-31 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 124.21 E-value: 4.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 6 LQAVTKSYDG-KTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMVF 82
Cdd:TIGR03375 466 FRNVSFAYPGqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVP 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYpHMSVYDNMAYGlkiRGFGKDhirQRVEEAARILELEPLLKRKP-----------RELSGGQRQRVAMGRAIVR 151
Cdd:TIGR03375 546 QDPRLF-YGTLRDNIALG---APYADD---EEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLR 618
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 152 EPAVFLFDEPLSNLDaklrvqMRLElQQLHRRLK-----TTSLYVTHdQVEAMTLAQRVIVMNKG 211
Cdd:TIGR03375 619 DPPILLLDEPTSAMD------NRSE-ERFKDRLKrwlagKTLVLVTH-RTSLLDLVDRIIVMDNG 675
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-226 |
5.26e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 117.44 E-value: 5.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYdGKTPVIKQIDLDVADGEfIV-MVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLePKDR--- 76
Cdd:COG1137 1 MMTLEAENLVKSY-GKRTVVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-PMHKrar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 77 -GI------AMVFQNyalyphMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAI 149
Cdd:COG1137 78 lGIgylpqeASIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 150 VREPAVFLFDEPLSNLDAkLRVQmrlELQQLHRRLKTTSLYV--T-HDQVEAMTLAQRVIVMNKG--VAEqiGTPSEVYQ 224
Cdd:COG1137 152 ATNPKFILLDEPFAGVDP-IAVA---DIQKIIRHLKERGIGVliTdHNVRETLGICDRAYIISEGkvLAE--GTPEEILN 225
|
..
gi 742395038 225 RP 226
Cdd:COG1137 226 NP 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-205 |
5.51e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 117.22 E-value: 5.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 17 TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDL------EPKDRGIAMVFQNYALYPH 90
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaELRNQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 91 MSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR 170
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190
....*....|....*....|....*....|....*
gi 742395038 171 VQMRLELQQLHRRLKTTSLYVTHDqveaMTLAQRV 205
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVTHD----LQLAKRM 212
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-225 |
2.24e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 117.13 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLE-------PKDR 76
Cdd:COG4152 2 LELKGLTKRFGDKT-AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 77 GiamvfqnyaLYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVF 156
Cdd:COG4152 81 G---------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 157 LFDEPLSNLD---AKLrvqMRLELQQLHRRlKTTSLYVTH--DQVEAmtLAQRVIVMNKG--VAEqiGTPSEVYQR 225
Cdd:COG4152 152 ILDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHqmELVEE--LCDRIVIINKGrkVLS--GSVDEIRRQ 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-222 |
3.03e-30 |
|
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: 120.68 E-value: 3.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY----DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI----DTRRVTDLEPKD 75
Cdd:TIGR03269 280 IKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 76 RG-----IAMVFQNYALYPHMSVYDNMA-----------------YGLKIRGFGKdhirqrvEEAARILElepllkRKPR 133
Cdd:TIGR03269 360 RGrakryIGILHQEYDLYPHRTVLDNLTeaiglelpdelarmkavITLKMVGFDE-------EKAEEILD------KYPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 134 ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVA 213
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
....*....
gi 742395038 214 EQIGTPSEV 222
Cdd:TIGR03269 507 VKIGDPEEI 515
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-227 |
4.30e-30 |
|
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: 120.17 E-value: 4.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 14 DGKTPVIKQIDLDVADGEFIVMVGPSGCGKS----TLLRMVAGLERTTSGDIYIDTRRVTDLEPKD----RG--IAMVFQ 83
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrriRGnrIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 N--YALYPHMSVYDNMAYGLKI-RGFGKDHIRQRVEEA---ARILELEPLLKRKPRELSGGQRQRV--AMgrAIVREPAV 155
Cdd:COG4172 100 EpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELlerVGIPDPERRLDAYPHQLSGGQRQRVmiAM--ALANEPDL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 156 FLFDEPLSNLDAKLRVQMrLEL-QQLHRRLKTTSLYVTHDQ--VEAMtlAQRVIVMNKG-VAEQiGTPSEVYQRPA 227
Cdd:COG4172 178 LIADEPTTALDVTVQAQI-LDLlKDLQRELGMALLLITHDLgvVRRF--ADRVAVMRQGeIVEQ-GPTAELFAAPQ 249
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-223 |
5.31e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.96 E-value: 5.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 17 TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEP--KDRGIA-MVFQNyalyPHMS- 92
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAgMVFQN----PDNQi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 93 ----VYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
Cdd:PRK13633 99 vatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 169 LRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTlAQRVIVMNKGVAEQIGTPSEVY 223
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-208 |
1.16e-29 |
|
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: 118.93 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMV 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNYALYPHmSVYDNMAYGlkiRGFGKDHIRQRVEEAARILELEP--------LLKRKPRELSGGQRQRVAMGRAIVREP 153
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLA---RPDASDAEIREALERAGLDEFVAalpqgldtPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 154 AVFLFDEPLSNLDAKLRVQMRLELQQLHRRlkTTSLYVTHDqVEAMTLAQRVIVM 208
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHR-LALAALADRIVVL 529
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-226 |
1.36e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 114.24 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGL-----ERTTSGDIYIDTRRV--TDLEPKDRGIAMVFQNYAL 87
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfkMDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 88 YPHMSVYDNMAYGLKIRGFGK------DHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
Cdd:PRK14247 94 IPNLSIFENVALGLKLNRLVKskkelqERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 162 LSNLD----AKLRVQMrLELQQlhrrlKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:PRK14247 174 TANLDpentAKIESLF-LELKK-----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-213 |
1.76e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 111.54 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY-DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG--IAM 80
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHmSVYDNMayglkirgfgkdhirqrveeaarilelepllkrkpreLSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 161 PLSNLDaklrVQMRLELQQLHRRLK---TTSLYVTHdQVEAMTLAQRVIVMNKGVA 213
Cdd:cd03246 123 PNSHLD----VEGERALNQAIAALKaagATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-225 |
7.61e-29 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 111.48 E-value: 7.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 18 PVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMvagLER---TTSGDIYIDTRRVTDLEPKD--RGIAMVFQNYALYPhMS 92
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSL---LERfydPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 93 VYDNMAYGLKirgfgkDHIRQRVEEAARILELEPLLKRKPR-----------ELSGGQRQRVAMGRAIVREPAVFLFDEP 161
Cdd:cd03249 93 IAENIRYGKP------DATDEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 162 LSNLDAK--LRVQMRLElqqlHRRLKTTSLYVTHdQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQR 225
Cdd:cd03249 167 TSALDAEseKLVQEALD----RAMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-224 |
2.49e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 111.75 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQ----IDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI------DTRRVTDLEP 73
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRalfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 74 KDRGIAMVFQnyalYPHMSVYDNMAygLKIRGFGKDHIRQRVEEAARI----LELEPLLK----RKPRELSGGQRQRVAM 145
Cdd:PRK13643 82 VRKKVGVVFQ----FPESQLFEETV--LKDVAFGPQNFGIPKEKAEKIaaekLEMVGLADefweKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 146 GRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLyVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQ 224
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVL-VTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-211 |
2.79e-28 |
|
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: 109.92 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDR---GIAM 80
Cdd:TIGR03410 1 LEVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSVYDNMAYGLKIRGFGKDHIrqrveeAARILELEPLLK----RKPRELSGGQRQRVAMGRAIVREPAVF 156
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGLAALPRRSRKI------PDEIYELFPVLKemlgRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 157 LFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERG 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-208 |
5.55e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.03 E-value: 5.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMVFQNYALYPHmS 92
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 93 VYDNMAYGLKIRGfgkdhirQRVEEAARILEL------EPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
Cdd:PRK10247 97 VYDNLIFPWQIRN-------QQPDPAIFLDDLerfalpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 742395038 167 AKLRVQMRLELQQLHRRLKTTSLYVTHDQVEaMTLAQRVIVM 208
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-223 |
6.80e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.18 E-value: 6.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPV--IKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVT--DLEPKDRGIA 79
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNY-ALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 159 DEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTlAQRVIVMNKGVAEQIGTPSEVY 223
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-229 |
9.04e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.46 E-value: 9.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTP-VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAM 80
Cdd:PRK13648 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQN--YALYPHMSVYDnMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:PRK13648 88 VFQNpdNQFVGSIVKYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 159 DEPLSNLDAklrvQMRLELQQLHRRLKT----TSLYVTHDQVEAMTlAQRVIVMNKGVAEQIGTPSEVYQRPASL 229
Cdd:PRK13648 167 DEATSMLDP----DARQNLLDLVRKVKSehniTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-224 |
9.52e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 109.33 E-value: 9.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMV 81
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNYALYPHMSVYDNMAYG----LKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFL 157
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 158 FDEPLSNLDAKLRVqmrlELQQLHRRLKT---TSLYVTHDQVEAMTLAQRVIVMNKG--VAEqiGTPSEVYQ 224
Cdd:PRK11231 162 LDEPTTYLDINHQV----ELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANGhvMAQ--GTPEEVMT 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-199 |
1.21e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.93 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 12 SYDGkTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGdiyidTRRVTDlepkDRGIAMVFQNYALYPHM 91
Cdd:NF040873 1 GYGG-RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG-----TVRRAG----GARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 92 --SVYDNMAYGL-KIRGFGKDHI---RQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
Cdd:NF040873 71 plTVRDLVAMGRwARRGLWRRLTrddRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|....
gi 742395038 166 DAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAM 199
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-205 |
1.24e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 109.10 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 13 YDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLR-------MVAGLErtTSGDIYIDTRRV--TDLEPKD--RGIAMV 81
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLyaPDVDPVEvrRRIGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNYALYPHmSVYDNMAYGLKIRGFgKDHIRQRVEEAARILELEPLLKRKPRE----LSGGQRQRVAMGRAIVREPAVFL 157
Cdd:PRK14243 97 FQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 742395038 158 FDEPLSNLD--AKLRVQmrlEL-QQLHRRLktTSLYVTHDqveaMTLAQRV 205
Cdd:PRK14243 175 MDEPCSALDpiSTLRIE---ELmHELKEQY--TIIIVTHN----MQQAARV 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.49e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 109.12 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVT--DLEPKDRGI 78
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQN---YALYPhmSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAV 155
Cdd:PRK13652 81 GLVFQNpddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742395038 156 FLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-222 |
3.09e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.94 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMVFQNYALYPHMS 92
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 93 VYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVR------EPAVFLFDEPLSNLD 166
Cdd:PRK13548 93 VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742395038 167 akLRVQ---MRLeLQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG--VAEqiGTPSEV 222
Cdd:PRK13548 173 --LAHQhhvLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGrlVAD--GTPAEV 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-194 |
3.50e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 107.82 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLL----RM--------VAGLERTTSGDIYidTRRV 68
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnRMnelesevrVEGRVEFFNQNIY--ERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 69 tDLEPKDRGIAMVFQNYALYPhMSVYDNMAYGLKIRGF-GKDHIRQRVEEAARILELEPLLKRK----PRELSGGQRQRV 143
Cdd:PRK14258 82 -NLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 742395038 144 AMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHD 194
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
36-226 |
3.51e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 109.28 E-value: 3.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 36 VGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-----RGIAMVFQN-YA-LYPHMSVYDNMAYGLKIR-GFG 107
Cdd:PRK11308 47 VGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNPRKKVGQILEEPLLINtSLS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 108 KDHIRQRVEEAARILELEP-LLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKT 186
Cdd:PRK11308 127 AAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGL 206
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 742395038 187 TSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:PRK11308 207 SYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-227 |
6.27e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.78 E-value: 6.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 13 YDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGL-----ERTTSGDIYIDTRRV----TDLEPKDRGIAMVFQ 83
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYALYPhMSVYDNMAYGLKIRGFGKDHIRQRVEE----AARIL-ELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:PRK14239 94 QPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEkslkGASIWdEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 159 DEPLSNLDAKLRVQMRLELQQLhrRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPA 227
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3-225 |
7.77e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.52 E-value: 7.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 3 GLKLQAVTKSYDGKTP----VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVT------DLE 72
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 73 PKDRGIAMVFQnyalYPHMSVYD-----NMAYGLKIRGFGKDHIRQRVEEAARILEL-EPLLKRKPRELSGGQRQRVAMG 146
Cdd:PRK13649 82 QIRKKVGLVFQ----FPESQLFEetvlkDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 147 RAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLyVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQR 225
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVL-VTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
12-226 |
9.51e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.09 E-value: 9.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 12 SYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRV----TDLEPKDRGIAMVFQN--- 84
Cdd:PRK13639 10 SYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkKSLLEVRKTVGIVFQNpdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 85 --YAlyPhmSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:PRK13639 90 qlFA--P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 163 SNLDAKLRVQ-MRLeLQQLHRRlKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:PRK13639 166 SGLDPMGASQiMKL-LYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-222 |
2.43e-26 |
|
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: 109.74 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG--IAMVFQNYALYPHmS 92
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 93 VYDNMAYglkirgFGKDHIRQRVEEAARILELEPLLKRKPR-----------ELSGGQRQRVAMGRAIVREPAVFLFDEP 161
Cdd:TIGR01842 408 VAENIAR------FGENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742395038 162 LSNLDAKLRVQMRLELQQLHRRlKTTSLYVTHdQVEAMTLAQRVIVMNKGVAEQIGTPSEV 222
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-234 |
2.73e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 109.81 E-value: 2.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 2 AGLKLQAVTKSY---DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGI 78
Cdd:PRK10535 3 ALLELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 ------AMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVRE 152
Cdd:PRK10535 83 lrrehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 153 PAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHD-QVEAMtlAQRVIVMNKG----------VAEQIGTPSE 221
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTV-IIVTHDpQVAAQ--AERVIEIRDGeivrnppaqeKVNVAGGTEP 239
|
250
....*....|....*
gi 742395038 222 VYQRPASL--FVAGF 234
Cdd:PRK10535 240 VVNTASGWrqFVSGF 254
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-226 |
3.59e-26 |
|
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: 109.66 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 3 GLKLQAVTKSYDGKTPVI-KQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIA 79
Cdd:TIGR03797 451 AIEVDRVTFRYRPDGPLIlDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAvrRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNYALYPHmSVYDNMAYGLKIRgfgkdhiRQRVEEAARILELEPLLKRKP-----------RELSGGQRQRVAMGRA 148
Cdd:TIGR03797 531 VVLQNGRLMSG-SIFENIAGGAPLT-------LDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARA 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 149 IVREPAVFLFDEPLSNLDAKLR--VQMRLElqqlhrRLKTTSLYVTHDQVEAMTlAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDNRTQaiVSESLE------RLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-223 |
6.93e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.09 E-value: 6.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 6 LQAVTKSYDGKTP----VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGL-----ERTTSGDIYI--DTRRVTDLEPK 74
Cdd:PRK13645 9 LDNVSYTYAKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIpaNLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 75 DRGIAMVFQ--NYALYPHmSVYDNMAYGLKIRGFGKDHIRQRVEEAARILEL-EPLLKRKPRELSGGQRQRVAMGRAIVR 151
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 152 EPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVY 223
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-211 |
7.13e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.55 E-value: 7.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 20 IKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIyidtrRVTDLEP-KDR-----GIAMVF-QNYALYPHMS 92
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV-----RVLGYVPfKRRkefarRIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 93 VYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQR--VAMgrAIVREPAVFLFDEPLSNLDAKLR 170
Cdd:COG4586 113 AIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRceLAA--ALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 742395038 171 VQMRLELQQLHRRLKTTSLYVTHD--QVEAmtLAQRVIVMNKG 211
Cdd:COG4586 191 EAIREFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHG 231
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-207 |
7.57e-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: 104.03 E-value: 7.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 26 DVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDtrrVTDLEPKDRGIAMVFQnyalyphMSVYDNMAYglKIRG 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE---LDTVSYKPQYIKADYE-------GTVRDLLSS--ITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 106 FGKDHirQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrVQMRLELQQLHRRL- 184
Cdd:cd03237 89 FYTHP--YFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD----VEQRLMASKVIRRFa 162
|
170 180
....*....|....*....|....*.
