|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-349 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 617.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 161 LSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGSPSMN 240
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 241 FLSGTISAGGFETGGVVLPPPATAAGLAGRGAVYGIRPEHFSL---DVSGVPAEIMLVEPLGSETQVTMELGGSRVLGVF 317
Cdd:COG3839 241 LLPGTVEGGGVRLGGVRLPLPAALAAAAGGEVTLGIRPEHLRLadeGDGGLEATVEVVEPLGSETLVHVRLGGQELVARV 320
|
330 340 350
....*....|....*....|....*....|..
gi 518853886 318 RERIGQVVGDEIRVSPALDCIHLFSDENGDRL 349
Cdd:COG3839 321 PGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-350 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 555.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSY-GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAM 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 160 PLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGSPSM 239
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 240 NFLSGTISAGG--FE-TGGVVLPPPATAAGLAGRGAVYGIRPEHFSL--DVSGVPAEIMLVEPLGSETQVTMELGGSRVl 314
Cdd:PRK11650 241 NLLDGRVSADGaaFElAGGIALPLGGGYRQYAGRKLTLGIRPEHIALssAEGGVPLTVDTVELLGADNLAHGRWGGQPL- 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 518853886 315 gVFR--ERIGQVVGDEIRVSPALDCIHLFSDENGDRLN 350
Cdd:PRK11650 320 -VVRlpHQERPAAGSTLWLHLPANQLHLFDADTGRRIE 356
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-346 |
2.73e-159 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 450.64 E-value: 2.73e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 161 LSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGSPSMN 240
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 241 FLSGTISAGGFETGGVVLPP------PATAAGL-AGRGAVYGIRPEHF-SLDVSGVP--AEIMLVEPLGSETQVTMELGG 310
Cdd:PRK11000 241 FLPVKVTATAIEQVQVELPNrqqvwlPVEGRGVqVGANMSLGIRPEHLlPSDIADVTleGEVQVVEQLGNETQIHIQIPA 320
|
330 340 350
....*....|....*....|....*....|....*....
gi 518853886 311 SRVLGVFRERIGQVV--GDEIRVS-PALDCiHLFSdENG 346
Cdd:PRK11000 321 IRQNLVYRQNDVVLVeeGATFAIGlPPERC-HLFR-EDG 357
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-343 |
5.46e-159 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 449.16 E-value: 5.46e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 161 LSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGspSMN 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--EAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 241 FLSGTISA---GGFETGGVVLPPPATAAGLAGRGAVYGIRPEHFSL----DVSGVPAEIMLVEPLGSETQVTMELGGSRV 313
Cdd:COG3842 241 LLPGTVLGdegGGVRTGGRTLEVPADAGLAAGGPVTVAIRPEDIRLspegPENGLPGTVEDVVFLGSHVRYRVRLGDGQE 320
|
330 340 350
....*....|....*....|....*....|...
gi 518853886 314 LGVF---RERIGQVVGDEIRVSPALDCIHLFSD 343
Cdd:COG3842 321 LVVRvpnRAALPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
2.31e-135 |
|
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: 383.91 E-value: 2.31e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQS 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518853886 164 LDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVG 216
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-333 |
4.26e-124 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 360.23 E-value: 4.26e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVN-DLDPKDRDIAMVFQ 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 163 NLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGSPsmNFL 242
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCV--NVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 243 SGTISAGGFETGGVVLPPPATAAGlaGRGAVYgIRPEHFSL-----DVSGVPAEIMLVEPLGSETQVTMELGGSRVLG-- 315
Cdd:COG1118 241 RGRVIGGQLEADGLTLPVAEPLPD--GPAVAG-VRPHDIEVsrepeGENTFPATVARVSELGPEVRVELKLEDGEGQPle 317
|
330 340
....*....|....*....|...
gi 518853886 316 --VFRERIGQ---VVGDEIRVSP 333
Cdd:COG1118 318 aeVTKEAWAElglAPGDPVYLRP 340
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
8-342 |
1.16e-121 |
|
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: 354.34 E-value: 1.16e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 8 DIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQSYALY 87
Cdd:TIGR03265 9 NIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 88 PHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK 167
Cdd:TIGR03265 89 PNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 168 LRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGspSMNFLSGTIS 247
Cdd:TIGR03265 169 VREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG--EVNWLPGTRG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 248 AGG-FETGGVVLPPPATAAGLAGRGAVYgIRPEHFSLDVSG-----VPAEIMLVEPLGSETQVTME---LGGSRVLGVF- 317
Cdd:TIGR03265 247 GGSrARVGGLTLACAPGLAQPGASVRLA-VRPEDIRVSPAGnaanlLLARVEDMEFLGAFYRLRLRlegLPGQALVADVs 325
|
330 340
....*....|....*....|....*...
gi 518853886 318 ---RERIGQVVGDEIRVSPALDCIHLFS 342
Cdd:TIGR03265 326 aseVERLGIRAGQPIWIELPAERLRAFA 353
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-235 |
1.95e-113 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 328.81 E-value: 1.95e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQS 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518853886 164 LDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIG 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 |
6.96e-111 |
|
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: 321.78 E-value: 6.96e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQS 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518853886 164 LDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVG 216
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-246 |
3.01e-105 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 313.42 E-value: 3.01e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQS 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 164 LDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGspSMNFLS 243
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINIFD 252
|
...
gi 518853886 244 GTI 246
Cdd:PRK09452 253 ATV 255
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-286 |
4.03e-104 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 310.01 E-value: 4.03e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 2 ANVTLSDIRKSYGA----VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVND-----LDP 72
Cdd:NF040933 1 VTVRVENVTKIFKKgkkeVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 73 KDRDIAMVFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNP 152
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 153 QVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAG 232
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 233 FIGspSMNFLSGTISAGGFETGGVVLPPpaTAAGLAGRGAVY-GIRPEHFSLDVS 286
Cdd:NF040933 241 LIG--DINLLEGKVEEEGLVDGNDLKIP--LPNPKLEAGEVIiGIRPEDIDISES 291
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-314 |
8.72e-100 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 298.56 E-value: 8.72e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQS 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 164 LDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGSPSMnfLS 243
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANI--FP 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 244 GTISAGGFETGGVVLPPPATAAGLAGRGAV-YGIRPEHFSLDVSGVPA---EIMLVEPLGSETQVTMELGGSRVL 314
Cdd:PRK11432 245 ATLSGDYVDIYGYRLPRPAAFAFNLPDGECtVGVRPEAITLSEQGEESqrcTIKHVAYMGPQYEVTVDWHGQELL 319
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-236 |
7.26e-97 |
|
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: 287.31 E-value: 7.26e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQS 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHMTVASNMGFSLEHR----GSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 160 PLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGS 236
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-235 |
6.13e-91 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 272.06 E-value: 6.13e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQS 83
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518853886 164 LDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIG 235
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-307 |
5.82e-90 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 273.50 E-value: 5.82e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQ 82
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPHMTVASNMGFSL----EHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFD 158
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 159 EPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGspS 238
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG--E 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 239 MNFLSGTISAGGFETGGVVLPPPATAAgLAGRGAVYgIRP------EHFSLDvSGVPAEIMLVEPLGSETQVTME 307
Cdd:PRK10851 240 VNRLQGTIRGGQFHVGAHRWPLGYTPA-YQGPVDLF-LRPwevdisRRTSLD-SPLPVQVLEVSPKGHYWQLVVQ 311
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-212 |
7.86e-88 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 264.64 E-value: 7.86e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY----GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPkdrDIAM 79
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---DRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 160 PLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNG--GRV 212
Cdd:COG1116 165 PFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRI 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-318 |
3.26e-87 |
|
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: 265.51 E-value: 3.26e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 34 LVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEK 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 114 VNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHD 193
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 194 QVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGSPSM-NFLSGTISAGGFETGGVVLPPPATAAGLAGRGA 272
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVfEATVIERKSEQVVLAGVEGRRCDIYTDVPVEKD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 273 V---YGIRPEHFSLD-------VSGVPAEIMLVEPLGSETQVTMEL--GGSRVLGVFR 318
Cdd:TIGR01187 241 QplhVVLRPEKIVIEeedeansSNAIIGHVIDITYLGMTLEVHVRLetGQKVLVSEFF 298
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-212 |
1.38e-84 |
|
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: 255.09 E-value: 1.38e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYG----AVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPkdrDIAM 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 160 PLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNG--GRV 212
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
6-341 |
4.66e-82 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 253.07 E-value: 4.66e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRKSYGAVKtIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQSYA 85
Cdd:NF040840 4 IENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 86 LYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:NF040840 83 LFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 166 AKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGSPsmNFLSGT 245
Cdd:NF040840 163 VQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NIIEGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 246 ISAGG----FETGGVVLPPPATAaglagRGAVY-GIRPEHFSLDVSGV--------PAEIMLVEPLGSETQVTMELGgsR 312
Cdd:NF040840 241 AEKGGegtiLDTGNIKIELPEEK-----KGKVRiGIRPEDITISTEKVktsarnefKGKVEEIEDLGPLVKLTLDVG--I 313
|
330 340 350
....*....|....*....|....*....|....
gi 518853886 313 VLGVFRER-----IGQVVGDEIRVSPALDCIHLF 341
Cdd:NF040840 314 ILVAFITRssfldLEINEGKEVYASFKASAVHVF 347
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
8-235 |
6.85e-81 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 246.48 E-value: 6.85e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 8 DIRKSYGAVKtIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQSYALY 87
Cdd:cd03299 5 NLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 88 PHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK 167
Cdd:cd03299 84 PHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 168 LRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIG 235
Cdd:cd03299 164 TKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-236 |
1.20e-80 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 248.08 E-value: 1.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKT-IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVF 81
Cdd:COG1125 3 EFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 QSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTP--LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 160 PLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGS 236
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-237 |
1.63e-76 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 235.27 E-value: 1.63e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKT-IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMV 80
Cdd:cd03295 1 IEFENVTKRYGGGKKaVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTP--LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 159 EPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGSP 237
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-234 |
1.85e-73 |
|
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: 228.68 E-value: 1.85e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 7 SDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD------RDIAMV 80
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518853886 161 LSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFI 234
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-294 |
6.29e-71 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 225.48 E-value: 6.29e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIR---KSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQ 82
Cdd:PRK11607 19 LLEIRnltKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNwaaDILGLTPLLD---RYPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVN---EMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 160 PLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGspSM 239
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG--SV 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 240 NFLSGTISAGgfETGGVVLPPPataaglagrGAVYGIRPEHFSLDVSGVPAEIML 294
Cdd:PRK11607 254 NVFEGVLKER--QEDGLVIDSP---------GLVHPLKVDADASVVDNVPVHVAL 297
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-212 |
3.85e-70 |
|
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: 218.13 E-value: 3.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGA----VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRD--- 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 ---IAMVFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 154 VFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMtMADRVVVLNGGRV 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-213 |
5.25e-70 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 217.99 E-value: 5.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANV-TLSDIRKSYG----AVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDR 75
Cdd:COG1136 1 MSPLlELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 76 D------IAMVFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIV 149
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 150 RNPQVFLFDEPLSNLDAKL-RVVMRgEIKALHQKLKTTTIYVTHDQvEAMTMADRVVVLNGGRVE 213
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTgEEVLE-LLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-211 |
7.34e-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: 215.90 E-value: 7.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLD----PKDRDIAM 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYPHMTVASNMGFSlehrgsskqeiaekvnwaadilgltplldryprqLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518853886 160 PLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGR 211
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-216 |
3.91e-69 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 215.62 E-value: 3.91e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIrDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVND------LDPKDRDIAMVFQSYALYPHMTVASN 95
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 96 MGFSLehRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGE 175
Cdd:cd03297 96 LAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518853886 176 IKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVG 216
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-234 |
3.22e-68 |
|
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: 214.07 E-value: 3.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRD-----IA 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrrIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 79 MVFQSYALYPHMTVASNMGFSL-EHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 158 DEPLSNLDAklrvVMRGE----IKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPaNQFVAGF 233
Cdd:COG1127 166 DEPTAGLDP----ITSAVidelIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQF 240
|
.
gi 518853886 234 I 234
Cdd:COG1127 241 L 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-228 |
7.67e-67 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 210.24 E-value: 7.67e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIvnDLDPKD-----RDI 77
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVdGEDL--TDSKKDinklrRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 AMVFQSYALYPHMTVASNMGFSLEH-RGSSKQEIAEKvnwAADIL---GLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEER---AMELLervGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 154 VFLFDEPLSNLDAKlrvvMRGE----IKALhQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQ 228
Cdd:COG1126 157 VMLFDEPTSALDPE----LVGEvldvMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-248 |
1.81e-65 |
|
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: 210.73 E-value: 1.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVND------LDPKDRDIAMVFQSYALYPHMTVASN 95
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 96 MGFSleHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLrvvmRGE 175
Cdd:COG4148 98 LLYG--RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR----KAE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 176 I----KALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGfiGSPSMNFLSGTISA 248
Cdd:COG4148 172 IlpylERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAGSVLEATVAA 246
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-221 |
2.98e-65 |
|
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: 206.20 E-value: 2.98e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAvKTIH-GVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVN----DLDPKDRDI 77
Cdd:cd03261 1 IELRGLTKSFGG-RTVLkGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdGEDISGlseaELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 AMVFQSYALYPHMTVASNMGFSL-EHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 157 FDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-225 |
3.40e-65 |
|
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: 206.03 E-value: 3.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY-GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMV 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQsyalYP-----HMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:COG1122 81 FQ----NPddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 156 LFDEPLSNLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-235 |
3.77e-64 |
|
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: 207.78 E-value: 3.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 11 KSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDP------KDRDIAMVFQSY 84
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 85 ALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518853886 165 DAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIG 235
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-225 |
2.48e-63 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 209.76 E-value: 2.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY-----GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD---- 74
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 -RDIAMVFQ--SYALYPHMTVASNMGFSLE-HRGSSKQEIAEKVNWAADILGLTP-LLDRYPRQLSGGQRQRVAMGRAIV 149
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRlHGLLSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 150 RNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-211 |
6.14e-63 |
|
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: 199.62 E-value: 6.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRKSY--GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVF 81
Cdd:cd03225 2 LKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 QsyalYP-HM----TVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:cd03225 82 Q----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 157 FDEPLSNLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGR 211
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-224 |
6.97e-63 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 200.29 E-value: 6.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKDRDIAMVFQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518853886 163 NLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
1.33e-61 |
|
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: 197.33 E-value: 1.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGA----VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDI 77
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 AMVFQSY--ALYPHMTVASNMG--FSLEHRGSSKQEIAEkvnwAADILGLTP-LLDRYPRQLSGGQRQRVAMGRAIVRNP 152
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAepLRIHGLPDREERIAE----LLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 153 QVFLFDEPLSNLDaklrVVMRGEI----KALHQKLKTTTIYVTHDqVEAMT-MADRVVVLNGGRVEQVGTPLELYDRPAN 227
Cdd:COG1124 158 ELLLLDEPTSALD----VSVQAEIlnllKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-234 |
8.46e-61 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 194.93 E-value: 8.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDI----AM 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYPHMTVASNMGFSLEH-RGSSKQEiAEKVnwAADIL---GLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPLRvRGASKEE-AEKQ--ARELLakvGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 156 LFDEPLSNLDAKLrvvmRGEIKALHQKLKT---TTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAG 232
Cdd:PRK09493 159 LFDEPTSALDPEL----RHEVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
..
gi 518853886 233 FI 234
Cdd:PRK09493 235 FL 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-235 |
1.22e-60 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 194.20 E-value: 1.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKSYGaVKTIHgVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQ 82
Cdd:COG3840 1 MLRLDDLTYRYG-DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPHMTVASNMGFSLEHRG--SSKQEiaEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGLRPGLklTAEQR--AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 161 LSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIG 235
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-237 |
9.71e-59 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 192.99 E-value: 9.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY----GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD----- 74
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 RDIAMVFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 155 FLFDEPLSNLDAK-----LRVvmrgeIKALHQKLKTTTIYVTHDqveaM----TMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:COG1135 162 LLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLDVFANP 232
|
250
....*....|..
gi 518853886 226 ANQFVAGFIGSP 237
Cdd:COG1135 233 QSELTRRFLPTV 244
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-214 |
2.22e-58 |
|
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: 188.48 E-value: 2.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY----GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDR---- 75
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 76 -DIAMVFQSY--ALYPHMTVASNMGFSLE-HRGSSKQEIAEKVNWAADI-LGLTP-LLDRYPRQLSGGQRQRVAMGRAIV 149
Cdd:cd03257 82 kEIQMVFQDPmsSLNPRMTIGEQIAEPLRiHGKLSKKEARKEAVLLLLVgVGLPEeVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 150 RNPQVFLFDEPLSNLDAKLRV-VMRgEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGR-VEQ 214
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAqILD-LLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKiVEE 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-212 |
1.93e-57 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 185.64 E-value: 1.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTI-HGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD-----RDI 77
Cdd:COG2884 2 IRFENVSKRYPGGREAlSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 AMVFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 158 DEPLSNLDAKL-RVVMRgEIKALHQkLKTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:COG2884 162 DEPTGNLDPETsWEIME-LLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-229 |
2.04e-57 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 186.42 E-value: 2.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY-GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD-----RDI 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 AMVFQSYALYPHMTVASN--MGfSLEHRGS--------SKQEIAEkvnwAADIL---GLTPLLDRYPRQLSGGQRQRVAM 144
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNvlAG-RLGRTSTwrsllglfPPEDRER----ALEALervGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 145 GRAIVRNPQVFLFDEPLSNLDAKL-RVVMRgEIKALHQKLKTTTIYVTHdQVE-AMTMADRVVVLNGGRVeqvgtpleLY 222
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTaRQVMD-LLRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDGRV--------VF 227
|
....*..
gi 518853886 223 DRPANQF 229
Cdd:COG3638 228 DGPPAEL 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-212 |
3.59e-57 |
|
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: 184.66 E-value: 3.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPK----DRDIAM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYPHMTVASNMGFSL-EHRGSSKQEIAEKvnwAADILGLTPLLDR---YPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEER---ALELLEKVGLADKadaYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518853886 156 LFDEPLSNLDAKlrvvMRGE----IKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:cd03262 158 LFDEPTSALDPE----LVGEvldvMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
4.02e-55 |
|
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: 180.08 E-value: 4.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYG----AVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD----- 74
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 RDIAMVFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518853886 155 FLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHdQVEAM-TMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-224 |
9.37e-55 |
|
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: 179.67 E-value: 9.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKDRDIAMVFQS 83
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDVRKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518853886 164 LDAKLRVVMRGEIKALHqKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:COG4555 163 LDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
1.94e-54 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 186.26 E-value: 1.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANV-TLSDIRKSY--GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITG---GELRIGERIVNDLDPKD 74
Cdd:COG1123 1 MTPLlEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 R--DIAMVFQS--YALYPhMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVR 150
Cdd:COG1123 81 RgrRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 151 NPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPA 226
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-221 |
2.34e-54 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 178.70 E-value: 2.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVF 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 QSYALYPHMTVasnmgfsLE--------HRGSSKQEIAE---KVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVR 150
Cdd:COG1120 82 QEPPAPFGLTV-------RElvalgrypHLGLFGRPSAEdreAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518853886 151 NPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-212 |
4.83e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.54 E-value: 4.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQ 82
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPhMTVASNMGFSLEHRGSSKQEiaEKVNWAADILGLTP-LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518853886 162 SNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-226 |
5.61e-52 |
|
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: 175.69 E-value: 5.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVND------LDPKDRDIAMVFQSYALYPHMTVASN 95
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 96 MGFSLEH-RGSSKQEIAEKVnwaADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRG 174
Cdd:TIGR02142 96 LRYGMKRaRPSERRISFERV---IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518853886 175 EIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPA 226
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
6.16e-51 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 170.30 E-value: 6.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY--GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELrigerIVNDLDPKDRD----- 76
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKV-----TVDGLDTLDEEnlwei 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 ---IAMVFQSyalyPH-----MTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAI 148
Cdd:TIGR04520 76 rkkVGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 149 VRNPQVFLFDEPLSNLDAKLRV-VMRgEIKALHQKLKTTTIYVTHDQVEAmTMADRVVVLNGGRVEQVGTPLELY 222
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKeVLE-TIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-212 |
8.93e-51 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 168.06 E-value: 8.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGavKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQS 83
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518853886 164 LDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-216 |
2.19e-50 |
|
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: 167.35 E-value: 2.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 23 DLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQSYALYPHMTVASNMGFSLEH 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 103 RGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQK 182
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 518853886 183 LKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVG 216
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-226 |
2.28e-50 |
|
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: 170.62 E-value: 2.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY----GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLE---TITGGELRIGERIVNDLDPKD-- 74
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 ----RDIAMVFQ-SY-ALYPHMTVASNMGFSLE-HRGSSKQEIAEKVNWAADILGLTP---LLDRYPRQLSGGQRQRVAM 144
Cdd:COG0444 82 kirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRiHGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 145 GRAIVRNPQVFLFDEPLSNLDaklrVVMRGEI----KALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGR-VEQvGTPL 219
Cdd:COG0444 162 ARALALEPKLLIADEPTTALD----VTIQAQIlnllKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRiVEE-GPVE 236
|
....*..
