|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-351 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 575.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 161 LSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGSPGMN 240
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 241 FLEASYDAGGVRLkDGTIVPLAKPLPLVDGAKVTLGIRPEHV-LMSDGGAGLAADVELVEPTGFGIILHLALHGLPFKIF 319
Cdd:COG3839 241 LLPGTVEGGGVRL-GGVRLPLPAALAAAAGGEVTLGIRPEHLrLADEGDGGLEATVEVVEPLGSETLVHVRLGGQELVAR 319
|
330 340 350
....*....|....*....|....*....|...
gi 517057676 320 TLTRDALKAGPKVNVAFPAQYLHVFDAE-GKRV 351
Cdd:COG3839 320 VPGDTRLRPGDTVRLAFDPERLHLFDAEtGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-352 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 547.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAY-GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAM 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDE 159
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 160 PLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGSPGM 239
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 240 NFLEASYDAGGVR--LKDGTIVPLAKPLPLVDGAKVTLGIRPEHVLMSDGGAGLAADVELVEPTGFGIILHLALHGLPFK 317
Cdd:PRK11650 241 NLLDGRVSADGAAfeLAGGIALPLGGGYRQYAGRKLTLGIRPEHIALSSAEGGVPLTVDTVELLGADNLAHGRWGGQPLV 320
|
330 340 350
....*....|....*....|....*....|....*.
gi 517057676 318 IFTLTRDALKAGPKVNVAFPAQYLHVFDAE-GKRVD 352
Cdd:PRK11650 321 VRLPHQERPAAGSTLWLHLPANQLHLFDADtGRRIE 356
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-349 |
4.53e-152 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 432.15 E-value: 4.53e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 161 LSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGSPGMN 240
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 241 FL-----EASYDAGGVRLKDGTIVPLakplpLVDGAKV------TLGIRPEHVLMSD-GGAGLAADVELVEPTGFGIILH 308
Cdd:PRK11000 241 FLpvkvtATAIEQVQVELPNRQQVWL-----PVEGRGVqvganmSLGIRPEHLLPSDiADVTLEGEVQVVEQLGNETQIH 315
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 517057676 309 LALHGLPFKIFTLTRDAL--KAGPKVNVAFPAQYLHVFDAEGK 349
Cdd:PRK11000 316 IQIPAIRQNLVYRQNDVVlvEEGATFAIGLPPERCHLFREDGT 358
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-346 |
6.81e-148 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 421.04 E-value: 6.81e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 161 LSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGSpgMN 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGE--AN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 241 FLEA---SYDAGGVRLkDGTIVPLAKPLPLVDGAKVTLGIRPEHVLMSDGGA--GLAADVELVEPTGFGIILHLAL-HGL 314
Cdd:COG3842 241 LLPGtvlGDEGGGVRT-GGRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGPenGLPGTVEDVVFLGSHVRYRVRLgDGQ 319
|
330 340 350
....*....|....*....|....*....|....
gi 517057676 315 PFKIFTLTRDA--LKAGPKVNVAFPAQYLHVFDA 346
Cdd:COG3842 320 ELVVRVPNRAAlpLEPGDRVGLSWDPEDVVVLPA 353
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
1.08e-121 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 349.25 E-value: 1.08e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQS 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517057676 164 LDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVG 216
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-343 |
3.09e-115 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 337.89 E-value: 3.09e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVN-ELHPKDRDIAMVF 81
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 82 QSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPL 161
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 162 SNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGSpgMNF 241
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGC--VNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 242 LEASYDAGGVRLkDGTIVPLAKPLPlvdGAKVTLGIRPEHVLMS---DGGAGLAADVELVEPTGFGIILHLALHGLPFKI 318
Cdd:COG1118 240 LRGRVIGGQLEA-DGLTLPVAEPLP---DGPAVAGVRPHDIEVSrepEGENTFPATVARVSELGPEVRVELKLEDGEGQP 315
|
330 340 350
....*....|....*....|....*....|..
gi 517057676 319 FT--LTRDA-----LKAGPKVNVAFPAQYLHV 343
Cdd:COG1118 316 LEaeVTKEAwaelgLAPGDPVYLRPRPARVFL 347
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-344 |
1.96e-108 |
|
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: 320.83 E-value: 1.96e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMV 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 161 LSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGSpgMN 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE--VN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 241 FLEASYDAGGVRLKDGTIVPLAKPLPLvDGAKVTLGIRPEHVLMSDGGA---GLAADVELVEPTGFGIILHLALHGLPFK 317
Cdd:TIGR03265 240 WLPGTRGGGSRARVGGLTLACAPGLAQ-PGASVRLAVRPEDIRVSPAGNaanLLLARVEDMEFLGAFYRLRLRLEGLPGQ 318
|
330 340 350
....*....|....*....|....*....|....
gi 517057676 318 IF-------TLTRDALKAGPKVNVAFPAQYLHVF 344
Cdd:TIGR03265 319 ALvadvsasEVERLGIRAGQPIWIELPAERLRAF 352
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-280 |
1.90e-105 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 314.19 E-value: 1.90e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQS 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 164 LDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGSpgMNFLE 243
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE--INIFD 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 517057676 244 ASYDAggvRLKD--------GTIVPLAKPLPLVDGAKVTLGIRPE 280
Cdd:PRK09452 253 ATVIE---RLDEqrvranveGRECNIYVNFAVEPGQKLHVLLRPE 294
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-235 |
4.05e-105 |
|
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: 308.01 E-value: 4.05e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQS 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 164 LDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIG 235
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
4.59e-104 |
|
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: 304.44 E-value: 4.59e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQS 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517057676 164 LDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVG 216
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-344 |
1.18e-94 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 285.74 E-value: 1.18e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 2 ASIDIQNIRKAYGH----VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELH-----P 72
Cdd:NF040933 1 VTVRVENVTKIFKKgkkeVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASPGkiivpP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 73 KDRDIAMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQP 152
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 153 KAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAG 232
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 233 FIGSpgMNFLEASYDAGGVRLKDGTIVPLakPLPLVDGAKVTLGIRPEHVLMSDGGAGLA--------ADVELVEPTGFG 304
Cdd:NF040933 241 LIGD--INLLEGKVEEEGLVDGNDLKIPL--PNPKLEAGEVIIGIRPEDIDISESDMRLPpgfvevgkGRVKVSSYAGGV 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 517057676 305 IILHLA-LHGLPFKIFTLTRDALKAGPKVNVAFPAQYLHVF 344
Cdd:NF040933 317 FRVVVSpIDDDSIEIIVNSDRPIEEGEEVNLYVRPDKIKIF 357
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-288 |
7.04e-91 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 275.83 E-value: 7.04e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQS 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 164 LDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGSPgmNFLE 243
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIFP 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 517057676 244 ASYDAGGVRLKDGTIV-PLAKPLPLVDGAkVTLGIRPEHVLMSDGG 288
Cdd:PRK11432 245 ATLSGDYVDIYGYRLPrPAAFAFNLPDGE-CTVGVRPEAITLSEQG 289
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-236 |
2.85e-90 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 270.36 E-value: 2.85e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQ 82
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 SYALYPHMNVAGNMSYSLRLRKVA----KEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFD 158
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 159 EPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGS 236
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-235 |
3.07e-88 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 265.12 E-value: 3.07e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQS 83
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 164 LDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIG 235
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-282 |
9.67e-83 |
|
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: 254.34 E-value: 9.67e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 34 LVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASA 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 114 VAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHD 193
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 194 QIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGSPGM-NFLEASYDAGGVRLKDGTIVPLA--KPLPLVDG 270
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVfEATVIERKSEQVVLAGVEGRRCDiyTDVPVEKD 240
|
250
....*....|..
gi 517057676 271 AKVTLGIRPEHV 282
Cdd:TIGR01187 241 QPLHVVLRPEKI 252
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-344 |
1.38e-82 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 254.62 E-value: 1.38e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQvLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQS 83
Cdd:NF040840 2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:NF040840 81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 164 LDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGSPGMNFLE 243
Cdd:NF040840 161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 244 ASYDAGGVRLKDGTIVplaKPLPLVDGAKVTLGIRPEHVLMSDGGAGLAA------DVELVEPTGFGIILHLALhGLPFK 317
Cdd:NF040840 241 AEKGGEGTILDTGNIK---IELPEEKKGKVRIGIRPEDITISTEKVKTSArnefkgKVEEIEDLGPLVKLTLDV-GIILV 316
|
330 340 350
....*....|....*....|....*....|..
gi 517057676 318 IFtLTRDAL-----KAGPKVNVAFPAQYLHVF 344
Cdd:NF040840 317 AF-ITRSSFldleiNEGKEVYASFKASAVHVF 347
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
1.12e-81 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 249.24 E-value: 1.12e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAY----GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPkdrD 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 77 IAMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517057676 157 FDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-286 |
1.37e-81 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 252.31 E-value: 1.37e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQ 82
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 SYALYPHMNVAGNMSYSL----RLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFD 158
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 159 EPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGSpg 238
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE-- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 517057676 239 MNFLEasydaGGVRLKDGTIVPLAKPL---PLVDGaKVTLGIRPEHVLMSD 286
Cdd:PRK10851 240 VNRLQ-----GTIRGGQFHVGAHRWPLgytPAYQG-PVDLFLRPWEVDISR 284
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-209 |
1.71e-79 |
|
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: 242.38 E-value: 1.71e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGH----VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPkdrDIAM 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517057676 160 PLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHG 209
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-235 |
2.05e-78 |
|
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: 239.93 E-value: 2.05e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQvLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQS 83
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 164 LDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIG 235
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-237 |
2.58e-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: 232.19 E-value: 2.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQ-VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMV 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDP--LLERRPKALSGGQRQRVAMGRAIVRQPKAFLFD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517057676 159 EPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGSP 237
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-265 |
2.54e-74 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 231.90 E-value: 2.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQV-LHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMV 80
Cdd:COG1125 2 IEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDP--LLERRPKALSGGQRQRVAMGRAIVRQPKAFLFD 158
Cdd:COG1125 82 IQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADPPILLMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 159 EPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGSPG 238
Cdd:COG1125 162 EPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGADR 241
|
250 260
....*....|....*....|....*..
gi 517057676 239 MNFLEASYDAGGVRLKDGTIVPLAKPL 265
Cdd:COG1125 242 GLRRLSLLRVEDLMLPEPPTVSPDASL 268
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-286 |
2.87e-73 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 231.65 E-value: 2.87e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQS 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 164 LDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIGSPGM--NF 241
Cdd:PRK11607 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVfeGV 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 517057676 242 LEASYDAGGVRLKDGTIVPLA--KPLPLVDGAKVTLGIRPEHVLMSD 286
Cdd:PRK11607 260 LKERQEDGLVIDSPGLVHPLKvdADASVVDNVPVHVALRPEKIMLCE 306
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-210 |
1.93e-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: 217.44 E-value: 1.93e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELH----PKDRDIAM 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALYPHMNVAGNMSYslrlrkvakekiasavaaaaaklgldpllerrpkALSGGQRQRVAMGRAIVRQPKAFLFDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517057676 160 PLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-212 |
1.86e-67 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 211.19 E-value: 1.86e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYG----HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRD--- 76
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 77 ---IAMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPK 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517057676 154 AFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQiEAMTLADRIVAMHGGVV 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-227 |
3.74e-66 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 208.69 E-value: 3.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNeLHPKD-----RDIA 78
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDinklrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQSYALYPHMNVAGNMSYSLR-LRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLF 157
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 158 DEPLSNLDArlreQMRAEIKKLHGDLKA---TSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPAN 227
Cdd:COG1126 161 DEPTSALDP----ELVGEVLDVMRDLAKegmTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
1.27e-65 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 206.82 E-value: 1.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MAS-IDIQNIRKAYG----HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR 75
Cdd:COG1136 1 MSPlLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 76 D------IAMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIV 149
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 150 RQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQiEAMTLADRIVAMHGGVV 212
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-234 |
3.49e-65 |
|
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: 207.50 E-value: 3.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 9 IRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD------RDIAMVFQ 82
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 SYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLS 162
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 163 NLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFI 234
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-216 |
2.93e-63 |
|
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: 200.60 E-value: 2.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 22 VDLEIhDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNE------LHPKDRDIAMVFQSYALYPHMNVAGN 95
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 96 MSYSLRLRKVAKEKIASAVAAAAakLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAE 175
Cdd:cd03297 96 LAFGLKRKRNREDRISVDELLDL--LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517057676 176 IKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVG 216
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-221 |
1.43e-61 |
|
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: 197.12 E-value: 1.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRD-----IA 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrrIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQSYALYPHMNVAGNMSYSLR---------LRKVAKEKIASavaaaaakLGLDPLLERRPKALSGGQRQRVAMGRAIV 149
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLRehtdlseaeIRELVLEKLEL--------VGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 150 RQPKAFLFDEPLSNLD---ARLREQMraeIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:COG1127 158 LDPEILLYDEPTAGLDpitSAVIDEL---IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-235 |
9.01e-61 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 198.92 E-value: 9.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 11 KAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHP------KDRDIAMVFQSY 84
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 85 ALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNL 164
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057676 165 DARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIG 235
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-224 |
3.73e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 193.36 E-value: 3.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRD-IAMVFQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 SYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLS 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 163 NLDARLREQMRAEIKKLHGDlKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDR 224
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-285 |
4.90e-60 |
|
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: 196.86 E-value: 4.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 22 VDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGV-------RVNeLHPKDRDIAMVFQSYALYPHMNVAG 94
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsarGIF-LPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 95 NMSYSLRLRKVAKEKIASAVAAAAakLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRA 174
Cdd:COG4148 97 NLLYGRKRAPRAERRISFDEVVEL--LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 175 EIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGfiGSPGMNFLEA---SYDAGG- 250
Cdd:COG4148 175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAGSVLEAtvaAHDPDYg 252
|
250 260 270
....*....|....*....|....*....|....*....
gi 517057676 251 ---VRLKDGTI-VPLakpLPLVDGAKVTLGIRPEHVLMS 285
Cdd:COG4148 253 ltrLALGGGRLwVPR---LDLPPGTRVRVRIRARDVSLA 288
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-235 |
2.02e-58 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 188.81 E-value: 2.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHvQVLHgVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQS 83
Cdd:COG3840 2 LRLDDLTYRYGD-FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGN----MSYSLRLRKVAKEKIASAVAaaaaKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDE 159
Cdd:COG3840 80 NNLFPHLTVAQNiglgLRPGLKLTAEQRAQVEQALE----RVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 160 PLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGFIG 235
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-212 |
5.47e-58 |
|
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: 186.97 E-value: 5.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVN----ELHPKDRDIAM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALYPHMNVAGNMSYSLR-LRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 159 EPLSNLDArlreQMRAEIKKLHGDLKA---TSIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:cd03262 161 EPTSALDP----ELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
1.67e-57 |
|
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: 186.93 E-value: 1.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYG----HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDI 77
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSY--ALYPHMNVAGNMSYSLRLRKVAkeKIASAVAAAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAIVRQPKA 154
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517057676 155 FLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDqIEAMT-LADRIVAMHGGVVQQVGSPLELYDRPAN 227
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-227 |
2.65e-57 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 186.07 E-value: 2.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDI----AM 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALYPHMNVAGNMSYS-LRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFD 158
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 159 EPLSNLDARLREqmraEIKKLHGDLK---ATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPAN 227
Cdd:PRK09493 162 EPTSALDPELRH----EVLKVMQDLAeegMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-210 |
5.27e-57 |
|
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: 184.21 E-value: 5.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGH--VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVF 81
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 82 QsyalYP-HM----NVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFL 156
Cdd:cd03225 82 Q----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517057676 157 FDEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-226 |
1.25e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 184.49 E-value: 1.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY-GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD-----RDI 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYPHMNV-----AGNMSY--SLR--LRKVAKEKIASAVAAAAaKLGLDPLLERRPKALSGGQRQRVAMGRAI 148
Cdd:COG3638 83 GMIFQQFNLVPRLSVltnvlAGRLGRtsTWRslLGLFPPEDRERALEALE-RVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517057676 149 VRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHdQIE-AMTLADRIVAMHGGVVqqvgspleLYDRPA 226
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDGRV--------VFDGPP 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-221 |
1.60e-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: 183.86 E-value: 1.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD-----RDIA 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQSYALYPHMNVAGNMSYSLR---------LRKVAKEKIASavaaaaakLGLDPLLERRPKALSGGQRQRVAMGRAIV 149
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLRehtrlseeeIREIVLEKLEA--------VGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 150 RQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-228 |
2.91e-56 |
|
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: 182.92 E-value: 2.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY-GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMV 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQsyalYP-----HMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAF 155
Cdd:COG1122 81 FQ----NPddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 156 LFDEPLSNLDARLREQMRAEIKKLHGDLKaTSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANL 228
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-225 |
1.86e-55 |
|
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: 188.96 E-value: 1.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY-----GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD---- 74
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 -RDIAMVFQ--SYALYPHMNVAGNMSYSLRLRKVA-KEKIASAVAAAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAIV 149
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 150 RQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDqIEAM-TLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHD-LAVVrYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-212 |
5.55e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 178.86 E-value: 5.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVF 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 82 QSYALYPhMNVAGNMS--YSLRLRKVAKEKIasavAAAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAIVRQPKAFLFD 158
Cdd:COG4619 81 QEPALWG-GTVRDNLPfpFQLRERKFDRERA----LELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517057676 159 EPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-224 |
3.88e-54 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 178.13 E-value: 3.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR-DIAMVFQ 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 SYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLS 162
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 163 NLDARLREQMRAEIKKLhGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDR 224
Cdd:COG4555 162 GLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-210 |
3.84e-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: 172.31 E-value: 3.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY----GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR---- 75
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 76 -DIAMVFQSY--ALYPHMNVAGNMSYSLRLRKV--AKEKIASAVAAAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAIV 149
Cdd:cd03257 82 kEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKlsKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 150 RQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDqIEAM-TLADRIVAMHGG 210
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHD-LGVVaKIADRVAVMYAG 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-210 |
1.78e-51 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 171.58 E-value: 1.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYG----HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNelHPkDRD 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GP-GAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 77 IAMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFL 156
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517057676 157 FDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-216 |
4.31e-51 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 169.46 E-value: 4.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGH-VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD-----RDI 77
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLF 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 158 DEPLSNLDARLREQ-MRAeIKKLHgDLKATSIYVTHDQ--IEAMtlADRIVAMHGGVVQQVG 216
Cdd:COG2884 162 DEPTGNLDPETSWEiMEL-LEEIN-RRGTTVLIATHDLelVDRM--PKRVLELEDGRLVRDE 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-221 |
1.61e-50 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 169.07 E-value: 1.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVF 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 82 QS--------------YALYPHMNVAGNMSYslRLRKVAKEKIasavaaaaAKLGLDPLLERRPKALSGGQRQRVAMGRA 147
Cdd:COG1120 82 QEppapfgltvrelvaLGRYPHLGLFGRPSA--EDREAVEEAL--------ERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517057676 148 IVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-223 |
8.37e-50 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 166.59 E-value: 8.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGH-VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD-----RDI 77
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYPHMNVAGN--------MSySLR--LRKVAKEKIaSAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRA 147
Cdd:cd03256 81 GMIFQQFNLIERLSVLENvlsgrlgrRS-TWRslFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 148 IVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYD 223
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
1.35e-49 |
|
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: 165.83 E-value: 1.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGH----VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD----- 74
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 RDIAMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKA 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 155 FLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHdQIEAM-TLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-214 |
2.28e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 165.57 E-value: 2.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVN---ELHPKD----- 74
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAirllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 RDIAMVFQSYALYPHMNVAGNMSYS-LRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPK 153
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 154 AFLFDEPLSNLDARLREQMRAEIKKLhGDLKATSIYVTHDQIEAMTLADRIVAM-HGGVVQQ 214
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMeKGRIIEQ 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-212 |
2.23e-48 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 162.28 E-value: 2.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHvQVLHgVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQS 83
Cdd:cd03298 1 VRLDKIRFSYGE-QPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGNM----SYSLRLRKVAKEKIASAVAaaaaKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDE 159
Cdd:cd03298 79 NNLFAHLTVEQNVglglSPGLKLTAEDRQAIEVALA----RVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517057676 160 PLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-228 |
3.78e-48 |
|
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: 169.70 E-value: 3.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY--GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGL---EEVTSGEIRIAGVRVNELHPKDR--D 76
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 77 IAMVFQS--YALYPhMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKA 154
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517057676 155 FLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANL 228
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-218 |
4.88e-48 |
|
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: 161.58 E-value: 4.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEV-----TSGEIRIAGVRVNELHPKD---- 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 RDIAMVFQSYALYPhMNVAGNMSYSLRLRKVA-KEKIASAVAAAAAKLGLDPLLERRPKA--LSGGQRQRVAMGRAIVRQ 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKlKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 152 PKAFLFDEPLSNLDARLREQMRAEIKKLHGDLkaTSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSP 218
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
7.53e-48 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 159.49 E-value: 7.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR-DIAMVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 SYALYPHMNVAGNMSYslrlrkvakekiasavaaaaaklgldpllerrpkalSGGQRQRVAMGRAIVRQPKAFLFDEPLS 162
Cdd:cd03230 81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517057676 163 NLDARLREQMRAEIKKLHGDLKaTSIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGK-TILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-226 |
9.81e-48 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 164.90 E-value: 9.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 8 NIRKAYGHVQVlhGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNE------LHPKDRDIAMVF 81
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 82 QSYALYPHMNVAGNMSYSLR-----LRKVAKEKIASAvaaaaakLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFL 156
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKrarpsERRISFERVIEL-------LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 157 FDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPA 226
Cdd:TIGR02142 155 MDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-214 |
1.20e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 161.34 E-value: 1.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVN---ELHPKD----- 74
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAirelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 RDIAMVFQSYALYPHMNVAGNMSYS-LRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPK 153
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 154 AFLFDEPLSNLDARLREQMRAEIKKLHGdLKATSIYVTHDQIEAMTLADRIVAMHGG-VVQQ 214
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGhIVEQ 222
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-216 |
2.19e-47 |
|
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: 159.64 E-value: 2.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 23 DLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQSYALYPHMNVAGNMSY---- 98
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLglhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 99 SLRLRKVAKEKIASAVAaaaaKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKK 178
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQ----QVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 517057676 179 LHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVG 216
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-237 |
4.80e-47 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 162.55 E-value: 4.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY----GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD----- 74
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 RDIAMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVaaaaaklglDPLLE---------RRPKALSGGQRQRVAMG 145
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRV---------AELLElvglsdkadAYPSQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 146 RAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDqieaM----TLADRIVAMHGGVVQQVGSPLEL 221
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLDV 228
|
250
....*....|....*.
