|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-346 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 605.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 161 LSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGSPAMN 240
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 241 FIKGRLTASGFEADGVVLPLPP---GPATGEAIYGIRPEHFELV---NHGLTANVLLVEPMGSETQVTMMLGNHQVVGVF 314
Cdd:COG3839 241 LLPGTVEGGGVRLGGVRLPLPAalaAAAGGEVTLGIRPEHLRLAdegDGGLEATVEVVEPLGSETLVHVRLGGQELVARV 320
|
330 340 350
....*....|....*....|....*....|..
gi 1654818414 315 RERVQAQPGATIQVQPDLASIHLFDATTSQRL 346
Cdd:COG3839 321 PGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-346 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 558.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSY-GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAM 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 160 PLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGSPAM 239
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 240 NFIKGRLTASG--FE-ADGVVLPLP---PGPATGEAIYGIRPEHFELVNH--GLTANVLLVEPMGSETQVTMMLGNHQVV 311
Cdd:PRK11650 241 NLLDGRVSADGaaFElAGGIALPLGggyRQYAGRKLTLGIRPEHIALSSAegGVPLTVDTVELLGADNLAHGRWGGQPLV 320
|
330 340 350
....*....|....*....|....*....|....*
gi 1654818414 312 GVFRERVQAQPGATIQVQPDLASIHLFDATTSQRL 346
Cdd:PRK11650 321 VRLPHQERPAAGSTLWLHLPANQLHLFDADTGRRI 355
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-340 |
3.60e-155 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 439.15 E-value: 3.60e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 161 LSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGSpaMN 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGE--AN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 241 FIKGRLTASG---FEADGVVLPLP---PGPATGEAIYGIRPEHFELVN----HGLTANVLLVEPMGSETQVTMMLGNHQV 310
Cdd:COG3842 241 LLPGTVLGDEgggVRTGGRTLEVPadaGLAAGGPVTVAIRPEDIRLSPegpeNGLPGTVEDVVFLGSHVRYRVRLGDGQE 320
|
330 340 350
....*....|....*....|....*....|...
gi 1654818414 311 VGVF---RERVQAQPGATIQVQPDLASIHLFDA 340
Cdd:COG3842 321 LVVRvpnRAALPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-346 |
9.23e-155 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 439.08 E-value: 9.23e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 161 LSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGSPAMN 240
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 241 FIKGRLTASgfEADGVVLPLPPG-----PATGEAI-------YGIRPEHF---ELVNHGLTANVLLVEPMGSETQVTMML 305
Cdd:PRK11000 241 FLPVKVTAT--AIEQVQVELPNRqqvwlPVEGRGVqvganmsLGIRPEHLlpsDIADVTLEGEVQVVEQLGNETQIHIQI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1654818414 306 -GNHQVVgVFRER--VQAQPGATIQVQPDLASIHLF--DATTSQRL 346
Cdd:PRK11000 319 pAIRQNL-VYRQNdvVLVEEGATFAIGLPPERCHLFreDGTACRRL 363
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
1.11e-132 |
|
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: 376.98 E-value: 1.11e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQN 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 YALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 164 LDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCG 216
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-337 |
1.31e-125 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 364.08 E-value: 1.31e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVN-EIEPKDRDIAMVFQ 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 163 NLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGspAMNFI 242
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVNVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 243 KGRLTASGFEADGVVLPLPPGPATGEAIYGIRPEHFELVNH-----GLTANVLLVEPMGSETQVTMMLGNHQVVG----V 313
Cdd:COG1118 241 RGRVIGGQLEADGLTLPVAEPLPDGPAVAGVRPHDIEVSREpegenTFPATVARVSELGPEVRVELKLEDGEGQPleaeV 320
|
330 340
....*....|....*....|....*..
gi 1654818414 314 FRERVQA---QPGATIQVQPDLASIHL 337
Cdd:COG1118 321 TKEAWAElglAPGDPVYLRPRPARVFL 347
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-338 |
3.54e-117 |
|
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: 342.79 E-value: 3.54e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQNYA 85
Cdd:TIGR03265 7 IDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 86 LYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:TIGR03265 87 LFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 166 AKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGSpaMNFIKG- 244
Cdd:TIGR03265 167 ARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE--VNWLPGt 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 245 RLTASGFEADGVVLPLPPG---PATGEAIYgIRPEHFEL-----VNHGLTANVLLVEPMGSETQVTMM---LGNHQVVGV 313
Cdd:TIGR03265 245 RGGGSRARVGGLTLACAPGlaqPGASVRLA-VRPEDIRVspagnAANLLLARVEDMEFLGAFYRLRLRlegLPGQALVAD 323
|
330 340
....*....|....*....|....*....
gi 1654818414 314 F----RERVQAQPGATIQVQPDLASIHLF 338
Cdd:TIGR03265 324 VsaseVERLGIRAGQPIWIELPAERLRAF 352
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-235 |
3.72e-112 |
|
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: 325.73 E-value: 3.72e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQN 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 YALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 164 LDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIG 235
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
1.28e-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: 323.32 E-value: 1.28e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQN 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 YALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 164 LDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCG 216
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-235 |
3.55e-104 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 310.73 E-value: 3.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQN 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 YALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 164 LDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIG 235
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG 246
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
4-276 |
1.16e-101 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 303.46 E-value: 1.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFAT----IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNE-----IEPKD 74
Cdd:NF040933 3 VRVENVTKIFKKGKKevvaLDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPPED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 75 RDIAMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:NF040933 83 RNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 155 FLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFI 234
Cdd:NF040933 163 LLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLI 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1654818414 235 GSpaMNFIKGRLTASG-FEADGVVLPLPPGPA-TGEAIYGIRPE 276
Cdd:NF040933 243 GD--INLLEGKVEEEGlVDGNDLKIPLPNPKLeAGEVIIGIRPE 284
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-332 |
7.18e-100 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 298.56 E-value: 7.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQN 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 YALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 164 LDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGSPamNFIK 243
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIFP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 244 GRLTASGFEADGVVLPLPP----GPATGEAIYGIRPEHFELVNHGLTAN---VLLVEPMGSETQVTMMLGNHQVVgvfre 316
Cdd:PRK11432 245 ATLSGDYVDIYGYRLPRPAafafNLPDGECTVGVRPEAITLSEQGEESQrctIKHVAYMGPQYEVTVDWHGQELL----- 319
|
330
....*....|....*.
gi 1654818414 317 rVQAQPGatiQVQPDL 332
Cdd:PRK11432 320 -LQVNAT---QLQPDL 331
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-236 |
2.78e-96 |
|
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: 285.39 E-value: 2.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQN 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 YALYPHMSVARNMAFSLEHRGG----SKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 160 PLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGS 236
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
9-235 |
1.77e-90 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 270.52 E-value: 1.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 9 VKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQNYALYP 88
Cdd:TIGR00968 6 ISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYALFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 89 HMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL 168
Cdd:TIGR00968 86 HLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 169 RVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIG 235
Cdd:TIGR00968 166 RKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-212 |
5.25e-86 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 260.02 E-value: 5.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSY----GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRvvnEIEPKDRD 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK---PVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 77 IAMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 157 FDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNA--GRV 212
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRI 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-236 |
4.76e-85 |
|
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: 260.12 E-value: 4.76e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 34 LVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAER 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 114 VSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHD 193
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1654818414 194 QVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGS 236
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE 203
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-212 |
2.09e-83 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 252.01 E-value: 2.09e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYG----AFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPkdrDIAM 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1654818414 160 PLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNA--GRV 212
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-309 |
8.64e-82 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 252.70 E-value: 8.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 9 VKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQNYALYP 88
Cdd:PRK10851 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 89 HMSVARNMAFSL----EHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:PRK10851 88 HMTVFDNIAFGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 165 DAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGSpaMNFIKG 244
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE--VNRLQG 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 245 RLTASGFEADGVVLPLPPGPA-TGEAIYGIRPEHFELVNHG-----LTANVLLVEPMGSETQVTMM-LGNHQ 309
Cdd:PRK10851 246 TIRGGQFHVGAHRWPLGYTPAyQGPVDLFLRPWEVDISRRTsldspLPVQVLEVSPKGHYWQLVVQpLGWYN 317
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
6-338 |
6.66e-79 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 244.99 E-value: 6.66e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFaTIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQNYA 85
Cdd:NF040840 4 IENLSKDWKEF-KLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 86 LYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:NF040840 83 LFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 166 AKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGspAMNFIKGR 245
Cdd:NF040840 163 VQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG--FENIIEGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 246 LTASG----FEADGVVLPLpPGPATGEAIYGIRPEHFELVNHGLT--------ANVLLVEPMGSETQVTMMLGNHQVVGV 313
Cdd:NF040840 241 AEKGGegtiLDTGNIKIEL-PEEKKGKVRIGIRPEDITISTEKVKtsarnefkGKVEEIEDLGPLVKLTLDVGIILVAFI 319
|
330 340
....*....|....*....|....*...
gi 1654818414 314 FR---ERVQAQPGATIQVQPDLASIHLF 338
Cdd:NF040840 320 TRssfLDLEINEGKEVYASFKASAVHVF 347
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-235 |
9.90e-79 |
|
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: 240.70 E-value: 9.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFaTIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQNYA 85
Cdd:cd03299 3 VENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 86 LYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:cd03299 82 LFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 166 AKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIG 235
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-236 |
2.25e-77 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 239.61 E-value: 2.25e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 5 TLRSVKKSY-GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVF 81
Cdd:COG1125 3 EFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTP--LLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADPPILLMDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 160 PLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGS 236
Cdd:COG1125 163 PFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-260 |
3.11e-76 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 238.97 E-value: 3.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQNYA 85
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 86 LYPHMSVARNMAFSLEHRGGSKTEIAERVswaADILGLTPLLE---RFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRV---NEMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 163 NLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGSpaMNFI 242
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVF 256
|
250 260
....*....|....*....|...
gi 1654818414 243 KGRLTASG-----FEADGVVLPL 260
Cdd:PRK11607 257 EGVLKERQedglvIDSPGLVHPL 279
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-237 |
1.81e-75 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 232.58 E-value: 1.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGA-FATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMV 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTP--LLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 159 EPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGSP 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 |
7.20e-70 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 219.05 E-value: 7.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 7 RSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD------RDIAMV 80
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 161 LSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFI 234
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-211 |
1.67e-69 |
|
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: 215.13 E-value: 1.67e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVN----EIEPKDRDIAM 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYPHMSVARNMAFSLehrggskteiaervswaadilgltpllerfprqlSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 160 PLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGR 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 ... |
20-216 |
3.39e-68 |
|
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: 212.93 E-value: 3.39e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 20 HGVDIDI-ADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNE------IEPKDRDIAMVFQNYALYPHMSV 92
Cdd:cd03297 13 FTLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 93 ARNMAFSLehRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVM 172
Cdd:cd03297 93 RENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654818414 173 RGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCG 216
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-212 |
2.07e-67 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 211.19 E-value: 2.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGA----FATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRD--- 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 77 ---IAMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 154 VFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMtMADKIVVMNAGRV 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-213 |
9.46e-67 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 209.51 E-value: 9.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPV-TLRSVKKSYG----AFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDR 75
Cdd:COG1136 1 MSPLlELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 76 D------IAMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIV 149
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654818414 150 RNPQVFLFDEPLSNLDAKL-RVVMRgEIKGLHQRLGVTTVYVTHDQvEAMTMADKIVVMNAGRVE 213
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTgEEVLE-LLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
8-248 |
1.28e-64 |
|
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: 208.42 E-value: 1.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 8 SVKKSYGAFaTIHgVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIE------PKDRDIAMVF 81
Cdd:COG4148 6 DFRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSArgiflpPHRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYALYPHMSVARNMAFSLEHRGGSKTEIA-ERVswaADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:COG4148 84 QEARLFPHLSVRGNLLYGRKRAPRAERRISfDEV---VELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 161 LSNLDAKLrvvmRGEI----KGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGfiGS 236
Cdd:COG4148 161 LAALDLAR----KAEIlpylERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GE 234
|
250
....*....|..
gi 1654818414 237 PAMNFIKGRLTA 248
Cdd:COG4148 235 EAGSVLEATVAA 246
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-234 |
2.90e-64 |
|
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: 203.67 E-value: 2.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRD-----IA 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrrIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 79 MVFQNYALYPHMSVARNMAFSL-EHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 158 DEPLSNLDAklrvVMRGE----IKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPaNPFVAGF 233
Cdd:COG1127 166 DEPTAGLDP----ITSAVidelIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQF 240
|
.
gi 1654818414 234 I 234
Cdd:COG1127 241 L 241
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-225 |
4.16e-64 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 202.95 E-value: 4.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY-GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMV 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNyalyP-----HMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:COG1122 81 FQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 156 LFDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRP 225
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-228 |
8.58e-64 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 202.53 E-value: 8.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEiEPKD-----RDIA 78
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDinklrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 79 MVFQNYALYPHMSVARNMAFSLEH-RGGSKTEIAERvswAADIL---GLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEER---AMELLervGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 155 FLFDEPLSNLDAKlrvvMRGE----IKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANP 228
Cdd:COG1126 158 MLFDEPTSALDPE----LVGEvldvMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-228 |
1.38e-62 |
|
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: 207.45 E-value: 1.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY-----GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD---- 74
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 75 -RDIAMVFQN--YALYPHMSVARNMAFSLE-HRGGSKTEIAERVSWAADILGLTP-LLERFPRQLSGGQRQRVAMGRAIV 149
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRlHGLLSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 150 RNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANP 228
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-236 |
5.54e-62 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 198.10 E-value: 5.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFAT----IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDI 77
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQNY--ALYPHMSVARNMAFSLEHRGgsKTEIAERVSWAADILGLTP-LLERFPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 155 FLFDEPLSNLDaklrVVMRGEI----KGLHQRLGVTTVYVTHDqVEAMT-MADKIVVMNAGRVEQCGAPLELYDRPANPF 229
Cdd:COG1124 160 LLLDEPTSALD----VSVQAEIlnllKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
....*..
gi 1654818414 230 VAGFIGS 236
Cdd:COG1124 235 TRELLAA 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-233 |
1.16e-61 |
|
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: 196.95 E-value: 1.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD-----RDIA 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 79 MVFQNYALYPHMSVARNMAFSL-EHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 158 DEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELyDRPANPFVAGF 233
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL-RASDDPLVRQF 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-211 |
1.20e-61 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 196.15 E-value: 1.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFAT--IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVF 81
Cdd:cd03225 2 LKNLSFSYPDGARpaLDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNyalyP-HM----SVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:cd03225 82 QN----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1654818414 157 FDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGR 211
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-224 |
3.58e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 195.67 E-value: 3.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISI--SSRVVNEIEPKDRdIAMVF 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgEDVARDPAEVRRR-IGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 162 SNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:COG1131 160 SGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-235 |
1.08e-58 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 189.20 E-value: 1.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 5 TLRSVKKSYGAFA-TIhgvDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQN 83
Cdd:COG3840 3 RLDDLTYRYGDFPlRF---DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 YALYPHMSVARNMAFSLeHRGGSKTEIA-ERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:COG3840 80 NNLFPHLTVAQNIGLGL-RPGLKLTAEQrAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 163 NLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIG 235
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-234 |
1.00e-57 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 186.84 E-value: 1.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDI----AM 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYPHMSVARNMAFSLEH-RGGSKTEiAERVswAADILGLTPLLER---FPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPLRvRGASKEE-AEKQ--ARELLAKVGLAERahhYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 156 LFDEPLSNLDAKLrvvmRGEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAG 232
Cdd:PRK09493 159 LFDEPTSALDPEL----RHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
..
gi 1654818414 233 FI 234
Cdd:PRK09493 235 FL 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-212 |
8.67e-57 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 184.10 E-value: 8.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATI-HGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD-----RDI 77
Cdd:COG2884 2 IRFENVSKRYPGGREAlSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 158 DEPLSNLDAKL-RVVMR--GEIkglhQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:COG2884 162 DEPTGNLDPETsWEIMEllEEI----NRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-238 |
8.16e-56 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 185.28 E-value: 8.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY----GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD----- 74
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 75 RDIAMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 155 FLFDEPLSNLDAK-----LRVvmrgeIKGLHQRLGVTTVYVTHDqveaM----TMADKIVVMNAGRVEQCGAPLELYDRP 225
Cdd:COG1135 162 LLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLDVFANP 232
|
250
....*....|...
gi 1654818414 226 ANPFVAGFIGSPA 238
Cdd:COG1135 233 QSELTRRFLPTVL 245
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-214 |
1.47e-55 |
|
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: 180.78 E-value: 1.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY----GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDR---- 75
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 76 -DIAMVFQNY--ALYPHMSVARNMAFSLE-HRGGSKTEIAERVSWAADI-LGLTP-LLERFPRQLSGGQRQRVAMGRAIV 149
Cdd:cd03257 82 kEIQMVFQDPmsSLNPRMTIGEQIAEPLRiHGKLSKKEARKEAVLLLLVgVGLPEeVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 150 RNPQVFLFDEPLSNLDAKLRV-VMRgEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGR-VEQ 214
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAqILD-LLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKiVEE 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-212 |
3.21e-55 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 179.65 E-value: 3.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVN----EIEPKDRDIAM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYPHMSVARNMAFSL-EHRGGSKTEIAERvswAADILGLTPLLER---FPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEER---ALELLEKVGLADKadaYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 156 LFDEPLSNLDAKlrvvMRGEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:cd03262 158 LFDEPTSALDPE----LVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-226 |
3.97e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 180.64 E-value: 3.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY-GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD-----RDI 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQNYALYPHMSVARN-MAFSLEHRGG--------SKTEIaERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAI 148
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNvLAGRLGRTSTwrsllglfPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 149 VRNPQVFLFDEPLSNLDAKL-RVVMRgEIKGLHQRLGVTTVYVTHdQVE-AMTMADKIVVMNAGRVeqcgapleLYDRPA 226
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTaRQVMD-LLRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDGRV--------VFDGPP 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
1.00e-53 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 176.23 E-value: 1.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYG----AFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD----- 74
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 75 RDIAMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 155 FLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHdQVEAM-TMADKIVVMNAGRVEQCGAPLELYDRP 225
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
1.34e-52 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 181.25 E-value: 1.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPV-TLRSVKKSY--GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL---ETVTSGDISISSRVVNEIEPKD 74
Cdd:COG1123 1 MTPLlEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 75 R--DIAMVFQN--YALYPhMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVR 150
Cdd:COG1123 81 RgrRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 151 NPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPA 226
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-306 |
2.85e-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: 176.46 E-value: 2.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 8 SVKKSYGAFATihGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNE------IEPKDRDIAMVF 81
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYALYPHMSVARNMAFslehrGGSKTEIAER-VSWAA--DILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFD 158
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRY-----GMKRARPSERrISFERviELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 159 EPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAgfiGSPA 238
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA---REDQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 239 MNFIKGR---------LTASGFEADGVVLPLPPGPATGEAIYGIRPEHFELVNHGLTA----NVLLVEPMGSETQVTMML 305
Cdd:TIGR02142 234 GSLIEGVvaehdqhygLTALRLGGGHLWVPENLGPTGARLRLRVPARDVSLALQKPEAtsirNILPARVVEIEDSDIGRV 313
|
.