gi 518853886 220 ELYDRPA 226
Cdd:COG0444 237 ELFENPR 243
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-212 |
2.96e-50 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 168.32 E-value: 2.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLdpKDrDIAMVFQS 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA--RE-DTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHMTVASNMGFSLehRGSSKQEIAEkvnwAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGL--KGQWRDAALQ----ALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518853886 164 LDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-225 |
4.40e-50 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 168.40 E-value: 4.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 15 AVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD-----RDIAMVFQsyalYPH 89
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrKKVGLVFQ----FPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 90 M-----TVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTP-LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:TIGR04521 93 HqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518853886 164 LDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:TIGR04521 173 LDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
11-211 |
1.14e-49 |
|
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: 165.50 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 11 KSY-GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD-----RDIAMVFQSY 84
Cdd:TIGR02673 9 KAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRIGVVFQDF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 85 ALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:TIGR02673 89 RLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518853886 165 DAKLRVVMRGEIKALHQkLKTTTIYVTHDQVEAMTMADRVVVLNGGR 211
Cdd:TIGR02673 169 DPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-217 |
3.89e-49 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 164.80 E-value: 3.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGER---IVNDLDPKD-----RDI 77
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdFSKTPSDKAirelrRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 AMVFQSYALYPHMTVASNMgfsLEH----RGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNL---IEApcrvLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518853886 154 VFLFDEPLSNLDAKLRVVMRGEIKALhQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGT 217
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-234 |
1.48e-48 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 163.65 E-value: 1.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGER---IVNDLDPKD----- 74
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdFSQKPSEKAirllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 RDIAMVFQSYALYPHMTVASNMgfsLEH----RGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVR 150
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENL---IEApckvLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 151 NPQVFLFDEPLSNLDAKLRVVMRGEIKALhQKLKTTTIYVTHdQVE-AMTMADRVVVLNGGRVEQVGTpLELYDRPANQF 229
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTH-EVEfARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEA 235
|
....*
gi 518853886 230 VAGFI 234
Cdd:COG4161 236 FAHYL 240
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-218 |
1.50e-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: 163.12 E-value: 1.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETI-----TGGELRIGERIVNDLDPKD----RD 76
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelrRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 IAMVFQSYALYPhMTVASNMGFSLEHRGS-SKQEIAEKVNWAADILGLTPLLDR--YPRQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:cd03260 83 VGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 154 VFLFDEPLSNLDAKLRVVMRGEIKALHQklKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTP 218
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-226 |
5.91e-48 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 164.52 E-value: 5.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 10 RKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD-----RDIAMVFQ-S 83
Cdd:COG4608 25 GRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQdP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YA-LYPHMTVASNMGFSLE-HRGSSKQEIAEKVNWAADILGLTP-LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:COG4608 105 YAsLNPRMTVGDIIAEPLRiHGLASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518853886 161 LSNLDaklrVVMRGEI----KALHQKLKTTTIYVTHD--QVEamTMADRVVVLNGGRVEQVGTPLELYDRPA 226
Cdd:COG4608 185 VSALD----VSIQAQVlnllEDLQDELGLTYLFISHDlsVVR--HISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-214 |
6.29e-48 |
|
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: 161.45 E-value: 6.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY----GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GErivnDLDPKDRD-- 76
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLaGQ----DLFALDEDar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 -------IAMVFQSYALYPHMTVASNMGFSLEHRGSSkqEIAEKvnwAADIL---GLTPLLDRYPRQLSGGQRQRVAMGR 146
Cdd:COG4181 85 arlrarhVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARAR---ARALLervGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 147 AIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAmTMADRVVVLNGGRVEQ 214
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-232 |
3.37e-47 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 160.35 E-value: 3.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERI------VNDLDPKDRD 76
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVgGEEIrlkpdrDGELVPADRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 --------IAMVFQSYALYPHMTVASNMGFSLEH-RGSSKQEIAEKvnwAADIL---GLTPLLDRYPRQLSGGQRQRVAM 144
Cdd:COG4598 89 qlqrirtrLGMVFQSFNLWSHMTVLENVIEAPVHvLGRPKAEAIER---AEALLakvGLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 145 GRAIVRNPQVFLFDEPLSNLDAKLrVvmrGEIKALHQKLKT---TTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPEL-V---GEVLKVMRDLAEegrTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
250
....*....|....*
gi 518853886 222 YDRPAN----QFVAG 232
Cdd:COG4598 242 FGNPKSerlrQFLSS 256
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-223 |
4.68e-47 |
|
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: 159.66 E-value: 4.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 11 KSYGAVKTI-HGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD-----RDIAMVFQSY 84
Cdd:cd03256 8 KTYPNGKKAlKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIGMIFQQF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 85 ALYPHMTVASN--MGFSLEH-------RGSSKQEIAEkvnwAADILGLTPLLDR-YPR--QLSGGQRQRVAMGRAIVRNP 152
Cdd:cd03256 88 NLIERLSVLENvlSGRLGRRstwrslfGLFPKEEKQR----ALAALERVGLLDKaYQRadQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518853886 153 QVFLFDEPLSNLDAKL-RVVMRgEIKALHQKLKTTTIYVTHdQVE-AMTMADRVVVLNGGRVEQVGTPLELYD 223
Cdd:cd03256 164 KLILADEPVASLDPASsRQVMD-LLKRINREEGITVIVSLH-QVDlAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
7.40e-47 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 156.79 E-value: 7.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKDRDIAMVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPHMTVASNMgfslehrgsskqeiaekvnwaadilgltplldryprQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518853886 163 NLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-224 |
1.03e-46 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 168.47 E-value: 1.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKSYG--AVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIA 78
Cdd:COG2274 473 DIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 79 MVFQSYALYpHMTVASNMGFSLEHRGSskqeiaEKVNWAADILGLTPLLDRYP-----------RQLSGGQRQRVAMGRA 147
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLGDPDATD------EEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 148 IVRNPQVFLFDEPLSNLDAKL-RVVMRGeIKALHQklKTTTIYVTHDqVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:COG2274 626 LLRNPRILILDEATSALDAETeAIILEN-LRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-232 |
1.04e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 159.26 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSYG----AVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPkDRd 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 iAMVFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 157 FDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNG--GRVEQVgtplelYDRPANQ-FVAG 232
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER------LELDFSRrFLAG 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-212 |
2.65e-46 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 156.80 E-value: 2.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 8 DIRKSYGA-VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD-----RDIAMVF 81
Cdd:cd03292 5 NVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 QSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:cd03292 85 QDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518853886 162 SNLDAKlrvvMRGEIKALHQKLK---TTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:cd03292 165 GNLDPD----TTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-225 |
2.94e-46 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 157.24 E-value: 2.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPkdrDIAMVFQSYALYPHMTVASNMGF 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 99 SLEH--RGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEI 176
Cdd:TIGR01184 78 AVDRvlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518853886 177 KALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL-YDRP 225
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-222 |
1.42e-45 |
|
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: 163.39 E-value: 1.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY-GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMV 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALyPHMTVASNMGFSleHRGSSKQEIAEkvnwAADILGLTPLLDRYP-----------RQLSGGQRQRVAMGRAIV 149
Cdd:COG4988 417 PQNPYL-FAGTIRENLRLG--RPDASDEELEA----ALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 150 RNPQVFLFDEPLSNLDAKL-RVVMRgeikALHQKLKT-TTIYVTHDQvEAMTMADRVVVLNGGRVEQVGTPLELY 222
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETeAEILQ----ALRRLAKGrTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-212 |
2.57e-45 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 152.97 E-value: 2.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 syalyphmtvasnmgfslehrgsskqeiaekvnwAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518853886 163 NLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-232 |
1.09e-44 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 153.20 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 23 DLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQSYALYPHMTVASNMGFSLeH 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGL-N 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 103 RG---SSKQ-----EIAEKVnwaadilGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRG 174
Cdd:PRK10771 98 PGlklNAAQreklhAIARQM-------GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 175 EIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVeqvgtpleLYDRPANQFVAG 232
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI--------AWDGPTDELLSG 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-235 |
1.55e-44 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 153.37 E-value: 1.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD------ 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 ----RDIAMVFQSYALYPHMTVASN-MGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIV 149
Cdd:PRK11264 81 rqlrQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 150 RNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP---- 225
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPqqpr 239
|
250
....*....|
gi 518853886 226 ANQFVAGFIG 235
Cdd:PRK11264 240 TRQFLEKFLL 249
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-211 |
7.80e-44 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 148.55 E-value: 7.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 syalyphmtvasnmgfslehrgsskqeiaekvnwaadilgltplldryprqLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518853886 163 NLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGR 211
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
7.98e-44 |
|
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: 150.35 E-value: 7.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYG-----AVKtihGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKDRDI 77
Cdd:cd03263 1 LQIRNLTKTYKkgtkpAVD---DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYInGYSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 AMVFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 158 DEPLSNLDaklrVVMRGEIKALHQKLKT--TTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:cd03263 158 DEPTSGLD----PASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
9.54e-44 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 148.69 E-value: 9.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYG--AVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAM 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYpHMTVASNMgfslehrgsskqeiaekvnwaadilgltplldryprqLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518853886 160 PLSNLDAKLRVVMRGEIKALHQklKTTTIYVTHDqVEAMTMADRVVVLNGGR 211
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-220 |
1.59e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 150.24 E-value: 1.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERivnDLDPKDRDIAMV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPH--MTVA--------SNMGFSLEHRGSSKQEIAEkvnwAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVR 150
Cdd:COG1121 81 PQRAEVDWDfpITVRdvvlmgryGRRGLFRRPSRADREAVDE----ALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 151 NPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQvGTPLE 220
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEE 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-222 |
2.16e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 151.35 E-value: 2.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 17 KTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELrigerIVNDLDPKD---------RDIAMVFQ--SYA 85
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI-----IIDGVDITDkkvklsdirKKVGLVFQypEYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 86 LYPHmTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLT--PLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:PRK13637 96 LFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 164 LDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELY 222
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-221 |
3.92e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 156.86 E-value: 3.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKSY-GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAM 79
Cdd:COG1132 339 EIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYpHMTVASNMGFSLEhrGSSKQEIAEkvnwAADILGLTPLLDRYP-----------RQLSGGQRQRVAMGRAI 148
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYGRP--DATDEEVEE----AAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 149 VRNPQVFLFDEPLSNLDAK--------LRVVMRGeikalhqklkTTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTPLE 220
Cdd:COG1132 492 LKDPPILILDEATSALDTEtealiqeaLERLMKG----------RTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEE 560
|
.
gi 518853886 221 L 221
Cdd:COG1132 561 L 561
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-218 |
4.33e-43 |
|
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: 149.12 E-value: 4.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDR---DIAMVFQ 82
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPHMTVASNM----------GFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNP 152
Cdd:cd03219 83 IPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 153 QVFLFDEPLSNLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTP 218
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-233 |
4.51e-43 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 153.65 E-value: 4.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 24 LDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKDRD-----IAMVFQSYALYPHMTVASNMG 97
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIdGVDIAKISDAELREvrrkkIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 98 FSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIK 177
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 178 ALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGF 233
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-211 |
6.50e-43 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 147.63 E-value: 6.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKDRDIAMVFQ 82
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPHMTVASNMGFSLEHRGS--SKQEIAEkvnwAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLraDREAIDE----ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518853886 161 LSNLDAKLRVVMRGEIKAlHQKLKTTTIYVTHDQVEAmtMADRVVVLNGGR 211
Cdd:COG4133 159 FTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-236 |
7.13e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 151.49 E-value: 7.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY----GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD----- 74
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 RDIAMVFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 155 FLFDEPLSNLD-AKLRVVMRgEIKALHQKLKTTTIYVTH--DQVEAmtMADRVVVLNGGR-VEQvGTPLELYDRPANQFV 230
Cdd:PRK11153 162 LLCDEATSALDpATTRSILE-LLKDINRELGLTIVLITHemDVVKR--ICDRVAVIDAGRlVEQ-GTVSEVFSHPKHPLT 237
|
....*.
gi 518853886 231 AGFIGS 236
Cdd:PRK11153 238 REFIQS 243
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
11-223 |
8.55e-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: 8.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 11 KSYG-AVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD-----RDIAMVFQSY 84
Cdd:TIGR02315 9 KVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRIGMIFQHY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 85 ALYPHMTVASN-----MGFSLEHRGS----SKQEIAEKVNwAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:TIGR02315 89 NLIERLTVLENvlhgrLGYKPTWRSLlgrfSEEDKERALS-ALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 156 LFDEPLSNLDAKL-RVVMRgEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYD 223
Cdd:TIGR02315 168 LADEPIASLDPKTsKQVMD-YLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-236 |
2.16e-42 |
|
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: 147.67 E-value: 2.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVN------DLDPKD-- 74
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVeGEQLYHmpgrngPLVPADek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 ------RDIAMVFQSYALYPHMTVASNMGFSLEH-RGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRA 147
Cdd:TIGR03005 81 hlrqmrNKIGMVFQSFNLFPHKTVLDNVTEAPVLvLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 148 IVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPAN 227
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
....*....
gi 518853886 228 QFVAGFIGS 236
Cdd:TIGR03005 241 ERTREFLSK 249
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-226 |
8.86e-42 |
|
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: 146.49 E-value: 8.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD-----RDIAMVFQ-SY-ALYPHMT 91
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQdSPsAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 92 VASNMGFSLEHRGS-SKQEIAEKVNWAADILGLTP-LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLR 169
Cdd:TIGR02769 107 VRQIIGEPLRHLTSlDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 170 VVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRV--EQVGTPLELYDRPA 226
Cdd:TIGR02769 187 AVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIveECDVAQLLSFKHPA 245
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-207 |
1.15e-41 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 144.55 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAG-LETI--TGGELRIGERIVNDLDPKDRDIAMVF 81
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 QSYALYPHMTVASNMGFSLEhRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:COG4136 83 QDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518853886 162 SNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQ--VEAmtmADRVVVL 207
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHDEedAPA---AGRVLDL 206
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-207 |
1.31e-41 |
|
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: 144.30 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKDRD-----IAM 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLnGQETPPLNSKKASKfrrekLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518853886 160 PLSNLDAKlrvvMRGEIKALHQKLK---TTTIYVTHDQvEAMTMADRVVVL 207
Cdd:TIGR03608 161 PTGSLDPK----NRDEVLDLLLELNdegKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-162 |
1.42e-41 |
|
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: 142.40 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSYALYPHMTVASNM 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 97 GFSLEHRGSSKQEIAEKVNWAADILGLTPLLDR----YPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-222 |
2.85e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 145.54 E-value: 2.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 18 TIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSyalyPH-----M 90
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGMVFQN----PDnqfvgA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 91 TVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRV 170
Cdd:PRK13635 98 TVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518853886 171 VMRGEIKALHQKLKTTTIYVTHDQVEAMTmADRVVVLNGGRVEQVGTPLELY 222
Cdd:PRK13635 178 EVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-225 |
1.30e-40 |
|
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: 149.45 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 10 RKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETiTGGELRIGERIVNDLDPKD-----RDIAMVFQS- 83
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YA-LYPHMTVASNM--GFSLEHRGSSKQEIAEKVNWAADILGLTP-LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:COG4172 372 FGsLSPRMTVGQIIaeGLRVHGPGLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518853886 160 PLSNLDaklrVVMRGEI----KALHQKLKTTTIYVTHDQ--VEAmtMADRVVVLNGGR-VEQvGTPLELYDRP 225
Cdd:COG4172 452 PTSALD----VSVQAQIldllRDLQREHGLAYLFISHDLavVRA--LAHRVMVMKDGKvVEQ-GPTEQVFDAP 517
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-228 |
7.51e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 141.75 E-value: 7.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSY---------GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLD 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 72 PKD-----RDIAMVFQSY--ALYPHMTVASNMGFSLEHRGS-SKQEIAEKVNWAADILGLTP-LLDRYPRQLSGGQRQRV 142
Cdd:PRK10419 81 RAQrkafrRDIQMVFQDSisAVNPRKTVREIIREPLRHLLSlDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 143 AMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRV--EQVGTPLE 220
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDKL 240
|
....*...
gi 518853886 221 LYDRPANQ 228
Cdd:PRK10419 241 TFSSPAGR 248
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
1.42e-39 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 140.22 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVF 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 QSYALYPHMTVASNMGFSL--EHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQR--VAMgrAIVRNPQVFLF 157
Cdd:COG4604 82 QENHINSRLTVRELVAFGRfpYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRafIAM--VLAQDTDYVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518853886 158 DEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-226 |
1.86e-39 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 146.83 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY--GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAM 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYpHMTVASNMGFSLEhrGSSKQEIAEkvnwAADILGLTPLLDRYP-----------RQLSGGQRQRVAMGRAI 148
Cdd:COG4987 414 VPQRPHLF-DTTLRENLRLARP--DATDEELWA----ALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 149 VRNPQVFLFDEPLSNLDAKL-RVVMRGEIKALHQKlktTTIYVTHDQVeAMTMADRVVVLNGGRVEQVGTPLELYDRPA 226
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATeQALLADLLEALAGR---TVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-221 |
3.84e-39 |
|
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: 138.34 E-value: 3.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDR---DIAMVF 81
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 QSYALYPHMTVASN--MGFSLEHRGSSKQEIAEkvnwaadILGLTPLL----DRYPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:cd03224 82 EGRRIFPELTVEENllLGAYARRRAKRKARLER-------VYELFPRLkerrKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 156 LFDEPLSNLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-220 |
1.07e-38 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 140.78 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 36 GPSGCGKSTLLRMIAGLETITGGELRIGERIVND------LDPKDRDIAMVFQSYALYPHMTVASNMGFSLehRGSSKQE 109
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKRRIGYVFQDARLFPHYKVRGNLRYGM--AKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 110 IAEKVnwaaDILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA-KLRVVMrGEIKALHQKLKTTTI 188
Cdd:PRK11144 109 FDKIV----ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLpRKRELL-PYLERLAREINIPIL 183
|
170 180 190
....*....|....*....|....*....|..