gi 742395038 185 ---KTTSLYVTHDQVEAMTLAQRVIV 207
Cdd:cd03237 163 ennEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
8.64e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.54 E-value: 8.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVtDLEPKD-----RGI 78
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGlmklrESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQ--NYALYPhMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVF 156
Cdd:PRK13636 85 GMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 157 LFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVY 223
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-225 |
1.05e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.24 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 6 LQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEpkdrgIAMVFQny 85
Cdd:COG1134 28 LLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLE-----LGAGFH-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 86 alyPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
Cdd:COG1134 101 ---PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVG 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742395038 166 DA--KLRVQMRLElqQLHRRLKTTsLYVTHD--QVEamTLAQRVIVMNKGVAEQIGTPSEVYQR 225
Cdd:COG1134 178 DAafQKKCLARIR--ELRESGRTV-IFVSHSmgAVR--RLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-211 |
1.15e-25 |
|
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: 102.90 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY-----DGKT-PVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTR-RVTDL---EP 73
Cdd:COG4778 5 LEVENLSKTFtlhlqGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDgGWVDLaqaSP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 74 KD------RGIAMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILEL-EPLLKRKPRELSGGQRQRVAMG 146
Cdd:COG4778 85 REilalrrRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 147 RAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQvEAM-TLAQRVIVMNKG 211
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDE-EVReAVADRVVDVTPF 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
13-220 |
2.08e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 103.28 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 13 YDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-RG-IAMVFQNyalyPH 90
Cdd:PRK13647 14 YKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSkVGLVFQD----PD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 91 -----MSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
Cdd:PRK13647 90 dqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 166 DAKLRVQMRLELQQLHRRLKTTsLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPS 220
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTV-IVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-226 |
2.11e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 103.31 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRV-----TDLEPKDRGIAMVFQNYALYP 89
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 90 HMSVYDNMAYGLkirgfgKDHIR--QRVEEAARILELEPLLKR-----KPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:PRK11831 98 DMNVFDNVAYPL------REHTQlpAPLLHSTVMMKLEAVGLRgaaklMPSELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 163 SNLDA-KLRVQMRLeLQQLHRRLKTTSLYVTHDQVEAMTLAQRV-IVMNKGVAEQiGTPSEVYQRP 226
Cdd:PRK11831 172 VGQDPiTMGVLVKL-ISELNSALGVTCVVVSHDVPEVLSIADHAyIVADKKIVAH-GSAQALQANP 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-222 |
2.67e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 102.28 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDL---EPKDRG 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 IAMVFQNYALYPHMSVYDNMAYGLKIR-GFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVF 156
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 157 LFDEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEV 222
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-228 |
2.99e-25 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 101.68 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 23 IDLDVADGEFIVMVGPSGCGKSTLLRMVAGL----ERTTSGDIYIDTRRVTDLEPKDRGIAMVFQN--YALYPHMSVYDN 96
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGNH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 97 MAYGLKIRGFGKDHIRQRVEEAARILEL---EPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQM 173
Cdd:TIGR02770 85 AIETLRSLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 174 RLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPAS 228
Cdd:TIGR02770 165 LKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-226 |
3.83e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 102.12 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMVFQNYALYPHMS 92
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLAFPFT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 93 VYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAI------VREPAVFLF-DEPLSNL 165
Cdd:COG4559 92 VEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPRWLFlDEPTSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742395038 166 DakLRVQ---MRLeLQQLHRRlKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:COG4559 172 D--LAHQhavLRL-ARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-217 |
4.27e-25 |
|
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: 101.07 E-value: 4.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 14 DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDtRRVTdlepkdrgiAMVFQNYALYPHMSV 93
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR-GRVS---------SLLGLGGGFNPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 94 YDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQM 173
Cdd:cd03220 102 RENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 742395038 174 RLELQQLHRRLKtTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIG 217
Cdd:cd03220 182 QRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-167 |
4.76e-25 |
|
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: 100.32 E-value: 4.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 11 KSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERT--TSGDIYIDTRRVTDLEPKDRgIAMVFQNYALY 88
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKI-IGYVPQDDILH 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 89 PHMSVYDNMAYGLKIRGfgkdhirqrveeaarilelepllkrkpreLSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
Cdd:cd03213 95 PTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-211 |
5.83e-25 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 101.01 E-value: 5.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGK--TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPK--DRGIA 79
Cdd:cd03248 12 VKFQNVTFAYPTRpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNYALYPHmSVYDNMAYGLKIRGFGkdhirqRVEEAAR-------ILELE----PLLKRKPRELSGGQRQRVAMGRA 148
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYGLQSCSFE------CVKEAAQkahahsfISELAsgydTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 149 IVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRlkTTSLYVTHdQVEAMTLAQRVIVMNKG 211
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGG 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-225 |
7.24e-25 |
|
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: 105.57 E-value: 7.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKT-PVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAM 80
Cdd:TIGR02203 331 VEFRNVTFRYPGRDrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHmSVYDNMAYGLkirgfGKDHIRQRVEEAARILELEPLLKRKPR-----------ELSGGQRQRVAMGRAI 149
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGR-----TEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 150 VREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRrlKTTSLYVTHdQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQR 225
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-194 |
9.85e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 100.24 E-value: 9.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 23 IDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG------IAMVFQNYALYPHMSVYDN 96
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 97 MAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLE 176
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170
....*....|....*...
gi 742395038 177 LQQLHRRLKTTSLYVTHD 194
Cdd:PRK10584 189 LFSLNREHGTTLILVTHD 206
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-235 |
1.27e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.89 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 13 YDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRV--------TDLEPKDRGIAMVFQN 84
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifqIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 85 YALYPHMSVYDNMAYGLKIRGFG-KDHIRQRVEEAARIL----ELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742395038 160 EPLSNLDaklrVQMRLELQQLHRRLKT--TSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGFI 235
Cdd:PRK14246 179 EPTSMID----IVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-225 |
1.41e-24 |
|
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: 104.44 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG--IAMVFQNYALYPHmS 92
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 93 VYDNMAyglkirGFGkDHIRQRVEEAAR-------ILEL----EPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
Cdd:COG4618 422 IAENIA------RFG-DADPEKVVAAAKlagvhemILRLpdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742395038 162 LSNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQvEAMTLAQRVIVMNKGVAEQIGTPSEVYQR 225
Cdd:COG4618 495 NSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-265 |
2.63e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.67 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQ----IDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVT------DLEP 73
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKgldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 74 KDRGIAMVFQnyalYPHMSVYDN-----MAYGLKIRGFGKDHIRQRVEEAARILEL-EPLLKRKPRELSGGQRQRVAMGR 147
Cdd:PRK13641 83 LRKKVSLVFQ----FPEAQLFENtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 148 AIVREPAVFLFDEPLSNLDAKLRVQMrLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPA 227
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 742395038 228 SLfVAGFIGSPAMNLLPGTLSADGGQLLladGMALPLP 265
Cdd:PRK13641 238 WL-KKHYLDEPATSRFASKLEKGGFKFS---EMPLTID 271
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
9-233 |
3.89e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSY-DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGL--------ERTTSGDIYIDTRRVTDLEPKdrgIA 79
Cdd:PRK13640 11 VSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWDIREK---VG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNyalyPH-----MSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPA 154
Cdd:PRK13640 88 IVFQN----PDnqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 155 VFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAmTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAG 233
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIG 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-226 |
5.70e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 103.01 E-value: 5.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 20 IKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRV-----TDLEPKDRGIAMVFQN-YA-LYPHMS 92
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspGKLQALRRDIQFIFQDpYAsLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 93 VYDNMAYGLKIRGFGK-DHIRQRVEEAARILELEPLLK-RKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR 170
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 171 VQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-225 |
6.57e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 102.57 E-value: 6.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLE--RTTSGDI-----------YID------ 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgYVErpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 65 ----------TRRVTDLEPKD--------RGIAMVFQ-NYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELE 125
Cdd:TIGR03269 80 epcpvcggtlEPEEVDFWNLSdklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 126 PLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD---AKLRVQMRLELQqlhrRLKTTSLYVTHDQVEAMT-L 201
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHNALEEAV----KASGISMVLTSHWPEVIEdL 235
|
250 260
....*....|....*....|....
gi 742395038 202 AQRVIVMNKGVAEQIGTPSEVYQR 225
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-194 |
6.77e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 6.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 6 LQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIdtrrvtdlePKDRGIAMVFQNY 85
Cdd:COG0488 1 LENLSKSFGGR-PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 86 ALYPHMSVYDNMAYGLKIRG---------------FGKDHIRQ-RVEE-------------AARILE----LEPLLKRKP 132
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAELRaleaeleeleaklaePDEDLERLaELQEefealggweaearAEEILSglgfPEEDLDRPV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 133 RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAklrvQMRLELQQLHRRLKTTSLYVTHD 194
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEFLKNYPGTVLVVSHD 208
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-211 |
1.30e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 99.00 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTP----VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDI------------------ 61
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 62 YIDT--------RRVTDLEPKDRGIAMVFQ--NYALYpHMSVYDNMAYGLKIRGFGKDHIRQRveeAARILEL----EPL 127
Cdd:PRK13651 83 VLEKlviqktrfKKIKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKR---AAKYIELvgldESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 128 LKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLyVTHDQVEAMTLAQRVIV 207
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIIL-VTHDLDNVLEWTKRTIF 237
|
....
gi 742395038 208 MNKG 211
Cdd:PRK13651 238 FKDG 241
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-227 |
1.80e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.15 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTP----VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI---------------- 63
Cdd:PRK13631 22 LRVKNLYCVFDEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 64 --DTRRVTDLEPKDRGIAMVFQ--NYALYPHmSVYDNMAYGLKIRGFGKDHIRQRveeAARILEL----EPLLKRKPREL 135
Cdd:PRK13631 102 npYSKKIKNFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKL---AKFYLNKmgldDSYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 136 SGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMrLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQ 215
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|..