gi 1654818414 306 G 306
Cdd:TIGR02142 314 G 314
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-212 |
1.24e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.00 E-value: 1.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 5 TLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQ 82
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPhMSVARNMAFSLEHRGGSKTEiaERVSWAADILGLTP-LLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 162 SNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-211 |
5.22e-51 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 168.58 E-value: 5.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY-GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD-----RDI 77
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 158 DEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGR 211
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-221 |
5.94e-51 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 169.84 E-value: 5.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVF 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYALYPHMSVARNMAFS-LEHRGGSKTEIAE---RVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:COG1120 82 QEPPAPFGLTVRELVALGrYPHLGLFGRPSAEdreAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 158 DEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-214 |
3.69e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 167.50 E-value: 3.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVN---EIEPKD-----RDI 77
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAirelrRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQNYALYPHMSVARNMafsLEH----RGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNL---IEApcrvLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 154 VFLFDEPLSNLDAKLRVVMRGEIKGLhQRLGVTTVYVTHDQVEAMTMADKIVVMNAGR-VEQ 214
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHiVEQ 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
1.14e-49 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 166.96 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSYGAFAT----IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRvvnEIEPKDRD 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQpqpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 77 IAMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 157 FDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVM--NAGRV 212
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-224 |
5.12e-49 |
|
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: 164.65 E-value: 5.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 5 TLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDR-DIAMVFQN 83
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 YALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 164 LDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:COG4555 163 LDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-212 |
5.29e-49 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 164.85 E-value: 5.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 3 PVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEpkdRDIAMVFQ 82
Cdd:PRK11247 12 PLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR---EDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPHMSVARNMAFSLehRGGSKTEIAErvswAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:PRK11247 89 DARLLPWKKVIDNVGLGL--KGQWRDAALQ----ALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1654818414 163 NLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
6.20e-49 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 165.30 E-value: 6.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY--GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISissrvVNEIEPKDRD----- 76
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVT-----VDGLDTLDEEnlwei 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 77 ---IAMVFQNyalyPH-----MSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAI 148
Cdd:TIGR04520 76 rkkVGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654818414 149 VRNPQVFLFDEPLSNLDAKLRV-VMRgEIKGLHQRLGVTTVYVTHDQVEAmTMADKIVVMNAGRVEQCGAPLELY 222
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKeVLE-TIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-212 |
2.83e-48 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 161.96 E-value: 2.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETV-----TSGDISISSRVVNEIEPKD----RD 76
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelrRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 77 IAMVFQNYALYPhMSVARNMAFSLEHRG-GSKTEIAERVSWAADILGLTPLLER--FPRQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:cd03260 83 VGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 154 VFLFDEPLSNLDAKLRVVMRGEIKGLHQRlgVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-225 |
5.39e-48 |
|
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: 163.01 E-value: 5.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGA---FAT--IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD---- 74
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpFEKkaLDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 75 -RDIAMVFQnyalYPHM-----SVARNMAFSLEHRGGSKTEIAERVSWAADILGLTP-LLERFPRQLSGGQRQRVAMGRA 147
Cdd:TIGR04521 81 rKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 148 IVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRP 225
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-212 |
1.30e-47 |
|
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: 159.97 E-value: 1.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 23 DIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQNYALYPHMSVARNMAFSLEH 102
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 103 RGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQR 182
Cdd:cd03298 98 GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAE 177
|
170 180 190
....*....|....*....|....*....|
gi 1654818414 183 LGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:cd03298 178 TKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-223 |
3.47e-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: 3.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 5 TLRSVKKSYGA-FATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD-----RDIA 78
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 79 MVFQNYALYPHMSVARNMafsLEHRGGSKTEIAERVSW--AADILGLTPLLER-------FPR--QLSGGQRQRVAMGRA 147
Cdd:cd03256 82 MIFQQFNLIERLSVLENV---LSGRLGRRSTWRSLFGLfpKEEKQRALAALERvglldkaYQRadQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 148 IVRNPQVFLFDEPLSNLDAKL-RVVMRgEIKGLHQRLGVTTVYVTHdQVE-AMTMADKIVVMNAGRVEQCGAPLELYD 223
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASsRQVMD-LLKRINREEGITVIVSLH-QVDlAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-212 |
4.36e-47 |
|
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: 158.73 E-value: 4.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGA-FATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD-----RDI 77
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1654818414 158 DEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-234 |
4.67e-47 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 159.41 E-value: 4.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISIS------SRVVNE--IEPKDRDI 77
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAghqfdfSQKPSEkaIRLLRQKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQNYALYPHMSVARNM-AFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:COG4161 85 GMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 157 FDEPLSNLDAKLRVVMRGEIKGLHQrLGVTTVYVTHDQVEAMTMADKIVVMNAGR-VEQCGAplELYDRPANPFVAGFI 234
Cdd:COG4161 165 FDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRiIEQGDA--SHFTQPQTEAFAHYL 240
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-225 |
5.50e-47 |
|
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: 158.78 E-value: 5.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPkdrDIAMVFQNYALYPHMSVARNMAF 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 99 SLEH--RGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEI 176
Cdd:TIGR01184 78 AVDRvlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1654818414 177 KGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLEL-YDRP 225
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-216 |
7.04e-47 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 158.10 E-value: 7.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 23 DIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQNYALYPHMSVARNMAFSLEH 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 103 RGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQR 182
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 1654818414 183 LGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCG 216
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-248 |
2.36e-46 |
|
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: 159.83 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY----GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLE---TVTSGDISISSRVVNEIEPKD-- 74
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 75 ----RDIAMVFQN-Y-ALYPHMSVARNMAFSLE-HRGGSKTEIAERVSWAADILGLTP---LLERFPRQLSGGQRQRVAM 144
Cdd:COG0444 82 kirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRiHGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 145 GRAIVRNPQVFLFDEPLSNLDaklrVVMRGEI----KGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGR-VEQcGAPL 219
Cdd:COG0444 162 ARALALEPKLLIADEPTTALD----VTIQAQIlnllKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRiVEE-GPVE 236
|
250 260 270
....*....|....*....|....*....|
gi 1654818414 220 ELYDRPANPFVAGFIGS-PAMNFIKGRLTA 248
Cdd:COG0444 237 ELFENPRHPYTRALLSSiPRLDPDGRRLIP 266
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
2.36e-46 |
|
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: 155.25 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEiEPKD--RDIAMVF 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEvkRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYALYPHMSVARNMafslehrggskteiaervswaadilgltpllerfprQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 162 SNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:cd03230 124 SGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-224 |
6.79e-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: 166.16 E-value: 6.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFAT--IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAM 79
Cdd:COG2274 474 IELENVSFRYPGDSPpvLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYpHMSVARNMAFSLEHRggskTEiaERVSWAADILGLTPLLERFP-----------RQLSGGQRQRVAMGRAI 148
Cdd:COG2274 554 VLQDVFLF-SGTIRENITLGDPDA----TD--EEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 149 VRNPQVFLFDEPLSNLDAKL-RVVMRGeIKGLHQrlGVTTVYVTHDqVEAMTMADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:COG2274 627 LRNPRILILDEATSALDAETeAIILEN-LRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-214 |
1.48e-45 |
|
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: 155.28 E-value: 1.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFA---TI-HGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRvvnEIEPKDRD--- 76
Cdd:COG4181 9 IELRGLTKTVGTGAgelTIlKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDEDara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 77 ------IAMVFQNYALYPHMSVARNMAFSLEHRGGSktEIAERvswAADIL---GLTPLLERFPRQLSGGQRQRVAMGRA 147
Cdd:COG4181 86 rlrarhVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARAR---ARALLervGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 148 IVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAmTMADKIVVMNAGRVEQ 214
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-228 |
8.76e-45 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 156.05 E-value: 8.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY----GAF----ATIH---GVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEP 72
Cdd:COG4608 8 LEVRDLKKHFpvrgGLFgrtvGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 73 KD-----RDIAMVFQN-YA-LYPHMSVARNMAFSLE-HRGGSKTEIAERVSWAADILGLTP-LLERFPRQLSGGQRQRVA 143
Cdd:COG4608 88 RElrplrRRMQMVFQDpYAsLNPRMTVGDIIAEPLRiHGLASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 144 MGRAIVRNPQVFLFDEPLSNLDaklrVVMRGEI----KGLHQRLGVTTVYVTHD--QVEAmtMADKIVVMNAGR-VEQcg 216
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALD----VSIQAQVlnllEDLQDELGLTYLFISHDlsVVRH--ISDRVAVMYLGKiVEI-- 239
|
250
....*....|...
gi 1654818414 217 APL-ELYDRPANP 228
Cdd:COG4608 240 APRdELYARPLHP 252
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
2.06e-44 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 150.66 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 5 TLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRdiamvfqny 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 85 alyphmsvARNMAFslehrggskteiaerVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:cd03214 72 --------ARKIAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 165 DAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCG 216
Cdd:cd03214 129 DIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
9-223 |
2.19e-44 |
|
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: 152.45 E-value: 2.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 9 VKKSYG-AFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD-----RDIAMVFQ 82
Cdd:TIGR02315 7 LSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPHMSVARNMafsLEHRGGSKTEIAERVSW--AADILGLTPLLERF---------PRQLSGGQRQRVAMGRAIVRN 151
Cdd:TIGR02315 87 HYNLIERLTVLENV---LHGRLGYKPTWRSLLGRfsEEDKERALSALERVgladkayqrADQLSGGQQQRVAIARALAQQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 152 PQVFLFDEPLSNLDAKL-RVVMRgEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYD 223
Cdd:TIGR02315 164 PDLILADEPIASLDPKTsKQVMD-YLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
19-193 |
4.20e-43 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 148.01 E-value: 4.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAG-LETV--TSGDISISSRVVNEIEPKDRDIAMVFQNYALYPHMSVARN 95
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 MAFSLEHRGGsKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGE 175
Cdd:COG4136 97 LAFALPPTIG-RAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175
|
170
....*....|....*...
gi 1654818414 176 IKGLHQRLGVTTVYVTHD 193
Cdd:COG4136 176 VFEQIRQRGIPALLVTHD 193
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-222 |
6.92e-43 |
|
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: 156.07 E-value: 6.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY-GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMV 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALyPHMSVARNMAFSleHRGGSKTEIAErvswAADILGLTPLLERFP-----------RQLSGGQRQRVAMGRAIV 149
Cdd:COG4988 417 PQNPYL-FAGTIRENLRLG--RPDASDEELEA----ALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 150 RNPQVFLFDEPLSNLDAKL-RVVMRGeIKGLHQrlGVTTVYVTHDQvEAMTMADKIVVMNAGRVEQCGAPLELY 222
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETeAEILQA-LRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-211 |
8.26e-43 |
|
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: 145.47 E-value: 8.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 5 TLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 nyalyphmsvarnmafslehrggskteiaervswaadilgltpllerfprqLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1654818414 163 NLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGR 211
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-222 |
1.49e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 149.04 E-value: 1.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDI----AMVFQ--NYALYPHmSVARN 95
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvGLVFQypEYQLFEE-TIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 MAFSLEHRGGSKTEIAERVSWAADILGLT--PLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMR 173
Cdd:PRK13637 105 IAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEIL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1654818414 174 GEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELY 222
Cdd:PRK13637 185 NKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
2.02e-42 |
|
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: 146.50 E-value: 2.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYG--AFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSR-VVNEIEPKDRDIAMV 80
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 161 LSNLDAKLRVVMRGEIkgLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:cd03263 161 TSGLDPASRRAIWDLI--LEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-221 |
2.68e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 146.65 E-value: 2.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 23 DIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQNYALYPHMSVARNMAFSLeH 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGL-N 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 103 RG--------GSKTEIAERVswaadilGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRG 174
Cdd:PRK10771 98 PGlklnaaqrEKLHAIARQM-------GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1654818414 175 EIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-222 |
4.33e-42 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 147.47 E-value: 4.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 18 TIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNyalyPH-----M 90
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGMVFQN----PDnqfvgA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 91 SVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRV 170
Cdd:PRK13635 98 TVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 171 VMRGEIKGLHQRLGVTTVYVTHDQVEAMTmADKIVVMNAGRVEQCGAPLELY 222
Cdd:PRK13635 178 EVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
4.49e-42 |
|
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: 144.06 E-value: 4.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFAT--IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAM 79
Cdd:cd03228 1 IEFKNVSFSYPGRPKpvLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYpHMSVARNMafslehrggskteiaervswaadilgltpllerfprqLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 160 PLSNLDAKLRVVMRGEIKGLHQrlGVTTVYVTHDqVEAMTMADKIVVMNAGR 211
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-162 |
4.97e-42 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 143.17 E-value: 4.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPHMSVARNM 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 97 AFSLEHRGGSKTEIAERVSWAADILGLTPLLER----FPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-215 |
1.41e-41 |
|
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: 146.10 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 17 ATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD-----RDIAMVFQNY--ALYPH 89
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQDSpsAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 90 MSVARNMAFSLEHRGG-SKTEIAERVSWAADILGLTP-LLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK 167
Cdd:TIGR02769 105 MTVRQIIGEPLRHLTSlDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1654818414 168 LRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGR-VEQC 215
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQiVEEC 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-212 |
1.79e-41 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 144.50 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDI-----SISSRVVNEIepKDRDIAMV 80
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeDITGLPPHEI--ARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYPHMSVARNMAFSLEHRGGS----------KTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVR 150
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 151 NPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-236 |
3.59e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 146.87 E-value: 3.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY----GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD----- 74
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 75 RDIAMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 155 FLFDEPLSNLD-AKLRVVMRgEIKGLHQRLGVTTVYVTH--DQVEAmtMADKIVVMNAGR-VEQcGAPLELYDRPANPFV 230
Cdd:PRK11153 162 LLCDEATSALDpATTRSILE-LLKDINRELGLTIVLITHemDVVKR--ICDRVAVIDAGRlVEQ-GTVSEVFSHPKHPLT 237
|
....*.
gi 1654818414 231 AGFIGS 236
Cdd:PRK11153 238 REFIQS 243
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-236 |
5.67e-41 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 144.17 E-value: 5.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 2 APVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVV-------NEIEPKD 74
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdGELVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 75 RD--------IAMVFQNYALYPHMSVARNMAFSLEH-RGGSKTEIAERvswAADIL---GLTPLLERFPRQLSGGQRQRV 142
Cdd:COG4598 87 RRqlqrirtrLGMVFQSFNLWSHMTVLENVIEAPVHvLGRPKAEAIER---AEALLakvGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 143 AMGRAIVRNPQVFLFDEPLSNLDAKLrVvmrGEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPL 219
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPEL-V---GEVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA 239
|
250
....*....|....*..
gi 1654818414 220 ELYDRPANPFVAGFIGS 236
Cdd:COG4598 240 EVFGNPKSERLRQFLSS 256
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-197 |
6.86e-41 |
|
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: 142.23 E-value: 6.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEI-EPKDRDIAMVFQ 82
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDArEDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPHMSVARNMAFSLEHRGGSKTEiaERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1654818414 163 NLDAKLRVVMRGEIKGlHQRLGVTTVYVTHDQVEA 197
Cdd:COG4133 161 ALDAAGVALLAELIAA-HLARGGAVLLTTHQPLEL 194
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-236 |
1.13e-40 |
|
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: 143.05 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--------- 74
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpadek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 75 ------RDIAMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAE-RVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRA 147
Cdd:TIGR03005 81 hlrqmrNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEkRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 148 IVRNPQVFLFDEPLSNLDAKLrvvmRGEIKGLHQRLG----VTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYD 223
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPEL----VGEVLNVIRRLAsehdLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFR 236
|
250
....*....|...
gi 1654818414 224 RPANPFVAGFIGS 236
Cdd:TIGR03005 237 QPKEERTREFLSK 249
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-220 |
1.32e-40 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 142.87 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDR---DIAMVFQ 82
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlGIARTFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPHMSVARNMAFSLEHRGGSK---------------TEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRA 147
Cdd:COG0411 87 NPRLFPELTVLENVLVAAHARLGRGllaallrlprarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 148 IVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDqVEA-MTMADKIVVMNAGRVEQCGAPLE 220
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD-MDLvMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-233 |
6.10e-40 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 145.18 E-value: 6.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 26 IADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEI------EPKDRDIAMVFQNYALYPHMSVARNMAFS 99
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelrEVRRKKIAMVFQSFALMPHMTVLDNTAFG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 100 LEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGL 179
Cdd:PRK10070 131 MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKL 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 180 HQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGF 233
Cdd:PRK10070 211 QAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-221 |
8.14e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 147.62 E-value: 8.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY-GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMV 80
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYpHMSVARNMAFSLEHRggskTEiaERVSWAADILGLTPLLERFP-----------RQLSGGQRQRVAMGRAIV 149
Cdd:COG1132 420 PQDTFLF-SGTIRENIRYGRPDA----TD--EEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 150 RNPQVFLFDEPLSNLDAK--------LRVVMRgeikglhqrlGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:COG1132 493 KDPPILILDEATSALDTEtealiqeaLERLMK----------GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-235 |
9.64e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 140.66 E-value: 9.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSG-----DISI-SSRVVNE----I 70
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIdTARSLSQqkglI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 71 EPKDRDIAMVFQNYALYPHMSVARN-MAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIV 149
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 150 RNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANP- 228
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPr 239
|
250
....*....|
gi 1654818414 229 ---FVAGFIG 235
Cdd:PRK11264 240 trqFLEKFLL 249
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
2.36e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.45 E-value: 2.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRvvnEIEPKDRDIAMV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYPH--MSVARNMAFSLEHRGG----SKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:COG1121 81 PQRAEVDWDfpITVRDVVLMGRYGRRGlfrrPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 155 FLFDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-255 |
2.48e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 140.25 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 18 TIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNE--IEPKDRDIAMVFQNyalyPH-----M 90
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEenVWDIRHKIGMVFQN----PDnqfvgA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 91 SVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRV 170
Cdd:PRK13650 98 TVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 171 VMRGEIKGLHQRLGVTTVYVTHDqVEAMTMADKIVVMNAGRVEQCGAPLELYDRpANPFVAGFIGSPAMNFIKGRLTASG 250
Cdd:PRK13650 178 ELIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELFSR-GNDLLQLGLDIPFTTSLVQSLRQNG 255
|
....*
gi 1654818414 251 FEADG 255
Cdd:PRK13650 256 YDLPE 260
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-205 |
4.33e-39 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 137.75 E-value: 4.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISI---SSRVVNEIEPKD--RD-IAM 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLngqETPPLNSKKASKfrREkLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1654818414 160 PLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQvEAMTMADKIV 205
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVI 204
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-226 |
1.52e-38 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 137.90 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 14 GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD-----RDIAMVFQNY--AL 86
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSisAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 87 YPHMSVARNMAFSLEHRGG-SKTEIAERVSWAADILGLTP-LLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:PRK10419 103 NPRKTVREIIREPLRHLLSlDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 165 DAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRV--EQCGAPLELYDRPA 226
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDKLTFSSPA 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-228 |
5.71e-38 |
|
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: 142.13 E-value: 5.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 10 KKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETvTSGDISISSRVVNEIEPKD-----RDIAMVFQN- 83
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 YA-LYPHMSVARNMA--FSLEHRGGSKTEIAERVSWAADILGLTP-LLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:COG4172 372 FGsLSPRMTVGQIIAegLRVHGPGLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 160 PLSNLDaklrVVMRGEI----KGLHQRLGVTTVYVTHDQ--VEAmtMADKIVVMNAGR-VEQcGAPLELYDRPANP 228
Cdd:COG4172 452 PTSALD----VSVQAQIldllRDLQREHGLAYLFISHDLavVRA--LAHRVMVMKDGKvVEQ-GPTEQVFDAPQHP 520
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-212 |
6.48e-38 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 135.98 E-value: 6.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 13 YGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVneiEPKDRDIAMVFQNYALYPHMSV 92
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV---EGPGAERGVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 93 ARNMAFSLEHRGGSKteiAERVSWAADIL---GLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLR 169
Cdd:PRK11248 88 QDNVAFGLQLAGVEK---MQRLEIAHQMLkkvGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1654818414 170 VVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVM--NAGRV 212
Cdd:PRK11248 165 EQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRV 209
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
9.79e-38 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 135.21 E-value: 9.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVF 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYAL--------------YPHmsvarnmafsleHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQR--VAMg 145
Cdd:COG4604 82 QENHInsrltvrelvafgrFPY------------SKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRafIAM- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 146 rAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:COG4604 149 -VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-234 |
2.09e-37 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 134.71 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 9 VKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDI----------- 77
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkvadknqlrll 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 ----AMVFQNYALYPHMSVARN-MAFSLEHRGGSKTEIAERVSWAADILGLTPLLE-RFPRQLSGGQRQRVAMGRAIVRN 151
Cdd:PRK10619 91 rtrlTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 152 PQVFLFDEPLSNLDAKLrvvmRGEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANP 228
Cdd:PRK10619 171 PEVLLFDEPTSALDPEL----VGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSP 246
|
....*.