gi 517057676 222 YDRPANLFVAGFIGSP 237
Cdd:COG1135 229 FANPQSELTRRFLPTV 244
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-210 |
9.86e-47 |
|
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: 155.87 E-value: 9.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQs 83
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 yalyphmnvagnmsyslrlrkvakekiasavaaaaaklgldpllerrpkaLSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517057676 164 LDARLREQMRAEIKKLHgDLKATSIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:cd00267 111 LDPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-210 |
3.94e-46 |
|
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: 156.25 E-value: 3.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY-GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD-----RDI 77
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLF 157
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517057676 158 DEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-225 |
1.04e-45 |
|
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: 155.70 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 19 LHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPkdrDIAMVFQSYALYPHMNVAGNMSY 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 99 SLR-----LRKVAKEKIASAVAAAaakLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMR 173
Cdd:TIGR01184 78 AVDrvlpdLSKSERRAIVEEHIAL---VGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517057676 174 AEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLEL-YDRP 225
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-236 |
8.99e-45 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 154.19 E-value: 8.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGV-------RVNELHPKDRD 76
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdRDGELVPADRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 77 --------IAMVFQSYALYPHMNVAGN-MSYSLRLRKVAKEKIASAVAAAAAKLGLdplLERR---PKALSGGQRQRVAM 144
Cdd:COG4598 89 qlqrirtrLGMVFQSFNLWSHMTVLENvIEAPVHVLGRPKAEAIERAEALLAKVGL---ADKRdayPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 145 GRAIVRQPKAFLFDEPLSNLDARLreqmRAEIKKLHGDLKA---TSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPEL----VGEVLKVMRDLAEegrTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
250
....*....|....*
gi 517057676 222 YDRPANLFVAGFIGS 236
Cdd:COG4598 242 FGNPKSERLRQFLSS 256
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-214 |
1.17e-44 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 152.97 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY----GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVrvnELHPKDRD--- 76
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDEDara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 77 ------IAMVFQSYALYPHM----NVAgnMSYSLRLRKVAKEKiasaVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGR 146
Cdd:COG4181 86 rlrarhVGFVFQSFQLLPTLtaleNVM--LPLELAGRRDARAR----ARALLERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057676 147 AIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQieamTLA---DRIVAMHGGVVQQ 214
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP----ALAarcDRVLRLRAGRLVE 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-212 |
1.34e-44 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 153.68 E-value: 1.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIrIAGVrvNELHPKDRDIAMVFQSYA 85
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT--APLAEAREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 86 LYPHMNVAGNMSYSLR--LRKVAKEKIASavaaaaakLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:PRK11247 92 LLPWKKVIDNVGLGLKgqWRDAALQALAA--------VGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517057676 164 LDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-228 |
1.67e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.94 E-value: 1.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNElhpKDRDIAMV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPH----------MNVAGNMSYSLRLRKVAKEKIasavAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVR 150
Cdd:COG1121 81 PQRAEVDWDfpitvrdvvlMGRYGRRGLFRRPSRADREAV----DEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 151 QPKAFLFDEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQvGSPLElYDRPANL 228
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEE-VLTPENL 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-225 |
4.16e-44 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 152.21 E-value: 4.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD------ 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 ----RDIAMVFQSYALYPHMNVAGN-MSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIV 149
Cdd:PRK11264 81 rqlrQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 150 RQPKAFLFDEPLSNLDARLREQMRAEIKKLhGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
6.54e-44 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 149.51 E-value: 6.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 5 DIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 SYALyphmnvagnmsyslrlrkvakekiasavaaaaakLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLS 162
Cdd:cd03214 81 ALEL----------------------------------LGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517057676 163 NLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVG 216
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-209 |
6.72e-44 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 150.32 E-value: 6.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAG-LEEV--TSGEIRIAGVRVNELHPKDRDIAM 79
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALYPHMNVAGNMSYSLRlRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDE 159
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517057676 160 PLSNLDARLREQMRA----EIKKLHGdlkaTSIYVTHDqIEAMTLADRIVAMHG 209
Cdd:COG4136 160 PFSKLDAALRAQFREfvfeQIRQRGI----PALLVTHD-EEDAPAAGRVLDLGN 208
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-210 |
1.77e-43 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 147.91 E-value: 1.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYG--HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAM 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALYpHMNVAGNMsyslrlrkvakekiasavaaaaaklgldpllerrpkaLSGGQRQRVAMGRAIVRQPKAFLFDE 159
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517057676 160 PLSNLDARLREQMRAEIKKLHGDlkATSIYVTHDqIEAMTLADRIVAMHGG 210
Cdd:cd03228 123 ATSALDPETEALILEALRALAKG--KTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-224 |
7.00e-43 |
|
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: 157.69 E-value: 7.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYG--HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIA 78
Cdd:COG2274 473 DIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQSYALYpHMNVAGNMSYSL------RLRKVAKekiasavaaaaaKLGLDPLLERRPK-----------ALSGGQRQR 141
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLGDpdatdeEIIEAAR------------LAGLHDFIEALPMgydtvvgeggsNLSGGQRQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 142 VAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDlkATSIYVTHDqIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
...
gi 517057676 222 YDR 224
Cdd:COG2274 697 LAR 699
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-223 |
8.34e-43 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 148.60 E-value: 8.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGH-VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD-----RDI 77
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYPHMNV-----AGNMSYSLRLRKVA---KEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIV 149
Cdd:TIGR02315 82 GMIFQHYNLIERLTVlenvlHGRLGYKPTWRSLLgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517057676 150 RQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYD 223
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-228 |
3.44e-42 |
|
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: 147.98 E-value: 3.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 17 QVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVN-----ELHPKDRDIAMVFQsyalYPHM- 90
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDLRKKVGLVFQ----FPEHq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 91 ----NVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLD 165
Cdd:TIGR04521 95 lfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 166 ARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANL 228
Cdd:TIGR04521 175 PKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDEL 237
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-212 |
4.79e-42 |
|
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: 145.63 E-value: 4.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGH-VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD-----RDI 77
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLF 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 158 DEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
1.23e-41 |
|
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: 144.96 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYG--HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNElHPKD--RDIAM 79
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAarQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDE 159
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 160 PLSNLDARLREQMRAEIKKLHGdlKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-233 |
6.93e-41 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 147.87 E-value: 6.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 24 LEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD------RDIAMVFQSYALYPHMNVAGNMS 97
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 98 YSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIK 177
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 178 KLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGF 233
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
8-204 |
9.31e-41 |
|
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: 142.49 E-value: 9.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 8 NIRKAYGH----VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR------DI 77
Cdd:TIGR02211 6 NLGKRYQEgkldTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLF 157
Cdd:TIGR02211 86 GFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517057676 158 DEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDqieaMTLADRI 204
Cdd:TIGR02211 166 DEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHD----LELAKKL 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-209 |
1.04e-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: 139.15 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 2 ASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPK-DRDIAMV 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNVAGNMSYSLRLRKVAKEkiASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517057676 161 LSNLD----ARLREQMRAeikklHGDLKATSIYVTHDQIEAmtLADRIVAMHG 209
Cdd:COG4133 159 FTALDaagvALLAELIAA-----HLARGGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-221 |
1.27e-39 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 140.10 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 23 DLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQSYALYPHMNVAGN----MSY 98
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNiglgLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 99 SLRLRKVAKEKIasavAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKK 178
Cdd:PRK10771 99 GLKLNAAQREKL----HAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517057676 179 LHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-205 |
1.32e-39 |
|
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: 138.90 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD-----RD-IAM 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrREkLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDE 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517057676 160 PLSNLDARLREqmraEIKKLHGDLK---ATSIYVTHDQiEAMTLADRIV 205
Cdd:TIGR03608 161 PTGSLDPKNRD----EVLDLLLELNdegKTIIIVTHDP-EVAKQADRVI 204
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-226 |
1.47e-39 |
|
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: 140.71 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 12 AYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD-----RDIAMVFQ-SY- 84
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQdSPs 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 85 ALYPHMNVAGNMSYSLR-LRKVAKEKIASAVAAAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLS 162
Cdd:TIGR02769 100 AVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 163 NLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGG--VVQQVGSPLELYDRPA 226
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGqiVEECDVAQLLSFKHPA 245
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-207 |
1.49e-39 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 140.61 E-value: 1.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNElhpKDRDIAMVFQSYA 85
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG---PGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 86 LYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLD 165
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517057676 166 ARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAM 207
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLL 202
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
1.85e-39 |
|
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: 140.64 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY--GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVR-VNELHPKD--RDIA 78
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEirKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQsyalyphmN---------VAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIV 149
Cdd:TIGR04520 81 MVFQ--------NpdnqfvgatVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 150 RQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDqIEAMTLADRIVAMHGGVVQQVGSPLELY 222
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHD-MEEAVLADRVIVMNKGKIVAEGTPREIF 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-212 |
1.89e-39 |
|
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: 137.17 E-value: 1.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD---RDIAMV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQsyalyphmnvagnmsyslrlrkvakekiasavaaaaaklgldpllerrpkaLSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517057676 161 LSNLDARLREQMRAEIKKLHGDlKATSIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
3.51e-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: 146.06 E-value: 3.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 2 ASIDIQNIRKAY-GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIA 78
Cdd:COG4988 335 PSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQSYALyPHMNVAGNmsysLRL----------RKVAKekiasavaaaaaKLGLDPLLERRPK-----------ALSGG 137
Cdd:COG4988 415 WVPQNPYL-FAGTIREN----LRLgrpdasdeelEAALE------------AAGLDEFVAALPDgldtplgeggrGLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 138 QRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDlkATSIYVTHDqIEAMTLADRIVAMHGGVVQQVGS 217
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHR-LALLAQADRILVLDDGRIVEQGT 554
|
....*
gi 517057676 218 PLELY 222
Cdd:COG4988 555 HEELL 559
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-216 |
8.87e-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: 137.50 E-value: 8.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY----GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNElHPKD--RDI 77
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEarRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLF 157
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517057676 158 DEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVG 216
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-226 |
1.02e-38 |
|
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: 140.19 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY----GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEE---VTSGEIRIAGVRVNELHPKD-- 74
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 ----RDIAMVFQ-SY-ALYPHMNVAGNMSYSLRL-----RKVAKEKIasavAAAAAKLGLDP---LLERRPKALSGGQRQ 140
Cdd:COG0444 82 kirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhgglsKAEARERA----IELLERVGLPDperRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 141 RVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHD-----QIeamtlADRIVAMHGGVVQQV 215
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDlgvvaEI-----ADRVAVMYAGRIVEE 232
|
250
....*....|.
gi 517057676 216 GSPLELYDRPA 226
Cdd:COG0444 233 GPVEELFENPR 243
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-226 |
1.47e-38 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 139.87 E-value: 1.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 10 RKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD-----RDIAMVFQ-S 83
Cdd:COG4608 25 GRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQdP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YA-LYPHMNVAGNMSYSLRLRKVA-KEKIASAVAAAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:COG4608 105 YAsLNPRMTVGDIIAEPLRIHGLAsKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 161 LSNLDArlreQMRAEIKKLHGDLKA----TSIYVTHD-----QIeamtlADRIVAMHGGVVQQVGSPLELYDRPA 226
Cdd:COG4608 185 VSALDV----SIQAQVLNLLEDLQDelglTYLFISHDlsvvrHI-----SDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-162 |
1.49e-38 |
|
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: 134.31 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 19 LHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAG--VRVNELHPKDRDIAMVFQSYALYPHMNVAGNM 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 97 SYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERR----PKALSGGQRQRVAMGRAIVRQPKAFLFDEPLS 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-221 |
2.17e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 144.15 E-value: 2.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAY-GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAM 79
Cdd:COG1132 339 EIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALYpHMNVAGNMSYSL------RLRKVAK-----EKIasavaaaaAKL--GLDPLLERRPKALSGGQRQRVAMGR 146
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYGRpdatdeEVEEAAKaaqahEFI--------EALpdGYDTVVGERGVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 147 AIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDlkATSIYVTHdQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMKG--RTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-236 |
4.05e-38 |
|
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: 136.50 E-value: 4.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAG-------VRVNELHPKD-- 74
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGeqlyhmpGRNGPLVPADek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 ------RDIAMVFQSYALYPHMNVAGNMSYS-LRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRA 147
Cdd:TIGR03005 81 hlrqmrNKIGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 148 IVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPAN 227
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
....*....
gi 517057676 228 LFVAGFIGS 236
Cdd:TIGR03005 241 ERTREFLSK 249
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
4.79e-38 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 136.37 E-value: 4.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVF 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 82 QSyalyPHMN--------VA-GNMSYSL-RLRKVAKEKIASAVAAaaakLGLDPLLERRPKALSGGQRQR--VAMgrAIV 149
Cdd:COG4604 82 QE----NHINsrltvrelVAfGRFPYSKgRLTAEDREIIDEAIAY----LDLEDLADRYLDELSGGQRQRafIAM--VLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 150 RQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-221 |
5.37e-38 |
|
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: 135.25 E-value: 5.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR---DIAMV 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNVAGN--MSYSLRLRKVAKEKIASAvaaaaakLGLDPLLERRPKA----LSGGQRQRVAMGRAIVRQPKA 154
Cdd:cd03224 81 PEGRRIFPELTVEENllLGAYARRRAKRKARLERV-------YELFPRLKERRKQlagtLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 155 FLFDEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-226 |
1.40e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 135.58 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHV---------QVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELH 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 72 PKD-----RDIAMVFQSY--ALYPHMNVAGNMSYSLR-LRKVAKEKIASAVAAAAAKLGLDP-LLERRPKALSGGQRQRV 142
Cdd:PRK10419 81 RAQrkafrRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 143 AMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGG--VVQQVGSPLE 220
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGqiVETQPVGDKL 240
|
....*.
gi 517057676 221 LYDRPA 226
Cdd:PRK10419 241 TFSSPA 246
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-222 |
1.91e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 135.95 E-value: 1.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYG-----HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDI 77
Cdd:PRK13637 2 SIKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 ----AMVFQ--SYALYPHmNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLD--PLLERRPKALSGGQRQRVAMGRAIV 149
Cdd:PRK13637 82 rkkvGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 150 RQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELY 222
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
3.74e-36 |
|
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: 137.59 E-value: 3.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 2 ASIDIQNIRKAY--GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDI 77
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYpHMNVAGNmsysLRL----------RKVAKekiasavaaaaaKLGLDPLLERRPK-----------ALSG 136
Cdd:COG4987 412 AVVPQRPHLF-DTTLREN----LRLarpdatdeelWAALE------------RVGLGDWLAALPDgldtwlgeggrRLSG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 137 GQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDlkATSIYVTHDQiEAMTLADRIVAMHGGVVQQVG 216
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHRL-AGLERMDRILVLEDGRIVEQG 551
|
250
....*....|
gi 517057676 217 SPLELYDRPA 226
Cdd:COG4987 552 THEELLAQNG 561
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
4.12e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.04 E-value: 4.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 2 ASIDIQNIRKAYG--HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDI 77
Cdd:PRK13632 6 VMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSyalyPH-----MNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQP 152
Cdd:PRK13632 86 GIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517057676 153 KAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAmTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-212 |
5.43e-36 |
|
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: 129.96 E-value: 5.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVrvnELHPKDRDIAMVFQSY- 84
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRRs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 85 ---------------ALYPHMNVAGnmsyslRLRKVAKEKIasavAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIV 149
Cdd:cd03235 79 idrdfpisvrdvvlmGLYGHKGLFR------RLSKADKAKV----DEALERVGLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 150 RQPKAFLFDEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-218 |
1.26e-35 |
|
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: 129.48 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR---DIAMV 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNVAGNM----------SYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVR 150
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 151 QPKAFLFDEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSP 218
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-210 |
1.71e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 134.76 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD-RD--IAMVFQ 82
Cdd:COG1129 7 MRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAagIAIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 SYALYPHMNVAGNM---SYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDE 159
Cdd:COG1129 87 ELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 160 PLSNLDARlreqmraEIKKLHG---DLKA---TSIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:COG1129 167 PTASLTER-------EVERLFRiirRLKAqgvAIIYISHRLDEVFEIADRVTVLRDG 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-216 |
7.77e-35 |
|
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: 126.63 E-value: 7.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHpkDRDIAMVFQS 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 164 LDARLREQMRAEIKKLHGDLKaTSIYVTH--DQIEAMtlADRIVAMHGGVVQQVG 216
Cdd:cd03269 159 LDPVNVELLKDVIRELARAGK-TVILSTHqmELVEEL--CDRVLLLNKGRAVLYG 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
1.20e-34 |
|
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: 126.33 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNElHPKD--RDIAMVF 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREvrRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 82 QSYALYPHMNVAGNMSYSLRL----RKVAKEKIASAVAAaaakLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLF 157
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLygvpGAERRERIDELLDF----VGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517057676 158 DEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-225 |
1.35e-34 |
|
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: 132.89 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 10 RKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEvTSGEIRIAGVRVNELHPKD-----RDIAMVFQS- 83
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YA-LYPHMNVA-----------GNMSYSLRLRKVAKekiasavaaAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAIVR 150
Cdd:COG4172 372 FGsLSPRMTVGqiiaeglrvhgPGLSAAERRARVAE---------ALEEVGLDPaARHRYPHEFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 151 QPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQ--IEAMtlADRIVAMHGG-VVQQvGSPLELYDRP 225
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLavVRAL--AHRVMVMKDGkVVEQ-GPTEQVFDAP 517
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-226 |
1.93e-34 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 126.25 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR---DI 77
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYPHMNVAGNM---SYSLRLRKVAKEKIASAvaaaaakLGLDPLLERRPK----ALSGGQRQRVAMGRAIVR 150
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLllgAYARRDRAEVRADLERV-------YELFPRLKERRRqragTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 151 QPKAFLFDEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPA 226
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-236 |
2.48e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 128.77 E-value: 2.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY----GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD----- 74
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 RDIAMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKA 154
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 155 FLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHdQIEAM-TLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGF 233
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITH-EMDVVkRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
...
