|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-359 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 586.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 161 LSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSPKMN 240
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 241 FLTAVVVEaqpGRAVIAlesnpETRLPVPIAEPVEAGTKVTLGIRPEHFADAGAGDADLTVAIDVAEHLGNTSYIYAAIG 320
Cdd:COG3839 241 LLPGTVEG---GGVRLG-----GVRLPLPAALAAAAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRLG 312
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1037261085 321 SEQLIIERPESRTAGNRETLTVGLPARHTFLFDGA-GKRL 359
Cdd:COG3839 313 GQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAEtGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-358 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 526.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAM 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 80 VFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 160 PLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSPKM 239
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 240 NFLTAVVVEAQpgravIALESNPETRLPVPIAEPVEAGTKVTLGIRPEHFADAGAGDAdLTVAIDVAEHLGNTSYIYAAI 319
Cdd:PRK11650 241 NLLDGRVSADG-----AAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIALSSAEGG-VPLTVDTVELLGADNLAHGRW 314
|
330 340 350
....*....|....*....|....*....|....*....
gi 1037261085 320 GSEQLIIERPESRTAGNRETLTVGLPARHTFLFDGAGKR 358
Cdd:PRK11650 315 GGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADTGR 353
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-359 |
0e+00 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 518.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 161 LSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSPKMN 240
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 241 FLTAVVVEAQPGRAVIALESNPETRLPVPiAEPVEAGTKVTLGIRPEHFADAGAGDADLTVAIDVAEHLGNTSYIYAAI- 319
Cdd:PRK11000 241 FLPVKVTATAIEQVQVELPNRQQVWLPVE-GRGVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGNETQIHIQIp 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1037261085 320 GSEQLIIER-PESRTAGNRETLTVGLPARHTFLF--DG-AGKRL 359
Cdd:PRK11000 320 AIRQNLVYRqNDVVLVEEGATFAIGLPPERCHLFreDGtACRRL 363
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-352 |
1.10e-157 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 446.08 E-value: 1.10e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 161 LSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGspKMN 240
Cdd:COG3842 163 LSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--EAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 241 FLTAVVVEAQPGRAVIalesnPETRLPVPIAEPVEAGTKVTLGIRPEHFA-DAGAGDADLTVAIDVAEHLGNTSYIYAAI 319
Cdd:COG3842 241 LLPGTVLGDEGGGVRT-----GGRTLEVPADAGLAAGGPVTVAIRPEDIRlSPEGPENGLPGTVEDVVFLGSHVRYRVRL 315
|
330 340 350
....*....|....*....|....*....|....*.
gi 1037261085 320 GS-EQLIIERPESRTAGNR--ETLTVGLPARHTFLF 352
Cdd:COG3842 316 GDgQELVVRVPNRAALPLEpgDRVGLSWDPEDVVVL 351
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
9.46e-133 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 377.75 E-value: 9.46e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQS 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 164 LDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-235 |
1.12e-116 |
|
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: 337.67 E-value: 1.12e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQS 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 164 LDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVG 235
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-347 |
9.57e-116 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 339.43 E-value: 9.57e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 3 ELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN-DVEPADRGIAMVF 81
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 82 QSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 162 SNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSpkMNF 241
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGC--VNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 242 LTAVVveaQPGRAVIAlesnpetRLPVPIAEPVEAGtKVTLGIRPEH--FADAGAGDADLTVAIDVAEHLGNTSYIYAAI 319
Cdd:COG1118 240 LRGRV---IGGQLEAD-------GLTLPVAEPLPDG-PAVAGVRPHDieVSREPEGENTFPATVARVSELGPEVRVELKL 308
|
330 340
....*....|....*....|....*....