gi 742395038 216 IGTPSEVYQRPA 227
Cdd:PRK13631 257 TGTPYEIFTDQH 268
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-226 |
3.12e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.95 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGK--TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPK--DRGIA 79
Cdd:TIGR00958 479 IEFQDVSFSYPNRpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNYALYPHmSVYDNMAYGLkiRGFGKDHIRQRVEEAAR---ILELE----PLLKRKPRELSGGQRQRVAMGRAIVRE 152
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGL--TDTPDEEIMAAAKAANAhdfIMEFPngydTEVGEKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742395038 153 PAVFLFDEPLSNLDAklrvQMRLELQQLHRRLKTTSLYVTHdQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:TIGR00958 636 PRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-225 |
4.08e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.16 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 19 VIKQIDLDVADGEFIVMVGPSGCGKST----LLRMVAglertTSGDIYIDTRRVTDLEPKD-----RGIAMVFQ--NYAL 87
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 88 YPHMSVYDNMAYGLKI--RGFGKDHIRQRVEEAARILELEPLLK-RKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742395038 165 LDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG-VAEQ------IGTPSEVYQR 225
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGeVVEQgdcervFAAPQQEYTR 523
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-211 |
5.46e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 95.42 E-value: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 19 VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLER---TTSGDIYIDTRRVTDLEPKDRgIAMVFQNYALYPHMSVYD 95
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 96 NMAYGLKIRG--FGKDHIRQRVEEAARILEL--EPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRV 171
Cdd:cd03234 101 TLTYTAILRLprKSSDAIRKKRVEDVLLRDLalTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 742395038 172 QMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSG 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-211 |
5.77e-23 |
|
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: 94.84 E-value: 5.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 17 TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRrvtdlepkdrgIAMVFQNyALYPHMSVYDN 96
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQE-PWIQNGTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 97 MAyglkirgFGKDHIRQRVEEAARILELEPLLKRKPR-------E----LSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
Cdd:cd03250 86 IL-------FGKPFDEERYEKVIKACALEPDLEILPDgdlteigEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 742395038 166 DAKLRVQ-MRLELQQLHRRLKTTSLyVTHdQVEAMTLAQRVIVMNKG 211
Cdd:cd03250 159 DAHVGRHiFENCILGLLLNNKTRIL-VTH-QLQLLPHADQIVVLDNG 203
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-245 |
6.36e-23 |
|
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: 95.30 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 25 LDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRrvtDLEPKDRGIAMVFQNYAL---YPhMSVYDNMAYGL 101
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 102 K-----IRGFGKDHIRQrVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMrLE 176
Cdd:TIGR03771 77 TghigwLRRPCVADFAA-VRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL-TE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 177 LQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQiGTPSEVyqRPASLFVAGFIGSPAMNLLPG 245
Cdd:TIGR03771 155 LFIELAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIAD-GTPQQL--QDPAPWMTTFGVSDSSPLLRI 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
15-249 |
1.42e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.60 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMVFQNYAL----- 87
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVPQDTSLsfefd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 88 ---------YPHMSVYDNMAyglkirgfgkDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:PRK09536 94 vrqvvemgrTPHRSRFDTWT----------ETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 159 DEPLSNLDAKLRVQMrLELQQLHRRLKTTSLYVTHDqveaMTLAQR----VIVMNKGVAEQIGTPSEVYQRPAslFVAGF 234
Cdd:PRK09536 164 DEPTASLDINHQVRT-LELVRRLVDDGKTAVAAIHD----LDLAARycdeLVLLADGRVRAAGPPADVLTADT--LRAAF 236
|
250
....*....|....*
gi 742395038 235 IGSPAMNLLPGTLSA 249
Cdd:PRK09536 237 DARTAVGTDPATGAP 251
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-218 |
2.60e-22 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 97.97 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 2 AGLKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIA 79
Cdd:COG5265 356 GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNYALYpHMSVYDNMAYGlkiRgfgKDHIRQRVEEAARILELEPLLKRKPR-----------ELSGGQRQRVAMGRA 148
Cdd:COG5265 436 IVPQDTVLF-NDTIAYNIAYG---R---PDASEEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIART 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 149 IVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRlkTTSLYVTH------DqveamtlAQRVIVMNKG-VAEQiGT 218
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVARG--RTTLVIAHrlstivD-------ADEILVLEAGrIVER-GT 575
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-211 |
3.05e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.98 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLE--RTTSGDIYIDTRRVTDLEPKDR---GI 78
Cdd:COG0396 1 LEIKNLHVSVEGK-EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYPHMSVYD--NMAYGlKIRGFGKDHI--RQRVEEAARILELEP-LLKRKPRE-LSGGQRQRVAMGRAIVRE 152
Cdd:COG0396 80 FLAFQYPVEIPGVSVSNflRTALN-ARRGEELSARefLKLLKEKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQMLLLE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 153 PAVFLFDEPLSNLDA-KLRVqMRLELQQLHRRlKTTSLYVTH-----DQVEamtlAQRVIVMNKG 211
Cdd:COG0396 159 PKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHyqrilDYIK----PDFVHVLVDG 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-222 |
4.78e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.87 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 2 AGLKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDR---GI 78
Cdd:PRK13537 6 APIDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARqrvGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNyaLYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:PRK13537 85 VPQFDN--LDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 159 DEPLSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHDQVEAMTLAQRVIVMNKG--VAEqiGTPSEV 222
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTI-LLTTHFMEEAERLCDRLCVIEEGrkIAE--GAPHAL 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-222 |
7.40e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.51 E-value: 7.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 2 AGLKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIA 79
Cdd:PRK10253 6 ARLRGEQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNYALYPHMSVYDNMAYG------LKIRGFGKDhiRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREP 153
Cdd:PRK10253 85 LLAQNATTPGDITVQELVARGryphqpLFTRWRKED--EEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 154 AVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEV 222
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-215 |
7.87e-22 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 92.55 E-value: 7.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 6 LQAVTKSYDGKTPVIKQ-IDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRV--TDLEPKDRGIAMVF 82
Cdd:cd03252 3 FEHVRFRYKPDGPVILDnISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLalADPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYpHMSVYDNMAYGLKirgfGKDhiRQRVEEAAR-------ILEL----EPLLKRKPRELSGGQRQRVAMGRAIVR 151
Cdd:cd03252 83 QENVLF-NRSIRDNIALADP----GMS--MERVIEAAKlagahdfISELpegyDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 152 EPAVFLFDEPLSNLDAKlrvQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG-VAEQ 215
Cdd:cd03252 156 NPRILIFDEATSALDYE---SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGrIVEQ 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-223 |
1.14e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 93.31 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTP----VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTD------LEP 73
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 74 KDRGIAMVFQnyalYPHMSVYDN-----MAYGLKirGFGKDhIRQRVEEAARIL-EL---EPLLKRKPRELSGGQRQRVA 144
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFEDtvereIIFGPK--NFKMN-LDEVKNYAHRLLmDLgfsRDVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 145 MGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVY 223
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-211 |
1.25e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 92.25 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD---RG 77
Cdd:PRK11614 3 KVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 IAMVFQNYALYPHMSVYDNMAYGlkirGF--GKDHIRQRVEeaaRILELEPLL--KRKPRE--LSGGQRQRVAMGRAIVR 151
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMG----GFfaERDQFQERIK---WVYELFPRLheRRIQRAgtMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 152 EPAVFLFDEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-227 |
2.13e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 95.31 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYID-------TRRVTDLEPKD-------RG--I 78
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRQVIELSEQSaaqmrhvRGadM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQN--YALYPHMSVYDNMAYGLKI-RGFGKDHI---RQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVRE 152
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 153 PAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPA 227
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-194 |
2.22e-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: 95.12 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 2 AGLKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIA 79
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNYALYpHMSVYDNMAYGlkiRGFGKDhirQRVEEAARILELEPLLKRKP-----------RELSGGQRQRVAMGRA 148
Cdd:TIGR02868 413 VCAQDAHLF-DTTVRENLRLA---RPDATD---EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 742395038 149 IVREPAVFLFDEPLSNLDAKLRVQM-RLELQQLHRRlktTSLYVTHD 194
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELlEDLLAALSGR---TVVLITHH 529
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-226 |
4.58e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.82 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 23 IDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDL---EPKDRGIAMVFQNYALYPHMSVYDNM-- 97
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghQIARMGVVRTFQHVRLFREMTVIENLlv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 98 -----------AYGLKIRGFGKDHiRQRVEEAARILE---LEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:PRK11300 104 aqhqqlktglfSGLLKTPAFRRAE-SEALDRAATWLErvgLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:PRK11300 183 GLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
18-226 |
5.08e-21 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 94.24 E-value: 5.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 18 PVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLePKDR---GIAMVFQNYALYpHMSVY 94
Cdd:TIGR03796 493 PLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVAMVDQDIFLF-EGTVR 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 95 DNMAyglkirgFGKDHIRQ-RVEEAARILELEPLLKRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:TIGR03796 571 DNLT-------LWDPTIPDaDLVRACKDAAIHDVITSRPggydaelaeggANLSGGQRQRLEIARALVRNPSILILDEAT 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742395038 163 SNLDAklrvQMRLELQQLHRRLKTTSLYVTHdQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:TIGR03796 644 SALDP----ETEKIIDDNLRRRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-193 |
5.78e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.10 E-value: 5.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 2 AGLKLQAVT-KSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIdtrrvtdlePKDRGIAM 80
Cdd:COG4178 361 GALALEDLTlRTPDGR-PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNyalyPHM---SVYDNMAYGLKIRGFGkdhiRQRVEEAARILELEPLLKR------KPRELSGGQRQRVAMGRAIVR 151
Cdd:COG4178 431 LPQR----PYLplgTLREALLYPATAEAFS----DAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLH 502
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 742395038 152 EPAVFLFDEPLSNLDAKLRVQMrleLQQLHRRL-KTTSLYVTH 193
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-235 |
6.63e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.87 E-value: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMvagLERT---TSGDIYID---TRRVTdLEPKDRGIAMVF 82
Cdd:PRK13657 340 VSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINL---LQRVfdpQSGRILIDgtdIRTVT-RASLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYpHMSVYDNmayglkIRgFGK-DHIRQRVEEAARILELEPLLKRKP-----------RELSGGQRQRVAMGRAIV 150
Cdd:PRK13657 416 QDAGLF-NRSIEDN------IR-VGRpDATDEEMRAAAERAQAHDFIERKPdgydtvvgergRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 151 REPAVFLFDEPLSNLDAKLRVQMRLELQQLhRRLKTTslYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQ---RPA 227
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDEL-MKGRTT--FIIAHRLSTVRNADRILVFDNGRVVESGSFDELVArggRFA 564
|
....*...
gi 742395038 228 SLFVAGFI 235
Cdd:PRK13657 565 ALLRAQGM 572
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-183 |
7.20e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.16 E-value: 7.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPkdrGIAMVF---QNyALYPHM 91
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYlghRN-AMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 92 SVYDNMAYGLKIRGFGKDHIrqrvEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKlRV 171
Cdd:PRK13539 89 TVAENLEFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AV 163
|
170
....*....|..
gi 742395038 172 QMRLELQQLHRR 183
Cdd:PRK13539 164 ALFAELIRAHLA 175
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-211 |
8.23e-21 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 88.26 E-value: 8.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 23 IDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDR---GIAMV---FQNYALYPHMSVYDN 96
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYVpedRKREGLVLDLSVAEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 97 MAYglkirgfgkdhirqrveeaarilelepllkrkPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrVQMRLE 176
Cdd:cd03215 99 IAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD----VGAKAE 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 742395038 177 LQQLHRRLK---TTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd03215 143 IYRLIRELAdagKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-223 |
1.45e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDR-GIA 79
Cdd:PRK13536 39 TVAIDLAGVSKSYGDK-AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNYALYPHMSVYDNM-AYGlkiRGFGKdHIRQRVEEAARILE---LEPLLKRKPRELSGGQRQRVAMGRAIVREPAV 155
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLlVFG---RYFGM-STREIEAVIPSLLEfarLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 156 FLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHDQVEAMTLAQRVIVMNKGVA-----------EQIGTPS-EVY 223
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTI-LLTTHFMEEAERLCDRLCVLEAGRKiaegrphalidEHIGCQViEIY 272
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
11-269 |
1.89e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 90.55 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 11 KSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKS----TLLRMVAGLERTtSGDIYIDTRRVTDLEPKD------RGIAM 80
Cdd:PRK09473 23 STPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRI-GGSATFNGREILNLPEKElnklraEQISM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQN--YALYPHMSVYDNMAYGLKI-RGFGKdhiRQRVEEAARIL------ELEPLLKRKPRELSGGQRQRVAMGRAIVR 151
Cdd:PRK09473 102 IFQDpmTSLNPYMRVGEQLMEVLMLhKGMSK---AEAFEESVRMLdavkmpEARKRMKMYPHEFSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 152 EPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFV 231
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYS 258
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 742395038 232 AGFigspaMNLLPgTLSADGGQLLLADGMA---LPLPAAKP 269
Cdd:PRK09473 259 IGL-----LNAVP-RLDAEGESLLTIPGNPpnlLRLPKGCP 293
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
3-224 |
2.07e-20 |
|
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: 92.50 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 3 GLKLQAVTKSYDGKTP-VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPK--DRGIA 79
Cdd:TIGR01846 455 AITFENIRFRYAPDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMG 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNYALYPHmSVYDNMAYGLKIRGFgkdhirQRVEEAARILELEPLLKRKPR-----------ELSGGQRQRVAMGRA 148
Cdd:TIGR01846 535 VVLQENVLFSR-SIRDNIALCNPGAPF------EHVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARA 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 149 IVREPAVFLFDEPLSNLDAKlrvQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQ 224
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYE---SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLA 680
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-214 |
1.12e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.69 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 18 PVIKQIDLDVADGEfIV-MVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD---RGIAMVFQN---YALYPH 90
Cdd:COG1129 266 GVVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVPEDrkgEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 91 MSVYDNMAYGL--KIRGFG---KDHIRQRVEEAARILELE-PLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
Cdd:COG1129 345 LSIRENITLASldRLSRGGlldRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRG 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 165 LD--AKlrvqmrLELQQLHRRLK---TTSLYVTHDQVEAMTLAQRVIVMNKG--VAE 214
Cdd:COG1129 425 IDvgAK------AEIYRLIRELAaegKAVIVISSELPELLGLSDRILVMREGriVGE 475
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-225 |
1.58e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIyidtRRVTDLEpkdrgIAMVFQ 83
Cdd:COG0488 316 LELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----KLGETVK-----IGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYA-LYPHMSVYDNMAYG------LKIRG------FGKDHIRQRVeeaarilelepllkrkpRELSGGQRQRVAMGRAIV 150
Cdd:COG0488 386 HQEeLDPDKTVLDELRDGapggteQEVRGylgrflFSGDDAFKPV-----------------GVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 151 REPAVFLFDEPLSNLDaklrVQMRLELQQLhrrLKT---TSLYVTHDQ--VEamTLAQRVI-VMNKGVAEQIGTPSEvYQ 224
Cdd:COG0488 449 SPPNVLLLDEPTNHLD----IETLEALEEA---LDDfpgTVLLVSHDRyfLD--RVATRILeFEDGGVREYPGGYDD-YL 518
|
.