gi 517057676 234 IGS 236
Cdd:PRK11153 241 IQS 243
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-225 |
5.93e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 123.16 E-value: 5.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRD------- 76
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 77 --------IAMVFQSYALYPHMNVAGN-MSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERR-PKALSGGQRQRVAMGR 146
Cdd:PRK10619 86 qlrllrtrLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517057676 147 AIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKaTSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-206 |
1.25e-32 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 122.12 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSG-EIRI-----AGVRVNELHPKdrdI 77
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVWELRKR---I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVfqSYALypHMNVAGNMS------------------YSLRLRKVAKEKIASavaaaaakLGLDPLLERRPKALSGGQR 139
Cdd:COG1119 81 GLV--SPAL--QLRFPRDETvldvvlsgffdsiglyrePTDEQRERARELLEL--------LGLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 140 QRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHdQIE--------AMTLAD-RIVA 206
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH-HVEeippgithVLLLKDgRVVA 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-225 |
1.96e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 123.66 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 21 GVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR-----DIAMVFQS--YALYPHMNVA 93
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 94 GNMSYSLRLR--KVAKEKIASAVAAAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLRE 170
Cdd:PRK15079 119 EIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 171 QMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:PRK15079 199 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-212 |
2.01e-32 |
|
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: 120.40 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVFQS 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAaaakLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDEVLDV----VGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517057676 164 LDARLREQMRAEIKklhgDLKATSIYV---THDQIEAMTLADRIVAMHGGVV 212
Cdd:cd03268 157 LDPDGIKELRELIL----SLRDQGITVlisSHLLSEIQKVADRIGIINKGKL 204
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-226 |
3.01e-32 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 123.45 E-value: 3.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 36 GPSGCGKSTLLRMIAGLEEVTSGEIRIAG-------VRVNeLHPKDRDIAMVFQSYALYPHMNVAGNMSYSLrlrkvaKE 108
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGIC-LPPEKRRIGYVFQDARLFPHYKVRGNLRYGM------AK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 109 KIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDA-RLREQMrAEIKKLHGDLKATS 187
Cdd:PRK11144 104 SMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLpRKRELL-PYLERLAREINIPI 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 517057676 188 IYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPA 226
Cdd:PRK11144 183 LYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-216 |
3.03e-32 |
|
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: 119.99 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVvLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRD-IAMVFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 SYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLS 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 163 NLDARLREQMRAEIKKLHGDlkATSIYVTH--DQIEAMtlADRIVAMHGGVVQQVG 216
Cdd:cd03264 160 GLDPEERIRFRNLLSELGED--RIVILSTHivEDVESL--CNQVAVLNKGKLVFEG 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-210 |
4.99e-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: 119.28 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 5 DIQNIRKAYGHVQ-VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRvneLHPKDR--DIAMVF 81
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERrkSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 82 QS--YALYphmnvaGNMSYS-LRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFD 158
Cdd:cd03226 78 QDvdYQLF------TDSVREeLLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517057676 159 EPLSNLDARLREQMRAEIKKLHGDLKAtSIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKA-VIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-225 |
5.11e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 120.40 E-value: 5.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEV-----TSGEIRIAG-----VRVNEL 70
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGqdifkMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 71 HpkdRDIAMVFQSYALYPHMNVAGNMSYSLRLRKVAKEK--IASAVAAAAAKLGLDPLLERRPKA----LSGGQRQRVAM 144
Cdd:PRK14247 81 R---RRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKkeLQERVRWALEKAQLWDEVKDRLDApagkLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 145 GRAIVRQPKAFLFDEPLSNLDArlreQMRAEIKKLHGDLKA--TSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELY 222
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDP----ENTAKIESLFLELKKdmTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
...
gi 517057676 223 DRP 225
Cdd:PRK14247 234 TNP 236
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-210 |
1.18e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 119.81 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGH-----VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNEL--HPKDRD 76
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 77 IAMVFQSYAL--YPHMNVAGNMS--------YSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGR 146
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLTKKRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517057676 147 AIVRQPKAFLFDEPLSNLDARlreqmRAEI-----KKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPK-----TAALvleltEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-210 |
1.57e-31 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 125.22 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 2 ASIDIQNIRKAY----GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--- 74
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 ---RDIAMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQ 151
Cdd:PRK10535 83 lrrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 152 PKAFLFDEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHD-QIEAMtlADRIVAMHGG 210
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDpQVAAQ--AERVIEIRDG 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
1.58e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 119.18 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVT-----SGEIRIAGVRV--NELHPK 73
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 74 D--RDIAMVFQSYALYPHMNVAGNMSYSLRLRKVAKEK--IASAVAAAAAKLGL-DPLLER---RPKALSGGQRQRVAMG 145
Cdd:PRK14267 82 EvrREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKkeLDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 146 RAIVRQPKAFLFDEPLSNLD---ARLREQMRAEIKKlhgdlKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELY 222
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-----EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
....*
gi 517057676 223 DRPAN 227
Cdd:PRK14267 237 ENPEH 241
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-222 |
1.63e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 119.73 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY--GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAM 79
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSyalyPH-----MNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKA 154
Cdd:PRK13635 86 VFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 155 FLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTlADRIVAMHGGVVQQVGSPLELY 222
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-222 |
3.07e-31 |
|
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: 118.03 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY---GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIA 78
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQSYALYPhMNVAGNMSYSLRLRKVaKEKIASAVAAAAAKL------GLDPLLERRPKALSGGQRQRVAMGRAIVRQP 152
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYGKPDATD-EEVEEAAKKANIHDFimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 153 KAFLFDEPLSNLDARLREQMRAEIKKLHGDlkATSIYVTHdQIEAMTLADRIVAMHGGVVQQVGSPLELY 222
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKG--RTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
15-214 |
4.54e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 117.61 E-value: 4.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 15 HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHP------KDRDIAMVFQSYALYP 88
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 89 HMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARL 168
Cdd:PRK11629 101 DFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517057676 169 RE---QMRAEIKKLHGdlkATSIYVTHDqieaMTLADRI---VAMHGGVVQQ 214
Cdd:PRK11629 181 ADsifQLLGELNRLQG---TAFLVVTHD----LQLAKRMsrqLEMRDGRLTA 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-212 |
5.63e-31 |
|
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: 115.39 E-value: 5.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQ--VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAM 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALYPHmNVAGNMsyslrlrkvakekiasavaaaaaklgldpllerrpkaLSGGQRQRVAMGRAIVRQPKAFLFDE 159
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517057676 160 PLSNLDARLREQMRAEIKKLHGDlKATSIYVTHdQIEAMTLADRIVAMHGGVV 212
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-207 |
8.97e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.41 E-value: 8.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 12 AYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGvrvnelhpkDRDIAMVFQSYALYPHM- 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 91 -NVAGNMSYSL--------RLRKVAKEKIASAVAaaaaKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPL 161
Cdd:NF040873 72 lTVRDLVAMGRwarrglwrRLTRDDRAAVDDALE----RVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517057676 162 SNLDARLREQMRAEIKKLHGDlKATSIYVTHDqIEAMTLADRIVAM 207
Cdd:NF040873 148 TGLDAESRERIIALLAEEHAR-GATVVVVTHD-LELVRRADPCVLL 191
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-224 |
2.23e-30 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 115.41 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYG--HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAM 79
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALYpHMNVAGNMSYSLR------LRKVAK-----EKIasavaaAAAKLGLDPLLERRPKALSGGQRQRVAMGRAI 148
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGRPgatreeVEEAARaanahEFI------MELPEGYDTVIGERGVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 149 VRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDlkATSIYVTHdQIEAMTLADRIVAMHGGVVQQVGSPLELYDR 224
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKN--RTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-228 |
4.71e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.27 E-value: 4.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 19 LHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRI------AGVRVNELHPKDRDIAMVFQsyalYPHMN- 91
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKPLRKKVGIVFQ----FPEHQl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 92 ----VAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDA 166
Cdd:PRK13634 99 feetVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 167 RLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANL 228
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDEL 240
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-207 |
6.09e-30 |
|
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: 119.70 E-value: 6.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQSyalyPHMnVAGN 95
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWVPQH----PFL-FAGT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 96 MSYSLRL-RKVAKE--------KIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDA 166
Cdd:TIGR02857 412 IAENIRLaRPDASDaeirealeRAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517057676 167 RLREQMRAEIKKLHGDlkATSIYVTHDqIEAMTLADRIVAM 207
Cdd:TIGR02857 492 ETEAEVLEALRALAQG--RTVLLVTHR-LALAALADRIVVL 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-224 |
9.71e-30 |
|
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: 113.86 E-value: 9.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGH-VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNEL--HPKDRDIAMV 80
Cdd:cd03254 3 IEFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHmNVAGNMSYSLRLRKVAKEKIASAVaaaaakLGLDPLLERRPKA-----------LSGGQRQRVAMGRAIV 149
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKE------AGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 150 RQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDlkATSIYVTHdQIEAMTLADRIVAMHGGVVQQVGSPLELYDR 224
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMKG--RTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
1.02e-29 |
|
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: 119.14 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY-----GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGE--IRIAG--VRVNELHPKD 74
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 RD-----IAMVFQSYALYPHMNVAGNMSYSLRLrKVAKEKIASAVAAAAAKLGLD-----PLLERRPKALSGGQRQRVAM 144
Cdd:TIGR03269 360 RGrakryIGILHQEYDLYPHRTVLDNLTEAIGL-ELPDELARMKAVITLKMVGFDeekaeEILDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 145 GRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-227 |
1.10e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 114.36 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 2 ASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLL----RMIAGLEEV-TSGEIRIAG-------VRVNE 69
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMNDLIPGArVEGEILLDGediydpdVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 70 LHpkdRDIAMVFQSYALYPhMNVAGNMSYSLRLRKVAKEKIasavaaaaaklgLDPLLER-----------------RPK 132
Cdd:COG1117 90 LR---RRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSE------------LDEIVEEslrkaalwdevkdrlkkSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 133 ALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLD----ARLREQMRaEIKKlhgdlKATSIYVTHDQIEAMTLADRIVAMH 208
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELIL-ELKK-----DYTIVIVTHNMQQAARVSDYTAFFY 227
|
250
....*....|....*....
gi 517057676 209 GGVVQQVGSPLELYDRPAN 227
Cdd:COG1117 228 LGELVEFGPTEQIFTNPKD 246
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-222 |
1.24e-29 |
|
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: 113.41 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR---DIAMV 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 161 LSNLDARlreqMRAEIKKLHGDLKATSIYV---THDQIEAMTLADRIVAMHGGVVQQVGSPLELY 222
Cdd:cd03218 161 FAGVDPI----AVQDIQKIIKILKDRGIGVlitDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-224 |
1.24e-29 |
|
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: 113.48 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYG-HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNE--LHPKDRDIAMV 80
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYpHMNVAGNMSYS---------LRLRKVAK--EKIASAVAAAAAKLGldpllERRPKaLSGGQRQRVAMGRAIV 149
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYGrpdatdeevIEAAKAAQihDKIMRFPDGYDTIVG-----ERGLK-LSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 150 RQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDlkATSIYVTHDQIEAMTlADRIVAMHGGVVQQVGSPLELYDR 224
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-259 |
1.37e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 115.21 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGvrvNELHPKDRD-IAmvf 81
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPEDRRrIG--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 82 qsY-----ALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFL 156
Cdd:COG4152 75 --YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 157 FDEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTH--DQIEAmtLADRIVAMHGG--VVQqvGSPLELYDR-PANLFVA 231
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELA-AKGTTVIFSSHqmELVEE--LCDRIVIINKGrkVLS--GSVDEIRRQfGRNTLRL 227
|
250 260
....*....|....*....|....*...
gi 517057676 232 GFIGSPGmnFLEASYDAGGVRLKDGTIV 259
Cdd:COG4152 228 EADGDAG--WLRALPGVTVVEEDGDGAE 253
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-193 |
3.28e-29 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 112.18 E-value: 3.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGH----VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR---- 75
Cdd:PRK10584 7 VEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 76 --DIAMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPK 153
Cdd:PRK10584 87 akHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517057676 154 AFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHD 193
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-228 |
4.59e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 113.29 E-value: 4.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQ---VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNE--LHPKDR 75
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 76 DIAMVFQSyalyPHMNVAG-----NMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVR 150
Cdd:PRK13650 82 KIGMVFQN----PDNQFVGatvedDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 151 QPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDqIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANL 228
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELFSRGNDL 234
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-214 |
5.55e-29 |
|
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: 111.85 E-value: 5.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR---DIAMVFQ 82
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 SYALYPHMNVAGNMSYSLRLRKVAKEKIASAVaaaaakLGLDPLLE----RRPKALSGGQRQRVAMGRAIVRQPKAFLFD 158
Cdd:TIGR03410 83 GREIFPRLTVEENLLTGLAALPRRSRKIPDEI------YELFPVLKemlgRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 159 EPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHDQIE-AMTLADRIVAM-HGGVVQQ 214
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLR-AEGGMAILLVEQYLDfARELADRYYVMeRGRVVAS 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-210 |
1.72e-28 |
|
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: 109.99 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGHVQ--VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIA 78
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQ-----SYALYPHMNVAGNMSYSLRLRKVAkEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPK 153
Cdd:cd03245 82 YVPQdvtlfYGTLRDNITLGAPLADDERILRAA-ELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 154 AFLFDEPLSNLDARLREQMRAEIKKLHGDlkATSIYVTHdQIEAMTLADRIVAMHGG 210
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITH-RPSLLDLVDRIIVMDSG 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-212 |
8.65e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.58 E-value: 8.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD---RDIAMV 80
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNVAGNM------SYSLRL-RKVAKEKIasavAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPK 153
Cdd:COG3845 86 HQHFMLVPNLTVAENIvlglepTKGGRLdRKAARARI----RELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 154 AFLFDEPLSNLDArlreqmrAEIKKLHGDLKA------TSIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:COG3845 162 ILILDEPTAVLTP-------QEADELFEILRRlaaegkSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
11-225 |
8.74e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 110.82 E-value: 8.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 11 KAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRV-----NELHPKDRDIAMVFQS-Y 84
Cdd:PRK11308 23 KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpEAQKLLRQKIQIVFQNpY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 85 A-LYPHMNVAGNMSYSLRL-----RKVAKEKIasavAAAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAIVRQPKAFLF 157
Cdd:PRK11308 103 GsLNPRKKVGQILEEPLLIntslsAAERREKA----LAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 158 DEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:PRK11308 179 DEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
18-215 |
3.71e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.72 E-value: 3.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQSYALYPHmNVAGN 95
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-TVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 96 MSYSLRLRKVAKEKiaSAVAAAAAKLGL-DPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRA 174
Cdd:PRK10247 101 LIFPWQIRNQQPDP--AIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517057676 175 EIKKLHGDLKATSIYVTHDQIEaMTLADRIVAM--HGGVVQQV 215
Cdd:PRK10247 179 IIHRYVREQNIAVLWVTHDKDE-INHADKVITLqpHAGEMQEA 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-220 |
6.08e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.12 E-value: 6.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVF 81
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 82 QSYAL--------------YPHMNVAGnmsyslRLRKVAKEKIAsavaaaaaKLGLDPLLERRPKALSGGQRQRVAMGRA 147
Cdd:COG4559 82 QHSSLafpftveevvalgrAPHGSSAA------QDRQIVREALA--------LVGLAHLAGRSYQTLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 148 I------VRQPKAFLF-DEPLSNLD-----------ARLREQMRAEIKKLHgDLKATSIYvthdqieamtlADRIVAMHG 209
Cdd:COG4559 148 LaqlwepVDGGPRWLFlDEPTSALDlahqhavlrlaRQLARRGGGVVAVLH-DLNLAAQY-----------ADRILLLHQ 215
|
250
....*....|.
gi 517057676 210 GVVQQVGSPLE 220
Cdd:COG4559 216 GRLVAQGTPEE 226
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
18-210 |
7.32e-27 |
|
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: 111.50 E-value: 7.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQSYALYpHMNVAGN 95
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTLRDN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 96 MSYSL------RLRKVAkEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLR 169
Cdd:TIGR03375 559 IALGApyaddeEILRAA-ELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSE 637
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517057676 170 EQMRAEIKKLHGDlkATSIYVTHdQIEAMTLADRIVAMHGG 210
Cdd:TIGR03375 638 ERFKDRLKRWLAG--KTLVLVTH-RTSLLDLVDRIIVMDNG 675
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-214 |
1.08e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 105.34 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY-GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD-----RDI 77
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLF 157
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517057676 158 DEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHD-------QIEAMTLADRivAMHGGVVQQ 214
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDiglisrrSYRMLTLSDG--HLHGGVGGE 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-212 |
2.42e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 105.48 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGL---EEVTSGEIRIAGVRVNELHPKDRDI--- 77
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIrks 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 ----AMVFQSYALYPHMNVAGN---------------MSYSLRLRKvakekiaSAVAAAAAKLGLDPLLERRPKALSGGQ 138
Cdd:PRK09984 85 rantGYIFQQFNLVNRLSVLENvligalgstpfwrtcFSWFTREQK-------QRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 139 RQRVAMGRAIVRQPKAFLFDEPLSNLDArlrEQMRAEIKKLHgDLKAT---SIYVTHDQIE-AMTLADRIVAMHGGVV 212
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDP---ESARIVMDTLR-DINQNdgiTVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-212 |
2.68e-26 |
|
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: 103.40 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKA------YGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGL--EEVTSGEIRIAGVRVNELHP 72
Cdd:cd03213 1 GVTLSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 73 KDRdIAMVFQSYALYPHMNVAGNMSYSLRLRKvakekiasavaaaaaklgldpllerrpkaLSGGQRQRVAMGRAIVRQP 152
Cdd:cd03213 81 RKI-IGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057676 153 KAFLFDEPLSNLDARLREQMRAEIKKLhGDLKATSIYVTHD-QIEAMTLADRIVAMHGGVV 212
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-218 |
2.83e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.24 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 2 ASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAM 79
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYAL-YP-------HMNVAGNMSYSLRLRKVAKEKIasavaaaaAKLGLDPLLERRPKALSGGQRQRVAMGRAIVR- 150
Cdd:PRK13548 81 LPQHSSLsFPftveevvAMGRAPHGLSRAEDDALVAAAL--------AQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQl 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 151 -----QPKAFLFDEPLSNLDarLREQ---MRAeIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSP 218
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSALD--LAHQhhvLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-225 |
4.05e-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: 109.28 E-value: 4.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGH--VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEI-----RIAGVRVNELHpkdR 75
Cdd:TIGR03797 451 AIEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVfydgqDLAGLDVQAVR---R 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 76 DIAMVFQSYALYP---HMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQP 152
Cdd:TIGR03797 528 QLGVVLQNGRLMSgsiFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKP 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 153 KAFLFDEPLSNLDARLREQMRAEIKKlhgdLKATSIYVTHdQIEAMTLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:TIGR03797 608 RILLFDEATSALDNRTQAIVSESLER----LKVTRIVIAH-RLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-220 |
9.69e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.56 E-value: 9.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMV 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQ--------------SYALYPHMNVAGNMSYSLRLR-KVAKEkiasavaaaaaKLGLDPLLERRPKALSGGQRQRVAMG 145
Cdd:PRK11231 82 PQhhltpegitvrelvAYGRSPWLSLWGRLSAEDNARvNQAME-----------QTRINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 146 RAIVRQPKAFLFDEPLSNLDarLREQmrAEIKKLHGDLKA---TSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLE 220
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLD--INHQ--VELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-225 |
1.16e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 103.19 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNEL--H------- 71
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmHkrarlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 72 ---PKDrdiAMVFQsyalypHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAI 148
Cdd:COG1137 81 gylPQE---ASIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 149 VRQPKAFLFDEPLSNLD--ArlreqmRAEIKKLHGDLKATSIYV--T-HDQIEAMTLADRIVAMHGGVVQQVGSPLELYD 223
Cdd:COG1137 152 ATNPKFILLDEPFAGVDpiA------VADIQKIIRHLKERGIGVliTdHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225
|
..