gi 518853886 189 YVTHDQVEAMTMADRVVVLNGGRVEQVGtPLE 220
Cdd:PRK11144 184 YVSHSLDEILRLADRVVVLEQGKVKAFG-PLE 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-217 |
1.21e-38 |
|
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: 134.86 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD---RDIAMV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FqsyalyphmtvasnmgfslehrgsskqeiaekvnwaadilgltplldryprQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:cd03216 81 Y---------------------------------------------------QLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 161 LSNLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRVeqVGT 217
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV--VGT 163
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-224 |
2.01e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 138.33 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 18 TIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVND-LDPKDRDIAMVFQSyalyPH-----M 90
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEEnVWDIRHKIGMVFQN----PDnqfvgA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 91 TVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRV 170
Cdd:PRK13650 98 TVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518853886 171 VMRGEIKALHQKLKTTTIYVTHDqVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:PRK13650 178 ELIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-221 |
3.84e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.04 E-value: 3.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSyalyPH-----MTVAS 94
Cdd:PRK13632 28 VSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGIIFQN----PDnqfigATVED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 95 NMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRG 174
Cdd:PRK13632 104 DIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKK 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518853886 175 EIKALHQKLKTTTIYVTHDQVEAmTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:PRK13632 184 IMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-217 |
7.67e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 141.31 E-value: 7.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD-RD--IAMV 80
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAagIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPHMTVASNMGFSLEHRGSSkqeiaeKVNWAADILGLTPLLDRY-----PRQ----LSGGQRQRVAMGRAIVRN 151
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGREPRRGG------LIDWRAMRRRARELLARLgldidPDTpvgdLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518853886 152 PQVFLFDEPLSNLDAKlrvvmrgEIKALHQ---KLK---TTTIYVTHDQVEAMTMADRVVVLNGGRVeqVGT 217
Cdd:COG1129 159 ARVLILDEPTASLTER-------EVERLFRiirRLKaqgVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-235 |
1.10e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 135.35 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 8 DIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGL-----ETITGGELRI-GERIVN-DLDPKD--RDIA 78
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLfGRNIYSpDVDPIEvrREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 79 MVFQSYALYPHMTVASNMGFSLEHRG--SSKQEIAEKVNWAADILGL----TPLLDRYPRQLSGGQRQRVAMGRAIVRNP 152
Cdd:PRK14267 89 MVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 153 QVFLFDEPLSNLDAklrvVMRGEIKALHQKLKT--TTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPAN--- 227
Cdd:PRK14267 169 KILLMDEPTANIDP----VGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHelt 244
|
....*....
gi 518853886 228 -QFVAGFIG 235
Cdd:PRK14267 245 eKYVTGALG 253
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-232 |
1.65e-37 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 135.10 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLS--DIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGE---RIVNDLDPK-- 73
Cdd:PRK10619 1 MSENKLNviDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtiNLVRDKDGQlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 74 --DRD--------IAMVFQSYALYPHMTVASN-MGFSLEHRGSSKQEIAEKVNWAADILGLTPLL-DRYPRQLSGGQRQR 141
Cdd:PRK10619 81 vaDKNqlrllrtrLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 142 VAMGRAIVRNPQVFLFDEPLSNLDAKLrvvmRGEIKALHQKLK---TTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTP 218
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPEL----VGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
250
....*....|....*...
gi 518853886 219 LELYDRPAN----QFVAG 232
Cdd:PRK10619 237 EQLFGNPQSprlqQFLKG 254
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
15-225 |
5.84e-37 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 135.60 E-value: 5.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 15 AVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDR-----DIAMVFQS--YALY 87
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 88 PHMTVASNMGFSLE--HRGSSKQEIAEKVNWAADILGLTP-LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:PRK15079 113 PRMTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518853886 165 DAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-221 |
9.54e-37 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 132.11 E-value: 9.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 7 SDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKDRDIAMVFQSYA 85
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVVREPREVRRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 86 LYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:cd03265 84 VDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 166 AKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
8-212 |
2.33e-36 |
|
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: 130.93 E-value: 2.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 8 DIRKSY--GAVKTI--HGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDR------DI 77
Cdd:TIGR02211 6 NLGKRYqeGKLDTRvlKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 AMVFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKvnwAADIL---GLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:TIGR02211 86 GFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKER---AYEMLekvGLEHRINHRPSELSGGERQRVAIARALVNQPSL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 155 FLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMaDRVVVLNGGRV 212
Cdd:TIGR02211 163 VLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-226 |
3.95e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 132.45 E-value: 3.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVN------DLDPKDRDIAMVFQsyalYP-HM---- 90
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQ----FPeHQlfee 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 91 TVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTP-LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLR 169
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 170 VVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPA 226
Cdd:PRK13634 182 KEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-212 |
7.50e-36 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 130.59 E-value: 7.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDldpKDRDIAMVFQSY 84
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG---PGAERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 85 ALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518853886 165 DAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVL--NGGRV 212
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRV 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-216 |
8.74e-36 |
|
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: 129.41 E-value: 8.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKT----IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKDRDIA 78
Cdd:cd03266 2 ITADALTKRFRDVKKtvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 79 MVFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFD 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 159 EPLSNLDAKLRVVMRGEIKALhQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVG 216
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-210 |
2.42e-35 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 128.03 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDldpkDRDIAMVFQSY 84
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLEKE----RKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 85 AL---YPhMTVASNMGFSLEHR----GSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:cd03235 78 SIdrdFP-ISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518853886 158 DEPLSNLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGG 210
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-212 |
2.71e-35 |
|
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: 127.72 E-value: 2.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVFQS 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHMTVASNMGFSLEHRGSSKQEIAEkvnwAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518853886 164 LDAKlrvvmrG--EIKALHQKLKTTTIYV---THDQVEAMTMADRVVVLNGGRV 212
Cdd:cd03268 157 LDPD------GikELRELILSLRDQGITVlisSHLLSEIQKVADRIGIINKGKL 204
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-234 |
5.98e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 128.11 E-value: 5.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGL-----ETITGGELRIGERIVNDLDPKD- 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 -RDIAMVFQSYALYPHMTVASN--MGFSLEHRGSSKQEIAEKVNWAADILGL----TPLLDRYPRQLSGGQRQRVAMGRA 147
Cdd:PRK14247 81 rRRVQMVFQIPNPIPNLSIFENvaLGLKLNRLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 148 IVRNPQVFLFDEPLSNLD----AKLRVVMrgeikaLHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYD 223
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDpentAKIESLF------LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
250
....*....|.
gi 518853886 224 RPANQFVAGFI 234
Cdd:PRK14247 235 NPRHELTEKYV 245
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-226 |
1.38e-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: 126.64 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDR---DIAMVF 81
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 QSYALYPHMTVASN--MGFsleHRGSSKQEIAEKVnwaADILGLTPLLDRYPRQ----LSGGQRQRVAMGRAIVRNPQVF 155
Cdd:COG0410 85 EGRRIFPSLTVEENllLGA---YARRDRAEVRADL---ERVYELFPRLKERRRQragtLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518853886 156 LFDEPLSNLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPA 226
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-217 |
2.35e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 131.69 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD---RDIAMV 80
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPHMTVASNMGFSLEHRGS---SKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:COG3845 86 HQHFMLVPNLTVAENIVLGLEPTKGgrlDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 158 DEPLSNLD----AKLRVVMRgeikalhqKLK---TTTIYVTHDQVEAMTMADRVVVLNGGRVeqVGT 217
Cdd:COG3845 166 DEPTAVLTpqeaDELFEILR--------RLAaegKSIIFITHKLREVMAIADRVTVLRRGKV--VGT 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-216 |
2.39e-34 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 125.47 E-value: 2.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDpkDRDIAMVFQS 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 164 LDAKLRVVMRGEIKALHQKlKTTTIYVTH--DQVEAmtMADRVVVLNGGRVEQVG 216
Cdd:cd03269 159 LDPVNVELLKDVIRELARA-GKTVILSTHqmELVEE--LCDRVLLLNKGRAVLYG 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-222 |
4.31e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 125.35 E-value: 4.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDR---DIAMV 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 161 LSNLDAKlrVVmrGEIKALHQKLKTTTIYV---THDQVEAMTMADRVVVLNGGRVEQVGTPLELY 222
Cdd:cd03218 161 FAGVDPI--AV--QDIQKIIKILKDRGIGVlitDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-212 |
6.71e-34 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 124.62 E-value: 6.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKSYGA--VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIA 78
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 79 MVFQSYALYpHMTVASNMGFSLEHrgSSKQEIAEkvnwAADILGLTPLLDRYP-----------RQLSGGQRQRVAMGRA 147
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLGAPL--ADDERILR----AAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 148 IVRNPQVFLFDEPLSNLDaklrvvMRGE---IKALHQKLKT-TTIYVTHDQVeAMTMADRVVVLNGGRV 212
Cdd:cd03245 155 LLNDPPILLLDEPTSAMD------MNSEerlKERLRQLLGDkTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-225 |
1.10e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 126.62 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 16 VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD-----RDIAMVFQS-YA-LYP 88
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 89 HMTVASNMGFSLE-HRGSSKQEIAEKVNWAADILGLTP-LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:PRK11308 108 RKKVGQILEEPLLiNTSLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 167 KLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:PRK11308 188 SVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-212 |
2.75e-33 |
|
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: 123.66 E-value: 2.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSdirksYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETIT-GGELRI-GERI----VNDLDPKd 74
Cdd:COG1119 6 LRNVTVR-----RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLfGERRggedVWELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 rdIAMVfqSYAL----YPHMT----VASnmGF--SLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAM 144
Cdd:COG1119 80 --IGLV--SPALqlrfPRDETvldvVLS--GFfdSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 145 GRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
8.65e-33 |
|
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: 127.61 E-value: 8.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY-----GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGEL--RIGERIVNDLDPK--- 73
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDEWVDMTKPGpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 74 ----DRDIAMVFQSYALYPHMTVASNM--GFSLEHrgssKQEIAE-KVNWAADILGLT-----PLLDRYPRQLSGGQRQR 141
Cdd:TIGR03269 360 rgraKRYIGILHQEYDLYPHRTVLDNLteAIGLEL----PDELARmKAVITLKMVGFDeekaeEILDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 142 VAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-222 |
2.36e-32 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 120.72 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGA---VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIA 78
Cdd:cd03249 1 IEFKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 79 MVFQSYALYPhMTVASNMGFSLEHRGSSKQEIAEKVNWAADILglTPLLDRY-----PR--QLSGGQRQRVAMGRAIVRN 151
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYGKPDATDEEVEEAAKKANIHDFI--MSLPDGYdtlvgERgsQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518853886 152 PQVFLFDEPLSNLDAKLRVVMRgeiKALHQKLK-TTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTPLELY 222
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQ---EALDRAMKgRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-212 |
3.61e-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: 3.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTI-HGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNdldPKDR--DIAMVF 81
Cdd:cd03226 1 RIENISFSYKKGTEIlDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERrkSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 QS--YALYPHmTVASNMGFSLEhRGSSKQEIAEKVnwaADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:cd03226 78 QDvdYQLFTD-SVREELLLGLK-ELDAGNEQAETV---LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518853886 160 PLSNLDAKLRVVMRGEIKALhQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:cd03226 153 PTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
17-212 |
3.85e-32 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 126.90 E-value: 3.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 17 KTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSYALYpHMTVAS 94
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTLRD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 95 NMgfSLEHRGSSKQEIAEkvnwAADILGLTPLLDRYP-----------RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:TIGR03375 558 NI--ALGAPYADDEEILR----AAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILLLDEPTSA 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518853886 164 LDaklrvvMRGE---IKALHQKL-KTTTIYVTHdQVEAMTMADRVVVLNGGRV 212
Cdd:TIGR03375 632 MD------NRSEerfKDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-207 |
3.99e-32 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 125.86 E-value: 3.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 14 GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSYALYPHmT 91
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 92 VASNMGFSLehRGSSKQEIAEKVNWA------ADI-LGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:TIGR02857 412 IAENIRLAR--PDASDAEIREALERAgldefvAALpQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518853886 165 DAKLRVVMRGEIKALHQklKTTTIYVTHDqVEAMTMADRVVVL 207
Cdd:TIGR02857 490 DAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-226 |
1.28e-31 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 124.41 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 8 DIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKS----TLLRMIAGLETITGGELRIGERIVNDLDPKD------RDI 77
Cdd:COG4172 15 AFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 AMVFQ--SYALYPHMTVASNMGFSLE-HRGSSKQEIAEKvnwAADILGLTPL------LDRYPRQLSGGQRQRV--AMgr 146
Cdd:COG4172 95 AMIFQepMTSLNPLHTIGKQIAEVLRlHRGLSGAAARAR---ALELLERVGIpdperrLDAYPHQLSGGQRQRVmiAM-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 147 AIVRNPQVFLFDEPLSNLDaklrVVMRGEI----KALHQKLKTTTIYVTHDqveaMT----MADRVVVLNGGRVEQVGTP 218
Cdd:COG4172 170 ALANEPDLLIADEPTTALD----VTVQAQIldllKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQGPT 241
|
....*...
gi 518853886 219 LELYDRPA 226
Cdd:COG4172 242 AELFAAPQ 249
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-234 |
1.88e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 118.99 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 13 YGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLL----RMIaglETITG----GELRI-GERIVN-DLDPKD--RDIAMV 80
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMN---DLIPGarveGEILLdGEDIYDpDVDVVElrRRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPhMTVASNMGFSLEHRG-SSKQEIAEKVNWA----------ADIlgltplLDRYPRQLSGGQRQRVAMGRAIV 149
Cdd:COG1117 98 FQKPNPFP-KSIYDNVAYGLRLHGiKSKSELDEIVEESlrkaalwdevKDR------LKKSALGLSGGQQQRLCIARALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 150 RNPQVFLFDEPLSNLD----AKlrvvmrgeIKALHQKLKT--TTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYD 223
Cdd:COG1117 171 VEPEVLLMDEPTSALDpistAK--------IEELILELKKdyTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFT 242
|
250
....*....|.
gi 518853886 224 RPANQFVAGFI 234
Cdd:COG1117 243 NPKDKRTEDYI 253
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-284 |
1.89e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 120.21 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERivndLDPKDRD-IAmvf 81
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEP----LDPEDRRrIG--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 qsY-----ALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:COG4152 75 --YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 157 FDEPLSNLDAKLRVVMRGEIKALHQKlKTTTIYVTH--DQVEAmtMADRVVVLNGGRVEQVGTPLELYDR-PANQFVAGF 233
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHqmELVEE--LCDRIVIINKGRKVLSGSVDEIRRQfGRNTLRLEA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 234 IGSPSM-NFLSGTISAgGFETGGVVLPPPATAAG------LAGRGAVYGIRPEHFSLD 284
Cdd:COG4152 230 DGDAGWlRALPGVTVV-EEDGDGAELKLEDGADAqellraLLARGPVREFEEVRPSLN 286
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-212 |
2.13e-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: 116.55 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSYALYPhmtvasnm 96
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLPQDDELFS-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 97 gfslehrGSskqeIAEKVnwaadilgltplldryprqLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEI 176
Cdd:cd03246 90 -------GS----IAENI-------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 518853886 177 KALhQKLKTTTIYVTHdQVEAMTMADRVVVLNGGRV 212
Cdd:cd03246 140 AAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-212 |
4.89e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 116.90 E-value: 4.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY-GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD-----RDI 77
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 AMVFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 158 DEPLSNLDAKLRvvmRGEIKALHQ--KLKTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:PRK10908 162 DEPTGNLDDALS---EGILRLFEEfnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-233 |
4.98e-31 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 123.68 E-value: 4.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRKSY----GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD------R 75
Cdd:PRK10535 7 LKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrrE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 76 DIAMVFQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 156 LFDEPLSNLDAKLRVVMRGEIKALHQKlKTTTIYVTHD-QVEAmtMADRVVVLNGGRV----------EQVGTPLELYDR 224
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDpQVAA--QAERVIEIRDGEIvrnppaqekvNVAGGTEPVVNT 243
|
250
....*....|.
gi 518853886 225 PA--NQFVAGF 233
Cdd:PRK10535 244 ASgwRQFVSGF 254
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-216 |
1.68e-30 |
|
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: 115.37 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVvLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKDRDIAMVFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 163 NLDAKLRVVMRGEIKALHQklKTTTIYVTH--DQVEAmtMADRVVVLNGGRVEQVG 216
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHivEDVES--LCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-223 |
1.73e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 116.77 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 18 TIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSyalyPH-----M 90
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQN----PDnqfvgS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 91 TVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRV 170
Cdd:PRK13648 100 IVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518853886 171 VMRGEIKALHQKLKTTTIYVTHDQVEAMTmADRVVVLNGGRVEQVGTPLELYD 223
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-224 |
2.30e-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: 115.40 E-value: 2.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKsygaVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMV 80
Cdd:cd03254 7 NVNFSYDEK----KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPHmTVASNMGFSlehRGSSKQeiaEKVNWAADILGLTPLLDRYPR-----------QLSGGQRQRVAMGRAIV 149
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLG---RPNATD---EEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 150 RNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQklKTTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-224 |
3.01e-30 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 115.41 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGA-VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVN-DLDPKDRDIAMV 80
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIREvTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYpHMTVASNMGFSLEhrGSSKQEIAEkvnwAADILGLTPLLDRYPRQ-----------LSGGQRQRVAMGRAIV 149
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYGRP--DATDEEVIE----AAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 150 RNPQVFLFDEPLSNLDA-KLRVVMRGEIKALHQKlktTTIYVTHDQVEAMTmADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:cd03253 154 KNPPILLLDEATSALDThTEREIQAALRDVSKGR---TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
12-220 |
1.17e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 114.34 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 12 SYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQ------- 82
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQhhltpeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 -------SYALYPHmtvasnmgfsLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:PRK11231 91 itvrelvAYGRSPW----------LSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 156 LFDEPLSNLDAKLRVVMRGEIKALHQKLKtTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLE 220
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-227 |
1.36e-29 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 113.23 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGL----ETITGGELRIGERIVNDLDPKDRDIAMVFQS--YALYPHMTV 92
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 93 ASNMGFSLEHRGS-SKQEIAEKVNwAADILGLTP---LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL 168
Cdd:TIGR02770 82 GNHAIETLRSLGKlSKQARALILE-ALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 169 RVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPAN 227
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-218 |
1.39e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.10 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 7 SDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSY 84
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 85 AL-YP---HMTVAsnMGfsLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVR------NPQV 154
Cdd:PRK13548 86 SLsFPftvEEVVA--MG--RAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 155 FLFDEPLSNLDakLR---VVMRgEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTP 218
Cdd:PRK13548 162 LLLDEPTSALD--LAhqhHVLR-LARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-207 |
1.66e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.94 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 12 SYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGerivndldpKDRDIAMVFQSYALYPHM- 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA---------GGARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 91 -TVASNMGFSL-EHRGSSKQEIAEK---VNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:NF040873 72 lTVRDLVAMGRwARRGLWRRLTRDDraaVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518853886 166 AKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTmADRVVVL 207
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-212 |
1.89e-29 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 113.20 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 10 RKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRigeriVNDLDPKDR------DIAMVF-Q 82
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR-----VAGLVPWKRrkkflrRIGVVFgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPHMTVASnmGFSLEHR--GSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:cd03267 103 KTQLWWDLPVID--SFYLLAAiyDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518853886 161 LSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-223 |
2.92e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 114.80 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 9 IRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRigeriVNDLDP-KDR-----DIAMVF- 81
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR-----VLGYVPfKRRkefarRIGVVFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 QSYALYPHMTVASnmgfSLE-HR---GSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQR--VAMgrAIVRNPQVF 155
Cdd:COG4586 103 QRSQLWWDLPAID----SFRlLKaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRceLAA--ALLHRPKIL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518853886 156 LFDEPLSNLD--AKLRVvmRGEIKALHQKLKTTTIYVTHD--QVEAmtMADRVVVLNGGRVeqvgtpleLYD 223
Cdd:COG4586 177 FLDEPTIGLDvvSKEAI--REFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHGRI--------IYD 236
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-224 |
4.05e-29 |
|
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: 112.32 E-value: 4.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYG--AVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAM 79
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYpHMTVASNMGFSLehRGSSKQEIAEkvnwAADILGLTPLLDRYPR-----------QLSGGQRQRVAMGRAI 148
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGR--PGATREEVEE----AARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 149 VRNPQVFLFDEPLSNLDAKL-RVVMrgeiKALHQKLKT-TTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:cd03251 154 LKDPPILILDEATSALDTESeRLVQ----AALERLMKNrTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-253 |
1.04e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.52 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 15 AVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVN------DLDPKDRDIAMVFQsyalYP 88
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQ----FP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 89 HM-----TVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTP-LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:PRK13643 94 ESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 163 NLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYdRPANQFVAGFIGSPSMNFL 242
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF-QEVDFLKAHELGVPKATHF 251
|
250
....*....|.