gi 1654818414 229 FVAGFI 234
Cdd:PRK10619 247 RLQQFL 252
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-221 |
3.00e-37 |
|
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: 133.33 E-value: 3.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 5 TLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDR---DIAMVF 81
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYALYPHMSVARN--MAFSLEHRGGSKTEIAErvswaadILGLTPLLERFPRQ----LSGGQRQRVAMGRAIVRNPQVF 155
Cdd:cd03224 82 EGRRIFPELTVEENllLGAYARRRAKRKARLER-------VYELFPRLKERRKQlagtLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 156 LFDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-226 |
3.02e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 132.45 E-value: 3.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGA---FAT--IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVV-NEIEPKD--- 74
Cdd:PRK13634 3 ITFQKVEHRYQYktpFERraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKlkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 75 --RDIAMVFQnyalYP-HM----SVARNMAFSLEHRGGSKTEIAERVSWAADILGLTP-LLERFPRQLSGGQRQRVAMGR 146
Cdd:PRK13634 83 lrKKVGIVFQ----FPeHQlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 147 AIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPA 226
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
7-212 |
6.06e-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: 129.78 E-value: 6.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 7 RSVKKSY--GAFATI--HGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDI-----SISSRVVNEI-EPKDRD 76
Cdd:TIGR02211 5 ENLGKRYqeGKLDTRvlKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVlfngqSLSKLSSNERaKLRNKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 77 IAMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERvswAADIL---GLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:TIGR02211 85 LGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKER---AYEMLekvGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 154 VFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMaDKIVVMNAGRV 212
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-212 |
6.55e-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: 129.80 E-value: 6.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGA----FATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISS-RVVNEIEPKDRDIA 78
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 79 MVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFD 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 159 EPLSNLDAKLRVVMRGEIKGLhQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-220 |
9.46e-36 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 132.69 E-value: 9.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 36 GPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIE------PKDRDIAMVFQNYALYPHMSVARNMafslehRGGSKTE 109
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclpPEKRRIGYVFQDARLFPHYKVRGNL------RYGMAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 110 IAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA-KLRVVMrGEIKGLHQRLGVTTV 188
Cdd:PRK11144 105 MVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLpRKRELL-PYLERLAREINIPIL 183
|
170 180 190
....*....|....*....|....*....|..
gi 1654818414 189 YVTHDQVEAMTMADKIVVMNAGRVEQCGaPLE 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 ... |
4-212 |
1.52e-35 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 126.77 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD---RDIAMV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQnyalyphmsvarnmafslehrggskteiaervswaadilgltpllerfprqLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 161 LSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-221 |
3.88e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.96 E-value: 3.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISI-----SSRVVNEIEPKdrdIAMVFQNyalyPH-----MS 91
Cdd:PRK13632 28 VSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitiSKENLKEIRKK---IGIIFQN----PDnqfigAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 92 VARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVV 171
Cdd:PRK13632 101 VEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKRE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1654818414 172 MRGEIKGLHQRLGVTTVYVTHDQVEAmTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:PRK13632 181 IKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-226 |
5.06e-35 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 134.12 E-value: 5.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYpHMSVARNM 96
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQRPHLF-DTTLRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 97 AFSlehRGGSkTEiaERVSWAADILGLTPLLERFP-----------RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:COG4987 430 RLA---RPDA-TD--EELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLD 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 166 AKL-RVVMRGEIKGLHQRlgvTTVYVTHDQVeAMTMADKIVVMNAGRVEQCGAPLELYDRPA 226
Cdd:COG4987 504 AATeQALLADLLEALAGR---TVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-229 |
1.21e-34 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 129.44 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 3 PVTLRSVKksygafatihGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDR-----DI 77
Cdd:PRK15079 31 PKTLKAVD----------GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQN--YALYPHMSVARNMAFSLE--HRGGSKTEIAERVSWAADILGLTP-LLERFPRQLSGGQRQRVAMGRAIVRNP 152
Cdd:PRK15079 101 QMIFQDplASLNPRMTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 153 QVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPF 229
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPY 257
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-212 |
7.53e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 124.22 E-value: 7.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY-GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISIS----SRVVN-EIEPKDRDI 77
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghdiTRLKNrEVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 158 DEPLSNLDAKLRvvmRGEIKGLHQ--RLGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:PRK10908 162 DEPTGNLDDALS---EGILRLFEEfnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-208 |
8.65e-34 |
|
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: 123.80 E-value: 8.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 12 SYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRvvnEIEPKDRDIAMVFQNYAL---YP 88
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRRSIdrdFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 89 hMSVARNMAFSLEHRGG-----SKTEiAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:cd03235 85 -ISVRDVVLMGLYGHKGlfrrlSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1654818414 164 LDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMN 208
Cdd:cd03235 163 VDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-212 |
6.41e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.44 E-value: 6.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD-RD--IAMV 80
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAagIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYPHMSVARNMAFSLE-HRGGskteiaeRVSWAADILGLTPLLERF-----PRQ----LSGGQRQRVAMGRAIVR 150
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGREpRRGG-------LIDWRAMRRRARELLARLgldidPDTpvgdLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 151 NPQVFLFDEPLSNLDAK-----LRVVMRgeikgLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:COG1129 158 DARVLILDEPTASLTEReverlFRIIRR-----LKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-226 |
7.87e-33 |
|
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: 122.01 E-value: 7.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 5 TLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDR---DIAMVF 81
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYALYPHMSVARNMAFSLEHRGGsKTEIAERVswaADILGLTPLLERFPRQ----LSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:COG0410 85 EGRRIFPSLTVEENLLLGAYARRD-RAEVRADL---ERVYELFPRLKERRRQragtLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 158 DEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPA 226
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-212 |
9.45e-33 |
|
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: 121.23 E-value: 9.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 9 VKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVnEIEPKDRdIAMVFQNYALYP 88
Cdd:cd03269 6 VTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNR-IGYLPEERGLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 89 HMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL 168
Cdd:cd03269 84 KMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1654818414 169 RVVMRGEIKGLhQRLGVTTVYVTH--DQVEAmtMADKIVVMNAGRV 212
Cdd:cd03269 164 VELLKDVIREL-ARAGKTVILSTHqmELVEE--LCDRVLLLNKGRA 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-221 |
2.78e-32 |
|
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: 120.17 E-value: 2.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 9 VKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSR-VVNEIEPKDRDIAMVFQNYALY 87
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdVVREPREVRRRIGIVFQDLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 88 PHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK 167
Cdd:cd03265 86 DELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 168 LRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:cd03265 166 TRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-234 |
5.99e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 120.14 E-value: 5.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 13 YGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLR-------MIAGLEtvTSGDI-----SISSRVVNEIEPKdRDIAMV 80
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEIlldgeDIYDPDVDVVELR-RRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYPhMSVARNMAFSLEHRGG-SKTEIAERVSWA----------ADILGlTPLLErfprqLSGGQRQRVAMGRAIV 149
Cdd:COG1117 98 FQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESlrkaalwdevKDRLK-KSALG-----LSGGQQQRLCIARALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 150 RNPQVFLFDEPLSNLD--AKLRVvmrgE--IKGLHQRlgVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRP 225
Cdd:COG1117 171 VEPEVLLMDEPTSALDpiSTAKI----EelILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244
|
....*....
gi 1654818414 226 ANPFVAGFI 234
Cdd:COG1117 245 KDKRTEDYI 253
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-207 |
7.89e-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: 125.09 E-value: 7.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 3 PVTLRSVKKSY-GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAM 79
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYPHmSVARNMAFSLehRGGSKTEIAErvswAADILGLTPLLERFP-----------RQLSGGQRQRVAMGRAI 148
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR--PDASDAEIRE----ALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 149 VRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQrlGVTTVYVTHDqVEAMTMADKIVVM 207
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-235 |
8.57e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 119.95 E-value: 8.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 13 YGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL-----ETVTSGDISISSRV-----VNEIEPKdRDIAMVFQ 82
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNiyspdVDPIEVR-REVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPHMSVARNMAFSLEHRG--GSKTEIAERVSWAADILGL----TPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 157 FDEPLSNLDAklrvVMRGEIKGLHQRLG--VTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANP----FV 230
Cdd:PRK14267 173 MDEPTANIDP----VGTAKIEELLFELKkeYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHEltekYV 248
|
....*
gi 1654818414 231 AGFIG 235
Cdd:PRK14267 249 TGALG 253
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-212 |
9.41e-32 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 118.47 E-value: 9.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQN 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 YALYPHMSVARNMAFSLEHRGGSKTEIAErvswAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1654818414 164 LDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-212 |
1.09e-31 |
|
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: 118.46 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGA--FATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAM 79
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYpHMSVARNMAFSlehrGGSKTEiaERVSWAADILGLTPLLERFP-----------RQLSGGQRQRVAMGRAI 148
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLG----APLADD--ERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 149 VRNPQVFLFDEPLSNLDaklrvvMRGEIKgLHQRL-----GVTTVYVTHDQVeAMTMADKIVVMNAGRV 212
Cdd:cd03245 156 LNDPPILLLDEPTSAMD------MNSEER-LKERLrqllgDKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-224 |
1.71e-31 |
|
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: 118.49 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYG--AFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAM 79
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYpHMSVARNMAFslehrgGSKTEIAERVSWAADILGLTPLLERFPR-----------QLSGGQRQRVAMGRAI 148
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAY------GRPGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 149 VRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQrlGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-225 |
8.24e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.94 E-value: 8.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL-----ETVTSGDISISSRVVNEIEPKD- 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 75 -RDIAMVFQNYALYPHMSVARNMAFSLE--HRGGSKTEIAERVSWAADILGL----TPLLERFPRQLSGGQRQRVAMGRA 147
Cdd:PRK14247 81 rRRVQMVFQIPNPIPNLSIFENVALGLKlnRLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 148 IVRNPQVFLFDEPLSNLD----AKLRVVMrgeikgLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYD 223
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDpentAKIESLF------LELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
..
gi 1654818414 224 RP 225
Cdd:PRK14247 235 NP 236
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
17-212 |
9.27e-31 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 123.05 E-value: 9.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 17 ATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYpHMSVAR 94
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTLRD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 95 NMAfsLEHRGGSKTEIAErvswAADILGLTPLLERFP-----------RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:TIGR03375 558 NIA--LGAPYADDEEILR----AAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILLLDEPTSA 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 164 LDaklrvvMRGE---IKGLHQRL-GVTTVYVTHdQVEAMTMADKIVVMNAGRV 212
Cdd:TIGR03375 632 MD------NRSEerfKDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-212 |
1.27e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 115.43 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 21 GVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEpKDRDIAMVFQN--YALYPHmSVARNMAF 98
Cdd:cd03226 18 DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-RRKSIGYVMQDvdYQLFTD-SVREELLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 99 SLEHRGGSKTEIAErvswAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKG 178
Cdd:cd03226 96 GLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRE 171
|
170 180 190
....*....|....*....|....*....|....
gi 1654818414 179 LhQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:cd03226 172 L-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-216 |
1.44e-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: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVvLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRD-IAMVFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 163 NLDAKLRVVMRGEIKGLHQrlGVTTVYVTH--DQVEAmtMADKIVVMNAGRVEQCG 216
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHivEDVES--LCNQVAVLNKGKLVFEG 211
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-229 |
1.71e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 118.14 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPV-TLRSVKKSY----GAF---ATIH---GVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVV-- 67
Cdd:PRK11308 2 QQPLlQAIDLKKHYpvkrGLFkpeRLVKaldGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 68 -NEIEPKD--RDIAMVFQN-YA-LYPHMSVARNMAFSLE-HRGGSKTEIAERVSWAADILGLTP-LLERFPRQLSGGQRQ 140
Cdd:PRK11308 82 aDPEAQKLlrQKIQIVFQNpYGsLNPRKKVGQILEEPLLiNTSLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 141 RVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLE 220
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241
|
....*....
gi 1654818414 221 LYDRPANPF 229
Cdd:PRK11308 242 IFNNPRHPY 250
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-224 |
2.17e-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: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGA-FATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMV 80
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYpHMSVARNMAFslehrgGSKTEIAERVSWAADILGLTPLLERFPRQ-----------LSGGQRQRVAMGRAIV 149
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRY------GRPDATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 150 RNPQVFLFDEPLSNLDA-KLRVVMRGEIKGLHQRlgvTTVYVTHDQVEAMTmADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:cd03253 154 KNPPILLLDEATSALDThTEREIQAALRDVSKGR---TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-207 |
5.64e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 113.10 E-value: 5.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 12 SYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSrvvneiepkDRDIAMVFQNYALYPHM- 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 91 -SVARNMAFSL-EHRGGSKTEIAE---RVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:NF040873 72 lTVRDLVAMGRwARRGLWRRLTRDdraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1654818414 166 AKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTmADKIVVM 207
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-223 |
7.76e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.85 E-value: 7.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 18 TIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNyalyPH-----M 90
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQN----PDnqfvgS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 91 SVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRV 170
Cdd:PRK13648 100 IVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 171 VMRGEIKGLHQRLGVTTVYVTHDQVEAMTmADKIVVMNAGRVEQCGAPLELYD 223
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-227 |
8.28e-30 |
|
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: 114.00 E-value: 8.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL----ETVTSGDISISSRVVNEIEPKDRDIAMVFQN--YALYPHMSV 92
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 93 ARNMAFSLEHRGGSKTEIAERVSWAADILGLTP---LLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLR 169
Cdd:TIGR02770 82 GNHAIETLRSLGKLSKQARALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 170 VVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPAN 227
Cdd:TIGR02770 162 ARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-212 |
8.48e-30 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 111.92 E-value: 8.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPhmsvarnm 96
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLPQDDELFS-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 97 afslehrgGSkteIAERVswaadilgltpllerfprqLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEI 176
Cdd:cd03246 90 --------GS---IAENI-------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 1654818414 177 KGLHQRlGVTTVYVTHdQVEAMTMADKIVVMNAGRV 212
Cdd:cd03246 140 AALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-212 |
1.07e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.59 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAP-VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD-RD-- 76
Cdd:COG3845 2 MPPaLELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIAlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 77 IAMVFQNYALYPHMSVARNMAFSLEHRGG---SKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLEPTKGgrlDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 154 VFLFDEPLSNLD----AKLRVVMRgeikglhqRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:COG3845 162 ILILDEPTAVLTpqeaDELFEILR--------RLaaeGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-228 |
1.17e-29 |
|
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: 119.02 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 14 GAFATIHGVDIDIADGEFVVLVGPSGCGKS----TLLRMIAGLETVTSGDISISSRVVNEIEPKD------RDIAMVFQN 83
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 --YALYPHMSVARNMAFSLE-HRGGSKTEIAERvswAADILGLTPL------LERFPRQLSGGQRQRV--AMgrAIVRNP 152
Cdd:COG4172 101 pmTSLNPLHTIGKQIAEVLRlHRGLSGAAARAR---ALELLERVGIpdperrLDAYPHQLSGGQRQRVmiAM--ALANEP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 153 QVFLFDEPLSNLDaklrVVMRGEI----KGLHQRLGVTTVYVTHDqveaMT----MADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:COG4172 176 DLLIADEPTTALD----VTVQAQIldllKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQGPTAELFAA 247
|
....
gi 1654818414 225 PANP 228
Cdd:COG4172 248 PQHP 251
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-224 |
3.07e-29 |
|
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: 112.32 E-value: 3.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 18 TIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPHmSVARN 95
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 MAFslehrgGSKTEIAERVSWAADILGLTPLLERFPR-----------QLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:cd03254 97 IRL------GRPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 165 DAKLRVVMRGEIKGLHQrlGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:cd03254 171 DTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-270 |
3.41e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.05 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRvvnEIEPKDRD-IAmvfq 82
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE---PLDPEDRRrIG---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 nY-----ALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:COG4152 75 -YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 158 DEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTH--DQVEAmtMADKIVVMNAGRVEQCGAPLELYDR-PANPFVAGFI 234
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHqmELVEE--LCDRIVIINKGRKVLSGSVDEIRRQfGRNTLRLEAD 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 1654818414 235 GSPAMNFIKGRLTASGFEADGVVLPLPPGpATGEAI 270
Cdd:COG4152 231 GDAGWLRALPGVTVVEEDGDGAELKLEDG-ADAQEL 265
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-211 |
5.01e-29 |
|
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: 111.02 E-value: 5.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRvvneiepkdrdIAMVFQN 83
Cdd:cd03250 6 ASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 yALYPHMSVARNMAFSLEHR---------------------GGSKTEIAERvswaadilGLTpllerfprqLSGGQRQRV 142
Cdd:cd03250 75 -PWIQNGTIRENILFGKPFDeeryekvikacalepdleilpDGDLTEIGEK--------GIN---------LSGGQKQRI 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 143 AMGRAIVRNPQVFLFDEPLSNLDAKL-RVVMRGEIKGlHQRLGVTTVYVTHdQVEAMTMADKIVVMNAGR 211
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVgRHIFENCILG-LLLNNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-250 |
7.65e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.90 E-value: 7.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVN------EIEPKDRDIAMVFQnyalYPHM----- 90
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQ----FPESqlfee 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 91 SVARNMAFSLEHRGGSKTEIAERVSWAADILGLTP-LLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLR 169
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 170 VVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYdRPANPFVAGFIGSPAMNFIKGRLTAS 249
Cdd:PRK13643 181 IEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF-QEVDFLKAHELGVPKATHFADQLQKT 258
|
.