gi 517057676 224 RP 225
Cdd:COG1137 226 NP 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-226 |
1.85e-25 |
|
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: 107.08 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGH----VQVLHGVDLEIHDGEFVVLVGPSGCGKS----TLLRMIAGLEEVTSGEIRIAGVRVNELHPKD- 74
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 -----RDIAMVFQ--SYALYPHMNVAGNMSYSLRL-RKVAKEKIASAVAAAAAKLGL-DPllERRPKA----LSGGQRQR 141
Cdd:COG4172 87 rrirgNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpDP--ERRLDAyphqLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 142 V--AMgrAIVRQPKAFLFDEPLSNLDARLreqmRAEIKKLHGDLKATS----IYVTHDqieaMTL----ADRIVAMHGGV 211
Cdd:COG4172 165 VmiAM--ALANEPDLLIADEPTTALDVTV----QAQILDLLKDLQRELgmalLLITHD----LGVvrrfADRVAVMRQGE 234
|
250
....*....|....*
gi 517057676 212 VQQVGSPLELYDRPA 226
Cdd:COG4172 235 IVEQGPTAELFAAPQ 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-213 |
1.35e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.38 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIagvrvnelhPKDRDIAMVFQSYA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 86 LYPHMNVAGNMSYSL-RLRKVAKEKIASAVAAAAA-------------------------------KLGLDP-LLERRPK 132
Cdd:COG0488 72 LDDDLTVLDTVLDGDaELRALEAELEELEAKLAEPdedlerlaelqeefealggweaearaeeilsGLGFPEeDLDRPVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 133 ALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGdlkaTSIYVTHDQ--IEAMtlADRIVAMHGG 210
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG----TVLVVSHDRyfLDRV--ATRILELDRG 225
|
...
gi 517057676 211 VVQ 213
Cdd:COG0488 226 KLT 228
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-223 |
1.55e-24 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 99.54 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 24 LEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGvrvNELHPKDRDIAMVFQSYAL---YP------HMNVAG 94
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG---ASPGKGWRHIGYVPQRHEFawdFPisvahtVMSGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 95 NMSYSLRLRKVAKekiASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRA 174
Cdd:TIGR03771 78 GHIGWLRRPCVAD---FAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517057676 175 EIKKLHGDlKATSIYVTHDQIEAMTLADRIVAMHGGVVQQvGSPLELYD 223
Cdd:TIGR03771 155 LFIELAGA-GTAILMTTHDLAQAMATCDRVVLLNGRVIAD-GTPQQLQD 201
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-293 |
1.67e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.00 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIA 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQSYALyphmnvagnmSYSLRLRKV--------------AKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAM 144
Cdd:PRK09536 81 SVPQDTSL----------SFEFDVRQVvemgrtphrsrfdtWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 145 GRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKaTSIYVTHDQIEAMTLADRIVAMHGGVVQQVGsplelydR 224
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAG-------P 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 225 PANLFVAGfigspgmnFLEASYDAGGVRLKD-GTIVPLAKPLPLVDGAKVTLGIRPeHVLmsdgGAGLAA 293
Cdd:PRK09536 223 PADVLTAD--------TLRAAFDARTAVGTDpATGAPTVTPLPDPDRTEAAADTRV-HVV----GGGQPA 279
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-234 |
2.13e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.12 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 5 DIQNIRKAYGHVQ---VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAG---------VRVNELHP 72
Cdd:PRK14246 9 DVFNISRLYLYINdkaILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlyfgkdiFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 73 KdRDIAMVFQSYALYPHMNVAGNMSYSLRLRKVA-KEKIASAVAAAAAKLGLDPLLERR----PKALSGGQRQRVAMGRA 147
Cdd:PRK14246 89 R-KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 148 IVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLkaTSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPAN 227
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
....*..
gi 517057676 228 LFVAGFI 234
Cdd:PRK14246 246 ELTEKYV 252
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-227 |
2.30e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.85 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGL----EEVT-SGEI-----RIAGVRVNELHPK 73
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnPEVTiTGSIvynghNIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 74 dRDIAMVFQSYALYPhMNVAGNMSYSLRLRKVAKEKIasavaaaaaklgLDPLLERRPK-----------------ALSG 136
Cdd:PRK14239 86 -KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQV------------LDEAVEKSLKgasiwdevkdrlhdsalGLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 137 GQRQRVAMGRAIVRQPKAFLFDEPLSNLD---ARLREQMRAEIKKlhgdlKATSIYVTHDQIEAMTLADRIVAMHGGVVQ 213
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDpisAGKIEETLLGLKD-----DYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
250
....*....|....
gi 517057676 214 QVGSPLELYDRPAN 227
Cdd:PRK14239 227 EYNDTKQMFMNPKH 240
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-225 |
5.53e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 103.26 E-value: 5.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 16 VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNEL--HPKDRDIAMVFQSYALYPHmNVA 93
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYdhHYLHRQVALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 94 GNMSYSLR------LRKVAKEKIASAVAAAAAKlGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDAR 167
Cdd:TIGR00958 573 ENIAYGLTdtpdeeIMAAAKAANAHDFIMEFPN-GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 168 LrEQMRAEIKKLHGdlkATSIYVTHdQIEAMTLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:TIGR00958 652 C-EQLLQESRSRAS---RTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-214 |
7.15e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.48 E-value: 7.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 9 IRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKST----LLRMIAgleevTSGEIRIAGVRVNELHPKD-----RDIAM 79
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQ--SYALYPHMNVAGNMSYSLRL--RKVAKEKIASAVAAAAAKLGLDPLLERR-PKALSGGQRQRVAMGRAIVRQPKA 154
Cdd:PRK15134 367 VFQdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057676 155 FLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHD-QIEAMTLADRIVAMHGGVVQQ 214
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDlHVVRALCHQVIVLRQGEVVEQ 507
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-225 |
7.52e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 99.07 E-value: 7.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRV-----NELHPKDRDIA 78
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQSYALYPHMNVAGNMSYSLRLR-KVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLF 157
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 158 DEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADR--IVAMHGGVVQqvGSPLELYDRP 225
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHayIVADKKIVAH--GSAQALQANP 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-209 |
8.17e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.57 E-value: 8.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVtSGEIRIAG-------------VRV 67
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrveffnqniyerrVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 68 NELHpkdRDIAMVFQSYALYPhMNVAGNMSYSLRLrkvakekiasavAAAAAKLGLDPLLERRPKA-------------- 133
Cdd:PRK14258 84 NRLR---RQVSMVHPKPNLFP-MSVYDNVAYGVKI------------VGWRPKLEIDDIVESALKDadlwdeikhkihks 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517057676 134 ---LSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHG 209
Cdd:PRK14258 148 aldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-212 |
1.05e-23 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 97.54 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY---GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNE-----LHpkdR 75
Cdd:cd03248 12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkyLH---S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 76 DIAMVFQSYALYPHmNVAGNMSY-----SLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVR 150
Cdd:cd03248 89 KVSLVGQEPVLFAR-SLQDNIAYglqscSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 151 QPKAFLFDEPLSNLDARLREQMRaeiKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-223 |
1.06e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.28 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 19 LHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQSyalyPHMNVAG-- 94
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQN----PDNQFVGsi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 95 ---NMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQ 171
Cdd:PRK13648 101 vkyDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517057676 172 MRAEIKKLHGDLKATSIYVTHDQIEAMTlADRIVAMHGGVVQQVGSPLELYD 223
Cdd:PRK13648 181 LLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-233 |
1.85e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.86 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY---GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIA 78
Cdd:PRK13642 5 LEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlrRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQSY-ALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLF 157
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 158 DEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTlADRIVAMHGGVVQQVGSPLELYDRPANLFVAGF 233
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGL 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-210 |
1.98e-23 |
|
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: 95.58 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRD---IAMV---FQSYALYPHMN 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 92 VAGNMSYSLRLrkvakekiasavaaaaaklgldpllerrpkalSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQ 171
Cdd:cd03215 95 VAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 517057676 172 MRAEIKKLHGDLKATsIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:cd03215 143 IYRLIRELADAGKAV-LLISSELDELLGLCDRILVMYEG 180
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-224 |
2.07e-23 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 96.79 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPK--DRDIAMVFQSYALYPHM---NV 92
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLFNRSirdNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 93 A-GNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDArlrEQ 171
Cdd:cd03252 97 AlADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY---ES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517057676 172 MRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDR 224
Cdd:cd03252 174 EHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-204 |
4.31e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 99.99 E-value: 4.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD---RDI 77
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYPHMNVAGNM---SYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKA 154
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517057676 155 FLFDEPLSNLDARLREQMRAEIKKLHGDLKATsIYVTHDQIEAMTLADRI 204
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVI-LYVSHRMEEIFALCDAI 210
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-221 |
5.33e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 95.90 E-value: 5.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLE--EVTSGEIRIAGVRVNELHPKDR---DIAMV 80
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQsyalYPhMNVAG-NMSYSLR--LRKVAKEKIASAVAAAAAK-----LGLDPLLERRP--KALSGGQRQRVAMGRAIVR 150
Cdd:COG0396 83 FQ----YP-VEIPGvSVSNFLRtaLNARRGEELSAREFLKLLKekmkeLGLDEDFLDRYvnEGFSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 151 QPKAFLFDEPLSNLDA-RLReQMRAEIKKLHGDlKATSIYVTH-----DQIEamtlADRIVAMHGGVVQQVGSPlEL 221
Cdd:COG0396 158 EPKLAILDETDSGLDIdALR-IVAEGVNKLRSP-DRGILIITHyqrilDYIK----PDFVHVLVDGRIVKSGGK-EL 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-207 |
9.91e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 94.81 E-value: 9.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYG-HVQ------VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRI--AGVRVNELHPKD 74
Cdd:COG4778 5 LEVENLSKTFTlHLQggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 RDIAMVFQSYALY-----------PHMNVagnMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKA-LSGGQRQRV 142
Cdd:COG4778 85 REILALRRRTIGYvsqflrviprvSALDV---VAEPLLERGVDREEARARARELLARLNLPERLWDLPPAtFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517057676 143 AMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKklhgDLKA---TSIYVTHDqIEAM-TLADRIVAM 207
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIE----EAKArgtAIIGIFHD-EEVReAVADRVVDV 225
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-216 |
1.25e-22 |
|
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: 98.67 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVrvnELHPKDRDiamvfqsyALYPHM------- 90
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGA---DLSQWDRE--------ELGRHIgylpqdv 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 91 -----NVAGNMSyslRLRKVAKEKIasavaAAAAKL-GLDPLLERRPK-----------ALSGGQRQRVAMGRAIVRQPK 153
Cdd:COG4618 416 elfdgTIAENIA---RFGDADPEKV-----VAAAKLaGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 154 AFLFDEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHDQiEAMTLADRIVAMHGGVVQQVG 216
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFG 548
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-210 |
1.28e-22 |
|
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: 92.13 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRiagvrvnelHPKDRDIAMVFQs 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------WGSTVKIGYFEQ- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 yalyphmnvagnmsyslrlrkvakekiasavaaaaaklgldpllerrpkaLSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:cd03221 71 --------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517057676 164 LDARLREQMRAEIKKLHGdlkaTSIYVTHDQ--IEAmtLADRIVAMHGG 210
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDRyfLDQ--VATKIIELEDG 143
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-216 |
1.37e-22 |
|
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: 98.57 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQSYALYPHmNVAGN 95
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 96 MSyslRLRKVAK-EKIASAVAAAaaklGLDPLLERRPK-----------ALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:TIGR01842 412 IA---RFGENADpEKIIEAAKLA----GVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517057676 164 LDARLREQMRAEIKKLHGDlKATSIYVTHdQIEAMTLADRIVAMHGGVVQQVG 216
Cdd:TIGR01842 485 LDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFG 535
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-224 |
1.47e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 98.64 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 16 VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQSYALYPHmNVA 93
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVALVSQDVVLFND-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 94 GNMSYSlRLRKVAKEKIASAVAAAAAK-------LGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDA 166
Cdd:TIGR02203 424 NNIAYG-RTEQADRAEIERALAAAYAQdfvdklpLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDN 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 167 RLREQMRAEIKKLHGDlkATSIYVTHdQIEAMTLADRIVAMHGGVVQQVGSPLELYDR 224
Cdd:TIGR02203 503 ESERLVQAALERLMQG--RTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-210 |
2.14e-22 |
|
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: 93.94 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 10 RKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD-RDIAMVF------- 81
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlRRIGVVFgqktqlw 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 82 ------QSYALYPHMNVAGNMSYSLRLRKVAKekiasavaaaaaKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAF 155
Cdd:cd03267 108 wdlpviDSFYLLAAIYDLPPARFKKRLDELSE------------LLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 156 LFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHD--QIEAmtLADRIVAMHGG 210
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmkDIEA--LARRVLVIDKG 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-210 |
4.49e-22 |
|
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: 92.53 E-value: 4.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGvrvnelhpkdrDIAMVFQSyalyP-HMN----- 91
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQE----PwIQNgtire 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 92 --VAGNMSYSLRLRKVAKekiasavaaaaaKLGLDPLLERRPK-----------ALSGGQRQRVAMGRAIVRQPKAFLFD 158
Cdd:cd03250 85 niLFGKPFDEERYEKVIK------------ACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 159 EPLSNLDARLREQMraeIKK-LHGDLK--ATSIYVTHdQIEAMTLADRIVAMHGG 210
Cdd:cd03250 153 DPLSAVDAHVGRHI---FENcILGLLLnnKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-275 |
5.08e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.13 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYG-----HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVN------ELH 71
Cdd:PRK13641 2 SIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 72 PKDRDIAMVFQsyalYPHMN-----VAGNMSYSLRLRKVAKEKIASAVAAAAAKLGL-DPLLERRPKALSGGQRQRVAMG 145
Cdd:PRK13641 82 KLRKKVSLVFQ----FPEAQlfentVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 146 RAIVRQPKAFLFDEPLSNLDARLREQMrAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 517057676 226 aNLFVAGFIGSPGMNFLEASYDAGGVRLKDgtiVPLAKPlPLVDGAKVTL 275
Cdd:PRK13641 237 -EWLKKHYLDEPATSRFASKLEKGGFKFSE---MPLTID-ELVDGIKNNL 281
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-209 |
5.19e-22 |
|
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: 93.24 E-value: 5.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 25 EIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNElhpKDRDIAMVFQS---YALYPHMNVAGNMSYSLR 101
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY---KPQYIKADYEGtvrDLLSSITKDFYTHPYFKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 102 lrKVAKekiasavaaaaaKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHG 181
Cdd:cd03237 98 --EIAK------------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180
....*....|....*....|....*...
gi 517057676 182 DLKATSIYVTHDQIEAMTLADRIVAMHG 209
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-212 |
6.75e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 6.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHP---KDRDIAMV 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLlerrPKALSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSS----AGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 161 LSNLD----ARLREQMRAEIKKLHGdlkatSIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:PRK15439 168 TASLTpaetERLFSRIRELLAQGVG-----IVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-232 |
7.04e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 93.71 E-value: 7.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGL---EEVTSGEIRIAGVRVNELHPKD-RD-IAMVFQSyalyPH--- 89
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDiREkVGIVFQN----PDnqf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 90 --MNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDAR 167
Cdd:PRK13640 98 vgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 168 LREQMRAEIKKLHGDLKATSIYVTHDqIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAG 232
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNLTVISITHD-IDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIG 241
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-224 |
8.92e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 96.73 E-value: 8.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGH-VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELhpkDRDIAMVF 81
Cdd:TIGR01193 473 DIVINDVSYSYGYgSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 82 QSYALYPHMNVAGNMSYSLRL---RKVAKEKIASAVAAAAAK-------LGLDPLLERRPKALSGGQRQRVAMGRAIVRQ 151
Cdd:TIGR01193 550 INYLPQEPYIFSGSILENLLLgakENVSQDEIWAACEIAEIKddienmpLGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517057676 152 PKAFLFDEPLSNLDARLREQMraeIKKLHGDLKATSIYVTHdQIEAMTLADRIVAM-HGGVVQQvGSPLELYDR 224
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKI---VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLdHGKIIEQ-GSHDELLDR 698
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
15-225 |
1.10e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 92.93 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 15 HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVN--ELHPKDRDIAMVFQ--SYALYPHM 90
Cdd:PRK15112 25 TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQdpSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 91 NVAGNMSYSLRLR-KVAKEKIASAVAAAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARL 168
Cdd:PRK15112 105 RISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 169 REQ---MRAEIKKLHGdlkATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:PRK15112 185 RSQlinLMLELQEKQG---ISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-218 |
1.28e-21 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 91.40 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAY--GHVQVLHGVDLEIHDGEFVVLVGPSGCGKST----LLRMIagleEVTSGEIRIAGVRVNELHPKD-- 74
Cdd:cd03244 2 DIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 RDIAMVFQSYALYP---HMNVAGNMSYS-LRLRKVAkEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVR 150
Cdd:cd03244 78 SRISIIPQDPVLFSgtiRSNLDPFGEYSdEELWQAL-ERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 151 QPKAFLFDEPLSNLD----ARLREQMRAEIKklhgdlKATSIYVTHdQIEAMTLADRIVAMHGGVVQQVGSP 218
Cdd:cd03244 157 KSKILVLDEATASVDpetdALIQKTIREAFK------DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-192 |
1.43e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.64 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRiagvrvnelHPKDRDIAMVFQ-SY--------AL-Y 87
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA---------RPAGARVLFLPQrPYlplgtlreALlY 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 88 PHMnvAGNMSySLRLRKVAKekiasavaaaaaKLGLDPLLER------RPKALSGGQRQRVAMGRAIVRQPKAFLFDEPL 161
Cdd:COG4178 449 PAT--AEAFS-DAELREALE------------AVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|.
gi 517057676 162 SNLDARLREQMRAEIKKLHGDlkATSIYVTH 192
Cdd:COG4178 514 SALDEENEAALYQLLREELPG--TTVISVGH 542
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-222 |
1.66e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.92 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 17 QVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVN------ELHPKDRDIAMVFQsyalYPHM 90
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkYIRPVRKRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 91 -----NVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLD-PLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNL 164
Cdd:PRK13646 97 qlfedTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 165 DARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELY 222
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-237 |
1.92e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.87 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 17 QVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVN------ELHPKDRDIAMVFQsyalYPHM 90
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQ----FPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 91 N-----VAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNL 164
Cdd:PRK13643 96 QlfeetVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 165 DARLREQMRAEIKKLHgDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYdRPANLFVAGFIGSP 237
Cdd:PRK13643 176 DPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF-QEVDFLKAHELGVP 246
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
10-168 |
2.81e-21 |
|
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: 90.79 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 10 RKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEE---VTSGEIRIAGVrvnELHPKD--RDIAMVFQSY 84
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQ---PRKPDQfqKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 85 ALYPHMNVAGNMSYS--LRLRKVAKEKI--ASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:cd03234 91 ILLPGLTVRETLTYTaiLRLPRKSSDAIrkKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
....*...