gi 518853886 243 SGTISAGGFET 253
Cdd:PRK13643 252 ADQLQKTGAVT 262
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-209 |
1.23e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 110.64 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 21 GVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDR------DIAMVFQSYALYPHMTVAS 94
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 95 NMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRG 174
Cdd:PRK10584 108 NVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170 180 190
....*....|....*....|....*....|....*
gi 518853886 175 EIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNG 209
Cdd:PRK10584 188 LLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-217 |
1.24e-28 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 110.69 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDR---DIAMVF 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 QSYALYPHMTVASNMGFSLEHRGSSKQEIAEkvnwaaDILGLTPLL----DRYPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPD------EIYELFPVLkemlGRRGGDLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 158 DEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGT 217
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-225 |
1.38e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 110.89 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLD--------- 71
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhkrarlgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 72 ---PKDrdiAMVFQsyalypHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAI 148
Cdd:COG1137 81 gylPQE---ASIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 149 VRNPQVFLFDEPLSNLDAkLRVvmrGEIKALHQKLKTTTIYV--T-HDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:COG1137 152 ATNPKFILLDEPFAGVDP-IAV---ADIQKIIRHLKERGIGVliTdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-220 |
1.54e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 111.36 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 7 SDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSY 84
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 85 AL---YPHMTVASnMGfsLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAI------VRNPQVF 155
Cdd:COG4559 85 SLafpFTVEEVVA-LG--RAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518853886 156 LF-DEPLSNLD-----AKLRVVmrgeiKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLE 220
Cdd:COG4559 162 LFlDEPTSALDlahqhAVLRLA-----RQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-222 |
1.66e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 111.72 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELrigerIVNDLDPKDR----DI----AMVFQSyalyP-HMTV 92
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-----YVDGLDTSDEenlwDIrnkaGMVFQN----PdNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 93 AS----NMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL 168
Cdd:PRK13633 100 ATiveeDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518853886 169 RVVMRGEIKALHQKLKTTTIYVTHDQVEAMTmADRVVVLNGGRVEQVGTPLELY 222
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-212 |
1.67e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 108.63 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGA-----VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDR--D 76
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 IAMVFQSYAL--YPHMTVASNM--------GFSLeHRGSSKQEIAEKVNWAADI-LGLTPLLDRYPRQLSGGQRQRVAMG 145
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLalayrrgkRRGL-RRGLTKKRRELFRELLATLgLGLENRLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518853886 146 RAIVRNPQVFLFDEPLSNLDAKL-RVVMrgeikALHQKL----KTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTaALVL-----ELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
29-223 |
1.69e-27 |
|
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: 107.63 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 29 GEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERivnDLDPKDRDIAMVFQSYAL---YP----HMTVASNMGFSLE 101
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFPisvaHTVMSGRTGHIGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 102 HRGSSKQEIAeKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQ 181
Cdd:TIGR03771 83 LRRPCVADFA-AVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELAG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518853886 182 KlKTTTIYVTHDQVEAMTMADRVVVLNgGRVEQVGTPLELYD 223
Cdd:TIGR03771 162 A-GTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQD 201
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-212 |
2.42e-27 |
|
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: 106.10 E-value: 2.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKSYGAVKTI-HGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGL--ETITGGELRIGERIVNDLDPKDRdIAM 79
Cdd:cd03213 8 NLTVTVKSSPSKSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI-IGY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYPHMTVASNMGFSLEHRGsskqeiaekvnwaadilgltplldryprqLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:cd03213 87 VPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 160 PLSNLDAKL-RVVMRgEIKALHQkLKTTTIYVTHD-QVEAMTMADRVVVLNGGRV 212
Cdd:cd03213 138 PTSGLDSSSaLQVMS-LLRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-217 |
4.87e-27 |
|
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: 111.76 E-value: 4.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 18 TIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSYALYPhmtvasn 95
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFD------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 96 mgfslehrGSSKQEIA-------EKVNWAAD-------ILGL-----TPLLDRyPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:COG4618 420 --------GTIAENIArfgdadpEKVVAAAKlagvhemILRLpdgydTRIGEG-GARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 157 FDEPLSNLDAklrvvmRGEiKALHQKL------KTTTIYVTHDQvEAMTMADRVVVLNGGRVEQVGT 217
Cdd:COG4618 491 LDEPNSNLDD------EGE-AALAAAIralkarGATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGP 549
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-225 |
5.43e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.58 E-value: 5.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGL--------ETITGGELRIGERIVNDLDPKdrdIAMVFQSyalyPH---- 89
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWDIREK---VGIVFQN----PDnqfv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 90 -MTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL 168
Cdd:PRK13640 99 gATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 169 RVVMRGEIKALHQKLKTTTIYVTHDQVEAmTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-222 |
5.79e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.79 E-value: 5.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGE-------RIVNDLDPKDR 75
Cdd:PRK13645 11 NVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 76 DIAMVFQ--SYALYPHmTVASNMGFSLEHRGSSKQEIAEKVNWAADILGL-TPLLDRYPRQLSGGQRQRVAMGRAIVRNP 152
Cdd:PRK13645 91 EIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 153 QVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELY 222
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-224 |
1.07e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 106.74 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 17 KTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSyalyPH----- 89
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGLVFQD----PDdqvfs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 90 MTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLR 169
Cdd:PRK13647 95 STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 170 VVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:PRK13647 175 ETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-218 |
1.16e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 109.16 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIA 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 79 MVFQSYALYPHMTVAS--NMGFSlEHRG--SSKQEIAEK-VNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQvvEMGRT-PHRSrfDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 154 VFLFDEPLSNLDAKLRVVMRGEIKALHQKLKtTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTP 218
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
16-222 |
2.01e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.95 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 16 VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIV-NDLDPKDRDIAMVFQSY-ALYPHMTV 92
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTaENVWNLRRKIGMVFQNPdNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 93 ASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVM 172
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518853886 173 RGEIKALHQKLKTTTIYVTHDQVEAMTmADRVVVLNGGRVEQVGTPLELY 222
Cdd:PRK13642 180 MRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-214 |
3.64e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 104.13 E-value: 3.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 11 KSY--GAVKT--IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDL------DPKDRDIAMV 80
Cdd:PRK11629 13 KRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaELRNQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518853886 161 LSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMaDRVVVLNGGRVEQ 214
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-234 |
5.22e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.47 E-value: 5.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLE------TITGGELRIGERIVN---DLDPKD 74
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpevTITGSIVYNGHNIYSprtDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 RDIAMVFQSYALYPhMTVASNMGFSLEHRGSSKQEIAEKV-----------NWAADILGLTPLldryprQLSGGQRQRVA 143
Cdd:PRK14239 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAvekslkgasiwDEVKDRLHDSAL------GLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 144 MGRAIVRNPQVFLFDEPLSNLDAklrvVMRGEIKALHQKLKT--TTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDP----ISAGKIEETLLGLKDdyTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
250
....*....|...
gi 518853886 222 YDRPANQFVAGFI 234
Cdd:PRK14239 235 FMNPKHKETEDYI 247
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-217 |
8.27e-26 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 107.82 E-value: 8.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 14 GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSYALYPHmT 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 92 VASN---MGFSLEhrgsskqeiAEKVNWAADILGLTPLLDRYPR-----------QLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:TIGR01842 408 VAENiarFGENAD---------PEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 158 DEPLSNLDAKLRVVMRGEIKALhQKLKTTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGT 217
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKAL-KARGITVVVITH-RPSLLGCVDKILVLQDGRIARFGE 536
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
9.50e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 104.89 E-value: 9.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 2 ANVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKDRDIAMV 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518853886 161 LSNLDAKLRVVMRGEIKALHQKLKTTTIyVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGKTILL-TTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-237 |
1.48e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 103.69 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIV----NDLDPKDRDIA 78
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIPamsrSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 79 MVFQSYALYPHMTVASNMGFSL-EHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 158 DEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELY---DRPANQFVAGFI 234
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQanpDPRVRQFLDGIA 247
|
...
gi 518853886 235 GSP 237
Cdd:PRK11831 248 DGP 250
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-212 |
2.90e-25 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 101.78 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKSygAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPK--DRDIAMV 80
Cdd:cd03248 16 NVTFAYPTRP--DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPHmTVASNMGFSLEHRGSSK-QEIAEKVNWAADI----LGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:cd03248 94 GQEPVLFAR-SLQDNIAYGLQSCSFECvKEAAQKAHAHSFIselaSGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 156 LFDEPLSNLDAKLRVVMRgeiKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:cd03248 173 ILDEATSALDAESEQQVQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-222 |
3.38e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.90 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 21 GVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDlDPKDRDI-------AMVFQsyalYPHM--- 90
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS-TSKNKDIkqirkkvGLVFQ----FPESqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 91 --TVASNMGFSLEHRGSSKQEiAEKVnwAADILGLT----PLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:PRK13649 100 eeTVLKDVAFGPQNFGVSQEE-AEAL--AREKLALVgiseSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 165 DAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELY 222
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-226 |
4.83e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.39 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 16 VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIG----------ERIVNDLDPKD--------RDI 77
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSKKiknfkelrRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 AMVFQ--SYALYPHmTVASNMGFSLEHRGSSKQEIAEKVNWAADILGL-TPLLDRYPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:PRK13631 119 SMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518853886 155 FLFDEPLSNLDAKLRVVMRGEIKALHQKLKtTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPA 226
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-211 |
5.05e-25 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 100.24 E-value: 5.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIvndldpkdrdiAMV 80
Cdd:cd03250 3 VEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI-----------AYV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSyALYPHMTVASNMGFSLEHRgsskqeiAEKVNWAADILGLTPLLDRYPRQ-----------LSGGQRQRVAMGRAIV 149
Cdd:cd03250 72 SQE-PWIQNGTIRENILFGKPFD-------EERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 150 RNPQVFLFDEPLSNLDAKLRV-----VMRGEIkalhqKLKTTTIYVTHdQVEAMTMADRVVVLNGGR 211
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRhifenCILGLL-----LNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
17-221 |
6.72e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.91 E-value: 6.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 17 KTI-HGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLE--TITGGELRI-GERIvNDLDPKDR---DIAMVFQsyalYPh 89
Cdd:COG0396 13 KEIlKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLdGEDI-LELSPDERaraGIFLAFQ----YP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 90 mtVA----SNMGF---SLEHRGSSKQEIAE---KVNWAADILGLTP-LLDRYPRQ-LSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:COG0396 87 --VEipgvSVSNFlrtALNARRGEELSAREflkLLKEKMKELGLDEdFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 158 DEPLSNLDA-KLRVVMRGeIKALHQKlKTTTIYVTH-----DQVEamtmADRVVVLNGGRVEQVGTPlEL 221
Cdd:COG0396 165 DETDSGLDIdALRIVAEG-VNKLRSP-DRGILIITHyqrilDYIK----PDFVHVLVDGRIVKSGGK-EL 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-225 |
9.57e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 105.32 E-value: 9.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 16 VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVN----DLDPKDRDIAMVFQS-YA-LYP 88
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFnGQRIDTlspgKLQALRRDIQFIFQDpYAsLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 89 HMTVA-SNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLD-RYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:PRK10261 417 RQTVGdSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 167 KLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-215 |
9.71e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.17 E-value: 9.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQS 83
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHmTVASNMGFSLEHRGSSKQEIAekvnWAADI--LGL-TPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:PRK10247 90 PTLFGD-TVYDNLIFPWQIRNQQPDPAI----FLDDLerFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 161 LSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEaMTMADRVVVL--NGGRVEQV 215
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLqpHAGEMQEA 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-193 |
1.37e-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: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIgerivndldPKDRDIAMVFQSYA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 86 LYPHMTVASN--MGFS-----------LEHRGSSKQEIAEKVN-----------WAAD-----I---LGLTP-LLDRYPR 132
Cdd:COG0488 72 LDDDLTVLDTvlDGDAelraleaeleeLEAKLAEPDEDLERLAelqeefealggWEAEaraeeIlsgLGFPEeDLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 133 QLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAklrvvmrgE-IKALHQKLKT---TTIYVTHD 193
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL--------EsIEWLEEFLKNypgTVLVVSHD 208
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-221 |
1.62e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 104.54 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLE------TITGGELRigerivnDLDPKD--RDIAMVFQSYALyPHMTVA 93
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLpyqgslKINGIELR-------ELDPESwrKHLSWVGQNPQL-PHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 94 SNMgfSLEHRGSSKQEIAEKVN--WAADIL-----GL-TPLLDRYPRqLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:PRK11174 441 DNV--LLGNPDASDEQLQQALEnaWVSEFLpllpqGLdTPIGDQAAG-LSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 166 AKL-RVVMRGEIKALHQKlktTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:PRK11174 518 AHSeQLVMQALNAASRRQ---TTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-229 |
1.72e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.47 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLET----------ITGGELRIGERIVNDLDPK 73
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshieLLGRTVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 74 DRDIAMVFQSYALYPHMTVASNMgfSLEHRGSS----------KQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVA 143
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENV--LIGALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 144 MGRAIVRNPQVFLFDEPLSNLDAK-LRVVMRgEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVeqvgtpleLY 222
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPEsARIVMD-TLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV--------FY 233
|
....*..
gi 518853886 223 DRPANQF 229
Cdd:PRK09984 234 DGSSQQF 240
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-239 |
1.92e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.45 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELrigerIVNDLDPKD--------RDIAMVFQS-YALYPHMTV 92
Cdd:PRK13644 21 INLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV-----LVSGIDTGDfsklqgirKLVGIVFQNpETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 93 ASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVM 172
Cdd:PRK13644 96 EEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 173 RGEIKALHQKLKtTTIYVTHDqVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAgfIGSPSM 239
Cdd:PRK13644 176 LERIKKLHEKGK-TIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG--LTPPSL 238
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
18-225 |
2.38e-24 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 104.27 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 18 TIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSYALYP---HMTV 92
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAvrRQLGVVLQNGRLMSgsiFENI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 93 ASNMGFSLEhrgsSKQEIAEKVNWAADI----LGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL 168
Cdd:TIGR03797 548 AGGAPLTLD----EAWEAARMAGLAEDIrampMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 169 RVVMRGEIKalhqKLKTTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:TIGR03797 624 QAIVSESLE----RLKVTRIVIAH-RLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-224 |
3.84e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.00 E-value: 3.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTI-HGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLdpkdrDIAMVFQs 83
Cdd:COG1134 27 LLLRRRRTRREEFWAlKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL-----ELGAGFH- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 yalyPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:COG1134 101 ----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518853886 164 LDAKLRVVMRGEIKALHQKlKTTTIYVTHD--QVEamTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:COG1134 177 GDAAFQKKCLARIRELRES-GRTVIFVSHSmgAVR--RLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-225 |
3.94e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.88 E-value: 3.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 8 DIRKSY-GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVN-DLDPKDRDIAMVFQS- 83
Cdd:PRK13652 8 DLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKeNIREVRKFVGLVFQNp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 --YALYPhmTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:PRK13652 88 ddQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518853886 162 SNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-225 |
4.27e-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: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKSYGA---VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVnDLDPK--DRD 76
Cdd:TIGR00958 478 LIEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdGVPLV-QYDHHylHRQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 IAMVFQSYALYPHmTVASNMGFSLEHRGSSKQEIAEKVNWAAD-ILGLTPLLD----RYPRQLSGGQRQRVAMGRAIVRN 151
Cdd:TIGR00958 557 VALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDfIMEFPNGYDtevgEKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 152 PQVFLFDEPLSNLDAklrvvmrgEIKALHQKLKT----TTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:TIGR00958 636 PRVLILDEATSALDA--------ECEQLLQESRSrasrTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-209 |
4.50e-24 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 99.02 E-value: 4.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 25 DIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELrigERIVNDLDPKDRDIAMVFQsyalyphMTVASNMGFSLEHRG 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKPQYIKADYE-------GTVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 105 SSKQEIAEkvnwAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLK 184
Cdd:cd03237 91 THPYFKTE----IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180
....*....|....*....|....*
gi 518853886 185 TTTIYVTHDQVEAMTMADRVVVLNG 209
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-223 |
5.53e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 100.68 E-value: 5.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKDRDIAMVFQ 82
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518853886 163 NLDAKLRVVMRGEIKALHQKLKtTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYD 223
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-234 |
6.98e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.58 E-value: 6.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIV---NDLDPKD-----RDIAMVFQSYALYPHM 90
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDaiklrKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 91 TVASNMGFSLEHRG-SSKQEIAEKVNWAADILGL-TPLLDRY---PRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:PRK14246 106 SIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518853886 166 aklrVVMRGEIKALHQKLKT--TTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFI 234
Cdd:PRK14246 186 ----IVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-166 |
7.23e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 97.25 E-value: 7.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 21 GVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRigerivndLDPKDRDIAMVFQS--Y-----ALYPHMTVA 93
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK--------LDGGDIDDPDVAEAchYlghrnAMKPALTVA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518853886 94 SNMGFSLEHRGSSKQEIAEkvnwAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:PRK13539 92 ENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-224 |
8.89e-24 |
|
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: 102.10 E-value: 8.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 16 VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSYALYPHmTVA 93
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVALVSQDVVLFND-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 94 SNMGFslehrGSSKQEIAEKVNWAADILGLTPLLDRYPR-----------QLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:TIGR02203 424 NNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEATS 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 163 NLD--------AKLRVVMRGEikalhqklktTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:TIGR02203 499 ALDneserlvqAALERLMQGR----------TTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-213 |
1.28e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVndldpkdrdIAMVFQS 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK---------IGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YA-LYPHMTVASNMgfsleHRGSSKQEIAEKVNWAADiLGLTP-LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:COG0488 387 QEeLDPDKTVLDEL-----RDGAPGGTEQEVRGYLGR-FLFSGdDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 162 SNLDaklrVVMRgeiKALHQKLKT---TTIYVTHDQ--VEamTMADRVVVLNGGRVE 213
Cdd:COG0488 461 NHLD----IETL---EALEEALDDfpgTVLLVSHDRyfLD--RVATRILEFEDGGVR 508
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-252 |
1.30e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.75 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKD-----RDIAMVFQsyalYPHM----- 90
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHITPETGNKNlkklrKKVSLVFQ----FPEAqlfen 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 91 TVASNMGFSLEHRGSSKQEIAEK-VNWAADIlGL-TPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL 168
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEKaLKWLKKV-GLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 169 RVVMRgEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPaNQFVAGFIGSPSMNFLSGTISA 248
Cdd:PRK13641 181 RKEMM-QLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK-EWLKKHYLDEPATSRFASKLEK 258
|
....