gi 1037261085 320 -GSEQLIIERPESRTAGNRETLTVGLPAR 347
Cdd:COG1118 309 eDGEGQPLEAEVTKEAWAELGLAPGDPVY 337
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-287 |
3.47e-114 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 336.53 E-value: 3.47e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQS 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 164 LDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGspKMNFLT 243
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINIFD 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1037261085 244 AVVVEAQPGRAVIAlesNPE-TRLPVPIAEPVEAGTKVTLGIRPE 287
Cdd:PRK09452 253 ATVIERLDEQRVRA---NVEgRECNIYVNFAVEPGQKLHVLLRPE 294
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
9.48e-112 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 324.47 E-value: 9.48e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQS 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 164 LDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-312 |
4.99e-105 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 312.36 E-value: 4.99e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMV 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 161 LSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGspKMN 240
Cdd:TIGR03265 162 LSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG--EVN 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 241 FLTAVVveAQPGRAVIA---LESNPETRLPvpiaepveaGTKVTLGIRPEHFADAGAGDADLTVAIDVAEH--LGNT 312
Cdd:TIGR03265 240 WLPGTR--GGGSRARVGgltLACAPGLAQP---------GASVRLAVRPEDIRVSPAGNAANLLLARVEDMefLGAF 305
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-287 |
1.99e-95 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 288.05 E-value: 1.99e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 2 AELSLTNIVKRFG-GFEIIH---GANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVND-----VEP 72
Cdd:NF040933 1 VTVRVENVTKIFKkGKKEVValdNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 73 ADRGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREP 152
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 153 EVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAG 232
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 233 FVGspKMNFLTAVVVEAQpgravIALESNPETRLPVPIAEpveaGTKVTLGIRPE 287
Cdd:NF040933 241 LIG--DINLLEGKVEEEG-----LVDGNDLKIPLPNPKLE----AGEVIIGIRPE 284
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-236 |
8.42e-95 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 282.31 E-value: 8.42e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 8 NIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQSYALY 87
Cdd:cd03296 7 NVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 88 PHLTVEENLSFGLRM----NGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03296 87 RHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 164 LDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGS 236
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-287 |
1.44e-94 |
|
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: 284.77 E-value: 1.44e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 35 VGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRV 114
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 115 SHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQ 194
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 195 TEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSpkMNFLTAVVVEAQPGRAVIAleSNPETRLPVPIAEPV 274
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE--INVFEATVIERKSEQVVLA--GVEGRRCDIYTDVPV 237
|
250
....*....|...
gi 1037261085 275 EAGTKVTLGIRPE 287
Cdd:TIGR01187 238 EKDQPLHVVLRPE 250
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-327 |
1.11e-90 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 275.83 E-value: 1.11e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQS 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 164 LDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSpkmnflt 243
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGD------- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 244 AVVVEAQPGRAVIALEsnpETRLPVPIA-EPVEAGTKVTLGIRPEHFADAGAGDADLTVAIDVAEHLGNTSYIYAAIGSE 322
Cdd:PRK11432 240 ANIFPATLSGDYVDIY---GYRLPRPAAfAFNLPDGECTVGVRPEAITLSEQGEESQRCTIKHVAYMGPQYEVTVDWHGQ 316
|
....*
gi 1037261085 323 QLIIE 327
Cdd:PRK11432 317 ELLLQ 321
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
1.27e-90 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 272.35 E-value: 1.27e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRF----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKvvnDVEPADRG 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK---PVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 IAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 157 FDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-235 |
3.03e-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: 3.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 6 LTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQSYA 85
Cdd:TIGR00968 3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 86 LYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 166 AELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVG 235
Cdd:TIGR00968 163 AKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-209 |
5.79e-87 |
|
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: 261.64 E-value: 5.79e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGG----FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAdrgIAM 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 80 VFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1037261085 160 PLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRA 209
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-250 |
1.00e-81 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 253.08 E-value: 1.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 8 NIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQSYALY 87
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 88 PHLTVEENLSFGLRM---NGNP-KADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PRK10851 87 RHMTVFDNIAFGLTVlprRERPnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 164 LDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGspKMNFLT 243
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG--EVNRLQ 244
|
....*..