gi 517057676 161 LSNLDARL 168
Cdd:cd03234 171 TSGLDSFT 178
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-213 |
3.01e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.36 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIA-GVRVNELhPKDRDiamvfq 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGeTVKIGYF-DQHQE------ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 syALYPHMNVAGNMsyslrlRKVAKEKIASAVAAAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPL 161
Cdd:COG0488 389 --ELDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFSGdDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517057676 162 SNLDArlreQMRAEIKKLHGDLKATSIYVTHDQ--IEamTLADRIVAMHGGVVQ 213
Cdd:COG0488 461 NHLDI----ETLEALEEALDDFPGTVLLVSHDRyfLD--RVATRILEFEDGGVR 508
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-210 |
3.05e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.47 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR---DIAMV 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNVAGNMsYSLRL--RKVAK------EKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQP 152
Cdd:PRK09700 86 YQELSVIDELTVLENL-YIGRHltKKVCGvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 153 KAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATsIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAI-VYISHKLAEIRRICDRYTVMKDG 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
3.93e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.71 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD---RDI 77
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYPHMNVAGNMS----------YSLRLRKVakekiasavaaaaakLGLDP-LLERRPK---ALSGGQRQRVA 143
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAmggffaerdqFQERIKWV---------------YELFPrLHERRIQragTMSGGEQQMLA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 144 MGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDlKATSIYVTHDQIEAMTLADRIVAMHGG--VVQQVGSPL 219
Cdd:PRK11614 148 IGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGhvVLEDTGDAL 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-222 |
4.05e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 91.69 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRV-NELHPKD-RDIA-MVFQS-----YALYPH 89
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsDEENLWDiRNKAgMVFQNpdnqiVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 90 MNVA---GNMSyslrlrkVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDA 166
Cdd:PRK13633 105 EDVAfgpENLG-------IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 167 RLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTlADRIVAMHGGVVQQVGSPLELY 222
Cdd:PRK13633 178 SGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-226 |
5.85e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.20 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGH-VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRV---NELHPKDRDIAM 79
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSyalyPHMNVAG-----NMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKA 154
Cdd:PRK13644 82 VFQN----PETQFVGrtveeDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 155 FLFDEPLSNLDARLREQMRAEIKKLHGDLKaTSIYVTHDqIEAMTLADRIVAMHGGVVQQVGSPLELYDRPA 226
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
6.87e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 6.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 2 ASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRD-IAMV 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517057676 161 LSNLDARLREQMRAEIKKLHGDLKaTSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDR 224
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-221 |
8.13e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.35 E-value: 8.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 2 ASIDIQNIRKAY--GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD-RD-I 77
Cdd:PRK11160 337 VSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYphmnvagnmSYSLR--LRKVAKEKIASAVAAAAAKLGLDPLLER------------RPkaLSGGQRQRVA 143
Cdd:PRK11160 417 SVVSQRVHLF---------SATLRdnLLLAAPNASDEALIEVLQQVGLEKLLEDdkglnawlgeggRQ--LSGGEQRRLG 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 144 MGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKlHGDLKaTSIYVTHdQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAE-HAQNK-TVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-223 |
1.69e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRV-NELHPKDRDIAM 79
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDE 159
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 160 PLSNLDARLR----EQMRAEIKKlhgdlKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYD 223
Cdd:PRK13536 199 PTTGLDPHARhliwERLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-225 |
1.92e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 92.61 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 16 VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVN-----ELHPKDRDIAMVFQS-YA-LYP 88
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspgKLQALRRDIQFIFQDpYAsLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 89 HMNVAGNMSYSLRLRKVAK-EKIASAVAAAAAKLGLDPLLE-RRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDA 166
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517057676 167 RLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3-222 |
2.37e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.42 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYG-----HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNElHPKDRDI 77
Cdd:PRK13649 2 GINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS-TSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 -------AMVFQsyalYPHMN-----VAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDP-LLERRPKALSGGQRQRVAM 144
Cdd:PRK13649 81 kqirkkvGLVFQ----FPESQlfeetVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 145 GRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDlKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELY 222
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-178 |
3.45e-20 |
|
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: 87.03 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPK-DRDIAMVFQSYALYPHMNVAGNM 96
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 97 SYSLRLRKVAKEKIasavAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLD----ARLREQM 172
Cdd:TIGR01189 95 HFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDkagvALLAGLL 170
|
....*.
gi 517057676 173 RAEIKK 178
Cdd:TIGR01189 171 RAHLAR 176
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-222 |
3.88e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.91 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 17 QVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRI------AGVR-VNELHPKDRDIAMVFQ--SYALY 87
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKkIKEVKRLRKEIGLVFQfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 88 PHmNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGL-DPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDA 166
Cdd:PRK13645 105 QE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 167 RLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELY 222
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-214 |
9.95e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.29 E-value: 9.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 17 QVLHG-VDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTsGEIRIAGVRVNELHPKD--RDIAMVFQSyalyPHM--- 90
Cdd:PRK11174 363 KTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQN----PQLphg 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 91 ----NVA-GNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLD 165
Cdd:PRK11174 438 tlrdNVLlGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517057676 166 ARLREQMRAEIKKLHGDLkaTSIYVTHdQIEAMTLADRIVAMHGG-VVQQ 214
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQ--TTLMVTH-QLEDLAQWDQIWVMQDGqIVQQ 564
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
4-225 |
1.35e-19 |
|
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: 90.00 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQ--VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELhPKDR---DIA 78
Cdd:TIGR03796 478 VELRNITFGYSPLEppLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVA 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQSYALYphmnvAGNMSYSLRL--RKVAKEKIASAV-------AAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIV 149
Cdd:TIGR03796 557 MVDQDIFLF-----EGTVRDNLTLwdPTIPDADLVRACkdaaihdVITSRPGGYDAELAEGGANLSGGQRQRLEIARALV 631
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 150 RQPKAFLFDEPLSNLDARLREQMRAEIKKlHGdlkATSIYVTHdQIEAMTLADRIVAM-HGGVVQQvGSPLELYDRP 225
Cdd:TIGR03796 632 RNPSILILDEATSALDPETEKIIDDNLRR-RG---CTCIIVAH-RLSTIRDCDEIIVLeRGKVVQR-GTHEELWAVG 702
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-226 |
2.46e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.21 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 16 VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRI----------AGVRVNELHPKD--------RDI 77
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKiknfkelrRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQ--SYALYPHmNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLD-PLLERRPKALSGGQRQRVAMGRAIVRQPKA 154
Cdd:PRK13631 119 SMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 155 FLFDEPLSNLDARLREQMRAEIKklhgDLKA---TSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPA 226
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLIL----DAKAnnkTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-214 |
2.90e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 85.75 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAG-----VRVNELHPKDR----- 75
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERrrllr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 76 -DIAMVFQSYA--LYPHMNVAGNMSYSL---------RLRKVAKEKIAsavaaaaaKLGLDPL-LERRPKALSGGQRQRV 142
Cdd:PRK11701 89 tEWGFVHQHPRdgLRMQVSAGGNIGERLmavgarhygDIRATAGDWLE--------RVEIDAArIDDLPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 143 AMGRAIVRQPKAFLFDEPLSNLD----ARLREQMRAeikkLHGDLKATSIYVTHDQIEAMTLADRIVAMHGG-VVQQ 214
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRG----LVRELGLAVVIVTHDLAVARLLAHRLLVMKQGrVVES 233
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
3-221 |
3.31e-19 |
|
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: 88.65 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGHVQ--VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPK--DRDIA 78
Cdd:TIGR01846 455 AITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMG 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQSYALY------------PHMNV---------AGNMSYSLRLRKvakekiasavaaaaaklGLDPLLERRPKALSGG 137
Cdd:TIGR01846 535 VVLQENVLFsrsirdnialcnPGAPFehvihaaklAGAHDFISELPQ-----------------GYNTEVGEKGANLSGG 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 138 QRQRVAMGRAIVRQPKAFLFDEPLSNLD----ARLREQMRaEIKKlhgdlKATSIYVTHdQIEAMTLADRIVAMHGGVVQ 213
Cdd:TIGR01846 598 QRQRIAIARALVGNPRILIFDEATSALDyeseALIMRNMR-EICR-----GRTVIIIAH-RLSTVRACDRIIVLEKGQIA 670
|
....*...
gi 517057676 214 QVGSPLEL 221
Cdd:TIGR01846 671 ESGRHEEL 678
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-202 |
3.87e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.60 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 7 QNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGeIRIAG---VRVNELHPKD-------RD 76
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGkvtFHGKNLYAPDvdpvevrRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 77 IAMVFQSYALYPHmNVAGNMSYSLRLRkvakekiasavaaaAAKLGLDPLLERRPK-----------------ALSGGQR 139
Cdd:PRK14243 93 IGMVFQKPNPFPK-SIYDNIAYGARIN--------------GYKGDMDELVERSLRqaalwdevkdklkqsglSLSGGQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 140 QRVAMGRAIVRQPKAFLFDEPLSNLD--ARLR-EQMRAEIKKlhgdlKATSIYVTHDQIEAMTLAD 202
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDpiSTLRiEELMHELKE-----QYTIIIVTHNMQQAARVSD 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-216 |
4.35e-19 |
|
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: 84.51 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 10 RKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGvrvnelhpkdRDIAMVFQSYALYPH 89
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------RVSSLLGLGGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 90 MNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLR 169
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517057676 170 EQMRAEIKKLHGDLKaTSIYVTHDQIEAMTLADRIVAMHGGVVQQVG 216
Cdd:cd03220 179 EKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-224 |
5.07e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.75 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 10 RKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGvRVNELhpkdRDIAMVFQsyalyPH 89
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSAL----LELGAGFH-----PE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 90 MNVAGNMSYSLRLRKVAKEKIasavaaaAAKL-------GLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLS 162
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEI-------DEKFdeivefaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517057676 163 NLDARLREQMRAEIKKLHGDLKaTSIYVTHD--QIEamTLADRIVAMHGGVVQQVGSPLELYDR 224
Cdd:COG1134 176 VGDAAFQKKCLARIRELRESGR-TVIFVSHSmgAVR--RLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-233 |
5.08e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.44 E-value: 5.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 13 YGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNE----LHPKDRDIAMVFQSyalyP 88
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYskrgLLALRQQVATVFQD----P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 89 -----HMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:PRK13638 87 eqqifYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 164 LDARLREQMRAEIKKLHGDLKATSIyVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLFVAGF 233
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-224 |
6.26e-19 |
|
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: 83.73 E-value: 6.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLE--EVTSGEIRIAGVRVNELHPKDR---DIAMV 80
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHMNvagNMSYslrLRKVAkekiasavaaaaaklgldpllerrpKALSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:cd03217 83 FQYPPEIPGVK---NADF---LRYVN-------------------------EGFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 161 LSNLDARLREQMRAEIKKLHGDLKATSIyVTH-DQIEAMTLADRIVAMHGGVVQQVGsPLELYDR 224
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREEGKSVLI-ITHyQRLLDYIKPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-212 |
8.74e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 8.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD---RDIAMV---FQSYALYPHMN 91
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVpedRKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 92 VAGNMSYSlRLRKVAK------EKIASAVAAAAAKLGLD-PLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNL 164
Cdd:COG1129 347 IRENITLA-SLDRLSRgglldrRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517057676 165 D--ArlreqmRAEIKKLHGDLKA---TSIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:COG1129 426 DvgA------KAEIYRLIRELAAegkAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-225 |
1.53e-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: 83.73 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRI-----AGVRVNELHPKDR--- 75
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERrrl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 76 ---DIAMVFQSYALYPHMNVAGNMSYSLRLRKVAKE---KIASAVAAAAAKLGLDP-LLERRPKALSGGQRQRVAMGRAI 148
Cdd:TIGR02323 84 mrtEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARhygNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQIARNL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 149 VRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-226 |
1.98e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.30 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAY---GHV-QVLHGVDLEIHDGEFVVLVGPSGCGKS----TLLRMIAGLEEV-TSGEIRIAGVRVneLH 71
Cdd:PRK15134 3 QPLLAIENLSVAFrqqQTVrTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESL--LH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 72 PKDR--------DIAMVFQS--YALYPHMNVAGNMSYSLRL-RKVAKEKIASAVAAAAAKLGLDPLLERR---PKALSGG 137
Cdd:PRK15134 81 ASEQtlrgvrgnKIAMIFQEpmVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 138 QRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAM-HGGVVQQvG 216
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMqNGRCVEQ-N 239
|
250
....*....|
gi 517057676 217 SPLELYDRPA 226
Cdd:PRK15134 240 RAATLFSAPT 249
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-224 |
2.38e-18 |
|
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: 86.54 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 19 LHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGvrvnelhpkdrDIAMVFQSyALYPHMNVAGNMSY 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------SVAYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 99 SLRLRKVAKEKIASAvaaaaakLGLDPLLERRPKA-----------LSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDAR 167
Cdd:TIGR00957 722 GKALNEKYYQQVLEA-------CALLPDLEILPSGdrteigekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 168 LREQMRAEIKKLHGDLK-ATSIYVTHDqIEAMTLADRIVAMHGGVVQQVGSPLELYDR 224
Cdd:TIGR00957 795 VGKHIFEHVIGPEGVLKnKTRILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-210 |
2.68e-18 |
|
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: 81.21 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGH--VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRD-IAMV 80
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSyalyPHMnvagnmsYSLRLRKvakekiasavaaaaaKLGldplleRRpkaLSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:cd03247 81 NQR----PYL-------FDTTLRN---------------NLG------RR---FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517057676 161 LSNLDARL-REQMRAEIKKLHGDlkaTSIYVTHdQIEAMTLADRIVAMHGG 210
Cdd:cd03247 126 TVGLDPITeRQLLSLIFEVLKDK---TLIWITH-HLTGIEHMDKILFLENG 172
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-210 |
3.59e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 83.60 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYG-----HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRI---------AGVRVNE 69
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 70 LHPKD-----------------RDIAMVFQ--SYALYPHMN----VAGNMSYSlrlrkVAKEKIASAVAAAAAKLGLD-P 125
Cdd:PRK13651 83 VLEKLviqktrfkkikkikeirRRVGVVFQfaEYQLFEQTIekdiIFGPVSMG-----VSKEEAKKRAAKYIELVGLDeS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 126 LLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKaTSIYVTHDQIEAMTLADRIV 205
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTI 236
|
....*
gi 517057676 206 AMHGG 210
Cdd:PRK13651 237 FFKDG 241
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-210 |
3.98e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.60 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 16 VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGvrvneLHP-KDR-----DIAMVF-QSYALYP 88
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVPfKRRkefarRIGVVFgQRSQLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 89 HMNVAGnmsySLRL--------RKVAKEKIASAVAAaaakLGLDPLLERRPKALSGGQRQR--VAMgrAIVRQPKAFLFD 158
Cdd:COG4586 110 DLPAID----SFRLlkaiyripDAEYKKRLDELVEL----LDLGELLDTPVRQLSLGQRMRceLAA--ALLHRPKILFLD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517057676 159 EPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHD--QIEAmtLADRIVAMHGG 210
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHG 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-166 |
4.09e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 4.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 14 GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRdIAMVFQSYALYPHMNVA 93
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 94 GNMSYSLRLRKVAKEKIASAVAAaaakLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDA 166
Cdd:PRK13539 92 ENLEFWAAFLGGEELDIAAALEA----VGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-224 |
4.24e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 82.86 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 17 QVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQSyalyP-----H 89
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGLVFQD----PddqvfS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 90 MNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLR 169
Cdd:PRK13647 95 STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 170 EQMRAEIKKLHGDLKaTSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDR 224
Cdd:PRK13647 175 ETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-221 |
4.51e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.73 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 7 QNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQ-- 82
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQna 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 ------------SYALYPHMNVAgnmsysLRLRKVAKEKIASAVAAAaaklGLDPLLERRPKALSGGQRQRVAMGRAIVR 150
Cdd:PRK10253 91 ttpgditvqelvARGRYPHQPLF------TRWRKEDEEAVTKAMQAT----GITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057676 151 QPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-221 |
5.97e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.86 E-value: 5.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRI--AGVRVNELHPKD-RDI 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddEDISLLPLHARArRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQSYALYPHMNVAGNMSYSLRLRK-VAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFL 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 157 FDEPLSNLDArlreQMRAEIKKLHGDLKATSIYV---THDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:PRK10895 161 LDEPFAGVDP----ISVIDIKRIIEHLRDSGLGVlitDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-192 |
8.83e-18 |
|
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: 79.51 E-value: 8.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIagvrvnelhPKDRDIAMVFQSyalyPHMNVAgnms 97
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR----PYLPLG---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 98 ySLRlrkvakEKIasavaaaaaklgldplleRRP--KALSGGQRQRVAMGRAIVRQPK-AFLfDEPLSNLDARLREQMRA 174
Cdd:cd03223 79 -TLR------EQL------------------IYPwdDVLSGGEQQRLAFARLLLHKPKfVFL-DEATSALDEESEDRLYQ 132
|
170
....*....|....*...
gi 517057676 175 EIKklhgDLKATSIYVTH 192
Cdd:cd03223 133 LLK----ELGITVISVGH 146
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-221 |
8.98e-18 |
|
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: 84.49 E-value: 8.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 17 QVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQSYALYphmN--V 92
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF---NdtI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 93 AGNMSYSlR-------LRKVAKekiasavaaaaaKLGLDPLLERRPKA-----------LSGGQRQRVAMGRAIVRQPKA 154
Cdd:COG5265 449 AYNIAYG-RpdaseeeVEAAAR------------AAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPI 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 155 FLFDEPLSNLDARLREQMRAEIKKLHGDlkATSIYVTH------DqieamtlADRIVAMHGGVVQQVGSPLEL 221
Cdd:COG5265 516 LIFDEATSALDSRTERAIQAALREVARG--RTTLVIAHrlstivD-------ADEILVLEAGRIVERGTHAEL 579
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-193 |
9.70e-18 |
|
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: 84.33 E-value: 9.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNEL-HPKDRDIAMVFQSYALYPHMNVAGNm 96
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLdQDEVRRRVSVCAQDAHLFDTTVREN- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 97 syslrLRKVAKEKIASAVAAAAAKLGLDPLLERRP-----------KALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLD 165
Cdd:TIGR02868 429 -----LRLARPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*...
gi 517057676 166 ARLREQMRAEIkkLHGDLKATSIYVTHD 193
Cdd:TIGR02868 504 AETADELLEDL--LAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-228 |
9.78e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.05 E-value: 9.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGH-VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVN----ELHPKDRDIA 78
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkkSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQS-----YALYPHMNVA-GNMSYSLrlrkvAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQP 152
Cdd:PRK13639 82 IVFQNpddqlFAPTVEEDVAfGPLNLGL-----SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 153 KAFLFDEPLSNLDARLREQmraeIKKLHGDLKA---TSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYD-----R 224
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQ----IMKLLYDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSdietiR 232
|
....
gi 517057676 225 PANL 228
Cdd:PRK13639 233 KANL 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
1.75e-17 |
|
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: 83.31 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLE--EVTSGEI--------------------R 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpskvgE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 62 IAGVRVNELHPKDRD---------------IAMVFQ-SYALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDP 125
Cdd:TIGR03269 81 PCPVCGGTLEPEEVDfwnlsdklrrrirkrIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 126 LLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTH--DQIEamTLADR 203
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpEVIE--DLSDK 238
|
250 260
....*....|....*....|.