gi 518853886 249 GGFE 252
Cdd:PRK13641 259 GGFK 262
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-216 |
1.40e-23 |
|
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: 96.83 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 10 RKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLdpkdrDIAMVFQsyalyPH 89
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN-----PE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 90 MTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLR 169
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518853886 170 VVMRGEIKALHQKLKtTTIYVTHDQVEAMTMADRVVVLNGGRVEQVG 216
Cdd:cd03220 179 EKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-229 |
2.86e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.55 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKST----LLRMIAgletiTGGELRIGERIVNDLDPKD-----RDIAMVFQ--SYALY 87
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 88 PHMTVASNM--GFSLEHRGSSKQEIAEKVNWAADILGLTPLL-DRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:PRK15134 377 PRLNVLQIIeeGLRVHQPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 165 DAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQF 229
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-211 |
3.14e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 100.37 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 9 IRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIV---NDLDPKDRDIAMVFQSYA 85
Cdd:PRK11288 10 IGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 86 LYPHMTVASNM-------GFSLEHRGSSKQEIAEKV-NWAADILGLTPLldrypRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:PRK11288 90 LVPEMTVAENLylgqlphKGGIVNRRLLNYEAREQLeHLGVDIDPDTPL-----KYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518853886 158 DEPLSNLDAK-----LRVV--MRGEIKALhqklktttIYVTHDQVEAMTMADRVVVLNGGR 211
Cdd:PRK11288 165 DEPTSSLSAReieqlFRVIreLRAEGRVI--------LYVSHRMEEIFALCDAITVFKDGR 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-210 |
3.53e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.27 E-value: 3.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIgerivndldPKDRDIAMVFQ-SY--------AL-YP 88
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQrPYlplgtlreALlYP 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 89 HmtvasnmgfslEHRGSSKQEIAEkvnwAADILGLTPLLDRY------PRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:COG4178 450 A-----------TAEAFSDAELRE----ALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518853886 163 NLDAKLRVVMrgeIKALHQKLKTTT-IYVTHdQVEAMTMADRVVVLNGG 210
Cdd:COG4178 515 ALDEENEAAL---YQLLREELPGTTvISVGH-RSTLAAFHDRVLELTGD 559
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-211 |
3.78e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 95.96 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI--GERIVNDLDPKDRDIAMVFQSYALY--------P 88
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREILALRRRTIGYvsqflrviP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 89 HMT----VASnmgfSLEHRGSSKQEIAEKvnwAADIL---GLTPLL-DRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:COG4778 107 RVSaldvVAE----PLLERGVDREEARAR---ARELLarlNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518853886 161 LSNLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQvEAM-TMADRVVVLNGGR 211
Cdd:COG4778 180 TASLDAANRAVVVELIEEAKAR-GTAIIGIFHDE-EVReAVADRVVDVTPFS 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-212 |
4.16e-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: 94.42 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRD---IAMV---FQSYALYPHMTV 92
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVpedRKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 93 ASNMGFslehrgsskqeiaekvnwaadilgltplldryPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAklrvvm 172
Cdd:cd03215 96 AENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV------ 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518853886 173 rGEIKALHQKLK------TTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:cd03215 138 -GAKAEIYRLIReladagKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-222 |
6.26e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.77 E-value: 6.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 17 KTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVND------LDPKDRDIAMVFQsyalYPHM 90
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 91 -----TVASNMGFSLEHRGSSKQEIAEK-------VNWAADILGLTPLldryprQLSGGQRQRVAMGRAIVRNPQVFLFD 158
Cdd:PRK13646 97 qlfedTVEREIIFGPKNFKMNLDEVKNYahrllmdLGFSRDVMSQSPF------QMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518853886 159 EPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELY 222
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-227 |
1.59e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.10 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 12 SYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGgELR-----------IGERIVNdLDPKDRDIAMV 80
Cdd:PRK14258 16 YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELES-EVRvegrveffnqnIYERRVN-LNRLRRQVSMV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPhMTVASNMGFSLE----HRGSSKQEIAEKVNWAADILG-LTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:PRK14258 94 HPKPNLFP-MSVYDNVAYGVKivgwRPKLEIDDIVESALKDADLWDeIKHKIHKSALDLSGGQQQRLCIARALAVKPKVL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 156 LFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNG-----GRVEQVGTPLELYDRPAN 227
Cdd:PRK14258 173 LMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHD 249
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-224 |
2.05e-22 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 94.09 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGA--VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPK--DRDIAM 79
Cdd:cd03252 1 ITFEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYpHMTVASNMgfSLEHRGSSKQEIAEkvnwAADILGLTPLLDRYPR-----------QLSGGQRQRVAMGRAI 148
Cdd:cd03252 81 VLQENVLF-NRSIRDNI--ALADPGMSMERVIE----AAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 149 VRNPQVFLFDEPLSNLDAKL-RVVMRGeikaLHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:cd03252 154 IHNPRILIFDEATSALDYESeHAIMRN----MHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-245 |
2.10e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.39 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKSYGAVKTihgVDLDIRDGEFVVLVGPSGCGKS----TLLRMI--AGLETITGGE-LRIGERIVNDL----- 70
Cdd:PRK10261 19 NIAFMQEQQKIAAVRN---LSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMlLRRRSRQVIELseqsa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 71 ----DPKDRDIAMVFQS--YALYPHMTVASNMGFSLE-HRGSSKQEI---AEKVNWAADILGLTPLLDRYPRQLSGGQRQ 140
Cdd:PRK10261 96 aqmrHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRlHQGASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 141 RVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLE 220
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQ 255
|
250 260
....*....|....*....|....*.
gi 518853886 221 LYDRPANQFVAGFIGS-PSMNFLSGT 245
Cdd:PRK10261 256 IFHAPQHPYTRALLAAvPQLGAMKGL 281
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-167 |
2.14e-22 |
|
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: 93.19 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 21 GVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPK-DRDIAMVFQSYALYPHMTVASNMGFs 99
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENLHF- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 100 LEHRGSSKQEIAEKvnwAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK 167
Cdd:TIGR01189 97 WAAIHGGAQRTIED---ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
4-221 |
5.01e-22 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 97.12 E-value: 5.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYG--AVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPK--DRDIAM 79
Cdd:TIGR01846 456 ITFENIRFRYApdSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYPHmTVASNMgfSLEHRGSSKqeiaEKVNWAADILGLTPLLDRYPR-----------QLSGGQRQRVAMGRAI 148
Cdd:TIGR01846 536 VLQENVLFSR-SIRDNI--ALCNPGAPF----EHVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARAL 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518853886 149 VRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQklKTTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-212 |
8.54e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 8.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 17 KTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD---RDIAMV---FQSYALYPHM 90
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVpedRKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 91 TVASNMGFSLEHRGS-----SKQEIAEKVNWAADILGL-TPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:COG1129 346 SIRENITLASLDRLSrggllDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518853886 165 D--AKlrvvmrGEIKALHQKLK---TTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:COG1129 426 DvgAK------AEIYRLIRELAaegKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-216 |
9.62e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 90.84 E-value: 9.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYG--AVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRD-IAMV 80
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYpHMTVASNMGfslehrgsskqeiaekvnwaadilgltplldrypRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:cd03247 81 NQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 161 LSNLDAKL-RVVMRGEIKALHQKlktTTIYVTHdQVEAMTMADRVVVLNGGRVEQVG 216
Cdd:cd03247 126 TVGLDPITeRQLLSLIFEVLKDK---TLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
1.01e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 96.02 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETI--TGGEL-----------------RIGE 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 65 RIV---NDLDPKDRD---------------IAMVFQ-SYALYPHMTVASNMGFSLEHRGSSKQEIAEKvnwAADILGLTP 125
Cdd:TIGR03269 81 PCPvcgGTLEPEEVDfwnlsdklrrrirkrIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGR---AVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 126 LLDRY---PRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMAD 202
Cdd:TIGR03269 158 LSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250 260
....*....|....*....|..
gi 518853886 203 RVVVLNGGRVEQVGTPLELYDR 224
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
19-221 |
1.17e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.54 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSYALYPHMTVAS-- 94
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQQLPAAEGMTVRElv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 95 NMGFSLEH--RGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVM 172
Cdd:PRK10575 107 AIGRYPWHgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518853886 173 RGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:PRK10575 187 LALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-212 |
1.28e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.23 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGA-----VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELrigERIVNDLDPKD---- 74
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI---EWIFKDEKNKKktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 -------------------------RDIAMVFQ--SYALYpHMTVASNMGFSLEHRGSSKQEIAEKvnwAADILGLTPL- 126
Cdd:PRK13651 80 kekvleklviqktrfkkikkikeirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKR---AAKYIELVGLd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 127 ---LDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKtTTIYVTHDQVEAMTMADR 203
Cdd:PRK13651 156 esyLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKR 234
|
....*....
gi 518853886 204 VVVLNGGRV 212
Cdd:PRK13651 235 TIFFKDGKI 243
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-236 |
1.29e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 92.55 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 16 VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVN--DLDPKDRDIAMVFQ--SYALYPHMT 91
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQdpSTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 92 VASNMGFSLE-HRGSSKQEIAEKVNWAADILGLTP-LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLR 169
Cdd:PRK15112 106 ISQILDFPLRlNTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 170 VVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGFIGS 236
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
4-225 |
1.88e-21 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 95.40 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKT--IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLdPKDR---DIA 78
Cdd:TIGR03796 478 VELRNITFGYSPLEPplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVA 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 79 MVFQSYALYpHMTVASNMgfSLEHRGSSKQEIAEKVNWAA---DILGLTPLLDrYP-----RQLSGGQRQRVAMGRAIVR 150
Cdd:TIGR03796 557 MVDQDIFLF-EGTVRDNL--TLWDPTIPDADLVRACKDAAihdVITSRPGGYD-AElaeggANLSGGQRQRLEIARALVR 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 151 NPQVFLFDEPLSNLDAKLRvvmrgeiKALHQKLK---TTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:TIGR03796 633 NPSILILDEATSALDPETE-------KIIDDNLRrrgCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-224 |
3.44e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 94.81 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKSYG-AVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAM 79
Cdd:TIGR01193 473 DIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSyalyPHM---TVASN--MGfslEHRGSSKQEIAEKVNWA---ADI----LGLTPLLDRYPRQLSGGQRQRVAMGRA 147
Cdd:TIGR01193 553 LPQE----PYIfsgSILENllLG---AKENVSQDEIWAACEIAeikDDIenmpLGYQTELSEEGSSISGGQKQRIALARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 148 IVRNPQVFLFDEPLSNLDAklrVVMRGEIKALHQKLKTTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDT---ITEKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-221 |
4.03e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 94.50 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTI-HGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMV 80
Cdd:COG5265 358 VRFENVSFGYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYpHMTVASNMGFSLEhrGSSKQEIAEkvnwAADILGLTPLLDRYPRQ-----------LSGGQRQRVAMGRAIV 149
Cdd:COG5265 438 PQDTVLF-NDTIAYNIAYGRP--DASEEEVEA----AARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 150 RNPQVFLFDEPLSNLDAK--------LRVVMRGeikalhqklkTTTIYVTH------DqveamtmADRVVVLNGGR-VEQ 214
Cdd:COG5265 511 KNPPILIFDEATSALDSRteraiqaaLREVARG----------RTTLVIAHrlstivD-------ADEILVLEAGRiVER 573
|
....*..
gi 518853886 215 vGTPLEL 221
Cdd:COG5265 574 -GTHAEL 579
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-222 |
4.68e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 91.29 E-value: 4.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 8 DIRKSY-GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIvnDLDPKD-----RDIAMV 80
Cdd:PRK13639 6 DLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPI--KYDKKSllevrKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQS-----YAlyPhmTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:PRK13639 84 FQNpddqlFA--P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518853886 156 LFDEPLSNLDAklrvvmRGEIKALH-----QKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELY 222
Cdd:PRK13639 160 VLDEPTSGLDP------MGASQIMKllydlNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-236 |
4.68e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.09 E-value: 4.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 14 GAVKTIHGVDLDIRDGEFVVLVGPSGCGKS----TLLRMIAGLETITGGELRIGERIVNdLDPKD------RDIAMVFQS 83
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIGGSATFNGREILN-LPEKElnklraEQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 --YALYPHMTVASN-MGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDR---YPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:PRK09473 106 pmTSLNPYMRVGEQlMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 158 DEPLSNLDaklrVVMRGEIKALHQKLK----TTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGF 233
Cdd:PRK09473 186 DEPTTALD----VTVQAQIMTLLNELKrefnTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGL 261
|
...
gi 518853886 234 IGS 236
Cdd:PRK09473 262 LNA 264
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-166 |
4.86e-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: 90.02 E-value: 4.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 16 VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLetITGGELRIGERIVNDlDPKDRD-----IAMVFQSYALYPHM 90
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR--VEGGGTTSGQILFNG-QPRKPDqfqkcVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 91 TVASNMGFSLEHRGSSKQEIAEKVNWAADI----LGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:cd03234 97 TVRETLTYTAILRLPRKSSDAIRKKRVEDVllrdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
7-225 |
6.31e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.43 E-value: 6.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 7 SDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLdpKDRDIA---MV--F 81
Cdd:PRK11300 9 SGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL--PGHQIArmgVVrtF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 QSYALYPHMTVASNMgFSLEHRGSS-------------KQEIAEKVNWAA---DILGLTPLLDRYPRQLSGGQRQRVAMG 145
Cdd:PRK11300 87 QHVRLFREMTVIENL-LVAQHQQLKtglfsgllktpafRRAESEALDRAAtwlERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 146 RAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-212 |
6.31e-21 |
|
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: 89.24 E-value: 6.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 9 IRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGletITGGELRIgERIV--NDLDPKD------RDIAMV 80
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSV-EGDIhyNGIPYKEfaekypGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPHMTVASNMGFSLEHRGsskqeiaekvnwaadilgltpllDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:cd03233 89 SEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 161 LSNLDAK--LRVVMRgeIKALHQKLKTTTIyVTHDQ--VEAMTMADRVVVLNGGRV 212
Cdd:cd03233 146 TRGLDSStaLEILKC--IRTMADVLKTTTF-VSLYQasDEIYDLFDKVLVLYEGRQ 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-209 |
6.94e-21 |
|
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: 93.70 E-value: 6.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVK-TIHGVDldIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIvndldpkdrdiamvfq 82
Cdd:COG1245 342 VEYPDLTKSYGGFSlEVEGGE--IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKI---------------- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SY------ALYPhMTVASNMGFSLEHR-GSS--KQEIAEKvnwaadiLGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:COG1245 404 SYkpqyisPDYD-GTVEEFLRSANTDDfGSSyyKTEIIKP-------LGLEKLLDKNVKDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 154 VFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDqveaMTM----ADRVVVLNG 209
Cdd:COG1245 476 LYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDRLMVFEG 531
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-209 |
1.47e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 92.56 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVK-TIHGVDldIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIvndldpkdrdiamvfq 82
Cdd:PRK13409 341 VEYPDLTKKLGDFSlEVEGGE--IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKI---------------- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SY------ALYPhMTVASNMGFSLEHRGSS--KQEIAEKvnwaadiLGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:PRK13409 403 SYkpqyikPDYD-GTVEDLLRSITDDLGSSyyKSEIIKP-------LQLERLLDKNVKDLSGGELQRVAIAACLSRDADL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 155 FLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNG 209
Cdd:PRK13409 475 YLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-225 |
1.61e-20 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 89.50 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLD------PKDRDI 77
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyqlseAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 A-----MVFQSYALYPHMTVASN-------MGFSLEHRGSSKqeiAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMG 145
Cdd:TIGR02323 84 MrtewgFVHQNPRDGLRMRVSAGanigerlMAIGARHYGNIR---ATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 146 RAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-216 |
1.95e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.21 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 8 DIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLD------PKDR-----D 76
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseAERRrllrtE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 IAMVFQSYA--LYPHMTVASNMGFSL-----EHRGSSKQEIA---EKVNWAADilgltpLLDRYPRQLSGGQRQRVAMGR 146
Cdd:PRK11701 91 WGFVHQHPRdgLRMQVSAGGNIGERLmavgaRHYGDIRATAGdwlERVEIDAA------RIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518853886 147 AIVRNPQVFLFDEPLSNLD----AKLRVVMRGeikaLHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVG 216
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDvsvqARLLDLLRG----LVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
3.96e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.01 E-value: 3.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLdPKDR----D 76
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW-QTAKimreA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 IAMVFQSYALYPHMTVASNM---GFSlehrgSSKQEIAEKVNWaadILGLTPLLDRYPRQ----LSGGQRQRVAMGRAIV 149
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLamgGFF-----AERDQFQERIKW---VYELFPRLHERRIQragtMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518853886 150 RNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRV--EQVGTPL 219
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVvlEDTGDAL 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-212 |
4.34e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.88 E-value: 4.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDP---KDRDIAMVFQ 82
Cdd:PRK15439 14 ARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNwaadILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:PRK15439 94 EPLLFPNLSVKENILFGLPKRQASMQKMKQLLA----ALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518853886 163 NLDAKLRVVMRGEIKALhQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:PRK15439 170 SLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-235 |
1.46e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 86.76 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 13 YGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGeLRIGERIV--------NDLDPKD--RDIAMVFQ 82
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTfhgknlyaPDVDPVEvrRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPhmtvasnmgfslehrgsskQEIAEKVNWAADILG----LTPLLDRYPRQ-----------------LSGGQRQR 141
Cdd:PRK14243 99 KPNPFP-------------------KSIYDNIAYGARINGykgdMDELVERSLRQaalwdevkdklkqsglsLSGGQQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 142 VAMGRAIVRNPQVFLFDEPLSNLD--AKLRvvmrgeIKALHQKLKT--TTIYVTHDQVEAMTMADRVVVLN------GGR 211
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDpiSTLR------IEELMHELKEqyTIIIVTHNMQQAARVSDMTAFFNveltegGGR 233
|
250 260 270
....*....|....*....|....*....|..
gi 518853886 212 ----VEQVGTPLeLYDRPANQ----FVAGFIG 235
Cdd:PRK14243 234 ygylVEFDRTEK-IFNSPQQQatrdYVSGRFG 264
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-221 |
1.67e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.58 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 13 YGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGEL-----------------RIGERIVNDLDPKDR 75
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaskevarRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 76 DIAMVFqSYALYPHMTVASNMgfslehrgssKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:PRK10253 97 TVQELV-ARGRYPHQPLFTRW----------RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 156 LFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-218 |
1.93e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.05 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 21 GVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLetITG-GELRIGERIVNDLDPKD--RDIAMVFQSYALYPHMTVASNMG 97
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGL--LPGqGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 98 FSLeHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVR-----NP--QVFLFDEPLSNLDAKLRV 170
Cdd:COG4138 92 LHQ-PAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptiNPegQLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518853886 171 VMRGEIKALHQkLKTTTIYVTHDQVEAMTMADRVVVLNGGRV------EQVGTP 218
Cdd:COG4138 171 ALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLvasgetAEVMTP 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-211 |
2.07e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 83.27 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIvndldpkdrdiamvfqs 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 yalyphmtvasnmgfslehrgsskqEIAekvnwaadilgltplldrYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:cd03221 64 -------------------------KIG------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518853886 164 LDAKLRVVMRGEIKalhqKLKTTTIYVTHD-----QVeamtmADRVVVLNGGR 211
Cdd:cd03221 101 LDLESIEALEEALK----EYPGTVILVSHDryfldQV-----ATKIIELEDGK 144
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-221 |
2.24e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.72 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDL---DPKDRDI 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 AMVFQSYALYPHMTVASNMGFSLEHRGS-SKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 157 FDEPLSNLDAkLRVVmrgEIKALHQKLKTTTIYV---THDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:PRK10895 161 LDEPFAGVDP-ISVI---DIKRIIEHLRDSGLGVlitDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-235 |
2.53e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.30 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 34 LVGPSGCGKSTLLRMIAGL-ETITG----GELRIGERIV---NDLDPKDRDIAMVFQSYALYPhMTVASNMGFSL----- 100
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMnDKVSGyrysGDVLLGGRSIfnyRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVrahkl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 101 ----EHRGSSKQEIAEKVNWAAdilgLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEI 176
Cdd:PRK14271 131 vprkEFRGVAQARLTEVGLWDA----VKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518853886 177 KALHQKLktTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPAN----QFVAGFIG 235
Cdd:PRK14271 207 RSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHaetaRYVAGLSG 267
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-222 |
3.41e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.05 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVnDLDPKD-----RDIAMVFQS--YALYPhMT 91
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGlmklrESVGMVFQDpdNQLFS-AS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 92 VASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVV 171
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518853886 172 MRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELY 222
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-218 |
4.41e-19 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 84.47 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLsdiRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKST----LLRMIagleTITGGELRIGERIVNDLDPKD--RD 76
Cdd:cd03244 7 NVSL---RYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlrSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 IAMVFQSYALYPHmTVASNMGFSLEHRGSSKQEIAEKVN----WAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNP 152
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLDPFGEYSDEELWQALERVGlkefVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 153 QVFLFDEPLSNLD----AKLRVVMRGEIKalhqklKTTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTP 218
Cdd:cd03244 159 KILVLDEATASVDpetdALIQKTIREAFK------DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
26-225 |
5.60e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 86.33 E-value: 5.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 26 IRDGEFVVLVGPSGCGKSTLLRMIAGL----ETITGGELRIGERIVNDLDPKDR------DIAMVFQS--YALYPHMTVA 93
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPCYTVG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 94 SNMGFSLE-HRGSSKQEIAEKvnwAADILGLTPL------LDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:PRK11022 110 FQIMEAIKvHQGGNKKTRRQR---AIDLLNQVGIpdpasrLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 167 KLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:PRK11022 187 TIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-217 |
5.69e-19 |
|
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: 87.57 E-value: 5.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLE---TITGGELRIGERIV--NDLDPKDRDIA 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgTWDGEIYWSGSPLKasNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 79 MVFQSYALYPHMTVASN--MGFSLEHRGSskqeiaeKVNWAADILGLTPLL----------DRYPRQLSGGQRQRVAMGR 146
Cdd:TIGR02633 82 IIHQELTLVPELSVAENifLGNEITLPGG-------RMAYNAMYLRAKNLLrelqldadnvTRPVGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518853886 147 AIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRveQVGT 217
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ--HVAT 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-221 |
6.29e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.80 E-value: 6.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLetITGGELRIGERIVN----DLDPKDRDIAMVFQSYALYPHMTVAS 94
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR--SPKGVKGSGSVLLNgmpiDAKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 95 NMGFSLE---HRGSSKQEIAEKVNWAADILGLTPLLD------RYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:TIGR00955 119 HLMFQAHlrmPRRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 166 AklrvVMRGEIKALHQKL--KTTTIYVTHDQ--VEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:TIGR00955 199 S----FMAYSVVQVLKGLaqKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-224 |
6.72e-19 |
|
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: 88.08 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 18 TIHGVDLDIRDGEFVVLVGPSGCGKSTLLR-MIAGLETITGGELRIGErivndldpkdrdIAMVFQSyALYPHMTVASNM 96
Cdd:TIGR00957 653 TLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVHMKGS------------VAYVPQQ-AWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 97 GFSLEHRGSSKQEIAEKVNWAADiLGLTPLLDRYP-----RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL--- 168
Cdd:TIGR00957 720 LFGKALNEKYYQQVLEACALLPD-LEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgkh 798
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 169 ---RVVmrGEIKALHQKlktTTIYVTHDqVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:TIGR00957 799 ifeHVI--GPEGVLKNK---TRILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-192 |
7.28e-19 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 82.59 E-value: 7.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 23 DLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIgerivndldPKDRDIAMVFQSyalyPHMTvasnmgfsleh 102
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR----PYLP----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 103 RGSSKQEIAekvnwaadilgltplldrYP--RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKlrvvMRGEIKALH 180
Cdd:cd03223 77 LGTLREQLI------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE----SEDRLYQLL 134
|
170
....*....|..