gi 742395038 225 R 225
Cdd:COG0488 519 E 519
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-234 |
2.31e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.60 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 18 PVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRrvtDLEPKDRG-------IAMVFQNyalyPH 90
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYSKRGllalrqqVATVFQD----PE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 91 MSVY-----DNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
Cdd:PRK13638 88 QQIFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 166 DAKLRVQMrlelQQLHRRLKTTSLYV---THDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGF 234
Cdd:PRK13638 168 DPAGRTQM----IAIIRRIVAQGNHViisSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-222 |
2.89e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.69 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDR---GIAM 80
Cdd:PRK09700 6 ISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSVYDNMAYG-LKIRGF-GKDHI-----RQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREP 153
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGrHLTKKVcGVNIIdwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 154 AVFLFDEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEV 222
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-215 |
4.43e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 85.36 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPvIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTR--RVTDL----EPKDRG 77
Cdd:PRK11701 7 LSVRGLTKLYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgQLRDLyalsEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 IA-----MVFQNYA--LYPHMSVYDN-----MA-----YGlKIRGFGKDHIrQRVE-EAARILELepllkrkPRELSGGQ 139
Cdd:PRK11701 86 LLrtewgFVHQHPRdgLRMQVSAGGNigerlMAvgarhYG-DIRATAGDWL-ERVEiDAARIDDL-------PTTFSGGM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 140 RQRVAMGRAIVREPAVFLFDEPLSNLDakLRVQMRL--ELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG-VAEQ 215
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLD--VSVQARLldLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGrVVES 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-211 |
6.21e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 83.13 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGK-TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRG-IAMV 81
Cdd:cd03247 1 LSINNVSFSYPEQeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNYALYpHMSVYDNMAyglkirgfgkdhirqrveeaarilelepllkrkpRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
Cdd:cd03247 81 NQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 742395038 162 LSNLDAKLRVQ-MRLELQQLHRRlktTSLYVTHdQVEAMTLAQRVIVMNKG 211
Cdd:cd03247 126 TVGLDPITERQlLSLIFEVLKDK---TLIWITH-HLTGIEHMDKILFLENG 172
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-215 |
8.06e-19 |
|
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: 87.87 E-value: 8.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLepkDRGIAMVFQ 83
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NY-ALYPHM---SVYDNMAYGLKiRGFGKDHIRQRVEEAARILELEPL-------LKRKPRELSGGQRQRVAMGRAIVRE 152
Cdd:TIGR01193 551 NYlPQEPYIfsgSILENLLLGAK-ENVSQDEIWAACEIAEIKDDIENMplgyqteLSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742395038 153 PAVFLFDEPLSNLDAKLRVQMRLELQQLHRRlktTSLYVTHdQVEAMTLAQRVIVMNKG-VAEQ 215
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAH-RLSVAKQSDKIIVLDHGkIIEQ 689
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-226 |
1.01e-18 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 84.50 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPViKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDL------EPKDRG 77
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGC-RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELelyqlsEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 IA-----MVFQNYALYPHMSVYDNMAYGLKIRGFGKDH---IRQRVEEAARILELEP-LLKRKPRELSGGQRQRVAMGRA 148
Cdd:TIGR02323 83 LMrtewgFVHQNPRDGLRMRVSAGANIGERLMAIGARHygnIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 149 IVREPAVFLFDEPLSNLDakLRVQMRL--ELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLD--VSVQARLldLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-211 |
1.46e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLQAVTKSYDGkTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRV---TDLEPKDRG 77
Cdd:PRK11288 2 SPYLSFDGIGKTFPG-VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 IAMVFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILE-----LEPLLKRKprELSGGQRQRVAMGRAIVRE 152
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEhlgvdIDPDTPLK--YLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 153 PAVFLFDEPLSNLDAKlrvqmrlELQQLHR---RLK---TTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:PRK11288 159 ARVIAFDEPTSSLSAR-------EIEQLFRvirELRaegRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-226 |
1.95e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 83.69 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 20 IKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVT--DLEPKDRGIAMVFQN--YALYPHMSVYD 95
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 96 NMAYGLKIR-GFGKDHIRQRVEEAARILELEP-LLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ- 172
Cdd:PRK15112 109 ILDFPLRLNtDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQl 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 173 --MRLELQQLHrrlKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:PRK15112 189 inLMLELQEKQ---GISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-211 |
2.35e-18 |
|
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: 80.57 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIyidtrrvtdlepkdrgiamvfq 83
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 nyALYPHMSVYdnmayglkirgfgkdHIRQrveeaarilelepllkrkpreLSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:cd03221 58 --TWGSTVKIG---------------YFEQ---------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 742395038 164 NLDaklrVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:cd03221 100 HLD----LESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
9-193 |
2.66e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 85.84 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDGK-TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMVFQNY 85
Cdd:PRK11176 347 VTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 86 ALYpHMSVYDNMAYGlkirgFGKDHIRQRVEEAAR-------ILELEPLLKRKPRE----LSGGQRQRVAMGRAIVREPA 154
Cdd:PRK11176 427 HLF-NDTIANNIAYA-----RTEQYSREQIEEAARmayamdfINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 742395038 155 VFLFDEPLSNLD--AKLRVQMRLELQQLHRrlktTSLYVTH 193
Cdd:PRK11176 501 ILILDEATSALDteSERAIQAALDELQKNR----TSLVIAH 537
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-168 |
2.76e-18 |
|
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: 82.02 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGkTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPK-DRGIAMVF 82
Cdd:TIGR01189 1 LAARNLACSRGE-RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYPHMSVYDNMAYglkIRGFGKDHIRQrVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:TIGR01189 80 HLPGLKPELSALENLHF---WAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
....*.
gi 742395038 163 SNLDAK 168
Cdd:TIGR01189 156 TALDKA 161
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-211 |
4.16e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.75 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDgKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGL---ERTTSGDIYIDTRRVT-------DLEP 73
Cdd:PRK09984 5 IRVEKLAKTFN-QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQregrlarDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 74 KDRGIAMVFQNYALYPHMSVYDNMAYGLK---------IRGFGKDHiRQRVEEAARILELEPLLKRKPRELSGGQRQRVA 144
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQ-KQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 145 MGRAIVREPAVFLFDEPLSNLDAKlrvQMRLELQQLHRRLKT--TSLYVTHDQVE-AMTLAQRVIVMNKG 211
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPE---SARIVMDTLRDINQNdgITVVVTLHQVDyALRYCERIVALRQG 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-218 |
5.93e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.15 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPK--DRGIAMVFQNYA 86
Cdd:PRK10790 346 VSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 87 LYPHmSVYDNMAYGlkiRGFGKDHIRQRVE-----EAARILE--LEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
Cdd:PRK10790 426 VLAD-TFLANVTLG---RDISEEQVWQALEtvqlaELARSLPdgLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 160 EPLSNLDAKLRVQMRLELQQLhrRLKTTSLYVTHdQVEAMTLAQRVIVMNKGVAEQIGT 218
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAAV--REHTTLVVIAH-RLSTIVEADTILVLHRGQAVEQGT 557
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-195 |
1.27e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.77 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 14 DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDtrrVTDLEpkdrgiamvfqnyaLYPHMSV 93
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD---VPDNQ--------------FGREASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 94 YDNMAyglkirgfgkdhIRQRVEEAARILEL-----EPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
Cdd:COG2401 103 IDAIG------------RKGDFKDAVELLNAvglsdAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*..
gi 742395038 169 LRVQMRLELQQLHRRLKTTSLYVTHDQ 195
Cdd:COG2401 171 TAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-236 |
2.50e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKLqavTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSG-----DIYIDTRRV---TDLE 72
Cdd:PRK14271 22 MAAVNL---TLGFAGKT-VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 73 PKDRGIAMVFQNYALYPhMSVYDNMAYGLK---------IRGFGKdhirQRVEEAARILELEPLLKRKPRELSGGQRQRV 143
Cdd:PRK14271 98 EFRRRVGMLFQRPNPFP-MSIMDNVLAGVRahklvprkeFRGVAQ----ARLTEVGLWDAVKDRLSDSPFRLSGGQQQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 144 AMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLktTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVY 223
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
250
....*....|....*..
gi 742395038 224 QRP----ASLFVAGFIG 236
Cdd:PRK14271 251 SSPkhaeTARYVAGLSG 267
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-179 |
1.14e-16 |
|
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: 77.53 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPK-DRGIAMVF 82
Cdd:cd03231 1 LEADELTCERDGRA-LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYPHMSVYDNMayglkiRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:cd03231 80 HAPGIKTTLSVLENL------RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180
....*....|....*....|.
gi 742395038 163 SNLD----AKLRVQMRLELQQ 179
Cdd:cd03231 154 TALDkagvARFAEAMAGHCAR 174
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-218 |
1.71e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 80.66 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTsGDIYIDTRRVTDLEPKD--RGIAMVFQNYA 86
Cdd:PRK11174 356 EILSPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQNPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 87 LyPHMSVYDNMAYGlkiRGFGKDHIRQRVEEAARILELEPLL--------KRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:PRK11174 434 L-PHGTLRDNVLLG---NPDASDEQLQQALENAWVSEFLPLLpqgldtpiGDQAAGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 159 DEPLSNLDAKLRVQMRLELQQLHRRlkTTSLYVTHdQVEAMTLAQRVIVMNKGVAEQIGT 218
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASRR--QTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-166 |
2.20e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 76.81 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 17 TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEpKDRGIAMVFQNYALYPHMSVYDN 96
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 97 MAYGLKIRGFgkdHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
Cdd:PRK13543 103 LHFLCGLHGR---RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
14-226 |
2.49e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 78.63 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 14 DGKTP--VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGL----ERTTSGDIYIDTRRVTDLEPKDR------GIAMV 81
Cdd:PRK11022 15 DESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERrnlvgaEVAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQN--YALYPHMSVYDNMAYGLKIRGFGKDhiRQRVEEAARILEL------EPLLKRKPRELSGGQRQRVAMGRAIVREP 153
Cdd:PRK11022 95 FQDpmTSLNPCYTVGFQIMEAIKVHQGGNK--KTRRQRAIDLLNQvgipdpASRLDVYPHQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 154 AVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-221 |
3.84e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 12 SYDGKTpvIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD---RGIAMVFQNY--- 85
Cdd:PRK09700 273 SRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdn 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 86 ALYPHMSVYDNMAYG--LKIRGFG------KDHIRQRVEEAAR-ILELE-PLLKRKPRELSGGQRQRVAMGRAIVREPAV 155
Cdd:PRK09700 351 GFFPNFSIAQNMAISrsLKDGGYKgamglfHEVDEQRTAENQReLLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 156 FLFDEPLSNLDaklrVQMRLELQQLHRRLK---TTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSE 221
Cdd:PRK09700 431 IIFDEPTRGID----VGAKAEIYKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-219 |
4.72e-16 |
|
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: 75.99 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSY-DGKTPVIKQIDLDVADGEFIVMVGPSGCGKST----LLRMVagleRTTSGDIYIDTRRVTDLEPKD--RGIAMV 81
Cdd:cd03244 8 VSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlrSRISII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNYALY---------PHMSVYDNMAYG-LKirgfgKDHIRQRVEEAARILELEplLKRKPRELSGGQRQRVAMGRAIVR 151
Cdd:cd03244 84 PQDPVLFsgtirsnldPFGEYSDEELWQaLE-----RVGLKEFVESLPGGLDTV--VEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 152 EPAVFLFDEPLSNLDaklrVQMRLELQQ-LHRRLK-TTSLYVTHdQVEAMTLAQRVIVMNKGVAEQIGTP 219
Cdd:cd03244 157 KSKILVLDEATASVD----PETDALIQKtIREAFKdCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-211 |
5.02e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.10 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY-DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAM 80
Cdd:PRK11160 339 LTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHmSVYDNMAyglkirgFGKDHIR-QRVEEAARILELEPLLKRKP----------RELSGGQRQRVAMGRAI 149
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNLL-------LAAPNASdEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 150 VREPAVFLFDEPLSNLDAKLRVQMrLELQQLHRRLKTTsLYVTHdQVEAMTLAQRVIVMNKG 211
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQI-LELLAEHAQNKTV-LMITH-RLTGLEQFDRICVMDNG 549
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-228 |
5.31e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.82 E-value: 5.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGkTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGL--ERTTSGDIYID-----TRRVTDLEPKdr 76
Cdd:PRK13549 6 LEMKNITKTFGG-VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEgeelqASNIRDTERA-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 77 GIAMVFQNYALYPHMSVYDNMAYGLKIRGFGkdhirqRVEEAARILELEPLLKR---------KPRELSGGQRQRVAMGR 147
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEITPGG------IMDYDAMYLRAQKLLAQlkldinpatPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 148 AIVREPAVFLFDEPLSNLDAKlRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGvaEQIGTpsevyqRPA 227
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG--RHIGT------RPA 227
|
.