gi 517057676 204 IVAMHGGVVQQVGSPLELYDR 224
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVAV 259
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
1.79e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 81.39 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAY-GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNE--LHPKDRDI 77
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQS---YALYPhmNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKA 154
Cdd:PRK13652 81 GLVFQNpddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057676 155 FLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-204 |
1.83e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.05 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 7 QNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTS--GEIRIAGVRVNELHPKDRD---IAMVF 81
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTEragIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 82 QSYALYPHMNVAGN------------MSYS---LRLRKVAKEkiasavaaaaAKLGLDPllERRPKALSGGQRQRVAMGR 146
Cdd:PRK13549 89 QELALVKELSVLENiflgneitpggiMDYDamyLRAQKLLAQ----------LKLDINP--ATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057676 147 AIVRQPKAFLFDEPLSNLDARLREQMRAEIKklhgDLKA---TSIYVTHDQIEAMTLADRI 204
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIR----DLKAhgiACIYISHKLNEVKAISDTI 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-227 |
1.85e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.37 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 16 VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGV-------RVNEL---------HPKDRDIAM 79
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrQVIELseqsaaqmrHVRGADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQS--YALYPHMNVAGNMSYSLRLRK-VAKEKIASAVAAAAAKLGL---DPLLERRPKALSGGQRQRVAMGRAIVRQPK 153
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517057676 154 AFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPAN 227
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-222 |
6.06e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.89 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 17 QVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNE----LHPKDRDIAMVFQS--YALYPhM 90
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkgLMKLRESVGMVFQDpdNQLFS-A 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 91 NVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLRE 170
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517057676 171 QMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELY 222
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-221 |
7.35e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.60 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 19 LHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNE--LHPKDRDIAMVFQSYALYpHMNVAGNM 96
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVALVSQNVHLF-NDTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 97 SYSlRLRKVAKEKIASAVAAA-----AAKL--GLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLR 169
Cdd:PRK11176 438 AYA-RTEQYSREQIEEAARMAyamdfINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESE 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517057676 170 EQMRAEIKKLHGDlkATSIYVTH--DQIEAmtlADRIVAMHGGVVQQVGSPLEL 221
Cdd:PRK11176 517 RAIQAALDELQKN--RTSLVIAHrlSTIEK---ADEILVVEDGEIVERGTHAEL 565
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-243 |
8.91e-17 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 81.37 E-value: 8.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 8 NIRKAYG--HVQVLHGvdlEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIrIAGVRVnelhpkdrdiamvfqSY- 84
Cdd:COG1245 346 DLTKSYGgfSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKI---------------SYk 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 85 ALYphmnVAGNMSYSLR--LRKVAKEKIASAVAAA--AAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:COG1245 407 PQY----ISPDYDGTVEefLRSANTDDFGSSYYKTeiIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 161 LSNLDARLREQMRAEIKKLHGDLKATSIYVTHD-QIEAMtLADRIVAMHG--GVVQQVGSPLELYDrpanlfvagfigsp 237
Cdd:COG1245 483 SAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDiYLIDY-ISDRLMVFEGepGVHGHASGPMDMRE-------------- 547
|
....*..
gi 517057676 238 GMN-FLE 243
Cdd:COG1245 548 GMNrFLK 554
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-217 |
1.34e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.64 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEE--VTSGEIRIAGVRVNELHPKDRD---IA 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTEragIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQSYALYPHMNVAGNM----SYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKA-LSGGQRQRVAMGRAIVRQPK 153
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 154 AFLFDEPLSNLDARLREQMRAEIKklhgDLKA---TSIYVTHDQIEAMTLADRIVAMHGGvvQQVGS 217
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIR----DLKAhgvACVYISHKLNEVKAVCDTICVIRDG--QHVAT 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-221 |
2.17e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.09 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 17 QVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEE---VTSGEIRIAGVRVNElhPKDRDI-AMVFQSYALYPHMNV 92
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDA--KEMRAIsAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 93 AGNMSYSLRLR---KVAKEKIASAVAAAAAKLGLDPL------LERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:TIGR00955 117 REHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCantrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 164 LDARLREQMRAEIKKLhgDLKATSIYVTHDQ--IEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGL--AQKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-235 |
3.91e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.44 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIdiqNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSG-----EIRIAGVRV---NELHP 72
Cdd:PRK14271 22 MAAV---NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 73 KDRDIAMVFQSYALYPhMNVAGNMSYSLRLRK-VAKEKIASAVAAAAAKLGL-DPLLER---RPKALSGGQRQRVAMGRA 147
Cdd:PRK14271 99 FRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwDAVKDRlsdSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 148 IVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLkaTSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPAN 227
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
250
....*....|..
gi 517057676 228 L----FVAGFIG 235
Cdd:PRK14271 256 AetarYVAGLSG 267
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-212 |
4.52e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.22 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAG-VRVNELH---PKD-- 74
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdLIVARLQqdpPRNve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 -----------RDIAMVFQSYALYPHMnVAGNMSYSLrLRKVAK--EKIASAVA--------AAAAKLGLDPllERRPKA 133
Cdd:PRK11147 81 gtvydfvaegiEEQAEYLKRYHDISHL-VETDPSEKN-LNELAKlqEQLDHHNLwqlenrinEVLAQLGLDP--DAALSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 134 LSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKklhgDLKATSIYVTHDQ--IEAMtlADRIVAMHGGV 211
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK----TFQGSIIFISHDRsfIRNM--ATRIVDLDRGK 230
|
.
gi 517057676 212 V 212
Cdd:PRK11147 231 L 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-210 |
6.82e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 6.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 16 VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAMVF------QSYALYPH 89
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 90 MNVAGNM---SYSL------------RLRKVAKEKIASavaaaaaklgLD---PLLERRPKALSGGQRQRVAMGRAIVRQ 151
Cdd:COG3845 351 MSVAENLilgRYRRppfsrggfldrkAIRAFAEELIEE----------FDvrtPGPDTPARSLSGGNQQKVILARELSRD 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057676 152 PKAFLFDEPLSNLDARLREQMRAEIKKL--HGdlkATSIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:COG3845 421 PKLLIAAQPTRGLDVGAIEFIHQRLLELrdAG---AAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-174 |
1.11e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.84 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGvrvnelHPKDRDIAMVFQSYALYPHMN-VAGNM 96
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG------GPLDFQRDSIARGLLYLGHAPgIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 97 SYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLD----ARLREQM 172
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARFAEAM 168
|
..
gi 517057676 173 RA 174
Cdd:cd03231 169 AG 170
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-210 |
1.14e-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: 75.06 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 19 LHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRD------IAMVFQSYALYpHMNV 92
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrysVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 93 AGNMSYSLRLRKvAKEKIASAVAAAAAKLGLDPL-----LERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDAR 167
Cdd:cd03290 96 EENITFGSPFNK-QRYKAVTDACSLQPDIDLLPFgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517057676 168 LREQ-MRAEIKKLHGDLKATSIYVTHdQIEAMTLADRIVAMHGG 210
Cdd:cd03290 175 LSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
8-242 |
1.20e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.93 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 8 NIRKAYG--HVQVLHGvdlEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAgVRVnelhpkdrdiamvfqSYA 85
Cdd:PRK13409 345 DLTKKLGdfSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKI---------------SYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 86 lyP-HMNVAGNMSYSLRLRKVA--------KEKIASavaaaaaKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFL 156
Cdd:PRK13409 406 --PqYIKPDYDGTVEDLLRSITddlgssyyKSEIIK-------PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 157 FDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHG--GVVQQVGSPLELYDrpanlfvagfi 234
Cdd:PRK13409 477 LDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEGepGKHGHASGPMDMRE----------- 545
|
....*....
gi 517057676 235 gspGMN-FL 242
Cdd:PRK13409 546 ---GMNrFL 551
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-217 |
1.47e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.84 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGHVQ-VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNEL-HPKDRD-IAM 79
Cdd:PRK10790 340 RIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLsHSVLRQgVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALyphmnVAGNMSYSLRL-RKVAKEKI-------ASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQ 151
Cdd:PRK10790 420 VQQDPVV-----LADTFLANVTLgRDISEEQVwqaletvQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 152 PKAFLFDEPLSNLDARlREQmrAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGS 217
Cdd:PRK10790 495 PQILILDEATANIDSG-TEQ--AIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-225 |
2.03e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.03 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 21 GVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELhpKDRDIA---MV--FQSYALYPHMNVAGN 95
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL--PGHQIArmgVVrtFQHVRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 96 M--------------------SYslrlRKVAKEKIASAVAAAAaKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAF 155
Cdd:PRK11300 101 LlvaqhqqlktglfsgllktpAF----RRAESEALDRAATWLE-RVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 156 LFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-234 |
2.75e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.92 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 17 QVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQSYALYpHMNVAG 94
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAVVFQDAGLF-NRSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 95 NmsysLRLRK---------VAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLD 165
Cdd:PRK13657 428 N----IRVGRpdatdeemrAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 166 ARLREQMRAEIKKL-HGdlkATSIYVTHdQIEAMTLADRIVAMHGGVVQQVGSPLELYD---RPANLFVAGFI 234
Cdd:PRK13657 504 VETEAKVKAALDELmKG---RTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDELVArggRFAALLRAQGM 572
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-228 |
3.89e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.11 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 19 LHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEvTSGEIRIAGVRVNELHPKD--RDIAM------------VFQSY 84
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYlsqqqsppfampVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 85 ALYPHmnvagnmsyslrlRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVR-------QPKAFLF 157
Cdd:COG4138 91 ALHQP-------------AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 158 DEPLSNLD-----------ARLREQMRAEIKKLHgDLkatsiyvTHdqieamTL--ADRIVAMHGGVVQQVGSPLELYDr 224
Cdd:COG4138 158 DEPMNSLDvaqqaaldrllRELCQQGITVVMSSH-DL-------NH------TLrhADRVWLLKQGKLVASGETAEVMT- 222
|
....
gi 517057676 225 PANL 228
Cdd:COG4138 223 PENL 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-221 |
3.92e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQ------------- 82
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQqlpaaegmtvrel 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 -SYALYPHMNVAGnmsyslRLRKVAKEKIASAVAAaaakLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPL 161
Cdd:PRK10575 106 vAIGRYPWHGALG------RFGAADREKVEEAISL----VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 162 SNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-245 |
7.21e-15 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 73.55 E-value: 7.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 28 DGEFVVLVGPSGCGKSTLLRMIAG--------LEEVTSGEIRIAGVRVNELH-------PKDRDIAMVFQSYALYPHMnV 92
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDEFRGSELQnyftkllEGDVKVIVKPQYVDLIPKA-V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 93 AGNMSYSLRlRKVAKEKIASAVAaaaaKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQM 172
Cdd:cd03236 104 KGKVGELLK-KKDERGKLDELVD----QLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 173 RAEIKKLHGDLKATsIYVTHDQIEAMTLADRIVAMHG-----GVVQQVGSPLElydrPANLFVAGFIGSPGMNFLEAS 245
Cdd:cd03236 179 ARLIRELAEDDNYV-LVVEHDLAVLDYLSDYIHCLYGepgayGVVTLPKSVRE----GINEFLDGYLPTENMRFREES 251
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-213 |
1.37e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.91 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAgVRVNELhpkDRDIAMVfqsYALYPHMNVagnms 97
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-VPDNQF---GREASLI---DAIGRKGDF----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 98 yslrlrKVAKEKIasavaaAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIK 177
Cdd:COG2401 113 ------KDAVELL------NAVGLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 517057676 178 KLHGDLKATSIYVT-HDQIEAMTLADRIVAMH-GGVVQ 213
Cdd:COG2401 181 KLARRAGITLVVAThHYDVIDDLQPDLLIFVGyGGVPE 218
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-194 |
1.60e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 72.37 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLE--EVTSGEIRIAGVRVNELHPKDRD---IA 78
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhlgIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQsyalYPhMNVAG--NMSYsLRLRKVAKEKIASAVAA--------AAAKL---GLDP-LLERR-PKALSGGQRQRVA 143
Cdd:CHL00131 88 LAFQ----YP-IEIPGvsNADF-LRLAYNSKRKFQGLPELdplefleiINEKLklvGMDPsFLSRNvNEGFSGGEKKRNE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517057676 144 MGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATsIYVTHDQ 194
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSI-ILITHYQ 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-209 |
1.72e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.45 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRiagvrvnelHPKDRDIAMVFQS 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLRIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAgnMSYSLRLRK-VAKEKIasavAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLS 162
Cdd:PRK09544 76 LYLDTTLPLT--VNRFLRLRPgTKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517057676 163 NLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHG 209
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-217 |
2.17e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.43 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAgvrvnelhpkdRDIAMVFQSYALyphMN--VAGN 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-----------RSIAYVPQQAWI---MNatVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 96 MSY-----SLRLRKVAKekiASAVAAAAAKL--GLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARL 168
Cdd:PTZ00243 741 ILFfdeedAARLADAVR---VSQLEADLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517057676 169 REQMRAE--IKKLHGDlkaTSIYVTHdQIEAMTLADRIVAMHGGVVQQVGS 217
Cdd:PTZ00243 818 GERVVEEcfLGALAGK---TRVLATH-QVHVVPRADYVVALGDGRVEFSGS 864
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-221 |
2.46e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 22 VDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNelhPKDRDIAM----VFQSYALYPHMNVAGNMS 97
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIATRRrvgyMSQAFSLYGELTVRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 98 YSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIK 177
Cdd:NF033858 362 LHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLI 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517057676 178 KLHGDLKATsIYV-THDQIEAMtLADRIVAMHGGVVQQVGSPLEL 221
Cdd:NF033858 442 ELSREDGVT-IFIsTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-174 |
3.13e-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: 73.43 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIaGVRVnelhpkdrDIAMVFQS 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------KLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 Y-ALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKL-GLDPllERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPL 161
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFkGSDQ--QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
170
....*....|...
gi 517057676 162 SNLDArlrEQMRA 174
Cdd:TIGR03719 472 NDLDV---ETLRA 481
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-229 |
4.36e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.47 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQSYALYphmnvAGN 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLF-----SGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 96 MSYSLR---------LRKvAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDA 166
Cdd:PLN03232 1326 VRFNIDpfsehndadLWE-ALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 167 RLREQMRAEIKKlhgDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLF 229
Cdd:PLN03232 1405 RTDSLIQRTIRE---EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-218 |
4.69e-14 |
|
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: 70.13 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYG-HV-QVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVN--ELHPKDRDIA 78
Cdd:cd03369 6 EIEVENLSVRYApDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIStiPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQSYALYphmnvAGNMSYSL-RLRKVAKEKIASAVAAAAAklGLDpllerrpkaLSGGQRQRVAMGRAIVRQPKAFLF 157
Cdd:cd03369 86 IIPQDPTLF-----SGTIRSNLdPFDEYSDEEIYGALRVSEG--GLN---------LSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 158 DEPLSNL----DARLREQMRAEIKklhgdlKATSIYVTHdQIEAMTLADRIVAMHGGVVQQVGSP 218
Cdd:cd03369 150 DEATASIdyatDALIQKTIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-215 |
5.30e-14 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 69.98 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQ-NIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVT---SGEIRIAGVRVNELHPK-DR 75
Cdd:cd03233 4 LSWRNISfTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKyPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 76 DIAMVFQSYALYPHMNVAGNMSYSLRLRkvAKEKIasavaaaaaklgldpllerrpKALSGGQRQRVAMGRAIVRQPKAF 155
Cdd:cd03233 84 EIIYVSEEDVHFPTLTVRETLDFALRCK--GNEFV---------------------RGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 156 LFDEPLSNLDARLREQMRAEIKKLHGDLKAT---SIYVTHDQIEAmtLADRIVAMHGGvvQQV 215
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTtfvSLYQASDEIYD--LFDKVLVLYEG--RQI 199
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-229 |
5.32e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 73.27 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLL----RMIagleEVTSGEIRIAGVRVNE--LHPKDRDIAMVFQSYALYP--- 88
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDgtv 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 89 HMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAF-LFDEPLSNLDAR 167
Cdd:PTZ00243 1401 RQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFiLMDEATANIDPA 1480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 168 LREQMRAEIKKLHGDLkaTSIYVTHdQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLF 229
Cdd:PTZ00243 1481 LDRQIQATVMSAFSAY--TVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-236 |
5.40e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.06 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAY----GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGL---EEVTSGEIRIAGVRVNELHPK 73
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 74 D------RDIAMVFQS--YALYPHMNVAGNMSYSLRLRKvakeKIASAVAAAAAKLGLD----PLLERR----PKALSGG 137
Cdd:PRK09473 90 ElnklraEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHK----GMSKAEAFEESVRMLDavkmPEARKRmkmyPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 138 QRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGS 217
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250
....*....|....*....
gi 517057676 218 PLELYDRPANLFVAGFIGS 236
Cdd:PRK09473 246 ARDVFYQPSHPYSIGLLNA 264
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-221 |
6.96e-14 |
|
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: 73.06 E-value: 6.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNE--LHPKDRDIAMVFQSYALYP---HMNV 92
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKigLHDLRFKITIIPQDPVLFSgslRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 93 AGNMSYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQM 172
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517057676 173 RAEIKKLHGDLKATSIYVTHDQIEAMTladRIVAMHGGVVQQVGSPLEL 221
Cdd:TIGR00957 1461 QSTIRTQFEDCTVLTIAHRLNTIMDYT---RVIVLDKGEVAEFGAPSNL 1506
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
11-209 |
8.87e-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: 68.75 E-value: 8.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 11 KAYG--HVQVLHGvdlEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNelhpkdrdiamvfqsyalyp 88
Cdd:cd03222 8 KRYGvfFLLVELG---VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 89 hmnvagnmsyslrlrkVAKEKIasavaaaaaklgldpllerrpkALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARL 168
Cdd:cd03222 65 ----------------YKPQYI----------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQ 106
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517057676 169 REQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHG 209
Cdd:cd03222 107 RLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-166 |
1.29e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 20 HGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNelhpKDRDiamVFQSYALY--------PHMN 91
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYHQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 92 VAGNMSYSLRLRKVAKEkiaSAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDA 166
Cdd:PRK13538 91 ALENLRFYQRLHGPGDD---EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-233 |
1.35e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 72.35 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 22 VDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRV-NELHPKDRDIAMVFQSYALYPHMNVAGNMSYSL 100
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 101 RLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLH 180
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR 1108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517057676 181 GDlkATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELydrpANLFVAGF 233
Cdd:TIGR01257 1109 SG--RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
7-218 |
1.58e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.86 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 7 QNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAG--LEEVTSGEIRIAG-----------------VRV 67
Cdd:PRK13547 5 DHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGdvtlngeplaaidaprlARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 68 NELHPKDRDIAMVFQSYAL-----YPHMNVAGNMSYslRLRKVAKEKIASAvaaaaaklGLDPLLERRPKALSGGQRQRV 142
Cdd:PRK13547 85 RAVLPQAAQPAFAFSAREIvllgrYPHARRAGALTH--RDGEIAWQALALA--------GATALVGRDVTTLSGGELARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 143 AMGRAI---------VRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQ 213
Cdd:PRK13547 155 QFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
....*
gi 517057676 214 QVGSP 218
Cdd:PRK13547 235 AHGAP 239
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-226 |
1.86e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.34 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRkAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKS----TLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRDIAM 79
Cdd:PRK10418 5 IELRNIA-LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQS--YALYPHMNVAGNMSYSLRLRkvAKEKIASAVAAAAAKLGL-DP--LLERRPKALSGGQRQRVAMGRAIVRQPKA 154
Cdd:PRK10418 84 IMQNprSAFNPLHTMHTHARETCLAL--GKPADDATLTAALEAVGLeNAarVLKLYPFEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 155 FLFDEPLSNLDARLreQMRaeIKKLHGDLKATS----IYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPA 226
Cdd:PRK10418 162 IIADEPTTDLDVVA--QAR--ILDLLESIVQKRalgmLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-212 |
2.66e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 14 GHVqVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRdIAMVFQSYAL---YP-- 88
Cdd:PRK15056 19 GHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-VAYVPQSEEVdwsFPvl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 89 -----HMNVAGNMSYslrLRKvAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:PRK15056 97 vedvvMMGRYGHMGW---LRR-AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517057676 164 LDARLREQMRAEIKKLHGDLKaTSIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMVKGTVL 220
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-225 |
3.76e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.55 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQN----IRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEE----VTSGEIRIAGVRVNELHP 72
Cdd:COG4170 1 MPLLDIRNltieIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 73 KDR------DIAMVFQ--SYALYPHMNVAGNMSYSL---RL------RKVAKEKIasaVAAAAAKLGL---DPLLERRPK 132
Cdd:COG4170 81 RERrkiigrEIAMIFQepSSCLDPSAKIGDQLIEAIpswTFkgkwwqRFKWRKKR---AIELLHRVGIkdhKDIMNSYPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 133 ALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQ---MRAEIKKLHGdlkaTSI-YVTHDqIEAMT-LADRIVAM 207
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQifrLLARLNQLQG----TSIlLISHD-LESISqWADTITVL 232
|
250
....*....|....*...