gi 1037261085 244 AVVVEAQ 250
Cdd:PRK10851 245 GTIRGGQ 251
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-236 |
1.03e-81 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 251.16 E-value: 1.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 6 LTNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQ 82
Cdd:COG1125 4 FENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQI--TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:COG1125 84 QIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 161 LSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGS 236
Cdd:COG1125 164 FGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-235 |
5.76e-81 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 246.86 E-value: 5.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIiHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQS 83
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 164 LDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVG 235
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-287 |
1.38e-80 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 249.99 E-value: 1.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIiHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQS 83
Cdd:NF040840 2 IRIENLSKDWKEFKL-RDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:NF040840 81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 164 LDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSPkmNFLT 243
Cdd:NF040840 161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NIIE 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1037261085 244 AVVVEAQPGRaviALESNpetrlPVPIAEPVEAGTKVTLGIRPE 287
Cdd:NF040840 239 GVAEKGGEGT---ILDTG-----NIKIELPEEKKGKVRIGIRPE 274
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-325 |
8.06e-80 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 248.98 E-value: 8.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQS 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 164 LDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSpkMNFLT 243
Cdd:PRK11607 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVFE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 244 AVVVEAQPGRAVIaleSNPETRLPVPIAEPVEA--GTKVTLGIRPE--HFADAGAGDAdLTVAIDVAEH---LGNTSYIY 316
Cdd:PRK11607 258 GVLKERQEDGLVI---DSPGLVHPLKVDADASVvdNVPVHVALRPEkiMLCEEPPADG-CNFAVGEVIHiayLGDLSIYH 333
|
....*....
gi 1037261085 317 AAIGSEQLI 325
Cdd:PRK11607 334 VRLKSGQMI 342
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-238 |
1.90e-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: 232.96 E-value: 1.90e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMV 80
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADI--LQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALvgLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 159 EPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGSPK 238
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGADR 240
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-210 |
4.75e-75 |
|
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: 229.77 E-value: 4.75e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVND----VEPADRGIAM 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 80 VFQSYALYPHLTVEENLSFGlrmngnpkadterrvshvadilqitelmkrrpkqLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 160 PLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-212 |
3.34e-74 |
|
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: 228.91 E-value: 3.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGG----FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG--- 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 ---IAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPE 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 154 VFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMtLADRIVVLRAGNI 212
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
9-216 |
2.26e-72 |
|
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: 224.10 E-value: 2.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 9 IVKRFGGFeiihgaNLEVK---DGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVE------PADRGIAM 79
Cdd:cd03297 6 IEKRLPDF------TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinlpPQQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 80 VFQSYALYPHLTVEENLSFGLRMngnpKADTERRVS--HVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGLKR----KRNREDRISvdELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 158 DEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
8-285 |
7.46e-72 |
|
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: 227.68 E-value: 7.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 8 NIVKRFGGFEIihGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVND------VEPADRGIAMVF 81
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 82 QSYALYPHLTVEENLSFGLRMNgnPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:COG4148 84 QEARLFPHLSVRGNLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 162 SNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGfvGSPKMNF 241
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAGSV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1037261085 242 LTAVVVEAQPGRAVIALESnPETRLPVPiAEPVEAGTKVTLGIR 285
Cdd:COG4148 240 LEATVAAHDPDYGLTRLAL-GGGRLWVP-RLDLPPGTRVRVRIR 281
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-213 |
1.08e-70 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 220.30 E-value: 1.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFG----GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG--- 76
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 ---IAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPE 153
Cdd:COG1136 85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 154 VFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQtEAMTLADRIVVLRAGNIE 213
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-234 |
1.97e-69 |
|
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: 218.67 E-value: 1.97e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 9 IVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD------RGIAMVFQ 82
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 163 NLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFV 234
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-235 |
2.37e-69 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 216.93 E-value: 2.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIihGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQS 83
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 164 LDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVG 235
Cdd:COG3840 160 LDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
9.53e-69 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 215.70 E-value: 9.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGK-VVNDVEPADRGIAMVFQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 163 NLDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-228 |
1.66e-68 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 214.86 E-value: 1.66e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN----DVEPADRGIAM 79
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 80 VFQSYALYPHLTVEENLSFGLRM-NGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 159 EPLSNLDAELrVQmrvEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQ 228
Cdd:COG1126 162 EPTSALDPEL-VG---EVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-235 |
2.39e-65 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 211.25 E-value: 2.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 11 KRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD------RGIAMVFQSY 84
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 85 ALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 165 DAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVG 235
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-230 |
6.28e-65 |
|
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: 205.98 E-value: 6.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD-----RGIA 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVFQSYALYPHLTVEENLSFGLRMNGN-PKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 158 DEPLSNLD-------AELrvqmrveISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLY--DDPA-N 227
Cdd:COG1127 166 DEPTAGLDpitsaviDEL-------IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLasDDPWvR 238
|
...