gi 518853886 181 QKLKTTTIYVTH 192
Cdd:cd03223 135 KELGITVISVGH 146
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-216 |
8.96e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 87.63 E-value: 8.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGleTITGGELrIGERIVNDLDPKD---RDIAMVF 81
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--RIQGNNF-TGTILANNRKPTKqilKRTGFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 QSYALYPHMTVASNMGF-SLEH--RGSSKQE---IAEKVnwaADILGLTP-----LLDRYPRQLSGGQRQRVAMGRAIVR 150
Cdd:PLN03211 147 QDDILYPHLTVRETLVFcSLLRlpKSLTKQEkilVAESV---ISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLI 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 151 NPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVG 216
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-210 |
1.36e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDR---DIAMV 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYPHMTVASNMGFSlehRGSSKQ----------EIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVR 150
Cdd:PRK09700 86 YQELSVIDELTVLENLYIG---RHLTKKvcgvniidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 151 NPQVFLFDEPLSNLDAK----LRVVM---RGEIKALhqklktttIYVTHDQVEAMTMADRVVVLNGG 210
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKevdyLFLIMnqlRKEGTAI--------VYISHKLAEIRRICDRYTVMKDG 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-233 |
1.60e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 86.99 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 28 DGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGER-IVNDLDPKDRDIAMVFQSYALYPHMTVASNMGFSLEHRGSS 106
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 107 KQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAklrvVMRGEIKALHQKLKT- 185
Cdd:TIGR01257 1035 WEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP----YSRRSIWDLLLKYRSg 1110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518853886 186 -TTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELydrpANQFVAGF 233
Cdd:TIGR01257 1111 rTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-221 |
2.41e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.03 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 2 ANVTLSDIRKSY--GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD-RD-I 77
Cdd:PRK11160 337 VSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 AMVFQSYALYPHmTVASNMGFSLEHRGSSK-QEIAEKVnwaadilGLTPLLDRYP----------RQLSGGQRQRVAMGR 146
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLAAPNASDEAlIEVLQQV-------GLEKLLEDDKglnawlgeggRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 147 AIVRNPQVFLFDEPLSNLDAKlrvvMRGEIKAL---HQKLKtTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAE----TERQILELlaeHAQNK-TVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-224 |
2.42e-18 |
|
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: 81.80 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLE--TITGGELRIGERIVNDLDPKDR---DIAM 79
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYPHMTVAS-----NMGFslehrgsskqeiaekvnwaadilgltplldryprqlSGGQRQRVAMGRAIVRNPQV 154
Cdd:cd03217 82 AFQYPPEIPGVKNADflryvNEGF------------------------------------SGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 155 FLFDEPLSNLDAK-LRVVMRGeIKALHQKlKTTTIYVTH-----DQVEamtmADRVVVLNGGRVEQVGtPLELYDR 224
Cdd:cd03217 126 AILDEPDSGLDIDaLRLVAEV-INKLREE-GKSVLIITHyqrllDYIK----PDRVHVLYDGRIVKSG-DKELALE 194
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-193 |
3.21e-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: 85.49 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY-GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD-RDIAMVF 81
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 82 QSYALYPHMTVASNMGFSLEhrGSSKQEIAekvnWAADILGLTPLLDRYP-----------RQLSGGQRQRVAMGRAIVR 150
Cdd:TIGR02868 415 AQDAHLFDTTVRENLRLARP--DATDEELW----AALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLA 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518853886 151 NPQVFLFDEPLSNLDAK--------LRVVMRGeikalhqklkTTTIYVTHD 193
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAEtadelledLLAALSG----------RTVVLITHH 529
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-217 |
4.14e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.98 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 9 IRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGL--ETITGGELRI-GERIV--NDLDPKDRDIAMVFQS 83
Cdd:PRK13549 11 ITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFeGEELQasNIRDTERAGIAIIHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHMTVASNM--GFSLEHRGsskqeiaeKVNWAADILGLTPLLDRYP---------RQLSGGQRQRVAMGRAIVRNP 152
Cdd:PRK13549 91 LALVKELSVLENIflGNEITPGG--------IMDYDAMYLRAQKLLAQLKldinpatpvGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 153 QVFLFDEPLSNLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRveQVGT 217
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR--HIGT 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-224 |
6.14e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.36 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 7 SDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGE-LRIGErivnDLDPKDR-------DIA 78
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAvLWQGK----PLDYSKRgllalrqQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 79 MVFQSYALYPHMT-VASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:PRK13638 81 TVFQDPEQQIFYTdIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 158 DEPLSNLDAKLRVVMRGEIKALHQKLKTTTIyVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-216 |
7.54e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 85.22 E-value: 7.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRigerivndldpKDRDIAMVFQSyALYPHMTVASNMGF 98
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 99 SLEHRGSSKQEIAEKVNWAADIL----GLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL--RVVM 172
Cdd:PTZ00243 744 FDEEDAARLADAVRVSQLEADLAqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeRVVE 823
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518853886 173 RGEIKALHQKlktTTIYVTHdQVEAMTMADRVVVLNGGRVEQVG 216
Cdd:PTZ00243 824 ECFLGALAGK---TRVLATH-QVHVVPRADYVVALGDGRVEFSG 863
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-209 |
8.90e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.70 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRigerivndLDPKDRdIAMVFQS 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLR-IGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YALYPHM--TVASnmgFSLEHRGSSKQEIA---EKVNWAAdilgltpLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFD 158
Cdd:PRK09544 76 LYLDTTLplTVNR---FLRLRPGTKKEDILpalKRVQAGH-------LIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518853886 159 EPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNG 209
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-241 |
1.02e-17 |
|
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: 81.64 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 27 RDGEFVVLVGPSGCGKSTLLRMIAG------------------LETITGGELRIG-ERIVNDldpkDRDIAMVFQSYALY 87
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdwdeiLDEFRGSELQNYfTKLLEG----DVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 88 PHmTVASNMGFSLEhrgssKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK 167
Cdd:cd03236 100 PK-AVKGKVGELLK-----KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 168 LRVVMRGEIKALHQKLKtTTIYVTHDQVEAMTMADRVVVLNG-GRVEQVGTPLELYDRPANQFVAGFIGSPSMNF 241
Cdd:cd03236 174 QRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLYGePGAYGVVTLPKSVREGINEFLDGYLPTENMRF 247
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-226 |
2.19e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.22 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKS-TLLRMIAGLET----ITGGELRI-GERIVNDLDPKDR-----DIAMVFQS--YA 85
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFhGESLLHASEQTLRgvrgnKIAMIFQEpmVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 86 LYPHMTVASNMGFSLE-HRGSSKQEIAEKVNWAADILGLTPLLDR---YPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:PRK15134 105 LNPLHTLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 162 SNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPA 226
Cdd:PRK15134 185 TALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-220 |
2.78e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.98 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 26 IRDGEFVVLVGPSGCGKSTLLRMIAGLeTITGGELRIGERIVNDLDPKDRD-------------IAM-VFQSYALYphmt 91
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELArhraylsqqqtppFAMpVFQYLTLH---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 92 vasnmgfslEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVR-----NP--QVFLFDEPLSNL 164
Cdd:PRK03695 94 ---------QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 165 DAKLRVVMRGEIKALHQkLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLE 220
Cdd:PRK03695 165 DVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-183 |
4.59e-17 |
|
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: 78.69 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 21 GVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPK-DRDIAMVFQSYALYPHMTVASNMGFS 99
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 100 leHRGSSKQEIAEkvnwAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD----AKLRVVMRGE 175
Cdd:cd03231 98 --HADHSDEQVEE----ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARFAEAMAGH 171
|
170
....*....|....*
gi 518853886 176 -------IKALHQKL 183
Cdd:cd03231 172 carggmvVLTTHQDL 186
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-212 |
6.62e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 81.92 E-value: 6.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDL--DPKdRDI 77
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVARLqqDPP-RNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 78 A-MVF---------QSYAL--YPHMT--VASNMGFSLEHRGSSKQEIAEKVN-WAAD--------ILGLTPllDRYPRQL 134
Cdd:PRK11147 80 EgTVYdfvaegieeQAEYLkrYHDIShlVETDPSEKNLNELAKLQEQLDHHNlWQLEnrinevlaQLGLDP--DAALSSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 135 SGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKlrvvmrgEIKALHQKLKT---TTIYVTHDQVEAMTMADRVVVLNGGR 211
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-------TIEWLEGFLKTfqgSIIFISHDRSFIRNMATRIVDLDRGK 230
|
.
gi 518853886 212 V 212
Cdd:PRK11147 231 L 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-224 |
9.98e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.16 E-value: 9.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSY-GAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMV 80
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYALYpHMTVASNMgfSLEHRGSSKQEIAEkvnwAADILGLTPLLDRYP-----------RQLSGGQRQRVAMGRAIV 149
Cdd:PRK13657 415 FQDAGLF-NRSIEDNI--RVGRPDATDEEMRA----AAERAQAHDFIERKPdgydtvvgergRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 150 RNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQklKTTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-221 |
1.16e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.83 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKSYGAVKTIhgvDLDIRDGEFVVLVGPSGCGKSTllrmIAGLET----ITGGELRIGERIVND--LDPKDRD 76
Cdd:PRK11176 346 NVTFTYPGKEVPALRNI---NFKIPAGKTVALVGRSGSGKST----IANLLTrfydIDEGEILLDGHDLRDytLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 IAMVFQSYALYpHMTVASNMGFSLEHRGSSKQ-EIAEKVNWAADIL-----GLTPLLDRYPRQLSGGQRQRVAMGRAIVR 150
Cdd:PRK11176 419 VALVSQNVHLF-NDTIANNIAYARTEQYSREQiEEAARMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518853886 151 NPQVFLFDEPLSNLDAKLRvvmRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:PRK11176 498 DSPILILDEATSALDTESE---RAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-167 |
1.53e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 20 HGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIvndldPKDRDiamVFQSYALY--------PHM 90
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPI-----RRQRD---EYHQDLLYlghqpgikTEL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 91 TVASNMGFSLEHRGSSKQEIAekvnWAA-DILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK 167
Cdd:PRK13538 90 TALENLRFYQRLHGPGDDEAL----WEAlAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-212 |
3.66e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 11 KSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRDIAMVF------QSY 84
Cdd:COG3845 266 RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 85 ALYPHMTVASNMGFSLEHRGS-------SKQEIAEkvnWAADILG----LTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:COG3845 346 GLVPDMSVAENLILGRYRRPPfsrggflDRKAIRA---FAEELIEefdvRTPGPDTPARSLSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 154 VFLFDEPLSNLDAklrvvmrGEIKALHQKLK------TTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:COG3845 423 LLIAAQPTRGLDV-------GAIEFIHQRLLelrdagAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-210 |
5.86e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 75.83 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 16 VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAG-LETITG----GELRIGERIVNDLDPKDR-DIAMVFQSYALYpH 89
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGkvhwSNKNESEPSFEATRSRNRySVAYAAQKPWLL-N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 90 MTVASNMGFSLEHRGSSKQEIAEKVNWAADIlGLTPLLDRYPR-----QLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:cd03290 93 ATVEENITFGSPFNKQRYKAVTDACSLQPDI-DLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518853886 165 DAKLR-VVMRGEIKALHQKLKTTTIYVTHdQVEAMTMADRVVVLNGG 210
Cdd:cd03290 172 DIHLSdHLMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-221 |
7.68e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 79.01 E-value: 7.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 18 TIHGVDLDIRDGEFVVLVGPSGCGKSTLLR-MIAGLETITGGELRIGERIvndldpkdrdiAMVFQSYALYpHMTVASNM 96
Cdd:PLN03130 632 TLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTV-----------AYVPQVSWIF-NATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 97 GFSLEHRgsskqeiAEKVNWAADILGLTPLLDRYPR-----------QLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:PLN03130 700 LFGSPFD-------PERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 166 AKL-RVVMRGEIK-ALHQKlktTTIYVThDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:PLN03130 773 AHVgRQVFDKCIKdELRGK---TRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-242 |
8.28e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.90 E-value: 8.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 26 IRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDldpkdrdIAMVFQSYALYPHMTVASNMGFSLEH-- 102
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSILTN-------ISDVHQNMGYCPQFDAIDDLLTGREHly 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 103 -----RGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIK 177
Cdd:TIGR01257 2035 lyarlRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 178 ALHQKLKtTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQFVAGF-IGSPSMNFL 242
Cdd:TIGR01257 2115 SIIREGR-AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMkIKSPKDDLL 2179
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-225 |
1.00e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 78.22 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVND--LDPKDRDIAMVFQSYALYPHmTVASNM 96
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqLDSWRSRLAVVSQTPFLFSD-TVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 97 gfSLEHRGSSKQEIAEKVNWAA---DILGL-----TPLLDRyPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAkl 168
Cdd:PRK10789 410 --ALGRPDATQQEIEHVARLASvhdDILRLpqgydTEVGER-GVMLSGGQKQRISIARALLLNAEILILDDALSAVDG-- 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 169 rvvmRGEIKALH---QKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRP 225
Cdd:PRK10789 485 ----RTEHQILHnlrQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
3-212 |
2.15e-15 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 76.92 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLSDIRKSYGAVKTIHG-----VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKDRD 76
Cdd:TIGR01194 337 SIELKDVHMNPKAPEGSEGfalgpIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLdGAAVSADSRDDYRD 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 I-AMVFQSYALYPHMtvasnMGFSLEHRGSSKQ--------EIAEKVnwAADILGLTPLLDryprqLSGGQRQRVAMGRA 147
Cdd:TIGR01194 417 LfSAIFADFHLFDDL-----IGPDEGEHASLDNaqqylqrlEIADKV--KIEDGGFSTTTA-----LSTGQQKRLALICA 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 148 IVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQvEAMTMADRVVVLNGGRV 212
Cdd:TIGR01194 485 WLEDRPILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHDD-QYFELADQIIKLAAGCI 548
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
3-225 |
2.56e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 75.71 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 3 NVTLsDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLE----TITGGELRIGERIVNDLDPKDR--- 75
Cdd:COG4170 8 NLTI-EIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRERrki 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 76 ---DIAMVFQ--SYALYPHMTVASNMGFSL----------EHRGSSKQEIAE---KVNwaadILGLTPLLDRYPRQLSGG 137
Cdd:COG4170 87 igrEIAMIFQepSSCLDPSAKIGDQLIEAIpswtfkgkwwQRFKWRKKRAIEllhRVG----IKDHKDIMNSYPHELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 138 QRQRVAMGRAIVRNPQVFLFDEPLSNLDAK-----LRVVMRgeikaLHQKLKTTTIYVTHDqVEAMT-MADRVVVLNGGR 211
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTtqaqiFRLLAR-----LNQLQGTSILLISHD-LESISqWADTITVLYCGQ 236
|
250
....*....|....
gi 518853886 212 VEQVGTPLELYDRP 225
Cdd:COG4170 237 TVESGPTEQILKSP 250
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-209 |
7.19e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.57 E-value: 7.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDpKDRDIAMVFQSYALYPHMTVASNMGFSLE 101
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLGHLPGLKADLSTLENLHFLCG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 102 HRGSSKQEIAEKvnwAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKlRVVMRGEIKALHQ 181
Cdd:PRK13543 109 LHGRRAKQMPGS---ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLVNRMISAHL 184
|
170 180
....*....|....*....|....*...
gi 518853886 182 KLKTTTIYVTHDQVEAMTMADRVVVLNG 209
Cdd:PRK13543 185 RGGGAALVTTHGAYAAPPVRTRMLTLEA 212
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-226 |
7.55e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.20 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKStlLRMIAGLETITGGELRIGERIVNDLDP------KDRDIAMVFQS--YALYPHM 90
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPvapcalRGRKIATIMQNprSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 91 TVASNMGFSLEHRGssKQEIAEKVNWAADILGLTP---LLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK 167
Cdd:PRK10418 97 TMHTHARETCLALG--KPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 168 LRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPA 226
Cdd:PRK10418 175 AQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-222 |
7.82e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.78 E-value: 7.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 18 TIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGletitggelrigerivnDLDPKDRDIAMVFQSYALYPHM------T 91
Cdd:PLN03232 632 TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVVIRGSVAYVPQVswifnaT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 92 VASNMGFSlehrgsSKQEiAEKVNWAADILGLTPLLDRYPRQ-----------LSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:PLN03232 695 VRENILFG------SDFE-SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518853886 161 LSNLDAKL-RVVMRGEIKalhQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELY 222
Cdd:PLN03232 768 LSALDAHVaHQVFDSCMK---DELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-217 |
1.10e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.14 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTI-HGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPK--DRDIAMV 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQ-----SYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADilGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:PRK10790 421 QQdpvvlADTFLANVTLGRDISEEQVWQALETVQLAELARSLPD--GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518853886 156 LFDEPLSNLDAklrvvmrGEIKALHQKL----KTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGT 217
Cdd:PRK10790 499 ILDEATANIDS-------GTEQAIQQALaavrEHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-283 |
1.47e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.78 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIvndlDPKDRDIAM----VFQSYALYPHMTVASNM 96
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfGQPV----DAGDIATRRrvgyMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 97 G-----FSLEhrgssKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAklrvV 171
Cdd:NF033858 361 ElharlFHLP-----AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP----V 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 172 MRGEIKALHQKL---KTTTIYV-THDQVEAMTmADRVVVLNGGRVEQVGTPLELYD-RPANQFVAGFIGspsmnFLsgtI 246
Cdd:NF033858 432 ARDMFWRLLIELsreDGVTIFIsTHFMNEAER-CDRISLMHAGRVLASDTPAALVAaRGAATLEEAFIA-----YL---E 502
|
250 260 270
....*....|....*....|....*....|....*..