gi 1654818414 250 G 250
Cdd:PRK13643 259 G 259
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-222 |
9.07e-29 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 111.09 E-value: 9.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 21 GVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPhMSVARNMAF 98
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 99 SLEHRGGSKTEIAERVSWAAD-ILGL-----TPLLERfPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVM 172
Cdd:cd03249 100 GKPDATDEEVEEAAKKANIHDfIMSLpdgydTLVGER-GSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLV 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1654818414 173 RGEIKGLhqRLGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAPLELY 222
Cdd:cd03249 179 QEALDRA--MKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-224 |
9.97e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.14 E-value: 9.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 21 GVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNyalyPH-----MSVA 93
Cdd:PRK13647 23 GLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGLVFQD----PDdqvfsSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 94 RNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMR 173
Cdd:PRK13647 99 DDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 174 GEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:PRK13647 179 EILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
12-220 |
1.49e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 111.26 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 12 SYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPH 89
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHLTPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 90 MSVARNMAFS----LEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:PRK11231 91 ITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 166 AKLRVvmrgEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLE 220
Cdd:PRK11231 171 INHQV----ELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-230 |
2.59e-28 |
|
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: 109.94 E-value: 2.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDR---DIAMV 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 161 LSNLDAKlrVVmrGEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYdrpANPFV 230
Cdd:cd03218 161 FAGVDPI--AV--QDIQKIIKILkdrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA---ANELV 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-216 |
3.92e-28 |
|
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: 114.75 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 18 TIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPHmSVARN 95
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 MAfslehRGGSKTEiAERVSWAADILGLTPLLERFPR-----------QLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:TIGR01842 412 IA-----RFGENAD-PEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 165 DAKLRVVMRGEIKGLHQRlGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCG 216
Cdd:TIGR01842 486 DEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFG 535
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-214 |
4.66e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 109.13 E-value: 4.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEI------EPKDRDIAMVFQNYALYPHMSV 92
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaELRNQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 93 ARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVM 172
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1654818414 173 RGEIKGLHQRLGVTTVYVTHDQVEAMTMaDKIVVMNAGRVEQ 214
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
18-225 |
8.91e-28 |
|
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: 114.28 E-value: 8.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 18 TIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVN--EIEPKDRDIAMVFQNYALYPHmSVARN 95
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLGVVLQNGRLMSG-SIFEN 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 MAfslehrGGSKT------EIAERVSWAADI----LGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:TIGR03797 547 IA------GGAPLtldeawEAARMAGLAEDIrampMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 166 AKLRVVMRGEIKglhqRLGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAPLELYDRP 225
Cdd:TIGR03797 621 NRTQAIVSESLE----RLKVTRIVIAH-RLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-212 |
1.02e-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: 107.25 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSvKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETV--TSGDISISSRVVNEIEPKDRdIAMVF 81
Cdd:cd03213 11 VTVKS-SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKI-IGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYALYPHMSVARNMAFSLEHRGgskteiaervswaadilgltpllerfprqLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:cd03213 89 QDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 162 SNLDAKL-RVVMRgEIKGLHQrLGVTTVYVTHD-QVEAMTMADKIVVMNAGRV 212
Cdd:cd03213 140 SGLDSSSaLQVMS-LLRRLAD-TGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-212 |
1.09e-27 |
|
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: 108.00 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 5 TLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDR---DIAMVF 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYALYPHMSVARNMAFSLEHRGGSKTEIAErvswaaDILGLTPLLERF-PRQ---LSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPD------EIYELFPVLKEMlGRRggdLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1654818414 158 DEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-220 |
2.83e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.89 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALyphmsvarNM 96
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSL--------AF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 97 AFS--------LEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAI------VRNPQVFLF-DEPL 161
Cdd:COG4559 89 PFTveevvalgRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPRWLFlDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 162 SNLD-----AKLRVVmrgeiKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLE 220
Cdd:COG4559 169 SALDlahqhAVLRLA-----RQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-217 |
3.62e-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: 3.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 17 ATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPHmSVAR 94
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 95 NMAfslehRGGSKTeiAERVSWAADILGLTPLLERFP-----------RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:COG4618 425 NIA-----RFGDAD--PEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 164 LDAklrvvmRGE------IKGLHQRlGVTTVYVTHDQvEAMTMADKIVVMNAGRVEQCGA 217
Cdd:COG4618 498 LDD------EGEaalaaaIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGP 549
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-222 |
4.06e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.87 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDIsissrVVNEIEPKDR----DI----AMVFQNyalyPHMS-- 91
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-----YVDGLDTSDEenlwDIrnkaGMVFQN----PDNQiv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 92 ---VARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL 168
Cdd:PRK13633 100 atiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 169 RVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTmADKIVVMNAGRVEQCGAPLELY 222
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
5.44e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 108.35 E-value: 5.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 2 APVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRD-IAMV 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 161 LSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-252 |
6.22e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.49 E-value: 6.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISIS-SRVVNE-IEPKDRDIAMVFQNY-ALYPHMSVARN 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDgELLTAEnVWNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 MAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGE 175
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 176 IKGLHQRLGVTTVYVTHDQVEAMTmADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGSPAMNFIKGrLTASGFE 252
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDVPFSSNLMKD-LRKNGFD 257
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
7.64e-27 |
|
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: 110.66 E-value: 7.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY-----GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISIssRV----VNEIEPK- 73
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV--RVgdewVDMTKPGp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 74 ------DRDIAMVFQNYALYPHMSVARNM--AFSLEHrggsKTEIAERVS-WAADILGLT-----PLLERFPRQLSGGQR 139
Cdd:TIGR03269 358 dgrgraKRYIGILHQEYDLYPHRTVLDNLteAIGLEL----PDELARMKAvITLKMVGFDeekaeEILDKYPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 140 QRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPL 219
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
..
gi 1654818414 220 EL 221
Cdd:TIGR03269 514 EI 515
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-222 |
8.76e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.14 E-value: 8.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHG-----VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSG-----DISISSRVVN-EIEP 72
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGralfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGsvrvdDTLITSTSKNkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 73 KDRDIAMVFQnyalYPHM-----SVARNMAFSLEHRGGSKTEiAERVswAADILGLT----PLLERFPRQLSGGQRQRVA 143
Cdd:PRK13649 83 IRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEE-AEAL--AREKLALVgiseSLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 144 MGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQrLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELY 222
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
32-225 |
1.40e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.43 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 32 VVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNE--IEPKDRDIAMVFQN---YALYPhmSVARNMAFSLEHRGGS 106
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenIREVRKFVGLVFQNpddQIFSP--TVEQDIAFGPINLGLD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 107 KTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVT 186
Cdd:PRK13652 111 EETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMT 190
|
170 180 190
....*....|....*....|....*....|....*....
gi 1654818414 187 TVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRP 225
Cdd:PRK13652 191 VIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-212 |
1.80e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 105.55 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSR-VVNEIEPK-DRDIAMVFQNYAL--YPHMSVAR 94
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEYKrAKYIGRVFQDPMMgtAPSMTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 95 NMAFSLeHRGGSKT-----------EIAERVSwaadILGLTplLERfpR------QLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:COG1101 102 NLALAY-RRGKRRGlrrgltkkrreLFRELLA----TLGLG--LEN--RldtkvgLLSGGQRQALSLLMATLTKPKLLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 158 DEPLSNLDAKL-RVVMRgeikgLHQRL----GVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:COG1101 173 DEHTAALDPKTaALVLE-----LTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-221 |
3.27e-26 |
|
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: 104.78 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSG-DISISSRV-----VNEIEPKdrdI 77
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggedVWELRKR---I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMV---FQNYaLYPHMSVaRNM---AF--SLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIV 149
Cdd:COG1119 81 GLVspaLQLR-FPRDETV-LDVvlsGFfdSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 150 RNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-222 |
3.51e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.48 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL---ETVTS--GDISISSRV--VNEIEPKDRD 76
Cdd:PRK13645 12 VSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisETGQTivGDYAIPANLkkIKEVKRLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 77 IAMVFQ--NYALYPHmSVARNMAFSLEHRGGSKTEIAERVSWAADILGL-TPLLERFPRQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:PRK13645 92 IGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 154 VFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELY 222
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-218 |
3.72e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.85 E-value: 3.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYAL-YPhMSVARN 95
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLsFP-FTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 MAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVR------NPQVFLFDEPLSNLDakLR 169
Cdd:PRK13548 97 VAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALD--LA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 170 ---VVMRgEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAP 218
Cdd:PRK13548 175 hqhHVLR-LARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
29-223 |
5.54e-26 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 103.39 E-value: 5.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 29 GEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRvvnEIEPKDRDIAMVFQNYAL---YPhMSVA------RNMAFS 99
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFP-ISVAhtvmsgRTGHIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 100 LEHRGGSKTEIAerVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGL 179
Cdd:TIGR03771 82 WLRRPCVADFAA--VRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIEL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654818414 180 HQRlGVTTVYVTHDQVEAMTMADKIVVMNaGRVEQCGAPLELYD 223
Cdd:TIGR03771 160 AGA-GTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQD 201
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-254 |
8.38e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 104.08 E-value: 8.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDI--------SISSRVVNEIEPKdr 75
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgenipAMSRSRLYTVRKR-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 76 dIAMVFQNYALYPHMSVARNMAFSL-EHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:PRK11831 86 -MSMLFQSGALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 155 FLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPaNPFVAGFI 234
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-DPRVRQFL 243
|
250 260
....*....|....*....|
gi 1654818414 235 GSPAMNFIKGRLTASGFEAD 254
Cdd:PRK11831 244 DGIADGPVPFRYPAGDYHAD 263
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-229 |
8.61e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 108.02 E-value: 8.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVN-----EIEPKDRDIAMVFQN-YA-LYPHMS 91
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspgKLQALRRDIQFIFQDpYAsLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 92 VARNMAFSLE-HRGGSKTEIAERVSWAADILGLTPLLE-RFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLR 169
Cdd:PRK10261 420 VGDSIMEPLRvHGLLPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 170 VVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPF 229
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPY 559
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-193 |
9.35e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 102.93 E-value: 9.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 21 GVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDR------DIAMVFQNYALYPHMSVAR 94
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 95 NMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRG 174
Cdd:PRK10584 108 NVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170
....*....|....*....
gi 1654818414 175 EIKGLHQRLGVTTVYVTHD 193
Cdd:PRK10584 188 LLFSLNREHGTTLILVTHD 206
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-212 |
2.41e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 106.73 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSY----GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD------R 75
Cdd:PRK10535 7 LKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrrE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 76 DIAMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 156 LFDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHD-QVEAmtMADKIVVMNAGRV 212
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDpQVAA--QAERVIEIRDGEI 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-225 |
3.64e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.57 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY--GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL--------ETVTSGDISISSRVVNEIEPK 73
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 74 drdIAMVFQNyalyPH-----MSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAI 148
Cdd:PRK13640 86 ---VGIVFQN----PDnqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 149 VRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAmTMADKIVVMNAGRVEQCGAPLELYDRP 225
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-226 |
3.65e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.37 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSY-GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDI---SISSRVVNEIEPKDRDIAM 79
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQN-YALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFD 158
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 159 EPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDqVEAMTMADKIVVMNAGRVEQCGAPLELYDRPA 226
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-166 |
8.12e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 99.95 E-value: 8.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 21 GVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISissrvvneIEPKDRDIAMVF--------QNyALYPHMSV 92
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK--------LDGGDIDDPDVAeachylghRN-AMKPALTV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 93 ARNMAFSLEHRGGSKTEIAErvswAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:PRK13539 91 AENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-223 |
9.74e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 102.09 E-value: 9.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISissrvVNEIEP-KDR-----DIAMVF-QNYALYPHMS 91
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR-----VLGYVPfKRRkefarRIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 92 VARnmafSLE-HR---GGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQR--VAMgrAIVRNPQVFLFDEPLSNLD 165
Cdd:COG4586 113 AID----SFRlLKaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRceLAA--ALLHRPKILFLDEPTIGLD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 166 --AKLRVvmRGEIKGLHQRLGVTTVYVTHD--QVEAmtMADKIVVMNAGRVeqcgapleLYD 223
Cdd:COG4586 187 vvSKEAI--REFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHGRI--------IYD 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-216 |
1.24e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 99.91 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 10 KKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVneiepkdrdiAMVFQNYALYPH 89
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS----------SLLGLGGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 90 MSVARNMAFSLEHRGGSKTEIAERVswaADILGLTPLLERF--P-RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEIDEKI---DEIIEFSELGDFIdlPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1654818414 167 KLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCG 216
Cdd:cd03220 176 AFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-234 |
1.30e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.51 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 17 ATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRV---------VNEIEPKdRDIAMVFQNYALY 87
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyfgkdifqIDAIKLR-KEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 88 PHMSVARNMAFSLEHRG-GSKTEIAERVSWAADILGL-TPLLERF---PRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 163 NLDaklrVVMRGEIKGLHQRLG--VTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFI 234
Cdd:PRK14246 183 MID----IVNSQAIEKLITELKneIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-224 |
1.33e-24 |
|
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: 99.87 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFA--TIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPK--DRDIAM 79
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYpHMSVARNMAFSLEHRGGSKTEIAERVSWAADI-----LGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALADPGMSMERVIEAAKLAGAHDFiselpEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 155 FLFDEPLSNLDAKL-RVVMRgeikGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:cd03252 160 LIFDEATSALDYESeHAIMR----NMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-211 |
1.44e-24 |
|
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: 99.82 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISS--RVVNEIEPKDRDIAMVFQNYALY--------P 88
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdgGWVDLAQASPREILALRRRTIGYvsqflrviP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 89 HMS----VARnmafSLEHRGGSKTEIAERvswAADILGLTPLLER----FPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:COG4778 107 RVSaldvVAE----PLLERGVDREEARAR---ARELLARLNLPERlwdlPPATFSGGEQQRVNIARGFIADPPLLLLDEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 161 LSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQvEAM-TMADKIVVMNAGR 211
Cdd:COG4778 180 TASLDAANRAVVVELIEEAKAR-GTAIIGIFHDE-EVReAVADRVVDVTPFS 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-212 |
1.53e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 99.71 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 5 TLRS-VKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD-RDIAMVF- 81
Cdd:cd03267 22 SLKSlFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlRRIGVVFg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYALYPHMSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:cd03267 102 QKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 162 SNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-166 |
1.63e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.99 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISIssrvvneiePKDRDIAMVFQNYA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 86 LYPHMSVARN--MAFS-----------LEHRGGSKTEIAERVS-----------WAAD-----I---LGLTP-LLERFPR 132
Cdd:COG0488 72 LDDDLTVLDTvlDGDAelraleaeleeLEAKLAEPDEDLERLAelqeefealggWEAEaraeeIlsgLGFPEeDLDRPVS 151
|
170 180 190
....*....|....*....|....*....|....
gi 1654818414 133 QLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-212 |
2.63e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.09 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETvtsGDISISSRV------VNEIEPKDRDI 77
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT---GDKSAGSHIellgrtVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 -------AMVFQNYALYPHMSVARNMafsLEHRGGSKTEIAERVSW-----------AADILGLTPLLERFPRQLSGGQR 139
Cdd:PRK09984 82 rksrantGYIFQQFNLVNRLSVLENV---LIGALGSTPFWRTCFSWftreqkqralqALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 140 QRVAMGRAIVRNPQVFLFDEPLSNLDAK-LRVVMRgEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPEsARIVMD-TLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-229 |
3.82e-24 |
|
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: 99.13 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEI------EPKDRDI 77
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELelyqlsEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 A-----MVFQNYALYPHMSVA-------RNMAFSLEHRGGSKteiAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMG 145
Cdd:TIGR02323 84 MrtewgFVHQNPRDGLRMRVSaganigeRLMAIGARHYGNIR---ATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 146 RAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRP 225
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
....
gi 1654818414 226 ANPF 229
Cdd:TIGR02323 241 QHPY 244
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-222 |
7.55e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.08 E-value: 7.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 16 FATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL-----ETVTSGDISISSRVVN-EIEPKDRDIAMVFQnyalYPH 89
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALlkpttGTVTVDDITITHKTKDkYIRPVRKRIGMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 90 M-----SVARNMAFSLEHRGGSKTEIAER-------VSWAADILGLTPLlerfprQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:PRK13646 96 SqlfedTVEREIIFGPKNFKMNLDEVKNYahrllmdLGFSRDVMSQSPF------QMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 158 DEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGR-VEQCgAPLELY 222
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSiVSQT-SPKELF 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-165 |
1.22e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.41 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISIssrvvneiepKDRDI--- 77
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL----------DGEDIthl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 ----------------AMVFQNyalyphMSVARN-MAFsLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQ 140
Cdd:COG1137 71 pmhkrarlgigylpqeASIFRK------LTVEDNiLAV-LELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERR 143
|
170 180
....*....|....*....|....*
gi 1654818414 141 RVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:COG1137 144 RVEIARALATNPKFILLDEPFAGVD 168
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-207 |
1.51e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.71 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQN 83
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 YALYPHmSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTpLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:PRK10247 90 PTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDT-ILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654818414 164 LDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEaMTMADKIVVM 207
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-226 |
2.18e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.38 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 16 FATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISI----------SSRVVNEIEPKD--------RDI 77
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKiknfkelrRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQ--NYALYPHmSVARNMAFSLEHRGGSKTEIAERVSWAADILGL-TPLLERFPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:PRK13631 119 SMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 155 FLFDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPA 226
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-229 |
2.81e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.92 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPV-TLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSR--VVNEI----EPK 73
Cdd:PRK11701 3 DQPLlSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgQLRDLyalsEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 74 DR-----DIAMVFQNYALYPHMSVA-------RNMAFSLEHRGGSKTEIA---ERVSWAADilgltpLLERFPRQLSGGQ 138
Cdd:PRK11701 83 RRrllrtEWGFVHQHPRDGLRMQVSaggnigeRLMAVGARHYGDIRATAGdwlERVEIDAA------RIDDLPTTFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 139 RQRVAMGRAIVRNPQVFLFDEPLSNLD----AKLRVVMRgeikGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQ 214
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLR----GLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
250
....*....|....*
gi 1654818414 215 CGAPLELYDRPANPF 229
Cdd:PRK11701 233 SGLTDQVLDDPQHPY 247
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-223 |
3.16e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.36 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISI-SSRVVNEIEPKDRDIAMVFQ 82
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPHMSVARNMAFSLEHRGGSKTEIAERVSwaadilgltPLLErFPR----------QLSGGQRQRVAMGRAIVRNP 152
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIP---------SLLE-FARleskadarvsDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 153 QVFLFDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYD 223
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
4-225 |
3.49e-23 |
|
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: 100.40 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFAT--IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIePKDR---DIA 78
Cdd:TIGR03796 478 VELRNITFGYSPLEPplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVA 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 79 MVFQNYALYpHMSVARNMafSLEHRGGSKTEIAERVSWAA---DILGL-----TPLLERfPRQLSGGQRQRVAMGRAIVR 150
Cdd:TIGR03796 557 MVDQDIFLF-EGTVRDNL--TLWDPTIPDADLVRACKDAAihdVITSRpggydAELAEG-GANLSGGQRQRLEIARALVR 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 151 NPQVFLFDEPLSNLDAKL-RVVMRgeikGLHQRlGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAPLELYDRP 225
Cdd:TIGR03796 633 NPSILILDEATSALDPETeKIIDD----NLRRR-GCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-224 |
4.14e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.92 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEpkdrdIAMVFQnya 85
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLE-----LGAGFH--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 86 lyPHMSVARNMAFSLEHRGGSKTEIAERVswaADILGLTPlLERF---P-RQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:COG1134 101 --PELTGRENIYLNGRLLGLSRKEIDEKF---DEIVEFAE-LGDFidqPvKTYSSGMRARLAFAVATAVDPDILLVDEVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654818414 162 SNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHD--QVEamTMADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:COG1134 175 AVGDAAFQKKCLARIRELRES-GRTVIFVSHSmgAVR--RLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-221 |
5.34e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.92 E-value: 5.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 26 IADGEFVVLVGPSGCGKSTLLRMIAGLETVTsGDISISSRVVNEIEPKD--RDIAMVFQNYALyPHMSVARNMAFSLEHR 103
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLLGNPDA 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 104 GGSKTEIAERVSWAADIL-----GL-TPLLERFPRqLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL-RVVMRgei 176
Cdd:PRK11174 451 SDEQLQQALENAWVSEFLpllpqGLdTPIGDQAAG-LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSeQLVMQ--- 526
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1654818414 177 kGLHQ-RLGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:PRK11174 527 -ALNAaSRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-167 |
5.63e-23 |
|
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: 94.73 E-value: 5.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 21 GVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPK-DRDIAMVFQNYALYPHMSVARNMAFs 99
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSALENLHF- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 100 LEHRGGSkteiAERVSWAA-DILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK 167
Cdd:TIGR01189 97 WAAIHGG----AQRTIEDAlAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-212 |
7.25e-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: 93.65 E-value: 7.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 17 ATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRD---IAMV---FQNYALYPHM 90
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVpedRKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 91 SVARNMAFslehrggskteiaervswaadilgltpllerfPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD--AKL 168
Cdd:cd03215 94 SVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDvgAKA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1654818414 169 rvvmrgEIkglHQRL------GVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:cd03215 142 ------EI---YRLIreladaGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-227 |
1.18e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 95.23 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 13 YGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLR-------MIAGLET---VTSGDISISSRVVNEIEPKDRdIAMVFQ 82
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRVegkVTFHGKNLYAPDVDPVEVRRR-IGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPHmSVARNMAFSLEHRG--GSKTEIAER-----VSW--AADILGLTPLlerfprQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGARINGykGDMDELVERslrqaALWdeVKDKLKQSGL------SLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 154 VFLFDEPLSNLD--AKLRVvmRGEIKGLHQRLgvTTVYVTHDQVEAMTMADKIVVMNA---------GRVEQCGAPLELY 222
Cdd:PRK14243 172 VILMDEPCSALDpiSTLRI--EELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNVeltegggryGYLVEFDRTEKIF 247
|
....*
gi 1654818414 223 DRPAN 227
Cdd:PRK14243 248 NSPQQ 252
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-261 |
1.47e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.67 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISI---------SSRVVNEIEPKdrdIAMVFQnyalYPHM-- 90
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitpetGNKNLKKLRKK---VSLVFQ----FPEAql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 91 ---SVARNMAFSLEHRGGSKTEIAER-VSWAADIlGL-TPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:PRK13641 99 fenTVLKDVEFGPKNFGFSEDEAKEKaLKWLKKV-GLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 166 AKLRVVMRgEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPaNPFVAGFIGSPAMNFIKGR 245
Cdd:PRK13641 178 PEGRKEMM-QLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK-EWLKKHYLDEPATSRFASK 255
|
250
....*....|....*.