gi 1037261085 228 QFV 230
Cdd:COG1127 239 QFL 241
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
3.84e-64 |
|
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: 204.27 E-value: 3.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFG----GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGI 77
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVFQSY--ALYPHLTVEENLSFGLRMNGNPkaDTERRVSHVADILQIT-ELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 155 FLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPAN 227
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-225 |
5.76e-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: 5.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQsyalYP--- 88
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQ----NPddq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 89 --HLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDA 166
Cdd:COG1122 88 lfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 167 ELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:COG1122 168 RGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-212 |
6.60e-64 |
|
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: 202.37 E-value: 6.60e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPA----DRGIAM 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 80 VFQSYALYPHLTVEENLSFGLR-MNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 159 EPLSNLDAElrvqMRVEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03262 161 EPTSALDPE----LVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-233 |
1.12e-63 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 202.63 E-value: 1.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 8 NIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGI----AMVFQS 83
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFG-LRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:PRK09493 86 FYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 163 NLDAELrvqmRVEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGF 233
Cdd:PRK09493 166 ALDPEL----RHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-210 |
1.61e-62 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 198.85 E-value: 1.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 5 SLTNIVKRFGGFE--IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG--IAMV 80
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQsyalYP-----HLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:cd03225 81 FQ----NPddqffGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 156 LFDEPLSNLDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-212 |
1.24e-60 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 194.12 E-value: 1.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD-----RGI 77
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 158 DEPLSNLDAELRVQ-MRVeISRLHkQLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG2884 162 DEPTGNLDPETSWEiMEL-LEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-225 |
2.08e-59 |
|
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: 199.74 E-value: 2.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRF-----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD---- 74
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 -RGIAMVFQ--SYALYPHLTVEENLSFGLRMNGN-PKADTERRVSHVADILQI-TELMKRRPKQLSGGQRQRVAIGRAIV 149
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 150 REPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-229 |
4.41e-59 |
|
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: 190.79 E-value: 4.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD-----RGIA 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVFQSYALYPHLTVEENLSFGLRMNGN-PKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 158 DEPLSNLD---AELRVQMrveISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLY--DDPA-NQF 229
Cdd:cd03261 161 DEPTAGLDpiaSGVIDDL---IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPLvRQF 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-212 |
1.68e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 188.49 E-value: 1.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVF 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 82 QSYALYPHlTVEENLSFGLRMNGnpKADTERRVSHVADILQITE-LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 161 LSNLDAELRVqmRVE--ISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG4619 158 TSALDPENTR--RVEelLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-216 |
3.23e-58 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 188.10 E-value: 3.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRF----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG--- 76
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 --IAMVFQSY--ALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQI---TELMKRRPKQLSGGQRQRVAIGRAIV 149
Cdd:cd03257 82 keIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 150 REPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-218 |
1.31e-57 |
|
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: 187.56 E-value: 1.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG--IAMVF 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELArrIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 82 QSYALYPHLTVEENLSFG----LRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:COG1120 82 QEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 158 DEPLSNLDaeLRVQMRV--EISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:COG1120 162 DEPTSHLD--LAHQLEVleLLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-232 |
4.45e-57 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 186.61 E-value: 4.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGF----EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDveP-ADR 75
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PgADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 76 GIamVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:COG4525 79 GV--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 156 LFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLrAGNIEQIGAPLDLydDPANQFVAG 232
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM-SPGPGRIVERLEL--DFSRRFLAG 230
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-229 |
4.51e-57 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 186.03 E-value: 4.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD-----RGI 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVFQSYALYPHLTVEENLSFGL--RMNG-------NPKADTERrVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAI 148
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRlgRTSTwrsllglFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 149 VREPEVFLFDEPLSNLDAEL-RVQMRVeISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIeqigapldLYDDPAN 227
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV--------VFDGPPA 232
|
..