gi 742395038 228 S 228
Cdd:PRK13549 228 A 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-313 |
6.22e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 79.22 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTrrvtdlepkdrGIAMVFQNyALYPHMSVY 94
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------SVAYVPQQ-AWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 95 DNMAYGLKIRgfgKDHIRQRVEEAARILELEPL-------LKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
Cdd:TIGR00957 717 ENILFGKALN---EKYYQQVLEACALLPDLEILpsgdrteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 168 KLRVQMRLELQQLHRRLKT-TSLYVTHDqVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLfvAGFIGSPAMNLLPGT 246
Cdd:TIGR00957 794 HVGKHIFEHVIGPEGVLKNkTRILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF--AEFLRTYAPDEQQGH 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 247 LSADGGQ---------LLLADGMALPLPAAKPqwAGRQLTL-----GIRPEHIQLVAQGQGVPLQLQTLELLGADNLAHG 312
Cdd:TIGR00957 871 LEDSWTAlvsgegkeaKLIENGMLVTDVVGKQ--LQRQLSAsssdsGDQSRHHGSSAELQKAEAKEETWKLMEADKAQTG 948
|
.
gi 742395038 313 Q 313
Cdd:TIGR00957 949 Q 949
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-218 |
6.23e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 78.71 E-value: 6.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGL--ERTTSGDIYID-----TRRVTDLEPKdr 76
Cdd:TIGR02633 2 LEMKGIVKTFGGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSgsplkASNIRDTERA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 77 GIAMVFQNYALYPHMSVYDNMAYGLKIrgfgkDHIRQRVEEAARILELEPLLK----------RKPRELSGGQRQRVAMG 146
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIFLGNEI-----TLPGGRMAYNAMYLRAKNLLRelqldadnvtRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 147 RAIVREPAVFLFDEPLSNLDAKlRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGvaEQIGT 218
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG--QHVAT 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-244 |
6.77e-16 |
|
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: 79.29 E-value: 6.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDG-KTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDlepkdrGIAMVF 82
Cdd:TIGR01257 1938 LRLNELTKVYSGtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYPHMSVYDNMAYG-------LKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAV 155
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLTGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 156 FLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLyVTHDQVEAMTLAQRVIVMNKGVAEQIGTpsevYQRPASLFVAGF- 234
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL-TSHSMEECEALCTRLAIMVKGAFQCLGT----IQHLKSKFGDGYi 2166
|
250
....*....|....
gi 742395038 235 ----IGSPAMNLLP 244
Cdd:TIGR01257 2167 vtmkIKSPKDDLLP 2180
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-207 |
6.82e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.70 E-value: 6.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 30 GEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRrvtdlepkdrgIAMVFQNYALYPHMSVYDNMAyglKIRG-FGK 108
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-----------ISYKPQYIKPDYDGTVEDLLR---SITDdLGS 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 109 DHIRqrvEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrVQMRLELQQLHRRL---- 184
Cdd:PRK13409 431 SYYK---SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VEQRLAVAKAIRRIaeer 503
|
170 180
....*....|....*....|...
gi 742395038 185 KTTSLYVTHDQVEAMTLAQRVIV 207
Cdd:PRK13409 504 EATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-212 |
8.45e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGkTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEP---KDRGIAM 80
Cdd:PRK15439 12 LCARSISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEpllkRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLD----SSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 161 PLSNLD----AKLRVQMRlELQQLHRRLkttsLYVTHDQVEAMTLAQRVIVMNKGV 212
Cdd:PRK15439 167 PTASLTpaetERLFSRIR-ELLAQGVGI----VFISHKLPEIRQLADRISVMRDGT 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-211 |
1.69e-15 |
|
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: 74.10 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERT--TSGDIYIDTRRVTDLEPKDR---GI 78
Cdd:cd03217 1 LEIKDLHVSVGGKE-ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDITDLPPEERarlGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYPhmsvydnmayGLKIrgfgKDHIRQrVEEAarilelepllkrkpreLSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:cd03217 80 FLAFQYPPEIP----------GVKN----ADFLRY-VNEG----------------FSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742395038 159 DEPLSNLDAklrVQMRL---ELQQLhRRLKTTSLYVTH-----DQVEamtlAQRVIVMNKG 211
Cdd:cd03217 129 DEPDSGLDI---DALRLvaeVINKL-REEGKSVLIITHyqrllDYIK----PDRVHVLYDG 181
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-224 |
1.78e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.21 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 2 AGLKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPK--DRGIA 79
Cdd:PRK10575 10 TTFALRNVSFRVPGRT-LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNYALYPHMSVYDNMAYGL-----KIRGFGKDHiRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPA 154
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAIGRypwhgALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 155 VFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQ 224
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-221 |
2.73e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.01 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 30 GEFIVMVGPSGCGKSTLLRMVAGLERT---TSGDIYIDTRRVTDLEPKDRGiAMVFQNYALYPHMSVYDNMAYG--LKI- 103
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS-AYVQQDDLFIPTLTVREHLMFQahLRMp 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 104 RGFGKDHIRQRVEEAARILELEPLLKRK------PRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEL 177
Cdd:TIGR00955 130 RRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVL 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 742395038 178 QQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSE 221
Cdd:TIGR00955 210 KGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-228 |
3.15e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 74.35 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 18 PVIKQIDLDVADGEFIVMVGPSGCGKS-----TLLRMVAGLERTtSGDIYIDTRRVTDLEPKDRGIAMVFQN--YALYPH 90
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQT-AGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 91 MSVYDNMAYGLKIRG-FGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREpAVFLF-DEPLSNLDak 168
Cdd:PRK10418 96 HTMHTHARETCLALGkPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCE-APFIIaDEPTTDLD-- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 169 LRVQMR-LEL-QQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPAS 228
Cdd:PRK10418 173 VVAQARiLDLlESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKH 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-207 |
5.55e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 75.98 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 8 AVTKSYDGKTpvikqidLDVADG-----EFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRrvtdlepkdrgIAMVF 82
Cdd:COG1245 346 DLTKSYGGFS-------LEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-----------ISYKP 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QnyalyphmsvYDNMAYGLKIRGFGKDHIRQRV------EEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVF 156
Cdd:COG1245 408 Q----------YISPDYDGTVEEFLRSANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 157 LFDEPLSNLDaklrVQMRLELQQLHRRL----KTTSLYVTHD-QVEAMtLAQRVIV 207
Cdd:COG1245 478 LLDEPSAHLD----VEQRLAVAKAIRRFaenrGKTAMVVDHDiYLIDY-ISDRLMV 528
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-211 |
7.45e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 72.75 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 12 SYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIY-----IDTRRVTDLEPKDRG-IAMVFQNY 85
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknESEPSFEATRSRNRYsVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 86 ALYpHMSVYDNMAyglkirgFGKDHIRQRVEEAARILELEPLLKRKPR-----------ELSGGQRQRVAMGRAIVREPA 154
Cdd:cd03290 89 WLL-NATVEENIT-------FGSPFNKQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 742395038 155 VFLFDEPLSNLDAKLRVQ-MRLELQQLHRRLKTTSLYVTHdQVEAMTLAQRVIVMNKG 211
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
236-285 |
8.10e-15 |
|
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: 67.99 E-value: 8.10e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 742395038 236 GSPAMNLLPGTLSADgGQLLLADGMALPLPAAKPQ----WAGRQLTLGIRPEHI 285
Cdd:pfam17912 1 GSPPMNFLPATVVED-GLLVLGGGVTLPLPEGQVLalklYVGKEVILGIRPEHI 53
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-268 |
8.32e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.51 E-value: 8.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 18 PVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERT-----TSGDIYIDTRRVTDL-EPKDRG-----IAMVFQN-- 84
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLLHAsEQTLRGvrgnkIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 85 YALYPHMSVYDNMAYGLKI-RGFGKDHIR-------QRV--EEAARilelepLLKRKPRELSGGQRQRVAMGRAIVREPA 154
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLhRGMRREAARgeilnclDRVgiRQAAK------RLTDYPHQLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 155 VFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLFVAGF 234
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKL 256
|
250 260 270
....*....|....*....|....*....|....*
gi 742395038 235 IGS-PAMNLLPgtLSADGGQLLLADGMALPLPAAK 268
Cdd:PRK15134 257 LNSePSGDPVP--LPEPASPLLDVEQLQVAFPIRK 289
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-219 |
9.14e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.82 E-value: 9.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 18 PVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRV-TDLEPKDRGIAMVFQNYALYPHMSVYDN 96
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 97 MAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLE 176
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 742395038 177 LqqLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTP 219
Cdd:TIGR01257 1104 L--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-226 |
9.94e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.13 E-value: 9.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 18 PVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD-RG-IAMVFQNYALYPHmSVYD 95
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSrLAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 96 NMAYGLkirgfgKDHIRQRVEEAARILELEPLLKRKPR-----------ELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
Cdd:PRK10789 408 NIALGR------PDATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 165 LDAKLRVQMrleLQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:PRK10789 482 VDGRTEHQI---LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-193 |
1.38e-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: 70.65 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 17 TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIdtrrvtdlePKDRGIAMVFQNyalyPHMSvydn 96
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR----PYLP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 97 mayglkiRGFGKDHIRqrveeaarilelepllkrKP--RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrVQMR 174
Cdd:cd03223 77 -------LGTLREQLI------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESE 127
|
170
....*....|....*....
gi 742395038 175 LELQQLHRRLKTTSLYVTH 193
Cdd:cd03223 128 DRLYQLLKELGITVISVGH 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-224 |
1.89e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.01 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 12 SYDGKT--PVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGlERTTSGDIYIDTRRVTDLEPKdrgIAMVFqnyalyp 89
Cdd:PLN03232 623 SWDSKTskPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-ELSHAETSSVVIRGSVAYVPQ---VSWIF------- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 90 HMSVYDNMAYGLKirgFGKDHIRQRVEEAARILELEPLLKRKPREL-------SGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:PLN03232 692 NATVRENILFGSD---FESERYWRAIDVTALQHDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 163 SNLDAKLRVQ-----MRLELQQLHRRLKTtslyvthDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQ 224
Cdd:PLN03232 769 SALDAHVAHQvfdscMKDELKGKTRVLVT-------NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-225 |
2.16e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.77 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 12 SYDGKT--PVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAG-LERTTSGDIYIdtrrvtdlepkdRG-IAMVFQNYAL 87
Cdd:PLN03130 623 SWDSKAerPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVI------------RGtVAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 88 YpHMSVYDNMAyglkirgFGKDHIRQRVEEAARILELEPLLKRKPR-----------ELSGGQRQRVAMGRAIVREPAVF 156
Cdd:PLN03130 691 F-NATVRDNIL-------FGSPFDPERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742395038 157 LFDEPLSNLDAKLRVQ-----MRLELQQLHRRLKTTSLYVThDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQR 225
Cdd:PLN03130 763 IFDDPLSALDAHVGRQvfdkcIKDELRGKTRVLVTNQLHFL-SQVDRIILVHEGMIKEEGTYEELSNNGPLFQK 835
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-194 |
2.58e-14 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 72.01 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 27 VADGEFIVMVGPSGCGKSTLLRMVAG--------LERTTSGDIYIDTRRVTDLE-------PKDRGIAMVFQNYALYPhm 91
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDEFRGSELQnyftkllEGDVKVIVKPQYVDLIP-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 92 svydNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRV 171
Cdd:cd03236 101 ----KAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|...
gi 742395038 172 QMRLELQQLHRRLKTTsLYVTHD 194
Cdd:cd03236 177 NAARLIRELAEDDNYV-LVVEHD 198
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-244 |
3.16e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.76 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 30 GEFIVMVGPSGCGKSTLLRMVAGLERTTS--GDIYIDTRRVTdlEPKDRGIAMVFQNYALYPHMSVYDNMAYGLKIRgFG 107
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT--KQILKRTGFVTQDDILYPHLTVRETLVFCSLLR-LP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 108 KDHIRQRVEEAARILELEPLLKRKP---------RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQ 178
Cdd:PLN03211 171 KSLTKQEKILVAESVISELGLTKCEntiignsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLG 250
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 179 QLHRRLKT--TSLYVTHDQVEAMTlaQRVIVMNKGVAEQIGTPSEvyqrpaSLFVAGFIG-SPAMNLLP 244
Cdd:PLN03211 251 SLAQKGKTivTSMHQPSSRVYQMF--DSVLVLSEGRCLFFGKGSD------AMAYFESVGfSPSFPMNP 311
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-194 |
3.20e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 2 AGLKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIdTRRVTDLEPKDRGIAMV 81
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI-LGQPTRQALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNYAL---YP-------HMSVYDNMAYgLKIrgfGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVR 151
Cdd:PRK15056 84 PQSEEVdwsFPvlvedvvMMGRYGHMGW-LRR---AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 742395038 152 EPAVFLFDEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTHD 194
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHN 201
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-207 |
4.01e-14 |
|
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: 69.91 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 26 DVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDtrRVTdlepkdrgiamvfqnyalyphmsvydnmayglkirg 105
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD--GIT------------------------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 106 fgkdhirqrveeaarilelePLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLK 185
Cdd:cd03222 63 --------------------PVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|..