gi 1654818414 246 LTASGFEADGVVLPLP 261
Cdd:PRK13641 256 LEKGGFKFSEMPLTID 271
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-224 |
1.54e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 98.64 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGA--FATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAM 79
Cdd:TIGR02203 331 VEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYPHmSVARNMAFS-LEHRGGSKTEIAERVSWAADILGLTPLLERFP-----RQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPigengVLLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 154 VFLFDEPLSNLD--------AKLRVVMRGEikglhqrlgvTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:TIGR02203 490 ILILDEATSALDneserlvqAALERLMQGR----------TTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-212 |
2.50e-22 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 93.69 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPK--DRDIAMVFQNYALYPHmSVARNM 96
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 97 AFSLehrGGSKTEIAERVSWAADILGLTPLLERFPR--------QLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL 168
Cdd:cd03248 109 AYGL---QSCSFECVKEAAQKAHAHSFISELASGYDtevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654818414 169 RVVMRGEIKGLHQRlgvTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:cd03248 186 EQQVQQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
8-206 |
3.34e-22 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 93.63 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 8 SVKKSYGAFaTIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVN----EIEPKdrdiamvfqn 83
Cdd:cd03237 5 TMKKTLGEF-TLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKAD---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 yalYPhMSVaRNMAFSLEHRGGS----KTEIAervswaaDILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:cd03237 74 ---YE-GTV-RDLLSSITKDFYThpyfKTEIA-------KPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1654818414 160 PLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVV 206
Cdd:cd03237 142 PSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-221 |
4.43e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.90 E-value: 4.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 13 YGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPHM 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 91 SVARNMAfslehRGGS---------KTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:PRK10253 97 TVQELVA-----RGRYphqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 162 SNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-227 |
5.18e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.30 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 13 YGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL-----ETVTSGDIS-----ISSRVVNEIEPKdRDIAMVFQ 82
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVynghnIYSPRTDTVDLR-KEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPhMSVARNMAFSLEHRGGSKTEI----AERVSWAADILG-LTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:PRK14239 94 QPNPFP-MSIYENVVYGLRLKGIKDKQVldeaVEKSLKGASIWDeVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 158 DEPLSNLDAklrvVMRGEIK----GLHQRLgvTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPAN 227
Cdd:PRK14239 173 DEPTSALDP----ISAGKIEetllGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-222 |
6.95e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.60 E-value: 6.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 21 GVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSrvvNEIEPKDRD-------IAMVFQN-----YAlyP 88
Cdd:PRK13639 20 GINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG---EPIKYDKKSllevrktVGIVFQNpddqlFA--P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 89 hmSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL 168
Cdd:PRK13639 95 --TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 169 RVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELY 222
Cdd:PRK13639 173 ASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-229 |
7.61e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.31 E-value: 7.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 29 GEFVVLVGPSGCGKST----LLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQ--NYALYPHMSVARNMAFSLE- 101
Cdd:PRK15134 312 GETLGLVGESGSGKSTtglaLLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQdpNSSLNPRLNVLQIIEEGLRv 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 102 -HRGGSKTEIAERVSWAADILGLTPLL-ERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGL 179
Cdd:PRK15134 392 hQPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1654818414 180 HQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPF 229
Cdd:PRK15134 472 QQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-218 |
7.84e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.29 E-value: 7.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIA 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 79 MVFQNYALYPHMSVARNMAFS-LEHRG--GSKTEIAER-VSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQV 154
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGrTPHRSrfDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 155 FLFDEPLSNLDAKLRVvmrgEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAP 218
Cdd:PRK09536 161 LLLDEPTASLDINHQV----RTLELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
16-229 |
8.73e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 94.04 E-value: 8.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 16 FATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL----ETVTSGDISISSRVVNEIEPKDR------DIAMVFQN-- 83
Cdd:PRK11022 20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 YALYPHMSVARNMAFSLE-HRGGSKTEIAERvswAADILGLTPL------LERFPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:PRK11022 100 TSLNPCYTVGFQIMEAIKvHQGGNKKTRRQR---AIDLLNQVGIpdpasrLDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 157 FDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPF 229
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPY 249
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-212 |
2.18e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.70 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD---RDIAMVFQN---YALYPHMSV 92
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVPEDrkgEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 93 ARNMAF-SLEH--RGG--SKTEIAERVSWAADILGL-TPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD- 165
Cdd:COG1129 348 RENITLaSLDRlsRGGllDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDv 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 166 -AKlrvvmrGEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:COG1129 428 gAK------AEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-202 |
2.73e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 91.64 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 12 SYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL-----ETVTSGDI-----SISSRVVNeIEPKDRDIAMVF 81
Cdd:PRK14258 16 YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVeffnqNIYERRVN-LNRLRRQVSMVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYALYPhMSVARNMAFSLEHRG-GSKTE---IAERVSWAADILG-LTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:PRK14258 95 PKPNLFP-MSVYDNVAYGVKIVGwRPKLEiddIVESALKDADLWDeIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1654818414 157 FDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMAD 202
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-192 |
2.96e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.49 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISIssrvvneiePKDRDIAMVFQNyalyPHM---SVARN 95
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQR----PYLplgTLREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 MAFSLEHRGGSKTEIAErvswAADILGLTPLLERF------PRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLR 169
Cdd:COG4178 446 LLYPATAEAFSDAELRE----ALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521
|
170 180
....*....|....*....|....
gi 1654818414 170 VVMrgeIKGLHQRL-GVTTVYVTH 192
Cdd:COG4178 522 AAL---YQLLREELpGTTVISVGH 542
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-225 |
4.56e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.40 E-value: 4.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 26 IADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPK--DRDIAMVFQNYALYPHmSVARNMAFSLEHR 103
Cdd:TIGR00958 504 LHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVRENIAYGLTDT 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 104 GGSKTEIAERVSWAADILGLTP-----LLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMrGEIKG 178
Cdd:TIGR00958 583 PDEEIMAAAKAANAHDFIMEFPngydtEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL-QESRS 661
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1654818414 179 LHQRlgvTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAPLELYDRP 225
Cdd:TIGR00958 662 RASR---TVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-214 |
5.32e-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: 94.12 E-value: 5.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATI-HGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMV 80
Cdd:COG5265 358 VRFENVSFGYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYpHMSVARNMAFSLEhrGGSKTEIAErvswAADILGLTPLLERFPRQ-----------LSGGQRQRVAMGRAIV 149
Cdd:COG5265 438 PQDTVLF-NDTIAYNIAYGRP--DASEEEVEA----AARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 150 RNPQVFLFDEPLSNLDAK--------LRVVMRGEikglhqrlgvTTVYVTH------DqveamtmADKIVVMNAGR-VEQ 214
Cdd:COG5265 511 KNPPILIFDEATSALDSRteraiqaaLREVARGR----------TTLVIAHrlstivD-------ADEILVLEAGRiVER 573
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
22-221 |
5.96e-21 |
|
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: 94.04 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPK--DRDIAMVFQNYALYPHmSVARNMAFS 99
Cdd:TIGR01846 476 LNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIRDNIALC 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 100 lehRGGSKTEiaeRVSWAADILGLTPLLERFPR-----------QLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL 168
Cdd:TIGR01846 555 ---NPGAPFE---HVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEATSALDYES 628
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 169 RVVMRGEIKGLHQrlGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:TIGR01846 629 EALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-244 |
6.02e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.77 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 16 FATIHGVDIDIADGEFVVLVGPSGCGKS----TLLRMI--AGLEtVTSGDISISSRVVNEIEPKDR-----------DIA 78
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGL-VQCDKMLLRRRSRQVIELSEQsaaqmrhvrgaDMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 79 MVFQN--YALYPHMSVARNMAFSLE-HRGGSKTEI---AERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNP 152
Cdd:PRK10261 108 MIFQEpmTSLNPVFTVGEQIAESIRlHQGASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 153 QVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAG 232
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRA 267
|
250
....*....|...
gi 1654818414 233 FIGS-PAMNFIKG 244
Cdd:PRK10261 268 LLAAvPQLGAMKG 280
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
9.04e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 89.55 E-value: 9.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD---RDI 77
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQNYALYPHMSVARNMAFslehrGG---SKTEIAERVSWaadILGLTP-LLERFPRQ---LSGGQRQRVAMGRAIVR 150
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAM-----GGffaERDQFQERIKW---VYELFPrLHERRIQRagtMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 151 NPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRV--EQCGAPL 219
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVvlEDTGDAL 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-222 |
9.28e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 90.68 E-value: 9.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNE----IEPKDRDIAMVFQ--NYALYPhMSV 92
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkgLMKLRESVGMVFQdpDNQLFS-ASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 93 ARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVM 172
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1654818414 173 RGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELY 222
Cdd:PRK13636 181 MKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-216 |
1.85e-20 |
|
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: 88.48 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL---ETVTSGDISISSRVVNEIEPKDRdIAMVFQNYALYPHMSVARN 95
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 MAFSLEHRGGSKTEIAERVSWAADI----LGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA----K 167
Cdd:cd03234 102 LTYTAILRLPRKSSDAIRKKRVEDVllrdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSftalN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 168 LRVVMRgeikglhqRLGVT--TVYVTHDQ--VEAMTMADKIVVMNAGRVEQCG 216
Cdd:cd03234 182 LVSTLS--------QLARRnrIVILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-213 |
4.00e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 3 PVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVneiepkdrdIAMVFQ 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK---------IGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYA-LYPHMSVARNMafSLEHRGGSKTEIAErvswaadilgltpLLERF---------P-RQLSGGQRQRVAMGRAIVRN 151
Cdd:COG0488 386 HQEeLDPDKTVLDEL--RDGAPGGTEQEVRG-------------YLGRFlfsgddafkPvGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 152 PQVFLFDEPLSNLDaklrVVMRGEI-------KGlhqrlgvTTVYVTHDQ--VEamTMADKIVVMNAGRVE 213
Cdd:COG0488 451 PNVLLLDEPTNHLD----IETLEALeealddfPG-------TVLLVSHDRyfLD--RVATRILEFEDGGVR 508
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
4.09e-20 |
|
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: 91.02 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETV--TSGDI-------------SISSRV-- 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyvERPSKVge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 67 -----VNEIEPKDRD---------------IAMVFQ-NYALYPHMSVARNMAFSLEHRGGSKTEIAERvswAADILGLTP 125
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDfwnlsdklrrrirkrIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGR---AVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 126 LLERF---PRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMAD 202
Cdd:TIGR03269 158 LSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237
|
250 260
....*....|....*....|..
gi 1654818414 203 KIVVMNAGRVEQCGAPLELYDR 224
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-221 |
4.72e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.31 E-value: 4.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 5 TLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPK--DRDIAMVFQ 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPHMSVARNMA------------FSLEHRggskteiaERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVR 150
Cdd:PRK10575 93 QLPAAEGMTVRELVAigrypwhgalgrFGAADR--------EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 151 NPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-220 |
5.38e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.59 E-value: 5.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 26 IADGEFVVLVGPSGCGKSTLLRMIAGLETvTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPHMSVARNMAFSLeHR 103
Cdd:COG4138 19 VNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALHQ-PA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 104 GGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVR-----NP--QVFLFDEPLSNLDAKLRVVMRGEI 176
Cdd:COG4138 97 GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptiNPegQLLLLDEPMNSLDVAQQAALDRLL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654818414 177 KGLHQrLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLE 220
Cdd:COG4138 177 RELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-224 |
7.21e-20 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 91.16 E-value: 7.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 18 TIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVV--------------------NEIEPKDrdI 77
Cdd:TIGR00957 653 TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAyvpqqawiqndslrenilfgKALNEKY--Y 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQNYALYPHMSVARnmafslehrGGSKTEIAERvswaadilGLtpllerfprQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:TIGR00957 731 QQVLEACALLPDLEILP---------SGDRTEIGEK--------GV---------NLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 158 DEPLSNLDAKLRVVMRGEIKGLHQRL-GVTTVYVTHDqVEAMTMADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-216 |
9.68e-20 |
|
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: 85.06 E-value: 9.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRD-IAMVFQNyalyPHMsvarnma 97
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVLNQR----PYL------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 98 FSlehrggskteiaervswaadilglTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL-RVVMRGEI 176
Cdd:cd03247 87 FD------------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQLLSLIF 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1654818414 177 KGLHQRlgvTTVYVTHdQVEAMTMADKIVVMNAGRVEQCG 216
Cdd:cd03247 143 EVLKDK---TLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-212 |
1.08e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 86.66 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLE--TVTSGDISISSRVVNEIEPKDR---DIAMVFQNYALYPHMSVA 93
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 94 RNMAFSLEHRGGSKTEIAE---RVSWAADILGLTP-LLER-----FprqlSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:COG0396 96 NFLRTALNARRGEELSAREflkLLKEKMKELGLDEdFLDRyvnegF----SGGEKKRNEILQMLLLEPKLAILDETDSGL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 165 DA-KLRVVMRGeIKGLHQRlGVTTVYVTH-----DQVEamtmADKIVVMNAGRV 212
Cdd:COG0396 172 DIdALRIVAEG-VNKLRSP-DRGILIITHyqrilDYIK----PDFVHVLVDGRI 219
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-218 |
1.14e-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: 86.01 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKST----LLRMIagleTVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPHmSV 92
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSG-TI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 93 ARNMAFSLEHrggSKTEIA---ERVS----WAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:cd03244 95 RSNLDPFGEY---SDEELWqalERVGlkefVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 166 ----AKLRVVMRGEIKglhqrlGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAP 218
Cdd:cd03244 172 petdALIQKTIREAFK------DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
10-212 |
1.51e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.45 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 10 KKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISI--------------------------S 63
Cdd:PRK13651 14 KKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkekekvleklviqktR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 64 SRVVNEIEPKDRDIAMVFQ--NYALYpHMSVARNMAFSLEHRGGSKTEIAERvswAADILGLTPL----LERFPRQLSGG 137
Cdd:PRK13651 94 FKKIKKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKR---AAKYIELVGLdesyLQRSPFELSGG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654818414 138 QRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-229 |
1.89e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.99 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKS----TLLRMIAGLETV-TSGDISIS-SRVVNEIEPKDR-----DIAMVFQN--YA 85
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHgESLLHASEQTLRgvrgnKIAMIFQEpmVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 86 LYPHMSVARNMAFSLE-HRG----GSKTEIA---ERVSwaadILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:PRK15134 105 LNPLHTLEKQLYEVLSlHRGmrreAARGEILnclDRVG----IRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 158 DEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPF 229
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPY 252
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-193 |
2.32e-19 |
|
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: 88.96 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 2 APVTLRSVKKSY-GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL-----ETVTSGDISISSRVVNEIEpkdR 75
Cdd:TIGR02868 333 PTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLldplqGEVTLDGVPVSSLDQDEVR---R 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 76 DIAMVFQNYALYpHMSVARNMAFslehrgGSKTEIAERVSWAADILGLTPLLERFP-----------RQLSGGQRQRVAM 144
Cdd:TIGR02868 410 RVSVCAQDAHLF-DTTVRENLRL------ARPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLAL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1654818414 145 GRAIVRNPQVFLFDEPLSNLDAKLRVVMrgeIKGLHQRL-GVTTVYVTHD 193
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADEL---LEDLLAALsGRTVVLITHH 529
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-211 |
2.39e-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: 88.73 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL--ETVTSGDI-----SISSRVVNEIEPKdrD 76
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIywsgsPLKASNIRDTERA--G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 77 IAMVFQNYALYPHMSVARN--MAFSLEHRGGskteiaeRVSWAADILGLTPLLE----------RFPRQLSGGQRQRVAM 144
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENifLGNEITLPGG-------RMAYNAMYLRAKNLLRelqldadnvtRPVGDYGGGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 145 GRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGR 211
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
12-224 |
2.52e-19 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 89.03 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 12 SYGAFATI-HGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIepkDRDIAMVFQNY-ALYPH 89
Cdd:TIGR01193 482 SYGYGSNIlSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFINYlPQEPY 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 90 M---SVARNMAFSlEHRGGSKTEIAERVSWA---ADI----LGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:TIGR01193 559 IfsgSILENLLLG-AKENVSQDEIWAACEIAeikDDIenmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654818414 160 PLSNLDAklrVVMRGEIKGLHQRLGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:TIGR01193 638 STSNLDT---ITEKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-211 |
3.01e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 5 TLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTS--GDISISSRVVNEIEPKDRD---IAM 79
Cdd:PRK13549 7 EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTEragIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYPHMSVARNMAFSLE-HRGGskteiaeRVSWAADILGLTPLLERFP---------RQLSGGQRQRVAMGRAIV 149
Cdd:PRK13549 87 IHQELALVKELSVLENIFLGNEiTPGG-------IMDYDAMYLRAQKLLAQLKldinpatpvGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 150 RNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGR 211
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
34-225 |
3.40e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 86.00 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 34 LVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVN--EIEPKDRDIAMVFQN--YALYPHMSVARNMAFSLE-HRGGSKT 108
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQRISQILDFPLRlNTDLEPE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 109 EIAERVSWAADILGLTP-LLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTT 187
Cdd:PRK15112 124 QREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISY 203
|
170 180 190
....*....|....*....|....*....|....*...
gi 1654818414 188 VYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRP 225
Cdd:PRK15112 204 IYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-192 |
3.91e-19 |
|
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: 84.08 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 21 GVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPK-DRDIAMVFQNYALYPHMSVARNMAFS 99
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 100 leHRGGSKTEIAErvswAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD----AKLRVVMRGe 175
Cdd:cd03231 98 --HADHSDEQVEE----ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARFAEAMAG- 170
|
170
....*....|....*..