gi 1037261085 228 QF 229
Cdd:COG3638 233 EL 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-223 |
7.57e-57 |
|
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: 185.06 E-value: 7.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGK-VVNDVEPADRGIAMVFQ 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 163 NLDAELRVQMRvEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYD 223
Cdd:COG4555 162 GLDVMARRLLR-EILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
7.87e-54 |
|
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: 174.89 E-value: 7.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG-IAMVFQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 SYALYPHLTVEENLsfglrmngnpkadterrvshvadilqitelmkrrpkQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1037261085 163 NLDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-212 |
5.61e-53 |
|
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: 174.22 E-value: 5.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 24 LEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQSYALYPHLTVEENLSFGLRMN 103
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 104 GNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQL 183
Cdd:cd03298 99 LKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAET 178
|
170 180
....*....|....*....|....*....
gi 1037261085 184 GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03298 179 KMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
7.01e-53 |
|
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: 182.41 E-value: 7.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRF--GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDIT---SGELRIGGKVVNDVEPADRG-- 76
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 IAMVFQS--YALYPhLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 155 FLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPA 226
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
8-226 |
7.02e-53 |
|
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: 178.38 E-value: 7.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 8 NIVKRFGGFEIihGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVE------PADRGIAMVF 81
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflpPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 82 QSYALYPHLTVEENLSFGLRmngnpKAD-TERRVS--HVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMK-----RARpSERRISfeRVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 159 EPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPA 226
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-237 |
1.38e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 177.19 E-value: 1.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRF----GGFEIIHGANLEVKDGEfvVF--VGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--- 74
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGE--IFgiIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 --RGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREP 152
Cdd:COG1135 80 arRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 153 EVFLFDEPLSNLDAE-----LRVqmrveISRLHKQLGTTMIYVTHDqteaM----TLADRIVVLRAGNIEQIGAPLDLYD 223
Cdd:COG1135 160 KVLLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLDVFA 230
|
250
....*....|....
gi 1037261085 224 DPANQFVAGFVGSP 237
Cdd:COG1135 231 NPQSELTRRFLPTV 244
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-232 |
1.47e-52 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 174.60 E-value: 1.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVV-------NDVEPADR- 75
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdGELVPADRr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 76 -------GIAMVFQSYALYPHLTVEENLSFG-LRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRA 147
Cdd:COG4598 89 qlqrirtRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 148 IVREPEVFLFDEPLSNLDAELrVQmrvEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:COG4598 169 LAMEPEVMLFDEPTSALDPEL-VG---EVLKVMRDLaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGN 244
|
250
....*....|..