gi 517057676 208 HGGVVQQVGSPLELYDRP 225
Cdd:COG4170 233 YCGQTVESGPTEQILKSP 250
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-225 |
8.91e-13 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 67.57 E-value: 8.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGvrvnelhpkdrDIAMVFQSYALYPHM---NVAG 94
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------RISFSSQFSWIMPGTikeNIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 95 NMSY-SLRLRKVAK-----EKIASAVAAAAAKLGLDPLlerrpkALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARL 168
Cdd:cd03291 121 GVSYdEYRYKSVVKacqleEDITKFPEKDNTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517057676 169 REQM-RAEIKKLHGDlkATSIYVThDQIEAMTLADRIVAMHGGVVQQVGSPLELYD-RP 225
Cdd:cd03291 195 EKEIfESCVCKLMAN--KTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSlRP 250
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-214 |
9.53e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.97 E-value: 9.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMV 80
Cdd:PRK10789 315 DVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSYALYPHmNVAGNMSY------SLRLRKVAK-----EKIASAVAaaaaklGLDPLLERRPKALSGGQRQRVAMGRAIV 149
Cdd:PRK10789 395 SQTPFLFSD-TVANNIALgrpdatQQEIEHVARlasvhDDILRLPQ------GYDTEVGERGVMLSGGQKQRISIARALL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517057676 150 RQPKAFLFDEPLSNLDARLREQMraeIKKLHGDLKATSIYVTHDQIEAMTLADRIVAM-HGGVVQQ 214
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQI---LHNLRQWGEGRTVIISAHRLSALTEASEILVMqHGHIAQR 530
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-166 |
2.56e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 8 NIRKAYGHVQ-------------VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTS--GEIRIAGVRVNElhP 72
Cdd:PLN03211 60 NIKRILGHKPkisdetrqiqertILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK--Q 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 73 KDRDIAMVFQSYALYPHMNVAGNMSYS--LRL-RKVAKEKIASAVAAAAAKLGLDP-----LLERRPKALSGGQRQRVAM 144
Cdd:PLN03211 138 ILKRTGFVTQDDILYPHLTVRETLVFCslLRLpKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSI 217
|
170 180
....*....|....*....|..
gi 517057676 145 GRAIVRQPKAFLFDEPLSNLDA 166
Cdd:PLN03211 218 AHEMLINPSLLILDEPTSGLDA 239
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-165 |
2.87e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 25 EIHDGEFVVLVGPSGCGKSTLLRMIAGLEEvTSGEIRIAGVRVNELHPKDRD-------------IAM-VFQSYALYPHM 90
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELArhraylsqqqtppFAMpVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 91 NVAGNMSYSLrLRKVAKekiasavaaaaaKLGLDPLLERRPKALSGGQRQRVAMGRAIVR-------QPKAFLFDEPLSN 163
Cdd:PRK03695 97 KTRTEAVASA-LNEVAE------------ALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNS 163
|
..
gi 517057676 164 LD 165
Cdd:PRK03695 164 LD 165
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
25-225 |
3.14e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 66.69 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 25 EIHDGEFVVLVGPSGCGKSTLLRMIAGLEE----VTSGEIRIAGVRVNELHPKDR------DIAMVFQS--YALYPHMNV 92
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPCYTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 93 AGNMSYSLRLRKVAKEKIASAVAAAAAKL-GL-DPL--LERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARL 168
Cdd:PRK11022 109 GFQIMEAIKVHQGGNKKTRRQRAIDLLNQvGIpDPAsrLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTI 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 169 REQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDRP 225
Cdd:PRK11022 189 QAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-221 |
3.60e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.84 E-value: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 19 LHGVDLEIHDGEFVVLVGPSGCGKSTLLR-MIAGLEEVTSGEIRIAGvrvnelhpkdrDIAMVFQSYALYpHMNVAGNMS 97
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-----------TVAYVPQVSWIF-NATVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 98 YSLRLRKVAKEKiASAVAAAAAKLGLDP---LLE--RRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQM 172
Cdd:PLN03130 701 FGSPFDPERYER-AIDVTALQHDLDLLPggdLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV 779
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517057676 173 RAeiKKLHGDLKA-TSIYVThDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:PLN03130 780 FD--KCIKDELRGkTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-192 |
4.14e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYG---HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIagvrvNELHP-KD----- 74
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII-----NDSHNlKDinlkw 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 --RDIAMVFQ-------------SYALYP---------HMNVAGNMSYS-LRLRKVAKEKIASAVAAAAAKLGLDPLLER 129
Cdd:PTZ00265 458 wrSKIGVVSQdpllfsnsiknniKYSLYSlkdlealsnYYNEDGNDSQEnKNKRNSCRAKCAGDLNDMSNTTDSNELIEM 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 130 RPK--------------------------------------ALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQ 171
Cdd:PTZ00265 538 RKNyqtikdsevvdvskkvlihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
250 260
....*....|....*....|.
gi 517057676 172 MRAEIKKLHGDLKATSIYVTH 192
Cdd:PTZ00265 618 VQKTINNLKGNENRITIIIAH 638
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-210 |
5.02e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 8 NIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPK---DRDIAMVFQSY 84
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 85 ALYPHMNVAGNM---SYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPL 161
Cdd:PRK10982 83 NLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517057676 162 SNLDARLREQMRAEIKKLHgDLKATSIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-217 |
9.59e-12 |
|
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: 66.58 E-value: 9.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 26 IHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNElhpkdrDIAMVFQSYALYPHMN-----VAGNMSYSL 100
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDVHQNMGYCPQFDaiddlLTGREHLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 101 --RLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKK 178
Cdd:TIGR01257 2036 yaRLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170 180 190
....*....|....*....|....*....|....*....
gi 517057676 179 LHGDLKATsIYVTHDQIEAMTLADRIVAMHGGVVQQVGS 217
Cdd:TIGR01257 2116 IIREGRAV-VLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-221 |
1.61e-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: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGvrvnelhpkdrDIAMVFQSYALYPHM---NVAG 94
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------RISFSPQTSWIMPGTikdNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 95 NMSY-SLRLRKVAK-----EKIASAVAAAAAKLGLDPLlerrpkALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARL 168
Cdd:TIGR01271 510 GLSYdEYRYTSVIKacqleEDIALFPEKDKTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517057676 169 -REQMRAEIKKLHGDlkATSIYVThDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:TIGR01271 584 eKEIFESCLCKLMSN--KTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-222 |
1.97e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.38 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 19 LHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGleevtsgeiriagvrvnELHPKDRDIAMVFQSYALYPHMNVAGNMSY 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVVIRGSVAYVPQVSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 99 S---LRLRKVAKEKIASAVAAAAAKLGLDPLLER-------RPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARL 168
Cdd:PLN03232 696 ReniLFGSDFESERYWRAIDVTALQHDLDLLPGRdlteigeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517057676 169 REQMRAEIKKlHGDLKATSIYVThDQIEAMTLADRIVAMHGGVVQQVGSPLELY 222
Cdd:PLN03232 776 AHQVFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-221 |
3.02e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.05 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 57 SGEIRIAGVRVNELHPKD-RDIAMVFQSYALYPHMNVAGNMsyslrlrKVAKEKIASAVAAAAAKLG-LDPLLERRP--- 131
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENI-------KFGKEDATREDVKRACKFAaIDEFIESLPnky 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 132 --------KALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHdQIEAMTLADR 203
Cdd:PTZ00265 1349 dtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
170 180
....*....|....*....|...
gi 517057676 204 IVAMH-----GGVVQQVGSPLEL 221
Cdd:PTZ00265 1428 IVVFNnpdrtGSFVQAHGTHEEL 1450
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-179 |
4.03e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 61.49 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 14 GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEE--VTSGEIRIAGVRVNELHPkdRDIAMVFQSYALYPHMN 91
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQ--RSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 92 VAGNMSYSLRLRkvakekiasavaaaaaklgldpllerrpkALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQ 171
Cdd:cd03232 96 VREALRFSALLR-----------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
....*...
gi 517057676 172 MRAEIKKL 179
Cdd:cd03232 147 IVRFLKKL 154
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-210 |
4.97e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 19 LHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR-DIAMVFQSY-----ALYPHMNV 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 93 AGNMSYSlRLRKVAKEKIASAVAAAAAKLGlD---------PLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:PRK10762 348 KENMSLT-ALRYFSRAGGSLKHADEQQAVS-DfirlfniktPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517057676 164 LDARLREqmraEIKKLHGDLKA---TSIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:PRK10762 426 VDVGAKK----EIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-177 |
5.29e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.12 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVN-ELHPKDRDIAMVFQ 82
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 SYALYPHMNVAGNMSYSLRLRKVAKEkiasaVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLS 162
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170
....*....|....*
gi 517057676 163 NLDARLREQMRAEIK 177
Cdd:PRK13540 157 ALDELSLLTIITKIQ 171
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-212 |
6.26e-11 |
|
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: 63.65 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 29 GEFVVLVGPSGCGKSTLLRMIAG------------------------------LEEVTSGEIRIAgvrvneLHPKDRD-I 77
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGelkpnlgdydeepswdevlkrfrgtelqdyFKKLANGEIKVA------HKPQYVDlI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 78 AMVFQsyalyphmnvaGNMSYSLR---LRKVAKEKIAsavaaaaaKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKA 154
Cdd:COG1245 173 PKVFK-----------GTVRELLEkvdERGKLDELAE--------KLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 155 FLFDEPLSNLDarLREQMRAE--IKKLHGDLKATsIYVTHDQIEAMTLADRIVAMHG-----GVV 212
Cdd:COG1245 234 YFFDEPSSYLD--IYQRLNVArlIRELAEEGKYV-LVVEHDLAILDYLADYVHILYGepgvyGVV 295
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-214 |
9.33e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 22 VDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQSYALYPHMnvagnmsys 99
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAVFTDFHLFDQL--------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 100 lrLRKVAKEKIASAVAAAAAKLGLDPLLE------RRPKaLSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMR 173
Cdd:PRK10522 413 --LGPEGKPANPALVEKWLERLKMAHKLEledgriSNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFY 489
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517057676 174 AEIKKLHGDLKATSIYVTHDQiEAMTLADRIVAMHGGVVQQ 214
Cdd:PRK10522 490 QVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLSE 529
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-165 |
1.73e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.86 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGvRVNELHPKDRDIAMVFQSYALYPHMNVAGNMS 97
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG-KTATRGDRSRFMAYLGHLPGLKADLSTLENLH 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 98 YSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRpkaLSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLD 165
Cdd:PRK13543 105 FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQ---LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
8-216 |
1.80e-10 |
|
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: 59.26 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 8 NIRKAYGHVqvLHGVDLEIHDGEFVVLVGPSGCGKSTLLRmiAGLEEVtsgeiriAGVRVNELHPKDRDIAMVFQSyaly 87
Cdd:cd03238 2 TVSGANVHN--LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYAS-------GKARLISFLPKFSRNKLIFID---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 88 phmnvagnmsySLRLrkvakekiasavaaaAAKLGLDPL-LERRPKALSGGQRQRVAMGRAIVRQPKA--FLFDEPLSNL 164
Cdd:cd03238 67 -----------QLQF---------------LIDVGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPGtlFILDEPSTGL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 165 DARLREQMRAEIKKLhGDLKATSIYVTHDQiEAMTLADRIVAM------HGGVVQQVG 216
Cdd:cd03238 121 HQQDINQLLEVIKGL-IDLGNTVILIEHNL-DVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-88 |
3.24e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.80 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLE--EVTSGEIRIAGVRVNELHPKDR---DIA 78
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIF 81
|
90
....*....|
gi 517057676 79 MVFQsyalYP 88
Cdd:PRK09580 82 MAFQ----YP 87
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-215 |
3.73e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 5 DIQNI-RKAYGHVQvlhGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD---RDIAMV 80
Cdd:PRK09700 267 EVRNVtSRDRKKVR---DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 81 FQSY---ALYPHMNVAGNMSYSLRLRK---------VAKEKIASAVAAAAAKLGLD-PLLERRPKALSGGQRQRVAMGRA 147
Cdd:PRK09700 344 TESRrdnGFFPNFSIAQNMAISRSLKDggykgamglFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 148 IVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATsIYVTHDQIEAMTLADRIVAMHGGVVQQV 215
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVI-LMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-224 |
3.99e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR---DIAMVFQ 82
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAvcpRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 SYA--LYPHMNVAGNMSYSLRL----RKVAKEKIAsavaaaaaKL----GLDPLLERRPKALSGGQRQRVAMGRAIVRQP 152
Cdd:NF033858 84 GLGknLYPTLSVFENLDFFGRLfgqdAAERRRRID--------ELlratGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 153 KAFLFDEPLSNLD--AR-----LREQMRAEikklHGD---LKATSiYvthdqieaMTLADR---IVAMHGGVVQQVGSPL 219
Cdd:NF033858 156 DLLILDEPTTGVDplSRrqfweLIDRIRAE----RPGmsvLVATA-Y--------MEEAERfdwLVAMDAGRVLATGTPA 222
|
....*
gi 517057676 220 ELYDR 224
Cdd:NF033858 223 ELLAR 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-212 |
9.54e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.54 E-value: 9.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 22 VDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVN------------ELHPKDRdiamvfQSYALYPH 89
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdairagiMLCPEDR------KAEGIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 90 MNVAGNMSYSLRL--------------RKVAKEKIAsavaaaaaKLGLD-PLLERRPKALSGGQRQRVAMGRAIVRQPKA 154
Cdd:PRK11288 346 HSVADNINISARRhhlragclinnrweAENADRFIR--------SLNIKtPSREQLIMNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057676 155 FLFDEPLSNLDArlreQMRAEIKKLHGDLKA---TSIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:PRK11288 418 ILLDEPTRGIDV----GAKHEIYNVIYELAAqgvAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
235-282 |
1.20e-09 |
|
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: 53.36 E-value: 1.20e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 517057676 235 GSPGMNFLEASYDAGGVRLK-DGTIVPLAKP----LPLVDGAKVTLGIRPEHV 282
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLLVLgGGVTLPLPEGqvlaLKLYVGKEVILGIRPEHI 53
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-221 |
1.23e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD--RDIAMVFQSYALYphmnvAGN 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGIIPQAPVLF-----SGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 96 MSYSL------------------RLRKVAKEKiasavaaaaaKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLF 157
Cdd:PLN03130 1329 VRFNLdpfnehndadlwesleraHLKDVIRRN----------SLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVL 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 158 DEPLSNLDAR----LREQMRAEIKklhgdlKATSIYVTHdQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:PLN03130 1399 DEATAAVDVRtdalIQKTIREEFK------SCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-197 |
1.48e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAG------LEEVT-------SGEI-----RIAGV 65
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgySNDLTlfgrrrgSGETiwdikKHIGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 66 RVNELHPKDRDIAMV--------FQSYALYphmnvagnMSYSLRLRKVAKEKIASavaaaaakLGLDPLLERRP-KALSG 136
Cdd:PRK10938 341 VSSSLHLDYRVSTSVrnvilsgfFDSIGIY--------QAVSDRQQKLAQQWLDI--------LGIDKRTADAPfHSLSW 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057676 137 GQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEA 197
Cdd:PRK10938 405 GQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
3-215 |
1.78e-09 |
|
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: 59.04 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGHVQVLHG-----VDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNelhPKDRD- 76
Cdd:COG4615 327 TLELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREa 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 77 ----IAMVFQSYALYPH-MNVAGNmsyslRLRKVAKEKIasavaaaaAKLGLDPLLERR-----PKALSGGQRQRVAM-- 144
Cdd:COG4615 404 yrqlFSAVFSDFHLFDRlLGLDGE-----ADPARARELL--------ERLELDHKVSVEdgrfsTTDLSQGQRKRLALlv 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 145 ----GRAIvrqpkaFLFDEPLSNLDARLREQMRAEIkkLhGDLKA---TSIYVTHDQiEAMTLADRIVAMHGGVVQQV 215
Cdd:COG4615 471 alleDRPI------LVFDEWAADQDPEFRRVFYTEL--L-PELKArgkTVIAISHDD-RYFDLADRVLKMDYGKLVEL 538
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-217 |
1.95e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 28 DGEFVVLVGPSGCGKSTLLRMIAG------------------------------LEEVTSGEIRIAgvrvneLHPKDRD- 76
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepswdevlkrfrgtelqnyFKKLYNGEIKVV------HKPQYVDl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 77 IAMVFQsyalyphmnvaGNMSYSLRL---RKVAKEKIAsavaaaaaKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPK 153
Cdd:PRK13409 172 IPKVFK-----------GKVRELLKKvdeRGKLDEVVE--------RLGLENILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517057676 154 AFLFDEPLSNLDarLREQMRAE--IKKLHGDlKATsIYVTHDQIEAMTLADRIVAMHG-----GVVQQVGS 217
Cdd:PRK13409 233 FYFFDEPTSYLD--IRQRLNVArlIRELAEG-KYV-LVVEHDLAVLDYLADNVHIAYGepgayGVVSKPKG 299
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-210 |
2.25e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDRD---IAMVFQ 82
Cdd:PRK10762 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 83 SYALYPHMNVAGNM----SYSLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFD 158
Cdd:PRK10762 87 ELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 159 EPLSNLDARLREQMRAEIKklhgDLKATS---IYVTHDQIEAMTLADRIVAMHGG 210
Cdd:PRK10762 167 EPTDALTDTETESLFRVIR----ELKSQGrgiVYISHRLKEIFEICDDVTVFRDG 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-215 |
3.05e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 16 VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIA----GLEEVTSGEIRIAGVRVNELHPKDR-DIAMVFQSYALYPHM 90
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 91 NVAGNMSYSLRLRKVA--------KEKIASAVAAAAAKLGLDplLERRPK-------ALSGGQRQRVAMGRAIVRQPKAF 155
Cdd:TIGR00956 154 TVGETLDFAARCKTPQnrpdgvsrEEYAKHIADVYMATYGLS--HTRNTKvgndfvrGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 156 LFDEPLSNLDARLREQMRAEIKKLHGDLKAT---SIYVTHDqiEAMTLADRIVAMHGGvvQQV 215
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALKTSANILDTTplvAIYQCSQ--DAYELFDKVIVLYEG--YQI 290
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-225 |
4.62e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.12 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQN----IRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEE----VTSGEIRIAGVRVNELHP 72
Cdd:PRK15093 1 MPLLDIRNltieFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 73 KDR------DIAMVFQ--SYALYPHMNVAGNM-------SYSLRLRKVAKEKiASAVAAAAAKLGL---DPLLERRPKAL 134
Cdd:PRK15093 81 RERrklvghNVSMIFQepQSCLDPSERVGRQLmqnipgwTYKGRWWQRFGWR-KRRAIELLHRVGIkdhKDAMRSFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 135 SGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQ 214
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
250
....*....|.