gi 1654818414 176 ikglHQRLGVTTVYVTH 192
Cdd:cd03231 171 ----HCARGGMVVLTTH 183
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-223 |
6.29e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.41 E-value: 6.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEP---KDRDIAMVFQ 82
Cdd:PRK15439 14 ARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPHMSVARNMAFSLEHRGGSKTEIAERVSwaadILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:PRK15439 94 EPLLFPNLSVKENILFGLPKRQASMQKMKQLLA----ALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 163 NLDAKLRVVMRGEIKGLhQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYD 223
Cdd:PRK15439 170 SLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-235 |
8.84e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.76 E-value: 8.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 34 LVGPSGCGKSTLLRMIAGLETVTSG-----DISISSRVV---NEIEPKDRDIAMVFQNYALYPhMSVARNMAFSL----- 100
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVrahkl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 101 ----EHRGGSKTEIAERVSWAAdilgLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEI 176
Cdd:PRK14271 131 vprkEFRGVAQARLTEVGLWDA----VKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 177 KGLHQRLgvTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANP----FVAGFIG 235
Cdd:PRK14271 207 RSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetarYVAGLSG 267
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-225 |
9.43e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 84.27 E-value: 9.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 13 YGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRvvnEIEPK-DRDIA---MV--FQNYAL 86
Cdd:PRK11300 15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ---HIEGLpGHQIArmgVVrtFQHVRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 87 YPHMSVARNMAFSlEHR--------GGSKTEI-----AERVSWAA---DILGLTPLLERFPRQLSGGQRQRVAMGRAIVR 150
Cdd:PRK11300 92 FREMTVIENLLVA-QHQqlktglfsGLLKTPAfrraeSEALDRAAtwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654818414 151 NPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRP 225
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-221 |
2.80e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.87 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLE---TVTSGDISISSRVVNEIEPKDRDiAMVFQNYALYPHMSVARN 95
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGMPIDAKEMRAIS-AYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 MAFSLE---HRGGSKTEIAERVSWAADILGLTPL------LERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:TIGR00955 120 LMFQAHlrmPRRVTKKEKRERVDEVLQALGLRKCantrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 167 klrvVMRGEI----KGLHQRlGVTTVYVTHD-QVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:TIGR00955 200 ----FMAYSVvqvlKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
8-206 |
3.17e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 85.63 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 8 SVKKSYGAFA-TIHGVDIdiADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVV---NEIEPKdrdiamvfqn 83
Cdd:PRK13409 345 DLTKKLGDFSlEVEGGEI--YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISykpQYIKPD---------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 yalyPHMSVARNMAFSLEHRGGS--KTEIAERvswaadiLGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:PRK13409 413 ----YDGTVEDLLRSITDDLGSSyyKSEIIKP-------LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1654818414 162 SNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVV 206
Cdd:PRK13409 482 AHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-224 |
3.73e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.13 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNE----IEPKDRDIAMVFQNyalyP-----H 89
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYskrgLLALRQQVATVFQD----PeqqifY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 90 MSVARNMAFSLEHRGGSKTEIAERVSWAADILGLtpllERFPRQ----LSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDA----QHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 166 AKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-208 |
4.02e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.47 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDIsissrvvnEIEPKDRdIAMVFQN 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR-IGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 YALYPHM--SVARNMAFslehRGGSKTeiaervswaADILgltPLLER--------FPRQ-LSGGQRQRVAMGRAIVRNP 152
Cdd:PRK09544 76 LYLDTTLplTVNRFLRL----RPGTKK---------EDIL---PALKRvqaghlidAPMQkLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 153 QVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMN 208
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-212 |
5.45e-18 |
|
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: 81.15 E-value: 5.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGletVTSGDISISSRVV-NEIEPKD------RDIAMVFQNYALYPHMS 91
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIHyNGIPYKEfaekypGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 92 VARNMAFSLEHRGGskteiaervswaadilgltplleRFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK--LR 169
Cdd:cd03233 100 VRETLDFALRCKGN-----------------------EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSStaLE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1654818414 170 VVMRgeIKGLHQRLGVTTVyVTHDQ--VEAMTMADKIVVMNAGRV 212
Cdd:cd03233 157 ILKC--IRTMADVLKTTTF-VSLYQasDEIYDLFDKVLVLYEGRQ 198
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-211 |
6.06e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.41 E-value: 6.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVvneiepkdrdiamvfqN 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------K 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 YALYPhmsvarnmafslehrggskteiaervswaadilgltpllerfprQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:cd03221 65 IGYFE--------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 164 LDAKLRVVMRGEIKGLHQrlgvTTVYVTHD-----QVeamtmADKIVVMNAGR 211
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDryfldQV-----ATKIIELEDGK 144
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-220 |
8.65e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.52 E-value: 8.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 26 IADGEFVVLVGPSGCGKSTLLRMIAGLeTVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPHMSVARNMAFSLeHR 103
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAElaRHRAYLSQQQTPPFAMPVFQYLTLHQ-PD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 104 GGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVR-----NP--QVFLFDEPLSNLDAKLRVVMRGEI 176
Cdd:PRK03695 97 KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLDVAQQAALDRLL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654818414 177 KGLHQrLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLE 220
Cdd:PRK03695 177 SELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-211 |
8.78e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 8.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVV---NEIEPKDRDI 77
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQNYALYPHMSVARN-MAFSLEHRGG--SKTEIAERVSWAADILGL-----TPLlerfpRQLSGGQRQRVAMGRAIV 149
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENlYLGQLPHKGGivNRRLLNYEAREQLEHLGVdidpdTPL-----KYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 150 RNPQVFLFDEPLSNLDAK-----LRVV--MRGEikglhqrlGVTTVYVTHDQVEAMTMADKIVVMNAGR 211
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAReieqlFRVIreLRAE--------GRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-210 |
9.02e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.07 E-value: 9.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDR---DIAMV 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYPHMSVARNMAFSlehRGGSK----------TEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVR 150
Cdd:PRK09700 86 YQELSVIDELTVLENLYIG---RHLTKkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 151 NPQVFLFDEPLSNLDAK----LRVVM---RGEIKGLhqrlgvttVYVTHDQVEAMTMADKIVVMNAG 210
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKevdyLFLIMnqlRKEGTAI--------VYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-221 |
1.07e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.09 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEI---EPKDRDI 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQNYALYPHMSVARNMAFSLEHRGGSKTEI-AERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 157 FDEPLSNLDAkLRVVmrgEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:PRK10895 161 LDEPFAGVDP-ISVI---DIKRIIEHLrdsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
8-206 |
1.91e-17 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 83.30 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 8 SVKKSYGAFA-TIHGVDIDIadGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVV---NEIEPkDRDiamvfqn 83
Cdd:COG1245 346 DLTKSYGGFSlEVEGGEIRE--GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISykpQYISP-DYD------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 yalyphMSVARNMAFSLEHRGGS---KTEIAERvswaadiLGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEP 160
Cdd:COG1245 416 ------GTVEEFLRSANTDDFGSsyyKTEIIKP-------LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1654818414 161 LSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDqveaMTM----ADKIVV 206
Cdd:COG1245 483 SAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDRLMV 528
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-263 |
2.32e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 81.69 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 14 GAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLeTVTSGDISISSR-----VVNEIEPK-----DRDIAMVFQN 83
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL-LAANGRIGGSATfngreILNLPEKElnklrAEQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 --YALYPHMSVARN-MAFSLEHRGGSKTEIAERVSWAADILGLTPLLER---FPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:PRK09473 106 pmTSLNPYMRVGEQlMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 158 DEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPFVAGFIGS- 236
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAv 265
|
250 260
....*....|....*....|....*..
gi 1654818414 237 PamnfikgRLtasgfEADGVVLPLPPG 263
Cdd:PRK09473 266 P-------RL-----DAEGESLLTIPG 280
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-224 |
3.64e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 82.32 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFAT-IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMV 80
Cdd:PRK13657 335 VEFDDVSFSYDNSRQgVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 81 FQNYALYpHMSVARNMafslehRGGSKTEIAERVSWAADILGLTPLLERFP-----------RQLSGGQRQRVAMGRAIV 149
Cdd:PRK13657 415 FQDAGLF-NRSIEDNI------RVGRPDATDEEMRAAAERAQAHDFIERKPdgydtvvgergRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654818414 150 RNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQrlGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAPLELYDR 224
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-210 |
4.52e-17 |
|
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: 78.91 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 16 FATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRD------IAMVFQNYALYpH 89
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrysVAYAAQKPWLL-N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 90 MSVARNMAFSLEHRGGSKTEIAERVSWAADILGL-----TPLLERfPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:cd03290 93 ATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLpfgdqTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1654818414 165 DAKLR-VVMRGEIKGLHQRLGVTTVYVTHdQVEAMTMADKIVVMNAG 210
Cdd:cd03290 172 DIHLSdHLMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-221 |
4.73e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.18 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEI-EPKDRD-IAMVFQNYALYPHmSVARNM 96
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYsEAALRQaISVVSQRVHLFSA-TLRDNL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 97 AFSLEHRGGSK-TEIAERVswaadilGLTPLLERFP----------RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:PRK11160 435 LLAAPNASDEAlIEVLQQV-------GLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 166 AK--------LRVVMRGEikglhqrlgvTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:PRK11160 508 AEterqilelLAEHAQNK----------TVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-233 |
6.59e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 82.37 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSR-VVNEIEPKDRDIAMVFQNYALYPHMSVARNMAFSL 100
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 101 EHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIkgLH 180
Cdd:TIGR01257 1029 QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LK 1106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 181 QRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELydrpANPFVAGF 233
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-221 |
7.51e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.60 E-value: 7.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTllrmIAGLET----VTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYpHMSVARN 95
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKST----IANLLTrfydIDEGEILLDGHDLRDYTLASlrNQVALVSQNVHLF-NDTIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 MAFSLEHRGgSKTEI--AERVSWAADIL-----GLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL 168
Cdd:PRK11176 437 IAYARTEQY-SREQIeeAARMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 169 RVVMRGEIKGLHQRlgvTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:PRK11176 516 ERAIQAALDELQKN---RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-224 |
1.47e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 76.80 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLE--TVTSGDISISSRVVNEIEPKDR---DIAMVFQnyalYPhmsva 93
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlGIFLAFQ----YP----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 94 rnmafslehrggskteiaervswaADILGLTplLERFPRQL----SGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA-KL 168
Cdd:cd03217 87 ------------------------PEIPGVK--NADFLRYVnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIdAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 169 RVVMRGeIKGLHQRlGVTTVYVTH-----DQVEamtmADKIVVMNAGRVeQCGAPLELYDR 224
Cdd:cd03217 141 RLVAEV-INKLREE-GKSVLIITHyqrllDYIK----PDRVHVLYDGRI-VKSGDKELALE 194
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-192 |
2.28e-16 |
|
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: 75.65 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 23 DIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISIssrvvneiePKDRDIAMVFQNyalyPHMSVArnmafSLeh 102
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR----PYLPLG-----TL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 103 rggskteiaervswaADILgltplleRFP--RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKlrvvMRGEIKGLH 180
Cdd:cd03223 81 ---------------REQL-------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE----SEDRLYQLL 134
|
170
....*....|..
gi 1654818414 181 QRLGVTTVYVTH 192
Cdd:cd03223 135 KELGITVISVGH 146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-216 |
2.69e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.21 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGdisissRVVNEiepkdRDIAMVFQNyALYPHMSVARNMAF 98
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG------RVWAE-----RSIAYVPQQ-AWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 99 SLEHRGgSKTEIAERVS-WAADILGLTPLLE----RFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL--RVV 171
Cdd:PTZ00243 744 FDEEDA-ARLADAVRVSqLEADLAQLGGGLEteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeRVV 822
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1654818414 172 MRGEIKGLHqrlGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCG 216
Cdd:PTZ00243 823 EECFLGALA---GKTRVLATH-QVHVVPRADYVVALGDGRVEFSG 863
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-211 |
3.57e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.54 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL--ETVTSGDISISSRVVNEiePKDRDIAMVFQNYALYPHMSVARNM 96
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTK--QILKRTGFVTQDDILYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 97 AF--------SLEHRggSKTEIAERVswaADILGLTP-----LLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSN 163
Cdd:PLN03211 162 VFcsllrlpkSLTKQ--EKILVAESV---ISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1654818414 164 LDAKLRVVMRGEIKGLHQRlGVTTVYVTHD-QVEAMTMADKIVVMNAGR 211
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-216 |
3.65e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 79.37 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPHmSVARNM 96
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFSD-TVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 97 AfsLEHRGGSKTEIaERVSWAA----DILGL-----TPLLERfPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAk 167
Cdd:PRK10789 410 A--LGRPDATQQEI-EHVARLAsvhdDILRLpqgydTEVGER-GVMLSGGQKQRISIARALLLNAEILILDDALSAVDG- 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 168 lrvvmRGEIKGLH-------QRlgvtTVYVTHDQVEAMTMADKIVVMNAGRVEQCG 216
Cdd:PRK10789 485 -----RTEHQILHnlrqwgeGR----TVIISAHRLSALTEASEILVMQHGHIAQRG 531
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-222 |
4.58e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 79.63 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 18 TIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGlETVTSGDISISSRVVNEIEPKdrdIAMVFqnyalypHMSVARNMA 97
Cdd:PLN03232 632 TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-ELSHAETSSVVIRGSVAYVPQ---VSWIF-------NATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 98 FslehrgGSKTEiAERVSWAADILGLTPLLERFPRQ-----------LSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:PLN03232 701 F------GSDFE-SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 167 KL-RVVMRGEIKglHQRLGVTTVYVThDQVEAMTMADKIVVMNAGRVEQCGAPLELY 222
Cdd:PLN03232 774 HVaHQVFDSCMK--DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-215 |
4.87e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 79.67 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 24 IDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEiepkdrDIAMVFQNYALYPHMSVARNMAFSLEH- 102
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDVHQNMGYCPQFDAIDDLLTGREHl 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 103 ------RGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEI 176
Cdd:TIGR01257 2034 ylyarlRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180 190
....*....|....*....|....*....|....*....
gi 1654818414 177 KGLhQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVeQC 215
Cdd:TIGR01257 2114 VSI-IREGRAVVLTSHSMEECEALCTRLAIMVKGAF-QC 2150
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-167 |
5.08e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.61 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 20 HGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNeiepKDRDiamVFQNYALY--------PHMS 91
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYHQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 92 VARNMAFSLEHRGGSKTEIAervsWAAdiLGLTPLL--ERFP-RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK 167
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDEAL----WEA--LAQVGLAgfEDVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-221 |
7.67e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 79.01 E-value: 7.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 18 TIHGVDIDIADGEFVVLVGPSGCGKSTLLR-MIAGLETVTSGDISISSRVvneiepkdrdiAMVFQNYALYpHMSVARNM 96
Cdd:PLN03130 632 TLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTV-----------AYVPQVSWIF-NATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 97 AF----------------SLEHR-----GGSKTEIAERvswaadilGLtpllerfprQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:PLN03130 700 LFgspfdperyeraidvtALQHDldllpGGDLTEIGER--------GV---------NISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 156 LFDEPLSNLDAKL-RVVMRGEIKGLHQrlGVTTVYVThDQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:PLN03130 763 IFDDPLSALDAHVgRQVFDKCIKDELR--GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-212 |
7.98e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.12 E-value: 7.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD---RDIAMVFQNY---ALYPHMSV 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 93 ARNMAFS----LEHRGGSKTEIAERVSwAADILGL----TPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:PRK10762 348 KENMSLTalryFSRAGGSLKHADEQQA-VSDFIRLfnikTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 165 DaklrVVMRGEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:PRK10762 427 D----VGAKKEIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-224 |
9.51e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.24 E-value: 9.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLE-------TVTSGDISiSSRVVNEIEPKdrd 76
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARkiqqgrvEVLGGDMA-DARHRRAVCPR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 77 IAMVFQ----NyaLYPHMSVARNMAFSLEHRGGSKTEIAERVswaADIL---GLTPLLERFPRQLSGGQRQRVAMGRAIV 149
Cdd:NF033858 78 IAYMPQglgkN--LYPTLSVFENLDFFGRLFGQDAAERRRRI---DELLratGLAPFADRPAGKLSGGMKQKLGLCCALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 150 RNPQVFLFDE------PLS-----NLDAKLRvvmrgeikglHQRLG----VTTVYvthdqveaMTMA---DKIVVMNAGR 211
Cdd:NF033858 153 HDPDLLILDEpttgvdPLSrrqfwELIDRIR----------AERPGmsvlVATAY--------MEEAerfDWLVAMDAGR 214
|
250
....*....|...
gi 1654818414 212 VEQCGAPLELYDR 224
Cdd:NF033858 215 VLATGTPAELLAR 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-228 |
1.47e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.12 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKS----TLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVFQN--YALYPHMSV 92
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 93 ARNMAFSLEHRGGSKTEIAERVSWAADILGLTP-LLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVV 171
Cdd:PRK10418 99 HTHARETCLALGKPADDATLTAALEAVGLENAArVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 172 MRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANP 228
Cdd:PRK10418 179 ILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-192 |
3.90e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.34 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEpKDRDIAMVFQNYALYPHMSVARNMAF--S 99
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLGHLPGLKADLSTLENLHFlcG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 100 LEHRGGSKTEiaervSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKlRVVMRGEIKGL 179
Cdd:PRK13543 109 LHGRRAKQMP-----GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLVNRMISA 182
|
170
....*....|...
gi 1654818414 180 HQRLGVTTVYVTH 192
Cdd:PRK13543 183 HLRGGGAALVTTH 195
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-212 |
4.95e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 8 SVKKSYGAfATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRDIAMVF------ 81
Cdd:COG3845 264 SVRDDRGV-PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedr 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYALYPHMSVARNMAFSLEHRGG-SK---------TEIAERVSWAADIlgLTPLLERFPRQLSGGQRQRVAMGRAIVRN 151
Cdd:COG3845 343 LGRGLVPDMSVAENLILGRYRRPPfSRggfldrkaiRAFAEELIEEFDV--RTPGPDTPARSLSGGNQQKVILARELSRD 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 152 PQVFLFDEPLSNLDAklrvvmrGEIKGLHQRL------GVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:COG3845 421 PKLLIAAQPTRGLDV-------GAIEFIHQRLlelrdaGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-221 |
8.87e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.55 E-value: 8.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 11 KSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRvvnEIEPKDRDIAM----VFQNYAL 86
Cdd:NF033858 274 MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---PVDAGDIATRRrvgyMSQAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 87 YPHMSVARNMA-----FSLEhrggsKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:NF033858 351 YGELTVRQNLElharlFHLP-----AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654818414 162 SNLDAklrvVMRGE-----IKgLHQRLGVTTVYVTHDQVEAMTmADKIVVMNAGRVEQCGAPLEL 221
Cdd:NF033858 426 SGVDP----VARDMfwrllIE-LSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
4-212 |
1.16e-14 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 74.99 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHG-----VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD-RDI 77
Cdd:TIGR01194 338 IELKDVHMNPKAPEGSEGfalgpIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDyRDL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 -AMVFQNYALYPHM---SVARNMAFSLEHRGGSKTEIAERVSwaadILGLTpllERFPRQLSGGQRQRVAMGRAIVRNPQ 153
Cdd:TIGR01194 418 fSAIFADFHLFDDLigpDEGEHASLDNAQQYLQRLEIADKVK----IEDGG---FSTTTALSTGQQKRLALICAWLEDRP 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1654818414 154 VFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQvEAMTMADKIVVMNAGRV 212
Cdd:TIGR01194 491 ILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHDD-QYFELADQIIKLAAGCI 548
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
12-193 |
1.72e-14 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 72.40 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 12 SYG--AFAtIHGVDIdIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDisissrvvNEIEPKDRDIAMVFQNYALYPH 89
Cdd:cd03236 9 RYGpnSFK-LHRLPV-PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--------FDDPPDWDEILDEFRGSELQNY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 90 MSVARNMAFSLEHR-----------GGSKTEIAERV------SWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNP 152
Cdd:cd03236 79 FTKLLEGDVKVIVKpqyvdlipkavKGKVGELLKKKdergklDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1654818414 153 QVFLFDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHD 193
Cdd:cd03236 159 DFYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHD 198
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-194 |
4.94e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.37 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 21 GVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISIssrvvneiepkdrdiamVFQNYALYPHMSVARNMAfsl 100
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-----------------DVPDNQFGREASLIDAIG--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 101 ehRGGSKTEIAERVSWAAdiLGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLH 180
Cdd:COG2401 108 --RKGDFKDAVELLNAVG--LSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLA 183
|
170
....*....|....