gi 1037261085 225 PAN----QFVAG 232
Cdd:COG4598 245 PKSerlrQFLSS 256
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-216 |
4.65e-52 |
|
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: 172.37 E-value: 4.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGELRIGGKVVNDVEPAD---- 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 RGIAMVFQSYALYPhLTVEENLSFGLRMNG-NPKADTERRVSHVADILQITELMKRR--PKQLSGGQRQRVAIGRAIVRE 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 152 PEVFLFDEPLSNLDAELRvqMRVE--ISRLHKQlgTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03260 160 PEVLLLDEPTSALDPIST--AKIEelIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-224 |
4.83e-52 |
|
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: 172.75 E-value: 4.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFG-GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD-----RGI 77
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVFQSYALYPHLTVEENLSFGL--RMN-------GNPKADTErRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAI 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgRRStwrslfgLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 149 VREPEVFLFDEPLSNLDAELRVQ-MRVeISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-210 |
6.85e-52 |
|
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: 171.66 E-value: 6.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSltNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD----- 74
Cdd:TIGR02673 1 MIEFH--NVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 RGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:TIGR02673 79 RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 155 FLFDEPLSNLDAELRVQ-MRVeISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERiLDL-LKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-216 |
2.69e-51 |
|
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: 170.04 E-value: 2.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQSYALYPHLTVEENLSFGLRM 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 103 NGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQ 182
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|....
gi 1037261085 183 LGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-212 |
2.69e-50 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 168.27 E-value: 2.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 3 ELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD-------- 74
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSekairllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 RGIAMVFQSYALYPHLTVEENLSFG-LRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPE 153
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 154 VFLFDEPLSNLDAELRVQMrVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG4161 162 VLLFDEPTAALDPEITAQV-VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
7.72e-50 |
|
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: 166.60 E-value: 7.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGG----FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD----- 74
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 RGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 155 FLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-232 |
7.90e-50 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 166.68 E-value: 7.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQSYALYPHLTVEENLSFG--- 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 100 -LRMNgnpkADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISR 178
Cdd:PRK10771 99 gLKLN----AAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 179 LHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIeqigapldLYDDPANQFVAG 232
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI--------AWDGPTDELLSG 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-216 |
1.31e-49 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 166.34 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--------R 75
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSdkairelrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 76 GIAMVFQSYALYPHLTVEENL-SFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 155 FLFDEPLSNLDAELRVQMrVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:PRK11124 163 LLFDEPTAALDPEITAQI-VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-225 |
9.61e-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 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: 165.32 E-value: 9.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN-----DVEPADRGIAMVFQsyalYPH---- 89
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDLRKKVGLVFQ----FPEhqlf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 90 -LTVEENLSFGLRMNGNPKADTERRVSHVADILQITE-LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:TIGR04521 97 eETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 168 LRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:TIGR04521 177 GRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-221 |
1.19e-48 |
|
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: 174.25 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 3 ELSLTNIVKRFGGFE--IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIA 78
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVFQSYALYpHLTVEENLSFglrmnGNPKADTErRVSHVADILQITELMKRRPK-----------QLSGGQRQRVAIGRA 147
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITL-----GDPDATDE-EIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 148 IVREPEVFLFDEPLSNLDA--ELRVQMRveISRLHKqlGTTMIYVTHDqTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:COG2274 626 LLRNPRILILDEATSALDAetEAIILEN--LRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-266 |
1.31e-48 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 164.47 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRgiaMVFQS 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRmnGNPKADTERRVSHVAdilqITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLK--GQWRDAALQALAAVG----LADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 164 LDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGnieQIGapLDLYDDPANQFVagfVGSPKMNFLT 243
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIG--LDLTVDLPRPRR---RGSARLAELE 235
|
250 260
....*....|....*....|...