gi 518853886 247 SAGGFETGGVvlPPPATAAGLAGRGAVYGIRPEHFSL 283
Cdd:NF033858 503 EAAGAAAAPA--AAAAPAAAAAAPAAPAPAPRRRFSL 537
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-209 |
2.49e-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: 70.29 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 25 DIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGgelrigerivndldpkdrdiamvfqsyalyphmtvasnmgfslehrg 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNG----------------------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 105 sskqeiaEKVNWAadilGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLK 184
Cdd:cd03222 54 -------DNDEWD----GITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|....*
gi 518853886 185 TTTIYVTHDQVEAMTMADRVVVLNG 209
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-195 |
2.64e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.75 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVNDLDPKDRDIAMVFQSYALYPHMTVASNMG 97
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 98 FSLeHRGSSKQEIAEKVNwaadILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIK 177
Cdd:PRK13540 97 YDI-HFSPGAVGITELCR----LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
170
....*....|....*...
gi 518853886 178 AlHQKLKTTTIYVTHDQV 195
Cdd:PRK13540 172 E-HRAKGGAVLLTSHQDL 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-212 |
3.39e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDR-DIAMVFQSY-----ALYPHMTV 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYISEdrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 93 ASNMGF-SLEH--RGSSKQEIAEKVNWAADILGL----TPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:PRK10762 348 KENMSLtALRYfsRAGGSLKHADEQQAVSDFIRLfnikTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518853886 166 aklrVVMRGEIKALHQKLKT---TTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:PRK10762 428 ----VGAKKEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
8-194 |
3.00e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.51 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 8 DIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLE--TITGGELRIGERIVNDLDPKDRD---IAMVFQ 82
Cdd:CHL00131 12 NLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhlgIFLAFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 syalYP-HMTVASNMGFsLEHRGSSKQ-----------EIAEKVNWAADILGLTP-LLDRYPRQ-LSGGQRQRVAMGRAI 148
Cdd:CHL00131 92 ----YPiEIPGVSNADF-LRLAYNSKRkfqglpeldplEFLEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518853886 149 VRNPQVFLFDEPLSNLDAK-LRVVMRGeIKALHQKlKTTTIYVTHDQ 194
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDaLKIIAEG-INKLMTS-ENSIILITHYQ 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-160 |
4.67e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.15 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GerivNDL-DPKDRD----- 76
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlG----GDMaDARHRRavcpr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 IAMVFQSYA--LYPHMTVASNMGFSLEHRGSSKQEIAEKVnwaADIL---GLTPLLDRYPRQLSGGQRQRVAMGRAIVRN 151
Cdd:NF033858 78 IAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRI---DELLratGLAPFADRPAGKLSGGMKQKLGLCCALIHD 154
|
....*....
gi 518853886 152 PQVFLFDEP 160
Cdd:NF033858 155 PDLLILDEP 163
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-208 |
5.97e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 8 DIRKSygaVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELrigerIVNDL-DPKD-------RDIAM 79
Cdd:PTZ00265 393 DTRKD---VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-----IINDShNLKDinlkwwrSKIGV 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYPHmTVASNMGFSL-------------EHRGSSKQEIAEKVNWA----------------------------- 117
Cdd:PTZ00265 465 VSQDPLLFSN-SIKNNIKYSLyslkdlealsnyyNEDGNDSQENKNKRNSCrakcagdlndmsnttdsneliemrknyqt 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 118 ---ADILGLT----------PLLDRY-------PRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIK 177
Cdd:PTZ00265 544 ikdSEVVDVSkkvlihdfvsALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
|
250 260 270
....*....|....*....|....*....|.
gi 518853886 178 ALHQKLKTTTIYVTHdQVEAMTMADRVVVLN 208
Cdd:PTZ00265 624 NLKGNENRITIIIAH-RLSTIRYANTIFVLS 653
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-213 |
8.00e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 8.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 21 GVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIgerivndldpkdrdiamVFQSYALYPHMTVASNMGfsl 100
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-----------------DVPDNQFGREASLIDAIG--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 101 ehrgsSKQEIAEKVNWAADI-LGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKAL 179
Cdd:COG2401 108 -----RKGDFKDAVELLNAVgLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKL 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 518853886 180 HQKLKTTTIYVT-HDQVEAMTMADRVVVLN-GGRVE 213
Cdd:COG2401 183 ARRAGITLVVAThHYDVIDDLQPDLLIFVGyGGVPE 218
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-229 |
8.99e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.62 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSYALYPHmTVASNM 96
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFSG-TVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 97 GFSLEHRGSSKQEIAEKVNWAADI----LGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVM 172
Cdd:PLN03232 1331 DPFSEHNDADLWEALERAHIKDVIdrnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 173 RgeiKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQF 229
Cdd:PLN03232 1411 Q---RTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
63-221 |
1.66e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.90 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 63 GERIVNDLDPKD---RDIAMVFQSYALYP---HMTVASNMGFSLEHrgSSKQEIAEKVNWAADILGLTPLLDRYP----- 131
Cdd:PTZ00265 1277 GKILLDGVDICDynlKDLRNLFSIVSQEPmlfNMSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDtnvgp 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 132 --RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHdQVEAMTMADRVVVLN- 208
Cdd:PTZ00265 1355 ygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFNn 1433
|
170
....*....|....*..
gi 518853886 209 ----GGRVEQVGTPLEL 221
Cdd:PTZ00265 1434 pdrtGSFVQAHGTHEEL 1450
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-209 |
1.71e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 68.27 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 27 RDGEFVVLVGPSGCGKSTLLRMIAGletitggELR--IGErivNDLDPKDRDIAMVFQSYALYPHMTVASNMGFSLEH-- 102
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSG-------ELKpnLGD---YDEEPSWDEVLKRFRGTELQDYFKKLANGEIKVAHkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 103 ----------RGSSKqEIAEKVN------WAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:COG1245 167 qyvdlipkvfKGTVR-ELLEKVDergkldELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518853886 167 KLRVVMRGEIKALHQKLKTTTIyVTHDQveAM--TMADRVVVLNG 209
Cdd:COG1245 246 YQRLNVARLIRELAEEGKYVLV-VEHDL--AIldYLADYVHILYG 287
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-165 |
1.73e-12 |
|
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: 68.04 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 8 DIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIvndldpkdrDIAMVFQSY-AL 86
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------KLAYVDQSRdAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 87 YPHMTVASNMGFSLEH-------------------RGSSKQeiaEKVNwaadilgltplldryprQLSGGQRQRVAMGRA 147
Cdd:TIGR03719 398 DPNKTVWEEISGGLDIiklgkreipsrayvgrfnfKGSDQQ---KKVG-----------------QLSGGERNRVHLAKT 457
|
170
....*....|....*...
gi 518853886 148 IVRNPQVFLFDEPLSNLD 165
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLD 475
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-211 |
1.86e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.60 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 26 IRDGEFVVLVGPSGCGKSTLLRMIAGleTITGGELRIGERIVNDLDPKDrDIAMVFQSYALY--------PHMTVASNMG 97
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGVITYDGITPE-EIKKHYRGDVVYnaetdvhfPHLTVGETLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 98 FSLEHR-------GSSKQEIAEKV-NWAADILGL-----TPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:TIGR00956 161 FAARCKtpqnrpdGVSREEYAKHIaDVYMATYGLshtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518853886 165 DAKLRVVMRGEIKALHQKLKTT---TIYVTHDqvEAMTMADRVVVLNGGR 211
Cdd:TIGR00956 241 DSATALEFIRALKTSANILDTTplvAIYQCSQ--DAYELFDKVIVLYEGY 288
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-215 |
3.69e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 9 IRKSYGAVKTIhgvDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIV--NDLDPKDRDIAMVFQSY- 84
Cdd:PRK09700 272 TSRDRKKVRDI---SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKDISprSPLDAVKKGMAYITESRr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 85 --ALYPHMTVASNMGFS--LEHRG----------SSKQEIAEKvnwAADILGLT-PLLDRYPRQLSGGQRQRVAMGRAIV 149
Cdd:PRK09700 349 dnGFFPNFSIAQNMAISrsLKDGGykgamglfheVDEQRTAEN---QRELLALKcHSVNQNITELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 150 RNPQVFLFDEPLSNLDaklrVVMRGEIKALHQKLK---TTTIYVTHDQVEAMTMADRVVVLNGGRVEQV 215
Cdd:PRK09700 426 CCPEVIIFDEPTRGID----VGAKAEIYKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-218 |
5.58e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 1 MANVTLSDIRKSYGAVktIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGleTITGGELRIGERIVNDLDPKDRDIAMV 80
Cdd:PRK13547 1 MLTADHLHVARRHRAI--LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGGGAPRGARVTGDVTLNGEPLAAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 --FQSYALYPHMTVASNMGFSLEHR--------------GSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAM 144
Cdd:PRK13547 77 daPRLARLRAVLPQAAQPAFAFSAReivllgrypharraGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 145 GRAI---------VRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQV 215
Cdd:PRK13547 157 ARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
...
gi 518853886 216 GTP 218
Cdd:PRK13547 237 GAP 239
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-218 |
7.20e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 66.36 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTIHG-----VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVndlDPKDRD--- 76
Cdd:COG4615 329 ELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREayr 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 77 --IAMVFQSYALYPHMtvasnMGfsLEHRGSSKQ--------EIAEKVNWAADILGLTplldryprQLSGGQRQRVAMGR 146
Cdd:COG4615 406 qlFSAVFSDFHLFDRL-----LG--LDGEADPARarellerlELDHKVSVEDGRFSTT--------DLSQGQRKRLALLV 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 147 AIVRNPQVFLFDEPLSNLDAKLRVVMRGEI-KALHQKLKtTTIYVTHD----QVeamtmADRVVVLNGGRVEQVGTP 218
Cdd:COG4615 471 ALLEDRPILVFDEWAADQDPEFRRVFYTELlPELKARGK-TVIAISHDdryfDL-----ADRVLKMDYGKLVELTGP 541
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-210 |
7.77e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 7.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRD---IAMVFQ 82
Cdd:PRK10762 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILgLTPL-LDRYPRQLSG----GQRQRVAMGRAIVRNPQVFLF 157
Cdd:PRK10762 87 ELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKL-LARLnLRFSSDKLVGelsiGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 158 DEPLSNL----DAKLRVVMRgEIKALHQKLktttIYVTHDQVEAMTMADRVVVLNGG 210
Cdd:PRK10762 166 DEPTDALtdteTESLFRVIR-ELKSQGRGI----VYISHRLKEIFEICDDVTVFRDG 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-212 |
8.28e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.09 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRI-GERIVND-----------LDPKDRdiamvfQSYALYPH 89
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPIDIRsprdairagimLCPEDR------KAEGIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 90 MTVASNMGFSlEHRGSSK-----QEIAEKVNWAADILGL---TPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:PRK11288 346 HSVADNINIS-ARRHHLRagcliNNRWEAENADRFIRSLnikTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518853886 162 SNLDaklrVVMRGEIKALHQKL---KTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:PRK11288 425 RGID----VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-192 |
8.77e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 66.31 E-value: 8.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIgerivndldPKDRDIAMVFQSyalyPHMTVAS---- 94
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQR----PYMTLGTlrdq 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 95 ----NMGFSLEHRGSSKQEIAEKVnwaaDILGLTPLLDR---------YPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:TIGR00954 535 iiypDSSEDMKRRGLSDKDLEQIL----DNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|.
gi 518853886 162 SnldaKLRVVMRGEIKALHQKLKTTTIYVTH 192
Cdd:TIGR00954 611 S----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-212 |
9.38e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.29 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 21 GVDLDIRDGEFVVLVGPSGCGKSTLLRMIAglETITGGELRIGERIVNDlDPKD----RDIAMVFQSYALYPHMTVASNM 96
Cdd:TIGR00956 781 NVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNG-RPLDssfqRSIGYVQQQDLHLPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 97 GFSLEHRGSSKQEIAEK---VNWAADILGLTPLLDRY---PRQ-LSGGQRQRVAMGRAIVRNPQVFLF-DEPLSNLDAKL 168
Cdd:TIGR00956 858 RFSAYLRQPKSVSKSEKmeyVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQT 937
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518853886 169 R-VVMRgeikaLHQKLKTT--TIYVTHDQVEAMTMA--DRVVVLN-GGRV 212
Cdd:TIGR00956 938 AwSICK-----LMRKLADHgqAILCTIHQPSAILFEefDRLLLLQkGGQT 982
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-246 |
1.41e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.82 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRK-------SYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLET----ITGGELRIGERIVNDLDPKD 74
Cdd:PRK15093 3 LLDIRNltiefktSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 R------DIAMVFQ--SYALYPHMTVASNMGFSLEhRGSSKQEIAEKVNW----AADILGLTPLLDR------YPRQLSG 136
Cdd:PRK15093 83 RrklvghNVSMIFQepQSCLDPSERVGRQLMQNIP-GWTYKGRWWQRFGWrkrrAIELLHRVGIKDHkdamrsFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 137 GQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVG 216
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 518853886 217 TPLELYDRPANQFVAGFI------GSP-----SMNFLSGTI 246
Cdd:PRK15093 242 PSKELVTTPHHPYTQALIraipdfGSAmphksRLNTLPGAI 282
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-212 |
1.65e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDR-DIAMVF-----QSYALYPHMTVASN 95
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 96 --------MGFSLehRGSSKQEIAEKVNWAADILGLTPllDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK 167
Cdd:PRK15439 362 vcalthnrRGFWI--KPARENAVLERYRRALNIKFNHA--EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518853886 168 LRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:PRK15439 438 ARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-193 |
3.07e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.19 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 5 TLSDIRKSYGAVKTI-HGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIV-------NDLDP-KD- 74
Cdd:TIGR03719 6 TMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKvgylpqePQLDPtKTv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 75 --------RDIAMVFQSY-ALYPHMTVASNMGFSLEHRGSSKQEIAEKVN-W--------AADILGLTPLlDRYPRQLSG 136
Cdd:TIGR03719 86 renveegvAEIKDALDRFnEISAKYAEPDADFDKLAAEQAELQEIIDAADaWdldsqleiAMDALRCPPW-DADVTKLSG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 137 GQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKlrvvmrgEIKALHQKLKT---TTIYVTHD 193
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAE-------SVAWLERHLQEypgTVVAVTHD 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
118-241 |
6.38e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 118 ADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQklKTTTIYVTHDQVEA 197
Cdd:PRK13409 197 VERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVL 274
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 518853886 198 MTMADRVVVLNG-----GRVEQV-GTplelydRPA-NQFVAGFIGSPSMNF 241
Cdd:PRK13409 275 DYLADNVHIAYGepgayGVVSKPkGV------RVGiNEYLKGYLPEENMRI 319
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-243 |
6.89e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 62.18 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIvndldpkdrdiAMVFQSYALYPHmTVASNMGFSLE 101
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRI-----------SFSSQFSWIMPG-TIKENIIFGVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 102 HRGSSKQEIAEKVNWAADILGLtPLLDRYPR-----QLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDaklrVVMRGEI 176
Cdd:cd03291 124 YDEYRYKSVVKACQLEEDITKF-PEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD----VFTEKEI 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518853886 177 ------KALHQKlktTTIYVThDQVEAMTMADRVVVLNGGRVEQVGTPLELYD-RPanQFVAGFIGSPSMNFLS 243
Cdd:cd03291 199 fescvcKLMANK---TRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSlRP--DFSSKLMGYDTFDQFS 266
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-216 |
1.60e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLE--TITGGELRIGERIVNDLDPKDR---DIA 78
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 79 MVFQsyalYPHMTVASNMGFSLEH-----RGSSKQEIAEKVNWAADILGLTPLLDRYPRQL--------SGGQRQRVAMG 145
Cdd:PRK09580 82 MAFQ----YPVEIPGVSNQFFLQTalnavRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLtrsvnvgfSGGEKKRNDIL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518853886 146 RAIVRNPQVFLFDEPLSNLDAK-LRVVMRGeIKALHQKlKTTTIYVTHDQ-VEAMTMADRVVVLNGGRVEQVG 216
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDaLKIVADG-VNSLRDG-KRSFIIVTHYQrILDYIKPDYVHVLYQGRIVKSG 228
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-211 |
1.95e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.91 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSYALYPHM------TVA 93
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAVFTDFHLFDQLlgpegkPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 94 SNMGFS-LEHrgsskQEIAEKVNWAADILGLTplldryprQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVM 172
Cdd:PRK10522 422 PALVEKwLER-----LKMAHKLELEDGRISNL--------KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREF 488
|
170 180 190
....*....|....*....|....*....|....*....
gi 518853886 173 RGEIKALHQKLKTTTIYVTHDQvEAMTMADRVVVLNGGR 211
Cdd:PRK10522 489 YQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQ 526
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-209 |
2.55e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.28 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 2 ANVTLSDIRKSYGAVKT-IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKDRdIAMV 80
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTaLRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-VAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 81 FQSYAL---YPHMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQ---LSGGQRQRVAMGRAIVRNPQV 154
Cdd:PRK15056 84 PQSEEVdwsFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQigeLSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 155 FLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIyVTHDQVEAMTMADRVVVLNG 209
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLV-STHNLGSVTEFCDYTVMVKG 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-166 |
2.87e-10 |
|
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: 58.79 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 26 IRDGEFVVLVGPSGCGKSTLLRMIAGLET--ITGGELRIGERivndldPKD----RDIAMVFQSYALYPHMTVASNMGFS 99
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGR------PLDknfqRSTGYVEQQDVHSPNLTVREALRFS 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 100 LEHRGsskqeiaekvnwaadilgltplldryprqLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:cd03232 104 ALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
235-281 |
3.04e-10 |
|
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK transport protein.