gi 1654818414 181 QRLGVTTVYVTHDQ 194
Cdd:COG2401 184 RRAGITLVVATHHY 197
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-218 |
9.66e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 69.36 E-value: 9.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYphMSVARNM 96
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLF--SGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 97 AFSLEHRGGSKTEIAERVSWAADilgltpllerfprQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL----DAKLRVVM 172
Cdd:cd03369 102 LDPFDEYSDEEIYGALRVSEGGL-------------NLSQGQRQLLCLARALLKRPRVLVLDEATASIdyatDALIQKTI 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1654818414 173 RGEIKglhqrlGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAP 218
Cdd:cd03369 169 REEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-211 |
1.85e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 16 FATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGlETVTSgDISISSRVV------NEIEPKDR-DIAMVFQNYALYP 88
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS-NTDGF-HIGVEGVITydgitpEEIKKHYRgDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 89 HMSVARNMAFSLEHR-------GGSKTEIAERV-SWAADILGL-----TPLLERFPRQLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:TIGR00956 152 HLTVGETLDFAARCKtpqnrpdGVSREEYAKHIaDVYMATYGLshtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 156 LFDEPLSNLDAKLRVVMrgeIKGLHQ--RLGVTTVYVTHDQV--EAMTMADKIVVMNAGR 211
Cdd:TIGR00956 232 CWDNATRGLDSATALEF---IRALKTsaNILDTTPLVAIYQCsqDAYELFDKVIVLYEGY 288
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-214 |
2.67e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPK--DRDIAMVFQN-----YALYPHMS 91
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDpvvlaDTFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 92 VARNmafslehrggskteIAERVSWAA-DILGLTPLLERFP-----------RQLSGGQRQRVAMGRAIVRNPQVFLFDE 159
Cdd:PRK10790 437 LGRD--------------ISEEQVWQAlETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 160 PLSNLDAKLRVVMRGEIKGLHQRlgvTTVYVTHDQVEAMTMADKIVVMNAGR-VEQ 214
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRGQaVEQ 555
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-211 |
2.83e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.39 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYG--AFAtIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVF 81
Cdd:PRK10522 325 LRNVTFAYQdnGFS-VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAVF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 82 QNYALYPHMsvarnmafsLEHRGG-SKTEIAErvSWAAdILGLTPLLE----RFPR-QLSGGQRQRVAMGRAIVRNPQVF 155
Cdd:PRK10522 404 TDFHLFDQL---------LGPEGKpANPALVE--KWLE-RLKMAHKLEledgRISNlKLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 156 LFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQvEAMTMADKIVVMNAGR 211
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQ 526
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-212 |
4.73e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.98 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 1 MAPVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSR-VVNEIE---PKDRD 76
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlIVARLQqdpPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 77 ----------IAMVFQNYALYPHMS--------------VARNMAfSLEHRGGSKTEiaERVSWAADILGL---TPLLEr 129
Cdd:PRK11147 81 gtvydfvaegIEEQAEYLKRYHDIShlvetdpseknlneLAKLQE-QLDHHNLWQLE--NRINEVLAQLGLdpdAALSS- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 130 fprqLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKlrvvmrgEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVV 206
Cdd:PRK11147 157 ----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-------TIEWLEGFLktfQGSIIFISHDRSFIRNMATRIVD 225
|
....*.
gi 1654818414 207 MNAGRV 212
Cdd:PRK11147 226 LDRGKL 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-165 |
6.14e-13 |
|
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: 69.58 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 9 VKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVvneiepkdrDIAMVFQNY-ALY 87
Cdd:TIGR03719 328 LTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------KLAYVDQSRdALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 88 PHMSVARNMAFSLEHRGGSKTEIAER--VSW----AADilgltplLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:TIGR03719 399 PNKTVWEEISGGLDIIKLGKREIPSRayVGRfnfkGSD-------QQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
....
gi 1654818414 162 SNLD 165
Cdd:TIGR03719 472 NDLD 475
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-208 |
2.00e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 26 IADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISIS-SRVVNEIEPK--DRDIAMVFQNYALYPHmSVARNMAFSL-- 100
Cdd:PTZ00265 408 LTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKwwRSKIGVVSQDPLLFSN-SIKNNIKYSLys 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 101 ------------EHRGGSKTEIAERVSWAADILG-----------------------------------------LTPLL 127
Cdd:PTZ00265 487 lkdlealsnyynEDGNDSQENKNKRNSCRAKCAGdlndmsnttdsneliemrknyqtikdsevvdvskkvlihdfVSALP 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 128 ERF-------PRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHdQVEAMTM 200
Cdd:PTZ00265 567 DKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH-RLSTIRY 645
|
....*...
gi 1654818414 201 ADKIVVMN 208
Cdd:PTZ00265 646 ANTIFVLS 653
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-214 |
2.57e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRvvnEIEPKD------RDIAMVFQNY---ALYPHMSV 92
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRSpldavkKGMAYITESRrdnGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 93 ARNMAFS--------------LEHRGGSKTEIAERvswaaDILGLT-PLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:PRK09700 359 AQNMAISrslkdggykgamglFHEVDEQRTAENQR-----ELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 158 DEPLSNLDaklrVVMRGEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRVEQ 214
Cdd:PRK09700 434 DEPTRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-218 |
3.05e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.00 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 17 ATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAG--LETVTSGDISISSRVVNEIEPKDR-DIAMVFQNYALYPHMSvA 93
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDVTLNGEPLAAiDAPRLARLRAVLPQAA-Q 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 94 RNMAFSLE-----------HRGGSKTEIAERVSWAA-DILGLTPLLERFPRQLSGGQRQRVAMGRAI---------VRNP 152
Cdd:PRK13547 94 PAFAFSAReivllgryphaRRAGALTHRDGEIAWQAlALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 153 QVFLFDEPLSNLDAKLRVVMRGEIKGLHQ--RLGVTTvyVTHDQVEAMTMADKIVVMNAGRVEQCGAP 218
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLA--IVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-212 |
3.11e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 29 GEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD---RDIAMVFQNY---ALYPHMSVARNMAFSLEH 102
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairAGIMLCPEDRkaeGIIPVHSVADNINISARR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 103 ---------RGGSKTEIAERVSWAADILglTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDaklrVVMR 173
Cdd:PRK11288 359 hhlragcliNNRWEAENADRFIRSLNIK--TPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID----VGAK 432
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1654818414 174 GEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:PRK11288 433 HEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-206 |
3.24e-12 |
|
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: 64.13 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 25 DIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISsrvvneiepkdrdiamvfqnyalyphmsvarnmafslehrg 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD----------------------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 105 gskteiaervswaadilGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLG 184
Cdd:cd03222 60 -----------------GITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|..
gi 1654818414 185 VTTVYVTHDQVEAMTMADKIVV 206
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHV 144
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-207 |
6.47e-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: 66.35 E-value: 6.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 29 GEFVVLVGPSGCGKSTLLRMIAGLETVTSGDIsissrvvnEIEPKDRDIAMVFQNYALYPHMSVARN------------- 95
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKRFRGTELQDYFKKLANgeikvahkpqyvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 ---MAFSlehrgGSKTEIAERV------SWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:COG1245 171 lipKVFK-----GTVRELLEKVdergklDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1654818414 167 KLRVVMRGEIKGLhQRLGVTTVYVTHDQveAM--TMADKIVVM 207
Cdd:COG1245 246 YQRLNVARLIREL-AEEGKYVLVVEHDL--AIldYLADYVHIL 285
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-229 |
1.37e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 21 GVDIDIADGEFVVLVGPSGCGKSTLL----RMIagleTVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPHmSVAR 94
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 95 NMAFSLEhrgGSKTEIaervsWAAdiLGLTPLLERF--------PRQLSG------GQRQRVAMGRAIVRNPQVF-LFDE 159
Cdd:PTZ00243 1403 NVDPFLE---ASSAEV-----WAA--LELVGLRERVasesegidSRVLEGgsnysvGQRQLMCMARALLKKGSGFiLMDE 1472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 160 PLSNLDAKLRVVMRGEIKGLHQRLGVTTvyVTHdQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPF 229
Cdd:PTZ00243 1473 ATANIDPALDRQIQATVMSAFSAYTVIT--IAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
78-208 |
1.56e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQNYALYpHMSVARNMAFslehrgGSKTEIAERVSWAADILGLTPLLERFPRQ-----------LSGGQRQRVAMGR 146
Cdd:PTZ00265 1299 SIVSQEPMLF-NMSIYENIKF------GKEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIAR 1371
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 147 AIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHdQVEAMTMADKIVVMN 208
Cdd:PTZ00265 1372 ALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFN 1432
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-166 |
1.91e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 62.26 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 29 GEFVVLVGPSGCGKSTLLRMIAGLET--VTSGDISISSRvvneiePKD----RDIAMVFQNYALYPHMSVARNMAFSLEH 102
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGR------PLDknfqRSTGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 103 RGgskteiaervswaadilgltpllerfprqLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:cd03232 107 RG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
235-278 |
3.14e-11 |
|
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: 57.98 E-value: 3.14e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1654818414 235 GSPAMNFIKGRLTASGF--EADGVVLPLPPGPATGEAIY-------GIRPEHF 278
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLlvLGGGVTLPLPEGQVLALKLYvgkevilGIRPEHI 53
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-195 |
3.32e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNeiepKDR-----DIAMVFQNYALYPHMSVA 93
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLctyqkQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 94 RNMAFSLeHRGGSKTEIAERVSwaadILGLTPLLErFP-RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVM 172
Cdd:PRK13540 93 ENCLYDI-HFSPGAVGITELCR----LFSLEHLID-YPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|...
gi 1654818414 173 RGEIKGlHQRLGVTTVYVTHDQV 195
Cdd:PRK13540 167 ITKIQE-HRAKGGAVLLTSHQDL 188
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-213 |
4.40e-11 |
|
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: 63.66 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVneiEPKDRD-----IAMVFQNYALYPHMSvarnm 96
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREayrqlFSAVFSDFHLFDRLL----- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 97 afslehrGGSKTEIAERVswaadilglTPLLERF--------------PRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLS 162
Cdd:COG4615 423 -------GLDGEADPARA---------RELLERLeldhkvsvedgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAA 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1654818414 163 NLDAKLRVVMRGEIKGLHQRLGVTTVYVTHD----QVeamtmADKIVVMNAGRVE 213
Cdd:COG4615 487 DQDPEFRRVFYTELLPELKARGKTVIAISHDdryfDL-----ADRVLKMDYGKLV 536
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
29-167 |
8.45e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.82 E-value: 8.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 29 GEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRdIAMVFQNYAL---YPHMSVARNMAFSLEHRG- 104
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-VAYVPQSEEVdwsFPVLVEDVVMMGRYGHMGw 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654818414 105 --GSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK 167
Cdd:PRK15056 112 lrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-210 |
8.78e-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: 61.80 E-value: 8.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRV-----VNEIEP---KDRDIAMVfqNYALYPHMSVA 93
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIsfssqFSWIMPgtiKENIIFGV--SYDEYRYKSVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 94 RnmAFSLEHrggSKTEIAERVSWAADILGLTpllerfprqLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDaklrVVMR 173
Cdd:cd03291 134 K--ACQLEE---DITKFPEKDNTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGYLD----VFTE 195
|
170 180 190
....*....|....*....|....*....|....*....
gi 1654818414 174 GEI--KGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAG 210
Cdd:cd03291 196 KEIfeSCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-229 |
9.13e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 9.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPHmSVARNM 96
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFSG-TVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 97 AFSLEHRGGSKTEIAERVSWAADI----LGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVM 172
Cdd:PLN03232 1331 DPFSEHNDADLWEALERAHIKDVIdrnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 173 RGEIKglhQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYDRPANPF 229
Cdd:PLN03232 1411 QRTIR---EEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
22-236 |
9.86e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 62.23 E-value: 9.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLE----TVTSGDISISSRVVNEIEPKDR------DIAMVFQN--YALYPH 89
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQEpsSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 90 MSVARNMAFSL----------EHRGGSKTEIAE---RVSwaadILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFL 156
Cdd:COG4170 106 AKIGDQLIEAIpswtfkgkwwQRFKWRKKRAIEllhRVG----IKDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 157 FDEPLSNLDAK-----LRVVMRgeikgLHQRLGVTTVYVTHDqVEAMT-MADKIVVMNAGRVEQCGAPLELYDRPANPFV 230
Cdd:COG4170 182 ADEPTNAMESTtqaqiFRLLAR-----LNQLQGTSILLISHD-LESISqWADTITVLYCGQTVESGPTEQILKSPHHPYT 255
|
....*.
gi 1654818414 231 AGFIGS 236
Cdd:COG4170 256 KALLRS 261
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-192 |
1.05e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 62.84 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISIssrvvneiePKDRDIAMVFQNyalyPHMSVAR---- 94
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQR----PYMTLGTlrdq 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 95 ----NMAFSLEHRGGSKTEIAERVswaaDILGLTPLLER---------FPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPL 161
Cdd:TIGR00954 535 iiypDSSEDMKRRGLSDKDLEQIL----DNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|.
gi 1654818414 162 SnldaKLRVVMRGEIKGLHQRLGVTTVYVTH 192
Cdd:TIGR00954 611 S----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-207 |
1.13e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 28 DGEFVVLVGPSGCGKSTLLRMIAG------------------------------LETVTSGDIsissRVVNEIEPKDRdI 77
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepswdevlkrfrgtelqnyFKKLYNGEI----KVVHKPQYVDL-I 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 78 AMVFQnyalyphmsvarnmafslehrgGSKTEIAERVSWA------ADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRN 151
Cdd:PRK13409 173 PKVFK----------------------GKVRELLKKVDERgkldevVERLGLENILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 152 PQVFLFDEPLSNLDAKLRVVMRGEIKGLHQrlGVTTVYVTHDQVEAMTMADKIVVM 207
Cdd:PRK13409 231 ADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-216 |
1.86e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.43 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 5 TLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLE--TVTSGDISISSRVVNEIEPKDRD---IAM 79
Cdd:CHL00131 9 EIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhlgIFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 80 VFQNYALYPHMSVAR--NMAFSLEHRGGSKTEIA-----ERVSWAADILGLTP-LLERFPRQ-LSGGQRQRVAMGRAIVR 150
Cdd:CHL00131 89 AFQYPIEIPGVSNADflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNVNEgFSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 151 NPQVFLFDEPLSNLDAK-LRVVMrgeiKGLHQRLGVTTVYV--THDQ-VEAMTMADKIVVMNAGRVEQCG 216
Cdd:CHL00131 169 DSELAILDETDSGLDIDaLKIIA----EGINKLMTSENSIIliTHYQrLLDYIKPDYVHVMQNGKIIKTG 234
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-234 |
2.78e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.59 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGletVTSGDISISSR--VVNEIE-----PKDR------DIAMVFQ--NYAL 86
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICG---VTKDNWRVTADrmRFDDIDllrlsPRERrklvghNVSMIFQepQSCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 87 YPHMSVARNM-----------------------AFSLEHRGGSKTEiaervswaADILGltplleRFPRQLSGGQRQRVA 143
Cdd:PRK15093 103 DPSERVGRQLmqnipgwtykgrwwqrfgwrkrrAIELLHRVGIKDH--------KDAMR------SFPYELTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 144 MGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYD 223
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
|
250
....*....|.
gi 1654818414 224 RPANPFVAGFI 234
Cdd:PRK15093 249 TPHHPYTQALI 259
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-169 |
3.66e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 58.73 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 36 GPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKdrDIAMVFQNYALYPHMSVARNMAFSLEHRGGSKTEIAervs 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP--YCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYA---- 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 116 wAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLR 169
Cdd:PRK13541 107 -AIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-257 |
5.77e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCG--KSTLLRMIAGLET--------VTSGDISISSRVVNEIEPK 73
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAgrrpwrf*TWCANRRALRRTIG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 74 DRDIAMVFQNYA-LYphmSVARNMAFSLEHRGGSKTEIAERVSwaadilgLTPLLERFPRQLSGGQRQRVAMGRAIVRNP 152
Cdd:NF000106 94 R*GRRESFSGREnLY---MIGR*LDLSRKDARARADELLERFS-------LTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 153 QVFLFDEPLSNLDAKLRVVMRGEIKGLhQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCGAPLELYD--------- 223
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTkvggrtlqi 242
|
250 260 270
....*....|....*....|....*....|....*
gi 1654818414 224 RPANPF-VAGFIGSPAMNFIKGRLTASGFEADGVV 257
Cdd:NF000106 243 RPAHAAeLDRMVGAIAQAGLDGIAGATADHEDGVV 277
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-210 |
6.00e-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: 60.69 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRvvneiepkdrdIAMVFQNYALYPHmSVARNMAFSLE 101
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNIIFGLS 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 102 HRGGSKTEIAERVSWAADILGL-----TPLLERfPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDaklrVVMRGEI 176
Cdd:TIGR01271 513 YDEYRYTSVIKACQLEEDIALFpekdkTVLGEG-GITLSGGQRARISLARAVYKDADLYLLDSPFTHLD----VVTEKEI 587
|
170 180 190
....*....|....*....|....*....|....*.
gi 1654818414 177 --KGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAG 210
Cdd:TIGR01271 588 feSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-212 |
8.97e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDR-DIAMVF-----QNYALYPHMSVARN 95
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 MAfSLEH-------RGGSKTEIAERVSWAADILGLTPllERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKL 168
Cdd:PRK15439 362 VC-ALTHnrrgfwiKPARENAVLERYRRALNIKFNHA--EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654818414 169 RVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:PRK15439 439 RNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-165 |
1.01e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 9 VKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVvneiepkdrDIAMVFQnyalyp 88
Cdd:PRK11819 330 LSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV---------KLAYVDQ------ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 89 hmsvarnmafSLEHRGGSKTeIAERVSWAADILGL----TP---LLERF----PRQ------LSGGQRQRVAMGRAIVRN 151
Cdd:PRK11819 395 ----------SRDALDPNKT-VWEEISGGLDIIKVgnreIPsraYVGRFnfkgGDQqkkvgvLSGGERNRLHLAKTLKQG 463
|
170
....*....|....
gi 1654818414 152 PQVFLFDEPLSNLD 165
Cdd:PRK11819 464 GNVLLLDEPTNDLD 477
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-214 |
2.16e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.15 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 8 SVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETvTSGDISISSRVVNEIEPKDRDIAmvfqnYALY 87
Cdd:TIGR01271 1224 TAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA-----FGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 88 PHMSVARNMAFSLE---HRGGSKTEIaervsW-AADILGLTPLLERFPRQL-----------SGGQRQRVAMGRAIVRNP 152
Cdd:TIGR01271 1298 PQKVFIFSGTFRKNldpYEQWSDEEI-----WkVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKA 1372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 153 QVFLFDEPLSNLDAKLRVVMRgeiKGLHQRLGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQ 214
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIR---KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-210 |
1.27e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKDRD---IAMVFQ 82
Cdd:PRK10762 7 LKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPHMSVARNMAFSLEhrggsKTEIAERVSW-----AADILgLTPL-LERFPRQLSG----GQRQRVAMGRAIVRNP 152
Cdd:PRK10762 87 ELNLIPQLTIAENIFLGRE-----FVNRFGRIDWkkmyaEADKL-LARLnLRFSSDKLVGelsiGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 153 QVFLFDEPLSNL----DAKLRVVMRgEIKGlhQRLGVttVYVTHDQVEAMTMADKIVVMNAG 210
Cdd:PRK10762 161 KVIIMDEPTDALtdteTESLFRVIR-ELKS--QGRGI--VYISHRLKEIFEICDDVTVFRDG 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-193 |
1.41e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.10 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 34 LVGPSGCGKSTLLRMIAGLETVTSGDISISsrvvneiepKDRDIAMVFQNYALYPHMSVARN------------------ 95
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQ---------PGIKVGYLPQEPQLDPTKTVRENveegvaeikdaldrfnei 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 -MAFS-------------------LEHRGGSktEIAERVSWAADILgltplleRFP------RQLSGGQRQRVAMGRAIV 149
Cdd:TIGR03719 107 sAKYAepdadfdklaaeqaelqeiIDAADAW--DLDSQLEIAMDAL-------RCPpwdadvTKLSGGERRRVALCRLLL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1654818414 150 RNPQVFLFDEPLSNLDAKlrVVMRGEiKGLHQRLGvTTVYVTHD 193
Cdd:TIGR03719 178 SKPDMLLLDEPTNHLDAE--SVAWLE-RHLQEYPG-TVVAVTHD 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-167 |
1.44e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 29 GEFVVLVGPSGCGKSTLLRMIAglETVTSGDISISSRVVNEIePKD----RDIAMVFQNYALYPHMSVARNMAFSLEHRG 104
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGR-PLDssfqRSIGYVQQQDLHLPTSTVRESLRFSAYLRQ 865
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 105 GSKTEIAER---VSWAADILGLTPLLERF---PRQ-LSGGQRQRVAMGRAIVRNPQVFLF-DEPLSNLDAK 167
Cdd:TIGR00956 866 PKSVSKSEKmeyVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQ 936
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-213 |
2.91e-08 |
|
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: 55.22 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGL-ETVTSGDISISSRVVNEIEPKD---RDIAMVFQN---YALYPHMSVAR 94
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 95 NMAFSLEHRGGSKTEI---AERVSWAADILGL-----TPLLErfPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:TIGR02633 359 NITLSVLKSFCFKMRIdaaAELQIIGSAIQRLkvktaSPFLP--IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1654818414 167 KLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVE 213
Cdd:TIGR02633 437 GAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-204 |
3.25e-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: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 29 GEFVVLVGPSGCGKSTLLRMIAgletvtsgdisissrvvNEIEPKDRDIAMVfqnyalyphmsvarnmafslehrggskt 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALA-----------------RELGPPGGGVIYI---------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 109 eIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLRVVMRGEI-----KGLHQRL 183
Cdd:smart00382 37 -DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSEK 115
|
170 180
....*....|....*....|.