gi 1037261085 244 AVVVEaqpgrAVIALESNPETRL 266
Cdd:PRK11247 236 AEVLQ-----RVMSRGESEPTRL 253
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-221 |
2.04e-48 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 163.02 E-value: 2.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPaDRGIamVFQSYALYPHLTVEENLSF 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 99 GLR--MNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEI 176
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1037261085 177 SRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
7.87e-47 |
|
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: 158.44 E-value: 7.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFE--IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGK-VVNDVEPADRGIAMV 80
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 161 LSNLDAELRVQMRVEISRLhkQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-207 |
9.36e-47 |
|
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: 157.78 E-value: 9.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 6 LTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGK---VVNDVEPAD---RGIAM 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKASKfrrEKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 80 VFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 160 PLSNLDAElrvqMRVEISRLHKQL---GTTMIYVTHDqTEAMTLADRIVVL 207
Cdd:TIGR03608 161 PTGSLDPK----NRDEVLDLLLELndeGKTIIIVTHD-PEVAKQADRVIEL 206
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-228 |
1.35e-46 |
|
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: 158.62 E-value: 1.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 8 NIVKRFG-GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD-----RGIAMVF 81
Cdd:TIGR02315 6 NLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 82 QSYALYPHLTVEENLSFGlRMNGNP----------KADTERRVSHVaDILQITELMKRRPKQLSGGQRQRVAIGRAIVRE 151
Cdd:TIGR02315 86 QHYNLIERLTVLENVLHG-RLGYKPtwrsllgrfsEEDKERALSAL-ERVGLADKAYQRADQLSGGQQQRVAIARALAQQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 152 PEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQ 228
Cdd:TIGR02315 164 PDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRH 240
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-222 |
2.83e-46 |
|
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: 158.75 E-value: 2.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGG------KVVNDVEpadRGIAMVFQSyalyPH-- 89
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtldeENLWEIR---KKVGMVFQN----PDnq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 90 ---LTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDA 166
Cdd:TIGR04520 90 fvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 167 ELRVQMRVEISRLHKQLGTTMIYVTHDQTEAmTLADRIVVLRAGNIEQIGAPLDLY 222
Cdd:TIGR04520 170 KGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-210 |
3.34e-46 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 154.71 E-value: 3.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 5 SLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEP--ADRGIAMVFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 syalyphltveenlsfglrmngnpkadterrvshvadilqitelmkrrpkqLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1037261085 163 NLDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-226 |
4.71e-46 |
|
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: 157.51 E-value: 4.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEP---ADRGI 77
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPhriARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVFQSYALYPHLTVEENL---------------SFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRV 142
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 143 AIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGniEQI--GAPLD 220
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFG--RVIaeGTPAE 239
|
....*.
gi 1037261085 221 LYDDPA 226
Cdd:COG0411 240 VRADPR 245
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-209 |
1.10e-45 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 155.33 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAG-LEDI--TSGELRIGGKVVNDVEPADRGIAMV 80
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGLRmNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:COG4136 82 FQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1037261085 161 LSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMtLADRIVVLRA 209
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP-AAGRVLDLGN 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-209 |
1.19e-45 |
|
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: 154.94 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG-IAMVFQ 82
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 SYALYPHLTVEENLSFGLRMNGNPkaDTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLR--ADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1037261085 163 NLDAElRVQMRVEISRLHKQLGTTMIYVTHDQTEAmtLADRIVVLRA 209
Cdd:COG4133 161 ALDAA-GVALLAELIAAHLARGGAVLLTTHQPLEL--AAARVLDLGD 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-207 |
1.23e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.40 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKvvnDVEPADRGIAMV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPH--LTVEENLSFGL----RMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:COG1121 81 PQRAEVDWDfpITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 155 FLFDEPLSNLDAELRVQ-MRVeISRLHKQlGTTMIYVTHDQTEAMTLADRIVVL 207
Cdd:COG1121 161 LLLDEPFAGVDAATEEAlYEL-LRELRRE-GKTILVVTHDLGAVREYFDRVLLL 212
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-226 |
2.19e-45 |
|
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: 157.91 E-value: 2.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRF----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED---ITSGELRIGGKVVNDVEPAD-- 74
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 ----RGIAMVFQ-SY-ALYPHLTVEENLSFGLRMNGN-PKADTERRVSHVADILQIT---ELMKRRPKQLSGGQRQRVAI 144
Cdd:COG0444 82 kirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 145 GRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFEN 241
|
..