Pssm-ID: 465563 [Multi-domain] Cd Length: 53 Bit Score: 55.28 E-value: 3.04e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 518853886 235 GSPSMNFLSGTISAGGF--ETGGVVLPPPATA----AGLAGRGAVYGIRPEHF 281
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLlvLGGGVTLPLPEGQvlalKLYVGKEVILGIRPEHI 53
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-169 |
3.47e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 58.73 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 36 GPSGCGKSTLLRMIAGLETITGGELRIGERIVNdldpkdrDIAMVFQSY-----ALYPHMTVASNMGFSLEHRGSskqei 110
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN-------NIAKPYCTYighnlGLKLEMTVFENLKFWSEIYNS----- 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 518853886 111 AEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLR 169
Cdd:PRK13541 101 AETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-221 |
3.85e-10 |
|
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: 61.46 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIvndldpkdrdiAMVFQSYALYPHmTVASNMGFSLE 101
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRI-----------SFSPQTSWIMPG-TIKDNIIFGLS 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 102 HRGSSKQEIAEKVNWAADIlGLTPLLDRYPR-----QLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDaklrVVMRGEI 176
Cdd:TIGR01271 513 YDEYRYTSVIKACQLEEDI-ALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD----VVTEKEI 587
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518853886 177 --KALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:TIGR01271 588 feSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-218 |
4.22e-10 |
|
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: 58.58 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 17 KTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSYALYPHmTVAS 94
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 95 NMGFSLEHrgsSKQEI--AEKVNWAADilgltplldryprQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL----DAKL 168
Cdd:cd03369 101 NLDPFDEY---SDEEIygALRVSEGGL-------------NLSQGQRQLLCLARALLKRPRVLVLDEATASIdyatDALI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518853886 169 RVVMRGEIKalhqklKTTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTP 218
Cdd:cd03369 165 QKTIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-165 |
5.29e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 8 DIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIvndldpkdrDIAMVFQSY-AL 86
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV---------KLAYVDQSRdAL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 87 YPHMTV-----------------------ASNMGFslehRGSSKQeiaEKVNwaadilgltplldryprQLSGGQRQRVA 143
Cdd:PRK11819 400 DPNKTVweeisggldiikvgnreipsrayVGRFNF----KGGDQQ---KKVG-----------------VLSGGERNRLH 455
|
170 180
....*....|....*....|..
gi 518853886 144 MGRAIVRNPQVFLFDEPLSNLD 165
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-212 |
5.59e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.64 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 21 GVDLDIRdgefVVLVGPSGCGKSTLLRMIAG-LETITGGELR--------IGERIVNDLDPKDRDIAMVFQSYALYPHMT 91
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGeLQPSSGTVFRsakvrmavFSQHHVDGLDLSSNPLLYMMRCFPGVPEQK 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 92 VASNMGfSLEHRGSskqeiaekvnwaadiLGLTPLLdryprQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKlrvv 171
Cdd:PLN03073 607 LRAHLG-SFGVTGN---------------LALQPMY-----TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD---- 661
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518853886 172 mrgEIKALHQKL---KTTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:PLN03073 662 ---AVEALIQGLvlfQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-229 |
1.18e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.79 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 21 GVDLDIRDGEFVVLVGPSGCGKSTLL----RMIagleTITGGELRIGERIVND--LDPKDRDIAMVFQSYALYPHmTVAS 94
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG-TVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 95 NMGFSLEhrgSSKQEIaekvnWAAdiLGLTPLLDRY--------PRQLSG------GQRQRVAMGRAIVRNPQVF-LFDE 159
Cdd:PTZ00243 1403 NVDPFLE---ASSAEV-----WAA--LELVGLRERVasesegidSRVLEGgsnysvGQRQLMCMARALLKKGSGFiLMDE 1472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518853886 160 PLSNLDAKL-RVVMRGEIKALHqklKTTTIYVTHdQVEAMTMADRVVVLNGGRVEQVGTPLELYDRPANQF 229
Cdd:PTZ00243 1473 ATANIDPALdRQIQATVMSAFS---AYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-277 |
1.83e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.21 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCG--KSTLLRMIAGLET--------ITGGELRIGERIVNDLDPK 73
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAgrrpwrf*TWCANRRALRRTIG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 74 DRDIAMVFQSYA-LYphmTVASNMGFSLEHRGSSKQEIAEKvnwaadiLGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNP 152
Cdd:NF000106 94 R*GRRESFSGREnLY---MIGR*LDLSRKDARARADELLER-------FSLTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 153 QVFLFDEPLSNLDAKLRVVMRGEIKALHQKLKT---TTIYVTHDQVEA--MTMADRVVVLNGGRVEQVGTPL---ELYDR 224
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATvllTTQYMEEAEQLAheLTVIDRGRVIADGKVDELKTKVggrTLQIR 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 518853886 225 PANQF-VAGFIGSPSMNFLSGTISAGGFETGGVVLPPPATAAGLAGRGAVYGIR 277
Cdd:NF000106 244 PAHAAeLDRMVGAIAQAGLDGIAGATADHEDGVVNVPIVSDEQLSAVVGMLGER 297
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-197 |
3.07e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 12 SYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLE--------TITGGELRIGERIvndLDPKdRDIAMVFQS 83
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpqgysndlTLFGRRRGSGETI---WDIK-KHIGYVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 84 YAL-YPHMTVASNM---GF----SLEHRGSSKQEIaeKVNWAADILGLTPLLDRYP-RQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:PRK10938 345 LHLdYRVSTSVRNVilsGFfdsiGIYQAVSDRQQK--LAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTL 422
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518853886 155 FLFDEPLSNLDAKLRVVMRGEIKALHQKLKTTTIYVTHDQVEA 197
Cdd:PRK10938 423 LILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-211 |
3.62e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPK---DRDIAMVFQ 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 83 SYALYPHMTVASNM--------GFSLEHRGSSKQEIAekvnwAADILGltplLDRYPRQ----LSGGQRQRVAMGRAIVR 150
Cdd:PRK10982 81 ELNLVLQRSVMDNMwlgryptkGMFVDQDKMYRDTKA-----IFDELD----IDIDPRAkvatLSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 151 NPQVFLFDEPLSNLDAKlrvvmrgEIKALH---QKLKTT---TIYVTHDQVEAMTMADRVVVLNGGR 211
Cdd:PRK10982 152 NAKIVIMDEPTSSLTEK-------EVNHLFtiiRKLKERgcgIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-165 |
4.75e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 29 GEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIvndldpkdrDIAMvFQSY--ALYPHMTVASNMgfslehrGSS 106
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL---------EVAY-FDQHraELDPEKTVMDNL-------AEG 407
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518853886 107 KQEIaeKVN--------WAADILgLTPLLDRYP-RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:PRK11147 408 KQEV--MVNgrprhvlgYLQDFL-FHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-212 |
9.05e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 4 VTLSDIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGEL------RIG-------ERIVNDL 70
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenaNIGyyaqdhaYDFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 71 D----------PKDRDIAmvfqsyalyphmtVASNMGFSLehrgSSKQEIAEKVnwaadilgltplldrypRQLSGGQRQ 140
Cdd:PRK15064 400 TlfdwmsqwrqEGDDEQA-------------VRGTLGRLL----FSQDDIKKSV-----------------KVLSGGEKG 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 141 RVAMGRAIVRNPQVFLFDEPLSNLDaklrvvMRGeIKALHQKLKT---TTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMD------MES-IESLNMALEKyegTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-193 |
1.09e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 34 LVGPSGCGKSTLLRMIAGLETITGGELRIGERIvndldpkdrDIAMVFQSYALYPHMTVASN------------------ 95
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGI---------KVGYLPQEPQLDPEKTVRENveegvaevkaaldrfnei 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 96 -MGFSLEHRGSSK--------QEIAEKVN-W--------AADILGLTPLlDRYPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:PRK11819 109 yAAYAEPDADFDAlaaeqgelQEIIDAADaWdldsqleiAMDALRCPPW-DAKVTKLSGGERRRVALCRLLLEKPDMLLL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518853886 158 DEPLSNLDAklrvvmrgEIKA-LHQKLKT---TTIYVTHD 193
Cdd:PRK11819 188 DEPTNHLDA--------ESVAwLEQFLHDypgTVVAVTHD 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-221 |
1.10e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSYALYPHmTVASNM 96
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGIIPQAPVLFSG-TVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 97 GFSLEHRGSSKQEIAEKVNWAADI----LGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVM 172
Cdd:PLN03130 1334 DPFNEHNDADLWESLERAHLKDVIrrnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALI 1413
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518853886 173 RgeiKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:PLN03130 1414 Q---KTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-221 |
3.19e-08 |
|
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: 55.34 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD--RDIAMVFQSYALYphmtvASNMGFS 99
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrFKITIIPQDPVLF-----SGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 100 LEHRGSSKQEiaeKVNWAADILGLTPLLDRYP-----------RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL 168
Cdd:TIGR00957 1380 LDPFSQYSDE---EVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518853886 169 RVVMRGEIKAlhqKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLEL 221
Cdd:TIGR00957 1457 DNLIQSTIRT---QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-203 |
3.96e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.99 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 29 GEFVVLVGPSGCGKSTLLRMIAGLetitggelrigerivndLDPKDRDIAMVfqsyalyphmtvasnmgfslehrgsskq 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARE-----------------LGPPGGGVIYI---------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 109 eIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEI-----KALHQKL 183
Cdd:smart00382 37 -DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSEK 115
|
170 180
....*....|....*....|
gi 518853886 184 KTTTIYVTHDQVEAMTMADR 203
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLR 135
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-214 |
1.09e-07 |
|
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: 53.76 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 26 IRDGEFVVLVGPSGCGKSTLLRMIAGLETiTGGELRIGERIVNDLDpkdrdIAMVFQSYALYPHMTVASNMGFSLE---H 102
Cdd:TIGR01271 1242 VEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVT-----LQTWRKAFGVIPQKVFIFSGTFRKNldpY 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 103 RGSSKQEIaekvnW-AADILGLTPLLDRYPRQL-----------SGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRV 170
Cdd:TIGR01271 1316 EQWSDEEI-----WkVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQ 1390
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518853886 171 VMRgeiKALHQKLKTTTIYVTHDQVEAMTMADRVVVLNGGRVEQ 214
Cdd:TIGR01271 1391 IIR---KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-212 |
1.91e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 18 TIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIGERIVNDLDPKD---RDIAMVFQ---SYALYPHMT 91
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainHGFALVTEerrSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 92 VA-----SNMGFSLEHRGS-SKQEIAEKVNWAADILGL-TPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:PRK10982 343 IGfnsliSNIRNYKNKVGLlDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518853886 165 DAKLRVVMRGEIKALHQKLKtTTIYVTHDQVEAMTMADRVVVLNGGRV 212
Cdd:PRK10982 423 DVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-211 |
3.02e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 8 DIRKSYGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGL--------ETITGGELRIGERIVndlDPKDRDIAM 79
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyegEILFDGEVCRFKDIR---DSEALGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 80 VFQSYALYPHMTVASNMgFsLEHrgsskqEIAEK--VNWAADILGLTPLLDRY-----PRQLSG----GQRQRVAMGRAI 148
Cdd:NF040905 83 IHQELALIPYLSIAENI-F-LGN------ERAKRgvIDWNETNRRARELLAKVgldesPDTLVTdigvGKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 149 VRNPQVFLFDEPLSNLD----AKLRVVMRgEIKAlhQKLktTTIYVTHDQVEAMTMADRVVVLNGGR 211
Cdd:NF040905 155 SKDVKLLILDEPTAALNeedsAALLDLLL-ELKA--QGI--TSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-213 |
5.73e-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: 50.98 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 16 VKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGL-ETITGGELRIGERIVNDLDPKD---RDIAMVFQS---YALYP 88
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 89 HMTVASNMGFSLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPR------QLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:TIGR02633 353 ILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518853886 163 NLDAKLRVVMRGEIKALHQKlKTTTIYVTHDQVEAMTMADRVVVLNGGRVE 213
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
27-173 |
5.73e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 27 RDGEFVVLVGPSGCGKSTLLRMIAGLETitGGELRIGERIVNDldPKDRDIAMVFQSYALY-----PHMTVASNMGFSLE 101
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRKT--GGYIEGDIRISGF--PKKQETFARISGYCEQndihsPQVTVRESLIYSAF 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 102 HR---GSSKQE----------IAEKVNWAADILGLTPLLDryprqLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK- 167
Cdd:PLN03140 980 LRlpkEVSKEEkmmfvdevmeLVELDNLKDAIVGLPGVTG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARa 1054
|
....*.
gi 518853886 168 LRVVMR 173
Cdd:PLN03140 1055 AAIVMR 1060
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-182 |
8.17e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 6 LSDIRksygavkTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIG-ERIV----------------- 67
Cdd:PRK10938 13 LSDTK-------TLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfSHITrlsfeqlqklvsdewqr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 68 --NDL---DPKD--RDIAMVFQSyalyphmtvasnmgfslehrGSSKQEIAEKVnwaADILGLTPLLDRYPRQLSGGQRQ 140
Cdd:PRK10938 86 nnTDMlspGEDDtgRTTAEIIQD--------------------EVKDPARCEQL---AQQFGITALLDRRFKYLSTGETR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518853886 141 RVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQK 182
Cdd:PRK10938 143 KTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-216 |
1.68e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.66 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRigerivndldpKDRDIAMVFQSYALYPHMTVASNMGFSLE 101
Cdd:PRK13546 43 ISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------RNGEVSVIAISAGLSGQLTGIENIEFKML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 102 HRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKALHQ 181
Cdd:PRK13546 112 CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKE 191
|
170 180 190
....*....|....*....|....*....|....*
gi 518853886 182 KLKtTTIYVTHDQVEAMTMADRVVVLNGGRVEQVG 216
Cdd:PRK13546 192 QNK-TIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-216 |
4.04e-06 |
|
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: 46.55 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLrmiagLETITggelRIGERIVNDLDPKdrdiamvfqsyaLYPHMTVA-SNMG 97
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV-----NEGLY----ASGKARLISFLPK------------FSRNKLIFiDQLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 98 FSLEhrgsskqeiaekvnwaadiLGLTPL-LDRYPRQLSGGQRQRVAMGRAIVRNPQ--VFLFDEPLSNLDAKLRVVMRG 174
Cdd:cd03238 70 FLID-------------------VGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518853886 175 EIKALHQkLKTTTIYVTHDqVEAMTMADRVVVL------NGGRVEQVG 216
Cdd:cd03238 131 VIKGLID-LGNTVILIEHN-LDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
275-341 |
9.27e-06 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 42.99 E-value: 9.27e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518853886 275 GIRPEHFSLDV--SGVPAEIMLVEPLGSETQVTMELGGSRVLGVFRERIGQV---VGDEIRVSPALDCIHLF 341
Cdd:pfam08402 2 AIRPEKIRLAAaaNGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARppaPGDRVGLGWDPEDAHVL 73
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-212 |
3.90e-05 |
|
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: 44.17 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 22 VDLDIRDGEFVVLVGPSGCGKSTLlrmiaGLETI-TGGELRIGERIV----NDLDPKDRD-----------IAMVFQSYA 85
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSL-----AFDTIyAEGQRRYVESLSayarQFLGQMDKPdvdsieglspaIAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 86 LYPHMTVASNMGFSLEHRG-SSKQEIAEKVNWAADIlGLTPL-LDRYPRQLSGGQRQRVAMGRAIVRNPQ--VFLFDEPL 161
Cdd:cd03270 89 RNPRSTVGTVTEIYDYLRLlFARVGIRERLGFLVDV-GLGYLtLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518853886 162 SNLDAKLRVVMRGEIKALhQKLKTTTIYVTHDQvEAMTMADRVVVL------NGGRV 212
Cdd:cd03270 168 IGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHVIDIgpgagvHGGEI 222
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
240-283 |
8.06e-05 |
|
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common architecture comprising two variable hydrophobic transmembrane domains (TMDs) that form the translocation pathway and two conserved hydrophilic ABC-ATPases that hydrolyze ATP. This is the C-terminal regulatory domain found at the ATPase subunit of CysA, a putative sulfate ABC transporter from Alicyclobacillus acidocaldarius. The regulatory domain of CysA is built up of an elongated beta-barrel composed of two beta-sandwiches that form a common hydrophobic core.
Pssm-ID: 465531 [Multi-domain] Cd Length: 43 Bit Score: 39.35 E-value: 8.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 518853886 240 NFLSGTISAGGFETGGVVLPPPAtAAGLAGRGAVYGIRPEHFSL 283
Cdd:pfam17850 1 NLFHGRVEDGRVRIGGLALPLPE-LAGAEGSEVVAYVRPHDLEI 43
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
108-221 |
2.85e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 108 QEIAEKVNWAADiLGLTPL-LDRYPRQLSGGQRQRVAMGRAI------VrnpqVFLFDEPLSNLDAKLRVVMRGEIKALh 180
Cdd:TIGR00630 463 KEIRERLGFLID-VGLDYLsLSRAAGTLSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHQRDNRRLINTLKRL- 536
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 518853886 181 QKLKTTTIYVTHDQvEAMTMADRVVVL------NGGRVEQVGTPLEL 221
Cdd:TIGR00630 537 RDLGNTLIVVEHDE-DTIRAADYVIDIgpgageHGGEVVASGTPEEI 582
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
117-192 |
4.83e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 117 AADIL-GL--TPLLD-RYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDakLRVVMRGEIKALhqKLKTTTIYVTH 192
Cdd:PLN03073 324 AASILaGLsfTPEMQvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWLETYLL--KWPKTFIVVSH 399
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
23-205 |
6.12e-04 |
|
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: 40.04 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 23 DLDIRDGEFVVLVGPSGCGKSTLLRMIAgleTITGGElrigerivndldpkdrdiamvfqsyalyphmtvasnmgFSLEH 102
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDAIG---LALGGA--------------------------------------QSATR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 103 RGSskqEIAEKVNWAADILGLTPLLDryprQLSGGQRQRVA----MGRAIVRNPQVFLFDEPLSNLDAK-----LRVVMR 173
Cdd:cd03227 54 RRS---GVKAGCIVAAVSAELIFTRL----QLSGGEKELSAlaliLALASLKPRPLYILDEIDRGLDPRdgqalAEAILE 126
|
170 180 190
....*....|....*....|....*....|..
gi 518853886 174 geikalHQKLKTTTIYVTHDQvEAMTMADRVV 205
Cdd:cd03227 127 ------HLVKGAQVIVITHLP-ELAELADKLI 151
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-224 |
9.57e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 13 YGAVKTIHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGletitggelrigerivnDLDPKDRDIAMV-------FQSYA 85
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG-----------------ELAPVSGEIGLAkgiklgyFAQHQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 86 LYPHMTVASnmgfSLEHRGS-SKQEIAEKVNwaaDILG--------LTPLLDRYprqlSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:PRK10636 385 LEFLRADES----PLQHLARlAPQELEQKLR---DYLGgfgfqgdkVTEETRRF----SGGEKARLVLALIVWQRPNLLL 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518853886 157 FDEPLSNLDAKLRvvmrgeiKALHQKL---KTTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDR 224
Cdd:PRK10636 454 LDEPTNHLDLDMR-------QALTEALidfEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
29-61 |
1.22e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.69 E-value: 1.22e-03
10 20 30
....*....|....*....|....*....|...
gi 518853886 29 GEFVVLVGPSGCGKSTLLRMIAGLETITGGELR 61
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
133-212 |
1.49e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.30 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 133 QLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDaklrVVMRGEIKALHQKLK---TTTIYVTHDQVEAMTMADRVVVLNG 209
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGID----VGAKYEIYKLINQLVqqgVAIIVISSELPEVLGLSDRVLVMHE 480
|
...
gi 518853886 210 GRV 212
Cdd:PRK13549 481 GKL 483
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
26-50 |
1.84e-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: 39.39 E-value: 1.84e-03
10 20
....*....|....*....|....*.
gi 518853886 26 IRDGE-FVVLVGPSGCGKSTLLRMIA 50
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRRLL 64
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-233 |
2.33e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.87 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 19 IHGVDLDIRDGEFVVLVGPSGCGKSTLLRMIAGLETITGGELRIgerivndldpkDRDIAMVFQSYALYPHMTVASNMGF 98
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-----------KGSAALIAISSGLNGQLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 99 SLEHRGSSKQEIAEKVNWAADILGLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKA 178
Cdd:PRK13545 109 KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNE 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518853886 179 LHQKLKtTTIYVTHDQVEAMTMADRVVVLNGGRVEQVGTPLELYDRpANQFVAGF 233
Cdd:PRK13545 189 FKEQGK-TIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH-YDEFLKKY 241
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
32-49 |
4.25e-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: 4.25e-03
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
122-221 |
6.86e-03 |
|
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: 37.58 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518853886 122 GLTPLLDRYPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRgeiKALHQKLKTTTIYVTHDQVEAMTMA 201
Cdd:cd03288 145 GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQ---KVVMTAFADRTVVTIAHRVSTILDA 221
|
90 100
....*....|....*....|
gi 518853886 202 DRVVVLNGGRVEQVGTPLEL 221
Cdd:cd03288 222 DLVLVLSRGILVECDTPENL 241
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
21-45 |
7.66e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 7.66e-03
10 20
....*....|....*....|....*
gi 518853886 21 GVDLDIRDGEFVVLVGPSGCGKSTL 45
Cdd:COG0178 18 NIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
36-62 |
7.87e-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: 36.31 E-value: 7.87e-03
10 20 30
....*....|....*....|....*....|
gi 518853886 36 GPSGCGKSTLLRMIA---GLETITGGELRI 62
Cdd:cd02020 6 GPAGSGKSTVAKLLAkklGLPYLDTGGIRT 35
|
|
| HprK |
COG1493 |
Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction ... |
18-50 |
8.55e-03 |
|
Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction mechanisms];
Pssm-ID: 441102 [Multi-domain] Cd Length: 142 Bit Score: 36.31 E-value: 8.55e-03
10 20 30
....*....|....*....|....*....|....
gi 518853886 18 TIHGVDLDIrDGEFVVLVGPSGCGKSTL-LRMIA 50
Cdd:COG1493 1 TLHGVLVDV-GGRGVLITGPSGSGKSELaLELIK 33
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
18-46 |
8.62e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.50 E-value: 8.62e-03
10 20
....*....|....*....|....*....
gi 518853886 18 TIHGVDLDIRDGEFVVLVGPSGCGKSTLL 46
Cdd:pfam13555 11 TFDGHTIPIDPRGNTLLTGPSGSGKSTLL 39
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