gi 1654818414 184 GVTTVYVTHDQVEAMTMADKI 204
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLRR 136
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-193 |
7.80e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 34 LVGPSGCGKSTLLRMIAGLETVTSGDISISS--RV-VNEIEPKDRDIAMVFQN------------------YALYphmsv 92
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAPgiKVgYLPQEPQLDPEKTVRENveegvaevkaaldrfneiYAAY----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 93 ARNMAFS-------------LEHRGG----SKTEIAervswaADILgltplleRFP------RQLSGGQRQRVAMGRAIV 149
Cdd:PRK11819 113 AEPDADFdalaaeqgelqeiIDAADAwdldSQLEIA------MDAL-------RCPpwdakvTKLSGGERRRVALCRLLL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1654818414 150 RNPQVFLFDEPLSNLDAK----LRvvmrgeiKGLHQRLGvTTVYVTHD 193
Cdd:PRK11819 180 EKPDMLLLDEPTNHLDAEsvawLE-------QFLHDYPG-TVVAVTHD 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-165 |
1.22e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 2 APVTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAG-----------L--------ET-------- 54
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLfgrrrgsgETiwdikkhi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 55 --VTSG---DISISSRVVNEIepkdrdIAMVFQNYALYPHMSVARNMafslehrggskteIAERvsWAaDILGLTPLLER 129
Cdd:PRK10938 339 gyVSSSlhlDYRVSTSVRNVI------LSGFFDSIGIYQAVSDRQQK-------------LAQQ--WL-DILGIDKRTAD 396
|
170 180 190
....*....|....*....|....*....|....*..
gi 1654818414 130 FP-RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:PRK10938 397 APfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
10-216 |
1.51e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 10 KKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISissrvvneiepKDRDIAMVFQNYALYPH 89
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------RNGEVSVIAISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 90 MSVARNMAFSLEHRGGSKTEIAERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKLR 169
Cdd:PRK13546 100 LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1654818414 170 VVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGRVEQCG 216
Cdd:PRK13546 180 QKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-211 |
1.56e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVN---EIEPKDRDIAMVFQ 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPHMSVARNM--------AFSLEHRGGSKTEIAERVSWAADIlgltpllerFPRQ----LSGGQRQRVAMGRAIVR 150
Cdd:PRK10982 81 ELNLVLQRSVMDNMwlgryptkGMFVDQDKMYRDTKAIFDELDIDI---------DPRAkvatLSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 151 NPQVFLFDEPLSNLDAKLRVVMRGEIKGLHQRlGVTTVYVTHDQVEAMTMADKIVVMNAGR 211
Cdd:PRK10982 152 NAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-165 |
2.89e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 29 GEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVvneiepkdrDIAMvFQNY--ALYPHMSVARNMAfslehRGGS 106
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKL---------EVAY-FDQHraELDPEKTVMDNLA-----EGKQ 409
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 107 KTEIAER----VSWAADILgLTPLLERFP-RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:PRK11147 410 EVMVNGRprhvLGYLQDFL-FHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
17-174 |
2.99e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.95 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 17 ATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLE--TVTSGDISISSRVVNEIEPKDR---DIAMVFQNYALYPHMS 91
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAFQYPVEIPGVS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 92 VARNMAFSL----EHRGgskTEIAERVSWaADILGLTPLLERFPRQL---------SGGQRQRVAMGRAIVRNPQVFLFD 158
Cdd:PRK09580 95 NQFFLQTALnavrSYRG---QEPLDRFDF-QDLMEEKIALLKMPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCILD 170
|
170
....*....|....*..
gi 1654818414 159 EPLSNLDAK-LRVVMRG 174
Cdd:PRK09580 171 ESDSGLDIDaLKIVADG 187
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-212 |
3.07e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 21 GVDIDiadgEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVvneiepkdrDIAMVFQNYALYPHMSVARNMAFSL 100
Cdd:PLN03073 531 GIDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV---------RMAVFSQHHVDGLDLSSNPLLYMMR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 101 EHRGGSKTEIAERVSwaadILGLTPLLERFPR-QLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAKlrvVMRGEIKGL 179
Cdd:PLN03073 598 CFPGVPEQKLRAHLG----SFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD---AVEALIQGL 670
|
170 180 190
....*....|....*....|....*....|...
gi 1654818414 180 HQRLGvTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:PLN03073 671 VLFQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-221 |
4.13e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.87 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 22 VDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD--RDIAMVFQNYALYPHmSVARNM-AF 98
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrFKITIIPQDPVLFSG-SLRMNLdPF 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 99 slehrgGSKTEiaERVSWAADILGLTPLLERFP-----------RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK 167
Cdd:TIGR00957 1384 ------SQYSD--EEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 168 LRVVMRGEIKGLHQRLGVTTVYVTHDQVEAMTmadKIVVMNAGRVEQCGAPLEL 221
Cdd:TIGR00957 1456 TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT---RVIVLDKGEVAEFGAPSNL 1506
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
28-213 |
4.74e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.53 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 28 DGEFVVLVGPSGCGKSTLlrmIAGLETVTSGDISISSRVVNeiepKDRDIA----------MVFQN-----YALYPHMSV 92
Cdd:cd03240 21 FSPLTLIVGQNGAGKTTI---IEALKYALTGELPPNSKGGA----HDPKLIregevraqvkLAFENangkkYTITRSLAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 93 ARNMAFSleHRGGSKTeiaervswaadilgltpLLERFPRQLSGGQRQ------RVAMGRAIVRNPQVFLFDEPLSNLDA 166
Cdd:cd03240 94 LENVIFC--HQGESNW-----------------PLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 167 -----KLRVVMRGEIKGLHQRLGVttvyVTHDQvEAMTMADKIVvmnagRVE 213
Cdd:cd03240 155 enieeSLAEIIEERKSQKNFQLIV----ITHDE-ELVDAADHIY-----RVE 196
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-173 |
5.34e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 29 GEFVVLVGPSGCGKSTLLRMIAGLET--VTSGDISISSRVVNEiEPKDRDIAMVFQNYALYPHMSVARNMAFSLEHRGGS 106
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKKQ-ETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPK 984
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654818414 107 KTEIAERVSWAADILGLTPL------LERFP--RQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDAK-LRVVMR 173
Cdd:PLN03140 985 EVSKEEKMMFVDEVMELVELdnlkdaIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARaAAIVMR 1060
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
49-212 |
9.32e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 49 IAGL------ETVTS----------GDISISSRVVNEIEPKD---RDIAMVFQN---YALYPHMSVARNMAFSLEHR--- 103
Cdd:PRK13549 293 IAGLvgagrtELVQClfgaypgrweGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVGKNITLAALDRftg 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 104 GGSKTEIAERVSWAADILGL---TPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLDaklrVVMRGEIKGLH 180
Cdd:PRK13549 373 GSRIDDAAELKTILESIQRLkvkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID----VGAKYEIYKLI 448
|
170 180 190
....*....|....*....|....*....|....*
gi 1654818414 181 QRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:PRK13549 449 NQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-211 |
1.05e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.79 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 17 ATIHG---VDIDIADGEFVVLVGPSGCGKSTL----------LRMIAGLETVTSGDISISSR-VVNEIEPKDRDIAMVFQ 82
Cdd:cd03270 6 AREHNlknVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYARQFLGQMDKpDVDSIEGLSPAIAIDQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 83 NYALYPHMSVarnmafslehrgGSKTEI-------------AERVSWAADIlGLTPL-LERFPRQLSGGQRQRVAMGRAI 148
Cdd:cd03270 86 TTSRNPRSTV------------GTVTEIydylrllfarvgiRERLGFLVDV-GLGYLtLSRSAPTLSGGEAQRIRLATQI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 149 VRNPQ--VFLFDEPLSnldaklrvvmrgeikGLHQR--------------LGVTTVYVTHDQvEAMTMADKIVVM--NAG 210
Cdd:cd03270 153 GSGLTgvLYVLDEPSI---------------GLHPRdndrlietlkrlrdLGNTVLVVEHDE-DTIRAADHVIDIgpGAG 216
|
.
gi 1654818414 211 R 211
Cdd:cd03270 217 V 217
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-210 |
1.25e-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: 48.09 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRmiAGLETVtsgdisissrvvneiepKDRDIAMVFQNYALYPHMSVarnmaf 98
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYAS-----------------GKARLISFLPKFSRNKLIFI------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 99 slehrGGSKTEIAervswaadiLGLTPL-LERFPRQLSGGQRQRVAMGRAIVRNPQ--VFLFDEPLSNLDAKLRVVMRGE 175
Cdd:cd03238 66 -----DQLQFLID---------VGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEV 131
|
170 180 190
....*....|....*....|....*....|....*
gi 1654818414 176 IKGLHQrLGVTTVYVTHDqVEAMTMADKIVVMNAG 210
Cdd:cd03238 132 IKGLID-LGNTVILIEHN-LDVLSSADWIIDFGPG 164
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-212 |
2.27e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 4 VTLRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVvnEIEPKDRDIAMVFQN 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA--NIGYYAQDHAYDFEN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 84 yalypHMSVARNMAfslEHRGGSKTEIAERvswaaDILGltPLL------ERFPRQLSGGQRQRVAMGRAIVRNPQVFLF 157
Cdd:PRK15064 398 -----DLTLFDWMS---QWRQEGDDEQAVR-----GTLG--RLLfsqddiKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1654818414 158 DEPLSNLDaklrvvMRGeIKGLHQRLGV---TTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:PRK15064 463 DEPTNHMD------MES-IESLNMALEKyegTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-190 |
6.01e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 18 TIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISIS-SRVVN-EIEPKDRDIAMVFQnyalyphmsvaRN 95
Cdd:PRK10938 18 TLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfSHITRlSFEQLQKLVSDEWQ-----------RN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 96 ----MAFSLEHRGGSKTEI-------AERVSWAADILGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:PRK10938 87 ntdmLSPGEDDTGRTTAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180
....*....|....*....|....*.
gi 1654818414 165 DAKLRVVMRGEIKGLHQRlGVTTVYV 190
Cdd:PRK10938 167 DVASRQQLAELLASLHQS-GITLVLV 191
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-221 |
1.20e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 19 IHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISIssrvvNEIEPKDRDIAMVFQNYALYPHMSV--ARNM 96
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILI-----DGCDISKFGLMDLRKVLGIIPQAPVlfSGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 97 AFSL----EHRGGSKTEIAERVSWAADI----LGLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL---- 164
Cdd:PLN03130 1330 RFNLdpfnEHNDADLWESLERAHLKDVIrrnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVdvrt 1409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1654818414 165 DAKLRVVMRGEIKglhqrlGVTTVYVTHdQVEAMTMADKIVVMNAGRVEQCGAPLEL 221
Cdd:PLN03130 1410 DALIQKTIREEFK------SCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-212 |
1.37e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 18 TIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISSRVVNEIEPKD---RDIAMVFQ---NYALYPHMS 91
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainHGFALVTEerrSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 92 VARNMAFS--LEHRGG----SKTEIAERVSWAADILGL-TPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNL 164
Cdd:PRK10982 343 IGFNSLISniRNYKNKvgllDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1654818414 165 DaklrVVMRGEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVVMNAGRV 212
Cdd:PRK10982 423 D----VGAKFEIYQLIAELakkDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
109-221 |
1.61e-05 |
|
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: 46.54 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 109 EIAERVSWAADiLGLTPL-LERFPRQLSGGQRQRVAMGRAI------VrnpqVFLFDEPlsnldaklrvvmrgEIkGLHQ 181
Cdd:TIGR00630 464 EIRERLGFLID-VGLDYLsLSRAAGTLSGGEAQRIRLATQIgsgltgV----LYVLDEP--------------SI-GLHQ 523
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 182 R--------------LGVTTVYVTHDQvEAMTMADKIVVM------NAGRVEQCGAPLEL 221
Cdd:TIGR00630 524 RdnrrlintlkrlrdLGNTLIVVEHDE-DTIRAADYVIDIgpgageHGGEVVASGTPEEI 582
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-211 |
5.70e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 6 LRSVKKSYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIAGL--------------ETVTSGDISISSRvvneie 71
Cdd:NF040905 4 MRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyegeilfdgEVCRFKDIRDSEA------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 72 pkdRDIAMVFQNYALYPHMSVARNMAFSLEH-RGGskteiaeRVSWAADILGLTPLLERF-----PRQLSG----GQRQR 141
Cdd:NF040905 78 ---LGIVIIHQELALIPYLSIAENIFLGNERaKRG-------VIDWNETNRRARELLAKVgldesPDTLVTdigvGKQQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654818414 142 VAMGRAIVRNPQVFLFDEPLSNLD----AKLRVVMRgEIKGlhQrlGVTTVYVTHDQVEAMTMADKIVVMNAGR 211
Cdd:NF040905 148 VEIAKALSKDVKLLILDEPTAALNeedsAALLDLLL-ELKA--Q--GITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-165 |
1.05e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 12 SYGAFATIHGVDIDIADGEFVVLVGPSGCGKSTLLRMIA-----GL----------ETVTSGDISISSRVVN-EIEPK-- 73
Cdd:PLN03073 186 SVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGIpkncqilhveQEVVGDDTTALQCVLNtDIERTql 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 74 -DRDIAMVFQNYALypHMSVARNMAFSLEHRGGSKTEIAERV----------------SWAADIL-GL--TPLLE-RFPR 132
Cdd:PLN03073 266 lEEEAQLVAQQREL--EFETETGKGKGANKDGVDKDAVSQRLeeiykrlelidaytaeARAASILaGLsfTPEMQvKATK 343
|
170 180 190
....*....|....*....|....*....|...
gi 1654818414 133 QLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD 165
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
272-338 |
1.14e-04 |
|
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: 39.91 E-value: 1.14e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654818414 272 GIRPEHFELV--NHGLTANVLLVEPMGSETQVTMMLGNHQVVGVFRERVQA---QPGATIQVQPDLASIHLF 338
Cdd:pfam08402 2 AIRPEKIRLAaaANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHArppAPGDRVGLGWDPEDAHVL 73
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
23-207 |
2.03e-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: 41.19 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 23 DIDIADGEFVVLVGPSGCGKSTLLRMIAgletvtsgdisissrvvneiepkdrdiamvfqnYALYphmsvarnMAFSLEH 102
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------LALG--------GAQSATR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 103 RGGsktEIAERVSWAADIlgLTPLLERFprQLSGGQRQRVA----MGRAIVRNPQVFLFDEPLSNLDakLRVVMRGEIKG 178
Cdd:cd03227 54 RRS---GVKAGCIVAAVS--AELIFTRL--QLSGGEKELSAlaliLALASLKPRPLYILDEIDRGLD--PRDGQALAEAI 124
|
170 180 190
....*....|....*....|....*....|
gi 1654818414 179 LHQRLGVTTVYV-THDQvEAMTMADKIVVM 207
Cdd:cd03227 125 LEHLVKGAQVIViTHLP-ELAELADKLIHI 153
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
240-280 |
5.27e-04 |
|
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common architecture comprising two variable hydrophobic transmembrane domains (TMDs) that form the translocation pathway and two conserved hydrophilic ABC-ATPases that hydrolyze ATP. This is the C-terminal regulatory domain found at the ATPase subunit of CysA, a putative sulfate ABC transporter from Alicyclobacillus acidocaldarius. The regulatory domain of CysA is built up of an elongated beta-barrel composed of two beta-sandwiches that form a common hydrophobic core.
Pssm-ID: 465531 [Multi-domain] Cd Length: 43 Bit Score: 37.04 E-value: 5.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1654818414 240 NFIKGRLTASGFEADGVVLPLP--PGPATGEAIYGIRPEHFEL 280
Cdd:pfam17850 1 NLFHGRVEDGRVRIGGLALPLPelAGAEGSEVVAYVRPHDLEI 43
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
122-229 |
5.96e-04 |
|
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: 41.05 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 122 GLTPLLERFPRQLSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD-AKLRVVMRGEIKGLHQRlgvTTVYVTHdQVEAMTM 200
Cdd:cd03288 145 GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDmATENILQKVVMTAFADR---TVVTIAH-RVSTILD 220
|
90 100
....*....|....*....|....*....
gi 1654818414 201 ADKIVVMNAGRVEQCGAPLELYDRPANPF 229
Cdd:cd03288 221 ADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
29-61 |
8.56e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.07 E-value: 8.56e-04
10 20 30
....*....|....*....|....*....|...
gi 1654818414 29 GEFVVLVGPSGCGKSTLLRMIAGLETVTSGDIS 61
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
134-212 |
1.02e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654818414 134 LSGGQRQRVAMGRAIVRNPQVFLFDEPLSNLD--AKLrvvmrgEIKGLHQRL---GVTTVYVTHDQVEAMTMADKIVVMN 208
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgAKY------EIYTIINELaaeGKGVIVISSELPELLGMCDRIYVMN 478
|
....
gi 1654818414 209 AGRV 212
Cdd:NF040905 479 EGRI 482
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
36-70 |
2.30e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 37.85 E-value: 2.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1654818414 36 GPSGCGKSTLLRMIA---GLETVTSGDISIS--SRVVNEI 70
Cdd:cd02020 6 GPAGSGKSTVAKLLAkklGLPYLDTGGIRTEevGKLASEV 45
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
26-50 |
2.37e-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: 39.00 E-value: 2.37e-03
10 20
....*....|....*....|....*.
gi 1654818414 26 IADGE-FVVLVGPSGCGKSTLLRMIA 50
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRRLL 64
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
28-64 |
3.41e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.91 E-value: 3.41e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1654818414 28 DGEFVVLVGPSGCGKSTLLRMIAGLETVTSGDISISS 64
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEISEKL 141
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
32-49 |
3.53e-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: 3.53e-03
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
18-46 |
4.27e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 4.27e-03
10 20
....*....|....*....|....*....
gi 1654818414 18 TIHGVDIDIADGEFVVLVGPSGCGKSTLL 46
Cdd:pfam13555 11 TFDGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| HprK |
COG1493 |
Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction ... |
18-50 |
4.54e-03 |
|
Serine kinase of the HPr protein, regulates carbohydrate metabolism [Signal transduction mechanisms];
Pssm-ID: 441102 [Multi-domain] Cd Length: 142 Bit Score: 37.08 E-value: 4.54e-03
10 20 30
....*....|....*....|....*....|....
gi 1654818414 18 TIHGVDIDIaDGEFVVLVGPSGCGKSTL-LRMIA 50
Cdd:COG1493 1 TLHGVLVDV-GGRGVLITGPSGSGKSELaLELIK 33
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
23-50 |
6.26e-03 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 37.23 E-value: 6.26e-03
10 20
....*....|....*....|....*...
gi 1654818414 23 DIDIADGEFVVLVGPSGCGKSTLLRMIA 50
Cdd:cd03243 23 DINLGSGRLLLITGPNMGGKSTYLRSIG 50
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
36-60 |
6.45e-03 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 37.09 E-value: 6.45e-03
10 20
....*....|....*....|....*...
gi 1654818414 36 GPSGCGKSTLLRMIA---GLETVTSGDI 60
Cdd:PRK04182 7 GPPGSGKTTVARLLAeklGLKHVSAGEI 34
|
|
| |