gi 517057676 215 VGSPLELYDRP 225
Cdd:PRK15093 240 TAPSKELVTTP 250
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-170 |
5.28e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.26 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 36 GPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKdrDIAMVFQSYALYPHMNVAGNMSYSLRLRKVAKekiasAVA 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP--YCTYIGHNLGLKLEMTVFENLKFWSEIYNSAE-----TLY 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 116 AAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLRE 170
Cdd:PRK13541 106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-193 |
5.34e-09 |
|
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: 57.64 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAY-GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIA-GVRVNELHpkdrdiamvfQS 83
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLP----------QE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGNMSYSLR----------------------LRKVAKEKIASAVAAAAAKL-GLDPLLERRPKAL------ 134
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVAeikdaldrfneisakyaepdadFDKLAAEQAELQEIIDAADAwDLDSQLEIAMDALrcppwd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 135 ------SGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDArlrEQMRAEIKKLHgDLKATSIYVTHD 193
Cdd:TIGR03719 157 advtklSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESVAWLERHLQ-EYPGTVVAVTHD 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-62 |
6.11e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 6.11e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRI 62
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-217 |
7.50e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.23 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAY--GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEvTSGEIRIAGVRVNE--LHPKDRDIAM 79
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSvtLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 80 VFQSYALYP---HMNVAGNMSYS-LRLRKVAKEkiasavaaaaakLGLDPLLERRPK-----------ALSGGQRQRVAM 144
Cdd:TIGR01271 1297 IPQKVFIFSgtfRKNLDPYEQWSdEEIWKVAEE------------VGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCL 1364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 145 GRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDlkATSIYVTHdQIEAMTLADRIVAMHGGVVQQVGS 217
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN--CTVILSEH-RVEALLECQQFLVIEGSSVKQYDS 1434
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
121-228 |
1.60e-08 |
|
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: 56.17 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 121 LGLDPL-LERRPKALSGGQRQRVAMGRAIVRQPKAFLF--DEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHDQiEA 197
Cdd:TIGR00630 475 VGLDYLsLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLR-DLGNTLIVVEHDE-DT 552
|
90 100 110
....*....|....*....|....*....|....*..
gi 517057676 198 MTLADRIVAM------HGGVVQQVGSPLELYDRPANL 228
Cdd:TIGR00630 553 IRAADYVIDIgpgageHGGEVVASGTPEEILANPDSL 589
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-181 |
1.76e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 1 MASIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEI-----RIAGVRVNELHP--- 72
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqfsHITRLSFEQLQKlvs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 73 ---KDRDIAMvfqsyaLYPHMNVAGnmsyslrlrKVAKEKIASAV------AAAAAKLGLDPLLERRPKALSGGQRQRVA 143
Cdd:PRK10938 81 dewQRNNTDM------LSPGEDDTG---------RTTAEIIQDEVkdparcEQLAQQFGITALLDRRFKYLSTGETRKTL 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 517057676 144 MGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHG 181
Cdd:PRK10938 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQ 183
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-210 |
3.41e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 14 GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAglEEVTSGEIRiAGVRVNELHPKD----RDIAMVFQSYALYPH 89
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVIT-GGDRLVNGRPLDssfqRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 90 MNVAGNMSYSLRLR---KVAKEKIASAVAAAAAKLGL----DPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLF-DEPL 161
Cdd:TIGR00956 851 STVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMesyaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPT 930
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517057676 162 SNLDARLREQMRAEIKKL--HGDlkatSIYVTHDQIEAMTLA--DRIVAMHGG 210
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLadHGQ----AILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
275-344 |
5.99e-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: 49.16 E-value: 5.99e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517057676 275 LGIRPEHVLMSDGGAGLAADVELVEPTGFGIILHLALHGLPFKIFTL---TRDALKAGPKVNVAFPAQYLHVF 344
Cdd:pfam08402 1 LAIRPEKIRLAAAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVpnaHARPPAPGDRVGLGWDPEDAHVL 73
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
8-212 |
7.49e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 52.26 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 8 NIRKAYGHVqvLHGVDLEIHDGEFVVLVGPSGCGKSTL----------LRMIAGLeevtSGEIRiagvrvNELHPKDRD- 76
Cdd:cd03270 2 IVRGAREHN--LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESL----SAYAR------QFLGQMDKPd 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 77 ----------IAMVFQSYALYPHMNVA---GNMSYsLRLRkVAKEKIASAVAAAAaKLGLDPL-LERRPKALSGGQRQRV 142
Cdd:cd03270 70 vdsieglspaIAIDQKTTSRNPRSTVGtvtEIYDY-LRLL-FARVGIRERLGFLV-DVGLGYLtLSRSAPTLSGGEAQRI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 143 AMGRAIVRQPKA--FLFDEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHDQiEAMTLADRIVAM------HGGVV 212
Cdd:cd03270 147 RLATQIGSGLTGvlYVLDEPSIGLHPRDNDRLIETLKRLR-DLGNTVLVVEHDE-DTIRAADHVIDIgpgagvHGGEI 222
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-217 |
7.92e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 52.93 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEvTSGEIRIAGVRVNE--LHPKDRDIAMVFQSYALYP---HMNV 92
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvpLQKWRKAFGVIPQKVFIFSgtfRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 93 AGNMSYS-LRLRKVAKEkiasavaaaaakLGLDPLLERRPK-----------ALSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:cd03289 98 DPYGKWSdEEIWKVAEE------------VGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 161 LSNLDARLREQMRAEIKKLHGDlkATSIYVTHdQIEAMTLADRIVAMHGGVVQQVGS 217
Cdd:cd03289 166 SAHLDPITYQVIRKTLKQAFAD--CTVILSEH-RIEAMLECQRFLVIEENKVRQYDS 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-193 |
8.73e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 8.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 7 QNIRKAYGH-VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIA-GVRVN------ELHP-KD--- 74
Cdd:PRK11819 10 NRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVGylpqepQLDPeKTvre 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 75 ------RDIAMVFQSY-ALYphMNVAGNMSYSLRL-RKVAK--EKIASAVAAAaaklgLDPLLE------RRP------K 132
Cdd:PRK11819 90 nveegvAEVKAALDRFnEIY--AAYAEPDADFDALaAEQGElqEIIDAADAWD-----LDSQLEiamdalRCPpwdakvT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517057676 133 ALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDAR----LrEQMraeikkLHgDLKATSIYVTHD 193
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAEsvawL-EQF------LH-DYPGTVVAVTHD 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-210 |
1.67e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 22 VDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDR-DIAMVF-----QSYALY---P-HMN 91
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYldaPlAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 92 VAG----NMSYSLRLRKVAKekiasAVAAAAAKLGLDPLLERRP-KALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDA 166
Cdd:PRK15439 362 VCAlthnRRGFWIKPARENA-----VLERYRRALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517057676 167 RLREQMRAEIKKLHGDLKATsIYVTHDQIEAMTLADRIVAMHGG 210
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAV-LFISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-207 |
2.40e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKDrdiamvfQS 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQD-------HA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YALYPHMNVAGNMSY-------SLRLRKVakekiasavaaaaaklgLDPLL------ERRPKALSGGQRQRVAMGRAIVR 150
Cdd:PRK15064 393 YDFENDLTLFDWMSQwrqegddEQAVRGT-----------------LGRLLfsqddiKKSVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 151 QPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLkatsIYVTHDQIEAMTLADRIVAM 207
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALEKYEGTL----IFVSHDREFVSSLATRIIEI 508
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-165 |
2.98e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 21 GVDLEIHdgefVVLVGPSGCGKSTLLRMIAGLEEVTSGEI-RIAGVRV---NELHPKDRDIAmvfQSYALYPHMNVAGNM 96
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVfRSAKVRMavfSQHHVDGLDLS---SNPLLYMMRCFPGVP 603
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517057676 97 SYSLRLRkvakekiaSAVAAAAAKLGLDPLLerrpkALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLD 165
Cdd:PLN03073 604 EQKLRAH--------LGSFGVTGNLALQPMY-----TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-213 |
3.86e-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: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 15 HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGL-EEVTSGEIRIAGVRVNELHPKD---RDIAMVFQS---YALY 87
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 88 PHMNVAGNMSYSL--------RLRKVAKEKIASAVAAAAAKLGLDPLLerrPKA-LSGGQRQRVAMGRAIVRQPKAFLFD 158
Cdd:TIGR02633 352 PILGVGKNITLSVlksfcfkmRIDAAAELQIIGSAIQRLKVKTASPFL---PIGrLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 159 EPLSNLDArlreQMRAEIKKLHGDLKATS---IYVTHDQIEAMTLADRIVAMHGGVVQ 213
Cdd:TIGR02633 429 EPTRGVDV----GAKYEIYKLINQLAQEGvaiIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-167 |
5.76e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 16 VQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEE--VTSGEIRIAGvrvnelHPKDRDIAMVFQSYALY-----P 88
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISG------FPKKQETFARISGYCEQndihsP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 89 HMNVAGNMSYS--LRLRK-VAKEKIASAVAAAAAKLGLDPLLER---RP--KALSGGQRQRVAMGRAIVRQPKAFLFDEP 160
Cdd:PLN03140 967 QVTVRESLIYSafLRLPKeVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
....*..
gi 517057676 161 LSNLDAR 167
Cdd:PLN03140 1047 TSGLDAR 1053
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-221 |
6.93e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.50 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 3 SIDIQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCG--KSTLLRMIAGLEE-------VTSGEIRIAGVRVNELHPK 73
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAgrrpwrf*TWCANRRALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 74 DRDIAMvfQSYALYPHMNVAGnmsyslRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPK 153
Cdd:NF000106 93 VR*GRR--ESFSGRENLYMIG------R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517057676 154 AFLFDEPLSNLDARLREQMRAEIKKLHGDlKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLEL 221
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-193 |
7.88e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 29 GEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIaGVRVnelhpkdrDIAMvFQSY--ALYPHMNVAGNMS-------YS 99
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL--------EVAY-FDQHraELDPEKTVMDNLAegkqevmVN 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 100 LRLRKVakekiasavaaaaakLG------LDPLLERRP-KALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDA---RLR 169
Cdd:PRK11147 415 GRPRHV---------------LGylqdflFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVetlELL 479
|
170 180
....*....|....*....|....
gi 517057676 170 EQMRAeikklhgDLKATSIYVTHD 193
Cdd:PRK11147 480 EELLD-------SYQGTVLLVSHD 496
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-206 |
3.96e-06 |
|
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: 46.21 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 29 GEFVVLVGPSGCGKSTLLRMIAG-LEEVTSGEIRIAGVRVNELHPKDRdiamvfqsyalyphmnvagnmsyslrlrkvak 107
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQL-------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 108 ekiasavaaaaaklgLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKKLHGDLKATS 187
Cdd:smart00382 50 ---------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSE 114
|
170 180
....*....|....*....|....
gi 517057676 188 -----IYVTHDQIEAMTLADRIVA 206
Cdd:smart00382 115 knltvILTTNDEKDLGPALLRRRF 138
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-210 |
5.33e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 15 HVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGL-EEVTSGEIRIAGVRVNELHPKD---RDIAMVFQS---YALY 87
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 88 PHMNVAGNM--------SYSLRLRKVAKEKIASAVAAAAAKLGLDPLLerRPKALSGGQRQRVAMGRAIVRQPKAFLFDE 159
Cdd:PRK13549 354 PVMGVGKNItlaaldrfTGGSRIDDAAELKTILESIQRLKVKTASPEL--AIARLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517057676 160 PLSNLDArlreQMRAEIKKLHGDLKATS---IYVTHDQIEAMTLADRIVAMHGG 210
Cdd:PRK13549 432 PTRGIDV----GAKYEIYKLINQLVQQGvaiIVISSELPEVLGLSDRVLVMHEG 481
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-204 |
6.21e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 7 QNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTS--GEIRIAGvrvNELHPKD-RD-----IA 78
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG---EVCRFKDiRDsealgIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 79 MVFQSYALYPHMNVAGNM-------SYSL----RLRKVAKEKIasavaaaaAKLGLDPLLERRPKALSGGQRQRVAMGRA 147
Cdd:NF040905 82 IIHQELALIPYLSIAENIflgneraKRGVidwnETNRRARELL--------AKVGLDESPDTLVTDIGVGKQQLVEIAKA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 148 IVRQPKAFLFDEPlsnlDARLREQMRAEIKKLHGDLKA---TSIYVTHDQIEAMTLADRI 204
Cdd:NF040905 154 LSKDVKLLILDEP----TAALNEEDSAALLDLLLELKAqgiTSIIISHKLNEIRRVADSI 209
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-229 |
9.48e-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: 46.44 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 18 VLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNEL--HPKDRDIAMVFQSYALYphmnvAGN 95
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplHTLRSRLSIILQDPILF-----SGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 96 MSYSLR-LRKVAKEKIASAVAAAAAKL-------GLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDAR 167
Cdd:cd03288 111 IRFNLDpECKCTDDRLWEALEIAQLKNmvkslpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 168 LREQMRAEIKKLHGDlkATSIYVTHdQIEAMTLADRIVAMHGGVVQQVGSPLELYDRPANLF 229
Cdd:cd03288 191 TENILQKVVMTAFAD--RTVVTIAH-RVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-212 |
1.33e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 22 VDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAGVRVNELHPKD---RDIAMVFQ---SYALYPHMNVA-- 93
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainHGFALVTEerrSTGIYAYLDIGfn 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 94 ---GNM-SYSLRLRKVAKEKIASAVaaaaaKLGLDPLLERRPK------ALSGGQRQRVAMGRAIVRQPKAFLFDEPLSN 163
Cdd:PRK10982 347 sliSNIrNYKNKVGLLDNSRMKSDT-----QWVIDSMRVKTPGhrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517057676 164 LDARLREQMRAEIKKLHGDLKATsIYVTHDQIEAMTLADRIVAMHGGVV 212
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKKDKGI-IIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-224 |
1.48e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 6 IQNIRKAYGHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIA-GVRVNelhpkdrdiamvfqSY 84
Cdd:PRK10636 315 MEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLG--------------YF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 85 ALYPHMNVAGNMSYSLRLRKVAKEKIASAVAAAAAKLGL--DPLLERRPKaLSGGQRQRVAMGRAIVRQPKAFLFDEPLS 162
Cdd:PRK10636 381 AQHQLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFqgDKVTEETRR-FSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517057676 163 NLDARLREQMRAEIKKLHGDLkatsIYVTHDQIEAMTLADRIVAMHGGVVQQVGSPLELYDR 224
Cdd:PRK10636 460 HLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
25-159 |
2.55e-05 |
|
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: 45.90 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 25 EIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIagvrvnelhPKDRDIAMVFQSyalyPHMNVAgnmsySLR--- 101
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQR----PYMTLG-----TLRdqi 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 102 -------------LRKVAKEKIASAvaaaaakLGLDPLLERR---------PKALSGGQRQRVAMGRAIVRQPKAFLFDE 159
Cdd:TIGR00954 536 iypdssedmkrrgLSDKDLEQILDN-------VQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-216 |
2.91e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 19 LHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRiagvrvnelhpKDRDIAMVFQSYALYPHMNVAGNMSY 98
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------RNGEVSVIAISAGLSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 99 SLRLRKVAKEKIASAVAAAAAKLGLDPLLERRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLDARLREQMRAEIKK 178
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 517057676 179 LHgDLKATSIYVTHDQIEAMTLADRIVAMHGGVVQQVG 216
Cdd:PRK13546 189 FK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
121-220 |
4.30e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 121 LGLDPL-LERRPKALSGGQRQRVAMGRAIVRQPKA--FLFDEPLSNLDARLREQMRAEIKKLHgDLKATSIYVTHDQiEA 197
Cdd:PRK00635 463 LGLPYLtPERALATLSGGEQERTALAKHLGAELIGitYILDEPSIGLHPQDTHKLINVIKKLR-DQGNTVLLVEHDE-QM 540
|
90 100
....*....|....*....|....*....
gi 517057676 198 MTLADRIV------AMHGGVVQQVGSPLE 220
Cdd:PRK00635 541 ISLADRIIdigpgaGIFGGEVLFNGSPRE 569
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
29-61 |
4.96e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.84 E-value: 4.96e-04
10 20 30
....*....|....*....|....*....|...
gi 517057676 29 GEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIR 61
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
129-165 |
9.30e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 9.30e-04
10 20 30
....*....|....*....|....*....|....*..
gi 517057676 129 RRPKALSGGQRQRVAMGRAIVRQPKAFLFDEPLSNLD 165
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-205 |
1.00e-03 |
|
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: 39.90 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 4 IDIQNIRKAYGHVQVlhgvdlEIHDGeFVVLVGPSGCGKSTLlrmIAGLEEVTSGEIRiagvRVNELHPKDRDIAMVFQS 83
Cdd:cd03240 4 LSIRNIRSFHERSEI------EFFSP-LTLIVGQNGAGKTTI---IEALKYALTGELP----PNSKGGAHDPKLIREGEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 84 YAlyphmnvagnmSYSLRLRKVAKEKIASAVAAAAAKL-------GLDPLLERRPKALSGGQRQ------RVAMGRAI-V 149
Cdd:cd03240 70 RA-----------QVKLAFENANGKKYTITRSLAILENvifchqgESNWPLLDMRGRCSGGEKVlasliiRLALAETFgS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517057676 150 RQPKAFLfDEPLSNLDA-RLREQMRAEIKKLHGDLKATSIYVTHDQiEAMTLADRIV 205
Cdd:cd03240 139 NCGILAL-DEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDE-ELVDAADHIY 193
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
36-62 |
2.26e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 37.85 E-value: 2.26e-03
10 20 30
....*....|....*....|....*....|
gi 517057676 36 GPSGCGKSTLLRMIA---GLEEVTSGEIRI 62
Cdd:cd02020 6 GPAGSGKSTVAKLLAkklGLPYLDTGGIRT 35
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-64 |
2.73e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.49 E-value: 2.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 517057676 19 LHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIRIAG 64
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
15-61 |
2.78e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.15 E-value: 2.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 517057676 15 HVQVLHGVdleIHDGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIR 61
Cdd:PRK01889 184 GLDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVR 227
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-207 |
4.06e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 37.34 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 14 GHVQVLHGVDLEIHDGEFVVLVGPSGCGKSTLLRMIagleevtsgeIRIAGVRVNELHPKDRDIAMVFQSYAlyphmnva 93
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI----------GLALGGAQSATRRRSGVKAGCIVAAV-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517057676 94 gnmSYSLRLrkvakekiasavaaaaaklgldplleRRPKaLSGGQRQRVAM-----GRAIVRQPkAFLFDEPLSNLDARl 168
Cdd:cd03227 68 ---SAELIF--------------------------TRLQ-LSGGEKELSALalilaLASLKPRP-LYILDEIDRGLDPR- 115
|
170 180 190
....*....|....*....|....*....|....*....
gi 517057676 169 REQMRAEIKKLHGDLKATSIYVTHDQiEAMTLADRIVAM 207
Cdd:cd03227 116 DGQALAEAILEHLVKGAQVIVITHLP-ELAELADKLIHI 153
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
32-49 |
4.36e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 37.13 E-value: 4.36e-03
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
26-50 |
4.65e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 38.23 E-value: 4.65e-03
10 20
....*....|....*....|....*.
gi 517057676 26 IHDGE-FVVLVGPSGCGKSTLLRMIA 50
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRRLL 64
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
28-61 |
5.51e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.14 E-value: 5.51e-03
10 20 30
....*....|....*....|....*....|....
gi 517057676 28 DGEFVVLVGPSGCGKSTLLRMIAGLEEVTSGEIR 61
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEIS 138
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
20-46 |
6.52e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.50 E-value: 6.52e-03
10 20
....*....|....*....|....*..
gi 517057676 20 HGVDLEIHDGEFVVLVGPSGCGKSTLL 46
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
3-47 |
8.64e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 37.67 E-value: 8.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 517057676 3 SIDIQNIRKayghvqvLHGVDLEIHDGeFVVLVGPSGCGKSTLLR 47
Cdd:COG3593 5 KIKIKNFRS-------IKDLSIELSDD-LTVLVGENNSGKSSILE 41
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
23-50 |
9.61e-03 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 36.84 E-value: 9.61e-03
10 20
....*....|....*....|....*...
gi 517057676 23 DLEIHDGEFVVLVGPSGCGKSTLLRMIA 50
Cdd:cd03243 23 DINLGSGRLLLITGPNMGGKSTYLRSIG 50
|
|
| |