gi 742395038 186 TTSLYVTHDQVEAMTLAQRVIV 207
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHV 144
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-211 |
6.13e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.75 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEfIVMV-GPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDR---GIA 79
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSLEVRAGE-ILGIaGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MV---FQNYALYPHMSVYDNMA---YGLKirGFGKDHI--RQRVEE-AARILE----LEPLLKRKPRELSGGQRQRVAMG 146
Cdd:COG3845 337 YIpedRLGRGLVPDMSVAENLIlgrYRRP--PFSRGGFldRKAIRAfAEELIEefdvRTPGPDTPARSLSGGNQQKVILA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742395038 147 RAIVREPAVFLFDEPLSNLDAKlrvqmrlELQQLHRRLK------TTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVG-------AIEFIHQRLLelrdagAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-196 |
7.76e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.59 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 18 PVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRV-TDLEPKDRGIAMVFQNYALYPHMSVYDN 96
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 97 MAYGLKIRGFGKDhirqrVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaKLRVQMRLE 176
Cdd:PRK13540 95 CLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD-ELSLLTIIT 168
|
170 180
....*....|....*....|
gi 742395038 177 LQQLHRRLKTTSLYVTHDQV 196
Cdd:PRK13540 169 KIQEHRAKGGAVLLTSHQDL 188
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
23-211 |
7.90e-14 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 72.30 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 23 IDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMVFQNYALYPHMSVYDNmayg 100
Cdd:TIGR01194 361 IDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDyrDLFSAIFADFHLFDDLIGPDE---- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 101 lkirgfGKDHIRQRVEEAARILELEPLLK------RKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMR 174
Cdd:TIGR01194 437 ------GEHASLDNAQQYLQRLEIADKVKiedggfSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKRFFY 510
|
170 180 190
....*....|....*....|....*....|....*..
gi 742395038 175 LELQQLHRRLKTTSLYVTHDQvEAMTLAQRVIVMNKG 211
Cdd:TIGR01194 511 EELLPDLKRQGKTIIIISHDD-QYFELADQIIKLAAG 546
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-194 |
7.95e-14 |
|
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: 72.28 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 6 LQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI-DTRRVTDL--EPKDRGIAMVF 82
Cdd:TIGR03719 7 MNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVGYLpqEPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYPH-----MSVYD--NMAYGL-----------------KIRGFGKDHIRQRVEEAARILELEPlLKRKPRELSGG 138
Cdd:TIGR03719 87 ENVEEGVAeikdaLDRFNeiSAKYAEpdadfdklaaeqaelqeIIDAADAWDLDSQLEIAMDALRCPP-WDADVTKLSGG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 139 QRQRVAMGRAIVREPAVFLFDEPLSNLDAklrvqmrlE----LQQLHRRLKTTSLYVTHD 194
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDA--------EsvawLERHLQEYPGTVVAVTHD 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-212 |
1.21e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.93 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD--RGIAMV 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 82 FQNYALYPHMsvydnmaygLKIRGFGKDhiRQRVEEAARILELEPLLKRKPRE-----LSGGQRQRVAMGRAIVREPAVF 156
Cdd:PRK10522 403 FTDFHLFDQL---------LGPEGKPAN--PALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 157 LFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQvEAMTLAQRVIVMNKGV 212
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQ 526
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-222 |
1.70e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.48 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 23 IDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERtTSGDIYIDTRRVTDLEPKD--RGIAMVFQNYALYPHMSVYDNMAYG 100
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 101 LKiRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVR-------EPAVFLFDEPLSNLDaklrVQM 173
Cdd:COG4138 94 QP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD----VAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 742395038 174 RLELQQLHRRLKTTSLYV---THDQVEAMTLAQRVIVMNKGVAEQIGTPSEV 222
Cdd:COG4138 169 QAALDRLLRELCQQGITVvmsSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-234 |
1.83e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 6 LQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIyidtrrvtDLEPKDRgIAMVFQNY 85
Cdd:PRK09544 7 LENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR-IGYVPQKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 86 ALYPHMSVYDNMAYGLKiRGFGKDHIR---QRVEeAARILElEPLLKrkpreLSGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:PRK09544 77 YLDTTLPLTVNRFLRLR-PGTKKEDILpalKRVQ-AGHLID-APMQK-----LSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 163 SNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQiGTPSEVYQRPAslFVAGF 234
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCS-GTPEVVSLHPE--FISMF 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-194 |
1.91e-12 |
|
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: 68.27 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 30 GEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIyidtrrvtDLEPKDRGIAMVFQNYALYPHMS-VYDNmayglKIR---- 104
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKRFRGTELQDYFKkLANG-----EIKvahk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 105 ------------GFGKDHI-----RQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
Cdd:COG1245 166 pqyvdlipkvfkGTVRELLekvdeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|....*..
gi 742395038 168 KLRVQMRLELQQLHRRLKTTsLYVTHD 194
Cdd:COG1245 246 YQRLNVARLIRELAEEGKYV-LVVEHD 271
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-168 |
2.09e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.21 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 22 QIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPkDRGIAMVF---QNyALYPHMSVYDNMA 98
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYlghQP-GIKTELTALENLR 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 99 YGLKIRGfgkdhiRQRVEEAARILELEPLLKRK--P-RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
Cdd:PRK13538 97 FYQRLHG------PGDDEALWEALAQVGLAGFEdvPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
58-209 |
2.18e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 58 SGDIYIDTRRVTDLEPKD-RGIAMVFQNYALYPHMSVYDNMAYGlkirgfGKDHIRQRVEEAARILELEPLLKRKP---- 132
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPnkyd 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 133 -------RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHdQVEAMTLAQRV 205
Cdd:PTZ00265 1350 tnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKI 1428
|
....
gi 742395038 206 IVMN 209
Cdd:PTZ00265 1429 VVFN 1432
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-218 |
2.52e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.61 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGlerttsgdiyidtrrvtDLEPkDRGIAMVFQ 83
Cdd:PRK15064 320 LEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-----------------ELEP-DSGTVKWSE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 NYAL--YPH---------MSVYDNMAY-------GLKIRG------FGKDHIrqrveeaarilelepllKRKPRELSGGQ 139
Cdd:PRK15064 381 NANIgyYAQdhaydfendLTLFDWMSQwrqegddEQAVRGtlgrllFSQDDI-----------------KKSVKVLSGGE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 140 RQRVAMGRAIVREPAVFLFDEPLSNLD--AKLRVQMRLELqqlhrrLKTTSLYVTHDQVEAMTLAQRVI-VMNKGVAEQI 216
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEPTNHMDmeSIESLNMALEK------YEGTLIFVSHDREFVSSLATRIIeITPDGVVDFS 517
|
..
gi 742395038 217 GT 218
Cdd:PRK15064 518 GT 519
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-170 |
1.05e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 63.35 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 37 GPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDRGiaMVFQNYALYPHMSVYDNMAYGLKIRgfgkdHIRQRVE 116
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCT--YIGHNLGLKLEMTVFENLKFWSEIY-----NSAETLY 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 742395038 117 EAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR 170
Cdd:PRK13541 106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-166 |
1.20e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.89 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLE--RTTSGDIYIDTRRVTDLEPKDR---GIAMVFQNYALYP 89
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERahlGIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 90 HMSVYD--NMAYGLKIRGFGKDHIR-----QRVEEAARILELEP-LLKRKPRE-LSGGQRQRVAMGRAIVREPAVFLFDE 160
Cdd:CHL00131 98 GVSNADflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDE 177
|
....*.
gi 742395038 161 PLSNLD 166
Cdd:CHL00131 178 TDSGLD 183
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-222 |
1.24e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.80 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 27 VADGEFIVMVGPSGCGKSTLLRMVAGLeRTTSGDIYIDTRRVTDLEPKD----RG---------IAM-VFQNYALYPHMS 92
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMpVFQYLTLHQPDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 93 VYdnmayglkirgfgKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVamgraivREPAVFL--------------F 158
Cdd:PRK03695 98 TR-------------TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRV-------RLAAVVLqvwpdinpagqlllL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 159 DEPLSNLDaklrVQMRLELQQLHRRLKTTSLYV---THDQVEAMTLAQRVIVMNKGVAEQIGTPSEV 222
Cdd:PRK03695 158 DEPMNSLD----VAQQAALDRLLSELCQQGIAVvmsSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-219 |
1.38e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 63.20 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 18 PVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVT--DLEPKDRGIAMVFQNYALYP-----H 90
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIStiPLEDLRSSLTIIPQDPTLFSgtirsN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 91 MSVYDNmayglkirgFGKDHIRqrveEAARILElepllkrKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL----D 166
Cdd:cd03369 102 LDPFDE---------YSDEEIY----GALRVSE-------GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIdyatD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 742395038 167 AKLRVQMRLELQqlhrrlKTTSLYVTHdQVEAMTLAQRVIVMNKGVAEQIGTP 219
Cdd:cd03369 162 ALIQKTIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-216 |
1.54e-11 |
|
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: 62.67 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 16 KTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTT---SGDIYIDTRRVTDLEPKDRG-IAMVFQNYALYPHM 91
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGeIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 92 SVYDNMAYGLKIRGfgkdhiRQRVeeaarilelepllkrkpRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRV 171
Cdd:cd03233 99 TVRETLDFALRCKG------NEFV-----------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 742395038 172 QMRLELQQLHRRLKTT---SLYVTHDqvEAMTLAQRVIVMNKGvaEQI 216
Cdd:cd03233 156 EILKCIRTMADVLKTTtfvSLYQASD--EIYDLFDKVLVLYEG--RQI 199
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-168 |
1.75e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTPV--IKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI-DTRRVTDLEPK--DRGI 78
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKwwRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 AMVFQNYALYPHmSVYDNMAYGL--------------------------------KIRGFGKD-----------HIRQR- 114
Cdd:PTZ00265 463 GVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscraKCAGDLNDmsnttdsneliEMRKNy 541
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 115 --------VEEAARIL----------ELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
Cdd:PTZ00265 542 qtikdsevVDVSKKVLihdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-222 |
1.78e-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: 65.70 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 17 TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRrvtdlepkdrgIAMVFQNYALYPHmSVYDN 96
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 97 MAYGLKIrgfgkDHIRQR-VEEAARILELEPLLKRKPR--------ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDa 167
Cdd:TIGR01271 507 IIFGLSY-----DEYRYTsVIKACQLEEDIALFPEKDKtvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD- 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 168 kLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEV 222
Cdd:TIGR01271 581 -VVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-161 |
2.13e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.15 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 6 LQAVTKSYdGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI------DTRRVTDLEPKdrgIA 79
Cdd:NF033858 4 LEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlggdmaDARHRRAVCPR---IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQ----NyaLYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAV 155
Cdd:NF033858 80 YMPQglgkN--LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
....*.
gi 742395038 156 FLFDEP 161
Cdd:NF033858 158 LILDEP 163
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
5-228 |
2.13e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.52 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 5 KLQAVTKSYdgKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVA----GLERTTSGDIYIDTRRVTDLEPKDRG-IA 79
Cdd:TIGR00956 64 KLKKFRDTK--TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGdVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 80 MVFQNYALYPHMSVYDNMAYGLKIRGFG--------KDHIRQRVEEAARILELEPLLKRKP-----RELSGGQRQRVAMG 146
Cdd:TIGR00956 142 YNAETDVHFPHLTVGETLDFAARCKTPQnrpdgvsrEEYAKHIADVYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 147 RAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLyVTHDQV--EAMTLAQRVIVMNKGvaeqigtpSEVYQ 224
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPL-VAIYQCsqDAYELFDKVIVLYEG--------YQIYF 292
|
....
gi 742395038 225 RPAS 228
Cdd:TIGR00956 293 GPAD 296
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-226 |
4.13e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 62.95 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 17 TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRrvtdlepkdrgIAMVFQNYALYPHmSVYDN 96
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 97 MAYGLKIRGFgkdhirqRVEEAARILELEPLLKRKPRE-----------LSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
Cdd:cd03291 118 IIFGVSYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 166 DAKLRVQMrLELQQLHRRLKTTSLYVThDQVEAMTLAQRVIVMNKGVAEQIGTPSEVY-QRP 226
Cdd:cd03291 191 DVFTEKEI-FESCVCKLMANKTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQsLRP 250
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-161 |
4.70e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGktpvIKQID---LDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDR---G 77
Cdd:PRK10762 5 LQLKGIDKAFPG----VKALSgaaLNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 IAMVFQNYALYPHMSVYDNMAYGLKIRG-FGKDHIRQRVEEAARIL-ELEplLKRKPR----ELSGGQRQRVAMGRAIVR 151
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGREFVNrFGRIDWKKMYAEADKLLaRLN--LRFSSDklvgELSIGEQQMVEIAKVLSF 158
|
170
....*....|
gi 742395038 152 EPAVFLFDEP 161
Cdd:PRK10762 159 ESKVIIMDEP 168
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-194 |
5.93e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 29 DGEFIVMVGPSGCGKSTLLRMVAG--------LERTTSGDIYIDTRRVTDLepkdrgiamvfQNYalypHMSVYDNmayg 100
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVLKRFRGTEL-----------QNY----FKKLYNG---- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 101 lKIRGFGK----DHIRQRV-----------------EEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
Cdd:PRK13409 159 -EIKVVHKpqyvDLIPKVFkgkvrellkkvdergklDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*..
gi 742395038 160 EPLSNLDaklrVQMRLELQQLHRRL--KTTSLYVTHD 194
Cdd:PRK13409 238 EPTSYLD----IRQRLNVARLIRELaeGKYVLVVEHD 270
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-194 |
6.08e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 6.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI-DTRRVTDL--EPKDRGIAMVFQNY 85
Cdd:PRK11819 12 VSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKVGYLpqEPQLDPEKTVRENV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 86 --ALYPHMSVYD-----NMAYGLKIRGFGK------------DH-----IRQRVEEAARILELEPlLKRKPRELSGGQRQ 141
Cdd:PRK11819 92 eeGVAEVKAALDrfneiYAAYAEPDADFDAlaaeqgelqeiiDAadawdLDSQLEIAMDALRCPP-WDAKVTKLSGGERR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 142 RVAMGRAIVREPAVFLFDEPLSNLDAklrvqmrlE----LQQLHRRLKTTSLYVTHD 194
Cdd:PRK11819 171 RVALCRLLLEKPDMLLLDEPTNHLDA--------EsvawLEQFLHDYPGTVVAVTHD 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-166 |
9.18e-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: 63.03 E-value: 9.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI-DTRRvtdlepkdrgIAMVFQNY-A 86
Cdd:TIGR03719 328 LTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVK----------LAYVDQSRdA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 87 LYPHMSVYDNMAYGLKIRGFGKDHIRQRVeEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
Cdd:TIGR03719 397 LDPNKTVWEEISGGLDIIKLGKREIPSRA-YVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-211 |
1.14e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.62 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 23 IDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD---RGIAMVFQNY---ALYPHMSVYDN 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairAGIMLCPEDRkaeGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 97 M---AYGLKIRGFGKDHIRQRVEEAAR-ILELE---PLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDakl 169
Cdd:PRK11288 352 InisARRHHLRAGCLINNRWEAENADRfIRSLNiktPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID--- 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 742395038 170 rVQMRLELQQLHRRL---KTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:PRK11288 429 -VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREG 472
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-194 |
1.31e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 6 LQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRrvtdLEpkdrgIAMvFQNY 85
Cdd:PRK11147 322 MENVNYQIDGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LE-----VAY-FDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 86 --ALYPHMSVYDNMAYGlkirgfgkdhiRQRVEEAAR---ILE------LEPLLKRKP-RELSGGQRQRVAMGRAIVREP 153
Cdd:PRK11147 391 raELDPEKTVMDNLAEG-----------KQEVMVNGRprhVLGylqdflFHPKRAMTPvKALSGGERNRLLLARLFLKPS 459
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 742395038 154 AVFLFDEPLSNLDAKlrvqmRLE-LQQLHRRLKTTSLYVTHD 194
Cdd:PRK11147 460 NLLILDEPTNDLDVE-----TLElLEELLDSYQGTVLLVSHD 496
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-193 |
1.51e-10 |
|
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: 62.46 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 19 VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIdtrrvtdlePKDRGIAMVFQNyalyPHMS------ 92
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQR----PYMTlgtlrd 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 93 --VYDNMAYGLKIRGFGKDHIRQRVEEaariLELEPLLKRK---------PRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
Cdd:TIGR00954 534 qiIYPDSSEDMKRRGLSDKDLEQILDN----VQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 742395038 162 LSnldaKLRVQMRLELQQLHRRLKTTSLYVTH 193
Cdd:TIGR00954 610 TS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-214 |
2.70e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.10 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 19 VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYidtrrvtdlepKDRGIAMVFQNyALYPHMSVYDNMA 98
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 99 yglkirgFGKDHIRQRVEEAARILELEPLLKR-----------KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
Cdd:PTZ00243 743 -------FFDEEDAARLADAVRVSQLEADLAQlgggleteigeKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 742395038 168 KL--RVQMRLELQQLHRRlktTSLYVTHdQVEAMTLAQRVIVMNKGVAE 214
Cdd:PTZ00243 816 HVgeRVVEECFLGALAGK---TRVLATH-QVHVVPRADYVVALGDGRVE 860
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
17-166 |
4.08e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.42 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 17 TPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLE--RTTSGDIYIDTRRVTDLEPKDR---GIAMVFQNYALYPHM 91
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAFQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 92 SVYDNMAYGLK-IRGFGKDHIRQR------VEEAARILELEP-LLKRKPRE-LSGGQRQRVAMGRAIVREPAVFLFDEPL 162
Cdd:PRK09580 94 SNQFFLQTALNaVRSYRGQEPLDRfdfqdlMEEKIALLKMPEdLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESD 173
|
....
gi 742395038 163 SNLD 166
Cdd:PRK09580 174 SGLD 177
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-211 |
4.30e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDGktpvIKQID---LDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRV---TDLEPKDRGIAMVF 82
Cdd:PRK10982 4 ISKSFPG----VKALDnvnLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYALYPHMSVYDNMAYG-LKIRGFGKDHIRQRVEEAARILELEplLKRKPRE----LSGGQRQRVAMGRAIVREPAVFL 157
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGrYPTKGMFVDQDKMYRDTKAIFDELD--IDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 158 FDEPLSNLDAKlrvqmrlELQQLH---RRLKTTS---LYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:PRK10982 158 MDEPTSSLTEK-------EVNHLFtiiRKLKERGcgiVYISHKMEEIFQLCDEITILRDG 210
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-160 |
4.64e-10 |
|
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: 60.58 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSY---DGKTP-VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDlepKDRG-- 77
Cdd:COG4615 328 LELRGVTYRYpgeDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA---DNREay 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 ---IAMVFQNYALYPHMsvydnmaYGLkirgfGKDHIRQRVEEAARILELEPLLKRK-----PRELSGGQRQRVAMGRAI 149
Cdd:COG4615 405 rqlFSAVFSDFHLFDRL-------LGL-----DGEADPARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVAL 472
|
170
....*....|.
gi 742395038 150 VREPAVFLFDE 160
Cdd:COG4615 473 LEDRPILVFDE 483
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-226 |
5.33e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 59.92 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 14 DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLE----RTTSGDIYIDTRRVTDLEPKDR------GIAMVFQ 83
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 N--YALYPHMSVYDNMAYGL---KIRGFGKDHIRQRVEEAARIL------ELEPLLKRKPRELSGGQRQRVAMGRAIVRE 152
Cdd:COG4170 97 EpsSCLDPSAKIGDQLIEAIpswTFKGKWWQRFKWRKKRAIELLhrvgikDHKDIMNSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 153 PAVFLFDEPLSNLDAKLRVQM-RLeLQQLHRRLKTTSLYVTHDqVEAMT-LAQRVIVMNKGVAEQIGTPSEVYQRP 226
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIfRL-LARLNQLQGTSILLISHD-LESISqWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
30-167 |
1.76e-09 |
|
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: 56.87 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 30 GEFIVMVGPSGCGKSTLLRMVAGleRTTS----GDIYIDTRRVTDLEPkdRGIAMVFQNYALYPHMSVYDNMAYGLKIRG 105
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAG--RKTAgvitGEILINGRPLDKNFQ--RSTGYVEQQDVHSPNLTVREALRFSALLRG 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 106 fgkdhirqrveeaarilelepllkrkpreLSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
Cdd:cd03232 109 -----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-212 |
2.06e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTR-RVTDLE---PKD----------RGIAM 80
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlIVARLQqdpPRNvegtvydfvaEGIEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 81 VFQNYALYPHMSV---YDNMAYGL--------KIRGFGKDHIRQRVEEAARILELEPllKRKPRELSGGQRQRVAMGRAI 149
Cdd:PRK11147 94 QAEYLKRYHDISHlveTDPSEKNLnelaklqeQLDHHNLWQLENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 150 VREPAVFLFDEPLSNLDaklrVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGV 212
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGK 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-166 |
2.36e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.98 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 22 QIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVtdlEPKD----RGIAMVFQNYALYPHMSVYDNM 97
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDiatrRRVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742395038 98 AygLKIRGFG--KDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
Cdd:NF033858 361 E--LHARLFHlpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-211 |
2.42e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 18 PVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKD---RGIAMVFQNY---ALYPHM 91
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRkrdGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 92 SVYDNMAYgLKIRGFGKD--HIRQRVEEAA-----RILELE-PLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:PRK10762 346 SVKENMSL-TALRYFSRAggSLKHADEQQAvsdfiRLFNIKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 742395038 164 NLDaklrVQMRLELQQLHRRLKTTSL---YVTHDQVEAMTLAQRVIVMNKG 211
Cdd:PRK10762 425 GVD----VGAKKEIYQLINQFKAEGLsiiLVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-247 |
2.58e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.89 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 14 DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLE----RTTSGDIYIDTRRVTDLEPKDR------GIAMVFQ 83
Cdd:PRK15093 17 DGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 84 --NYALYPHMSVYDNM-----AYGLKIRGFGKDHIRQRveeaaRILEL---------EPLLKRKPRELSGGQRQRVAMGR 147
Cdd:PRK15093 97 epQSCLDPSERVGRQLmqnipGWTYKGRWWQRFGWRKR-----RAIELlhrvgikdhKDAMRSFPYELTEGECQKVMIAI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 148 AIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPA 227
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPH 251
|
250 260 270
....*....|....*....|....*....|.
gi 742395038 228 SLFVAGFI------GSPA-----MNLLPGTL 247
Cdd:PRK15093 252 HPYTQALIraipdfGSAMphksrLNTLPGAI 282
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-224 |
7.06e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.65 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 19 VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLepkdrGIAMVFQNYALYPHMSVYDNMA 98
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI-----GLHDLRFKITIIPQDPVLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 99 YGLKIRGFGKdHIRQRVEEAARILELEPLLKRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
Cdd:TIGR00957 1376 LRMNLDPFSQ-YSDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 742395038 168 K----LRVQMRLELQQlhrrlkTTSLYVTHDQVEAMTLAqRVIVMNKGVAEQIGTPSEVYQ 224
Cdd:TIGR00957 1455 EtdnlIQSTIRTQFED------CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-211 |
7.30e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 21 KQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLEPKDR-GIAMVF-----QNYALYPHMSVY 94
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 95 DNM-AYGLKIRGFGKDHIRQR--VEEAARILELEPLLKRKP-RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklr 170
Cdd:PRK15439 360 WNVcALTHNRRGFWIKPARENavLERYRRALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD---- 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 742395038 171 VQMRLELQQLHRRL---KTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:PRK15439 436 VSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
278-347 |
2.67e-08 |
|
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: 50.31 E-value: 2.67e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 278 LGIRPEHIQLVAQGQGVPLQLQTLELLGADNLAHGQWGGHGVIARL---SHETLPAAGSTLYLQLPAQALHFF 347
Cdd:pfam08402 1 LAIRPEKIRLAAAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRvpnAHARPPAPGDRVGLGWDPEDAHVL 73
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-198 |
3.50e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 6 LQAVTKSYDGKtPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGL-------------ERTTSG----DI------- 61
Cdd:PRK10938 263 LNNGVVSYNDR-PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndltlfgRRRGSGetiwDIkkhigyv 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 62 ----YIDTRRVTDLepKDRGIAMVFQNYALYPHMSvydnmayglkirgfgkDHIRQRVEEAARILELEPLLKRKP-RELS 136
Cdd:PRK10938 342 ssslHLDYRVSTSV--RNVILSGFFDSIGIYQAVS----------------DRQQKLAQQWLDILGIDKRTADAPfHSLS 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742395038 137 GGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEA 198
Cdd:PRK10938 404 WGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-211 |
4.26e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 19 VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAglERTTSGDIYIDTRRVtDLEPKD----RGIAMVFQNYALYPHMSVY 94
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLV-NGRPLDssfqRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 95 DNMAYGLKIRGFGKDHIRQR---VEEAARILELEPL---LKRKPRE-LSGGQRQRVAMGRAIVREPAVFLF-DEPLSNLD 166
Cdd:TIGR00956 855 ESLRFSAYLRQPKSVSKSEKmeyVEEVIKLLEMESYadaVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLD 934
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 742395038 167 AklrvQMRLELQQLHRRLKTT--SLYVTHDQVEAMTLAQ--RVIVMNKG 211
Cdd:TIGR00956 935 S----QTAWSICKLMRKLADHgqAILCTIHQPSAILFEEfdRLLLLQKG 979
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-230 |
7.33e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 14 DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLL----RMVagleRTTSGDIYIDTRRVTD--LEPKDRGIAMVFQNYAL 87
Cdd:PTZ00243 1320 EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 88 YphmsvydnmayglkirgfgKDHIRQRV--------EEAARILELEPLLKRKPRELSG--------------GQRQRVAM 145
Cdd:PTZ00243 1396 F-------------------DGTVRQNVdpfleassAEVWAALELVGLRERVASESEGidsrvleggsnysvGQRQLMCM 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 146 GRAIVREPAVF-LFDEPLSNLDAKLRVQMRLELQQLHRrlKTTSLYVTHdqvEAMTLAQ--RVIVMNKGVAEQIGTPSEV 222
Cdd:PTZ00243 1457 ARALLKKGSGFiLMDEATANIDPALDRQIQATVMSAFS--AYTVITIAH---RLHTVAQydKIIVMDHGAVAEMGSPREL 1531
|
....*...
gi 742395038 223 YQRPASLF 230
Cdd:PTZ00243 1532 VMNRQSIF 1539
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-230 |
1.19e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDLepkdrGIAMVFQNYALYPHMSVY 94
Cdd:PLN03232 1247 GLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF-----GLTDLRRVLSIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 95 DNMAYGLKIRGFgKDHIRQRVEEAARILELEPLLKRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
Cdd:PLN03232 1322 FSGTVRFNIDPF-SEHNDADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 164 NLDAKLRVQMRlelQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQRPASLF 230
Cdd:PLN03232 1401 SVDVRTDSLIQ---RTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-224 |
1.32e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 19 VIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAG--------LERTTSGDIYIDTRRVTDLEPK-------------DRG 77
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggapRGARVTGDVTLNGEPLAAIDAPrlarlravlpqaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 IAMVFQNYAL---YPHmsvydnmayglkIRGFGKDHIRQRvEEAARILEL---EPLLKRKPRELSGGQRQRVAMGRAI-- 149
Cdd:PRK13547 96 FAFSAREIVLlgrYPH------------ARRAGALTHRDG-EIAWQALALagaTALVGRDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 150 -------VREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEV 222
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
..
gi 742395038 223 YQ 224
Cdd:PRK13547 243 LT 244
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-183 |
1.73e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 1 MAGLKL-QAVTKSYDGKTPVIKQidLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRVTDL--EPKDRG 77
Cdd:PRK10938 1 MSSLQIsQGTFRLSDTKTLQLPS--LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLsfEQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 78 IAMVFQ---NYALYPhmsvyDNMAYGLKIRGFGKDHIR--QRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVRE 152
Cdd:PRK10938 79 VSDEWQrnnTDMLSP-----GEDDTGRTTAEIIQDEVKdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSE 153
|
170 180 190
....*....|....*....|....*....|.
gi 742395038 153 PAVFLFDEPLSNLDAKLRVQMRLELQQLHRR 183
Cdd:PRK10938 154 PDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-204 |
1.96e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.06 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 30 GEFIVMVGPSGCGKSTLLRMVAG-LERTTSGDIYIDTrrvtdlepkdrgiamvfqnyalyphmsvydnmayglkirgfgk 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDG------------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 109 dhirQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLE-----LQQLHRR 183
Cdd:smart00382 39 ----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSE 114
|
170 180
....*....|....*....|.
gi 742395038 184 LKTTSLYVTHDQVEAMTLAQR 204
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLR 135
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-166 |
3.11e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 2 AGLKLQAVTKSYDGKTPVIKQIDLD-----VADGEFIV-------------MVGPSGCGKSTLLRMVA------------ 51
Cdd:PLN03073 157 AGMPGVYVNHDGNGGGPAIKDIHMEnfsisVGGRDLIVdasvtlafgrhygLVGRNGTGKTTFLRYMAmhaidgipkncq 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 52 --GLERTTSGD--------IYIDTRRVTDLEPKDRGIAMvfQNYALYPHMSVYDNMAyglKIRGFGKDHIRQRVEEAARI 121
Cdd:PLN03073 237 ilHVEQEVVGDdttalqcvLNTDIERTQLLEEEAQLVAQ--QRELEFETETGKGKGA---NKDGVDKDAVSQRLEEIYKR 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742395038 122 LEL--------------------EPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
Cdd:PLN03073 312 LELidaytaearaasilaglsftPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
15-211 |
3.40e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.27 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 15 GKTPVIKQIDLDVADGEFIVMVGPSGCG--KSTLLRMVAGLE---RTTSGDIYIDTRR-----VTDLEPKDRGIAMVFqn 84
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrRPWRF*TWCANRRalrrtIG*HRPVR*GRRESF-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 85 yalyphmSVYDNMAYGLKIRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
Cdd:NF000106 102 -------SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 742395038 165 LDAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:NF000106 175 LDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRG 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-211 |
3.52e-07 |
|
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: 51.75 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 13 YDGKTPVIKQID---LDVADGEFIVMVGPSGCGKSTLLRMVAGL-ERTTSGDIYIDTRRVTDLEPKD---RGIAMVFQN- 84
Cdd:TIGR02633 266 WDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDr 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 85 --YALYPHMSVYDNMAYGLKIRGFGKDHIRQRVEEAArILELEPLLKRKPRE-------LSGGQRQRVAMGRAIVREPAV 155
Cdd:TIGR02633 346 krHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQI-IGSAIQRLKVKTASpflpigrLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 156 FLFDEPLSNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-166 |
3.65e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 23 IDLDvadgEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYidtrrvtdLEPKDRgIAMVFQNYALYPHMSVyDNMAYGLK 102
Cdd:PLN03073 532 IDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------RSAKVR-MAVFSQHHVDGLDLSS-NPLLYMMR 597
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742395038 103 -IRGFGKDHIRQRVEE--AARILELEPLLKrkpreLSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
Cdd:PLN03073 598 cFPGVPEQKLRAHLGSfgVTGNLALQPMYT-----LSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-194 |
3.73e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.97 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 23 IDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIyidtrrvtdlePKDRGIAMVFQNYALYPHMSVYDNMAYGLK 102
Cdd:PRK13546 43 ISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAISAGLSGQLTGIENIEFKML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 103 IRGFGKDHIRQRVEEAARILELEPLLKRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLrVQMRLELQQLHR 182
Cdd:PRK13546 112 CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF-AQKCLDKIYEFK 190
|
170
....*....|..
gi 742395038 183 RLKTTSLYVTHD 194
Cdd:PRK13546 191 EQNKTIFFVSHN 202
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-166 |
9.04e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 9 VTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYI-DTRRvtdlepkdrgIAMVFQNY-A 86
Cdd:PRK11819 330 LSKSFGDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVK----------LAYVDQSRdA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 87 LYPHMSVYDNMAYGLKIRGFGKdhirqrVEEAARilelePLLKR----------KPRELSGGQRQRVAMGRAIVREPAVF 156
Cdd:PRK11819 399 LDPNKTVWEEISGGLDIIKVGN------REIPSR-----AYVGRfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVL 467
|
170
....*....|
gi 742395038 157 LFDEPLSNLD 166
Cdd:PRK11819 468 LLDEPTNDLD 477
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-230 |
1.03e-06 |
|
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: 49.52 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGK-TPVIKQIDLDVADGEFIVMVGPSGCGKSTL----LRMVAGLErttsGDIYIDTRRVTDLEPkdrgi 78
Cdd:cd03288 20 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPL----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 79 amvfqnYALYPHMSVY--DNMAYGLKIRgFGKDHIRQ----RVEEAARILELEPLLKRKPREL-----------SGGQRQ 141
Cdd:cd03288 91 ------HTLRSRLSIIlqDPILFSGSIR-FNLDPECKctddRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 142 RVAMGRAIVREPAVFLFDEPLSNLD-AKLRVQMRLELQQLHRRlktTSLYVTHdQVEAMTLAQRVIVMNKGVAEQIGTPS 220
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASIDmATENILQKVVMTAFADR---TVVTIAH-RVSTILDADLVLVLSRGILVECDTPE 239
|
250
....*....|
gi 742395038 221 EVYQRPASLF 230
Cdd:cd03288 240 NLLAQEDGVF 249
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
30-168 |
4.28e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 30 GEFIVMVGPSGCGKSTLLRMVAGleRTTSGDIYIDTRrVTDLEPKDRGIAMVF----QNYALYPHMSVYDNMAYGLKIR- 104
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-ISGFPKKQETFARISgyceQNDIHSPQVTVRESLIYSAFLRl 982
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742395038 105 --GFGKDHIRQRVEEAARILELEPLlkrkpRE----------LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
Cdd:PLN03140 983 pkEVSKEEKMMFVDEVMELVELDNL-----KDaivglpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-97 |
5.19e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYdgktPVIKQID---LDVADGEFIVMVGPSGCGKSTLLRMVAGL--ERTTSGDIYID--TRRVTDL-EPKD 75
Cdd:NF040905 2 LEMRGITKTF----PGVKALDdvnLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDgeVCRFKDIrDSEA 77
|
90 100
....*....|....*....|..
gi 742395038 76 RGIAMVFQNYALYPHMSVYDNM 97
Cdd:NF040905 78 LGIVIIHQELALIPYLSIAENI 99
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-224 |
4.18e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 16 KTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIDTRRV---TDLEPKDRGIAMVFQN------YA 86
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnhNANEAINHGFALVTEErrstgiYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 87 --------LYPHMSVYDNMAYGLKIRGFGKDhiRQRVEEAARILElePLLKRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
Cdd:PRK10982 340 yldigfnsLISNIRNYKNKVGLLDNSRMKSD--TQWVIDSMRVKT--PGHRTQIGSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742395038 159 DEPLSNLD--AKLRV-QMRLELQQLHRRLkttsLYVTHDQVEAMTLAQRVIVMNKGVAEQIGTPSEVYQ 224
Cdd:PRK10982 416 DEPTRGIDvgAKFEIyQLIAELAKKDKGI----IIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQ 480
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-206 |
6.83e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 34 VMVGPSGCGKSTLLRmvaGLERTTSGDIYIDTRRVTDLePKDRG-------IAMVFQN-----YALYPHMSVYDNMAYgl 101
Cdd:cd03240 26 LIVGQNGAGKTTIIE---ALKYALTGELPPNSKGGAHD-PKLIRegevraqVKLAFENangkkYTITRSLAILENVIF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 102 kirgfgkdhIRQrvEEAARILELEPllKRkpreLSGGQRQ------RVAMGRAI-VREPAVFLfDEPLSNLDA-----KL 169
Cdd:cd03240 100 ---------CHQ--GESNWPLLDMR--GR----CSGGEKVlasliiRLALAETFgSNCGILAL-DEPTTNLDEenieeSL 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 742395038 170 RVQMRLELQQLHRRLkttsLYVTHDQ--VEAMTLAQRVI 206
Cdd:cd03240 162 AEIIEERKSQKNFQL----IVITHDEelVDAADHIYRVE 196
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-197 |
2.75e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 4 LKLQAVTKSYDGKTpVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVAGLERTTSGDIYIdtrrvtdlepkDRGIAM-VF 82
Cdd:PRK10636 313 LKMEKVSAGYGDRI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-----------AKGIKLgYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 83 QNYAL---------YPHMSVYDNMAYGLKIR------GFGKDHIrqrVEEAARilelepllkrkpreLSGGQRQRVAMGR 147
Cdd:PRK10636 381 AQHQLeflradespLQHLARLAPQELEQKLRdylggfGFQGDKV---TEETRR--------------FSGGEKARLVLAL 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 148 AIVREPAVFLFDEPLSNLDAKLRVQMRLELQQL--------HRR--LKTTS--LYVTHD-QVE 197
Cdd:PRK10636 444 IVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFegalvvvsHDRhlLRSTTddLYLVHDgKVE 506
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-211 |
3.90e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 13 YDGKTPVIKQIDlDVA----DGEFIVMVGPSGCGKSTLLRMVAGLER-TTSGDIYIDTRRVTDLEPKD---RGIAMVFQN 84
Cdd:PRK13549 268 WDPVNPHIKRVD-DVSfslrRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPED 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 85 ---YALYPHMSVYDNMAYGLkIRGFGKdhiRQRVEEAARILELEPLLKR------KPR----ELSGGQRQRVAMGRAIVR 151
Cdd:PRK13549 347 rkrDGIVPVMGVGKNITLAA-LDRFTG---GSRIDDAAELKTILESIQRlkvktaSPElaiaRLSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742395038 152 EPAVFLFDEPLSNLDaklrVQMRLELQQLHRRLKTTS---LYVTHDQVEAMTLAQRVIVMNKG 211
Cdd:PRK13549 423 NPKILILDEPTRGID----VGAKYEIYKLINQLVQQGvaiIVISSELPEVLGLSDRVLVMHEG 481
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
128-229 |
6.28e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 128 LKRKPRELSGGQRQRVAMGRAIVRE--PAVFLFDEPLSNLDAK-----LRVQMRLelqqlhRRLKTTSLYVTHDQvEAMT 200
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRdnrrlINTLKRL------RDLGNTLIVVEHDE-DTIR 554
|
90 100 110
....*....|....*....|....*....|....*..
gi 742395038 201 LAQRVIVMNKG--------VAEqiGTPSEVYQRPASL 229
Cdd:TIGR00630 555 AADYVIDIGPGagehggevVAS--GTPEEILANPDSL 589
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
128-218 |
1.16e-03 |
|
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: 39.23 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742395038 128 LKRKPRELSGGQRQRVAMGRAIVREP--AVFLFDEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTHDqVEAMTLAQRV 205
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHN-LDVLSSADWI 158
|
90
....*....|...
gi 742395038 206 IVMNKGVAEQIGT 218
Cdd:cd03238 159 IDFGPGSGKSGGK 171
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
241-287 |
3.16e-03 |
|
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: 35.11 E-value: 3.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 742395038 241 NLLPGTLsaDGGQLLLaDGMALPLPAAKpQWAGRQLTLGIRPEHIQL 287
Cdd:pfam17850 1 NLFHGRV--EDGRVRI-GGLALPLPELA-GAEGSEVVAYVRPHDLEI 43
|
|
| ABC_MSH6_euk |
cd03286 |
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
14-51 |
8.47e-03 |
|
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213253 [Multi-domain] Cd Length: 218 Bit Score: 37.02 E-value: 8.47e-03
10 20 30
....*....|....*....|....*....|....*...
gi 742395038 14 DGKTPVIKQIDLDVADGEFIVMVGPSGCGKSTLLRMVA 51
Cdd:cd03286 14 TASSFVPNDVDLGATSPRILVLTGPNMGGKSTLLRTVC 51
|
|
| |