gi 1037261085 225 PA 226
Cdd:COG0444 242 PR 243
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-214 |
2.30e-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: 2.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFE----IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKvvnDVEPAD----- 74
Cdd:COG4181 9 IELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDedara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 ----RGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKAdtERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVR 150
Cdd:COG4181 86 rlraRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDA--RARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 151 EPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQteamTLA---DRIVVLRAGNIEQ 214
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP----ALAarcDRVLRLRAGRLVE 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-212 |
3.50e-45 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 154.10 E-value: 3.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 8 NIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVND-----VEPADRGIAMVF 81
Cdd:cd03292 5 NVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 82 QSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:cd03292 85 QDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 162 SNLDAElrvqMRVEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03292 165 GNLDPD----TTWEIMNLLKKInkaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-235 |
4.18e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 154.91 E-value: 4.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEP--ADRG-- 76
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsQQKGli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 ------IAMVFQSYALYPHLTVEENLSFG-LRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIV 149
Cdd:PRK11264 81 rqlrqhVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 150 REPEVFLFDEPLSNLDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP---- 225
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPqqpr 239
|
250
....*....|
gi 1037261085 226 ANQFVAGFVG 235
Cdd:PRK11264 240 TRQFLEKFLL 249
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
4.32e-45 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 162.23 E-value: 4.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 2 AELSLTNIVKRF-GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIA 78
Cdd:COG4988 335 PSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVFQSyalyPHL---TVEENLSFglrmnGNPKAdTERRVSHVADILQITELMKRRPK-----------QLSGGQRQRVAI 144
Cdd:COG4988 415 WVPQN----PYLfagTIRENLRL-----GRPDA-SDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 145 GRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKqlGTTMIYVTHDqTEAMTLADRIVVLRAGNIEQIGAPLDLY 222
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-212 |
8.33e-45 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 153.75 E-value: 8.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEP---ADRGIAMV 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENL----------SFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVR 150
Cdd:cd03219 81 FQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 151 EPEVFLFDEPLSNLDAELRVQMRVEISRLhKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-207 |
1.99e-44 |
|
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: 151.92 E-value: 1.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 5 SLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKvvnDVEPADRGIAMVFQSY 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 85 AL---YPhLTVEENLSFGL----RMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:cd03235 78 SIdrdFP-ISVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 158 DEPLSNLDaelrVQMRVEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVL 207
Cdd:cd03235 157 DEPFAGVD----PKTQEDIYELLRELrreGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-162 |
2.11e-44 |
|
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: 149.72 E-value: 2.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSYALYPHLTVEENL 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 97 SFGLRMNGNPKADTERRVSHVADILQITELMKRR----PKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-210 |
4.33e-44 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 149.84 E-value: 4.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGF--EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAM 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 80 VFQSYALYpHLTVEENLsfglrmngnpkadterrvshvadilqitelmkrrpkqLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 160 PLSNLDAELRVQMRVEISRLHKqlGTTMIYVTHDqTEAMTLADRIVVLRAG 210
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-216 |
5.83e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 159.56 E-value: 5.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSYALYpHLT 91
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 92 VEENLSFglrmnGNPKAdTERRVSHVADILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:COG1132 430 IRENIRY-----GRPDA-TDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 161 LSNLDA--ELRVQMRveISRLHKqlGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:COG1132 504 TSALDTetEALIQEA--LERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQG 556
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-221 |
5.87e-44 |
|
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: 150.98 E-value: 5.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 8 NIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGG-KVVNDVEPADRGIAMVFQSYAL 86
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhDVVREPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 87 YPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDA 166
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 167 ELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-224 |
5.95e-44 |
|
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: 151.05 E-value: 5.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADR---GIAMV 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGLRmnGNPKADTERRVSHVADILQI-TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAY--ARRRAKRKARLERVYELFPRlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 160 PLSNLdAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:cd03224 159 PSEGL-APKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-210 |
3.22e-43 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 150.24 E-value: 3.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDvEPADRGIamVFQS 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1037261085 164 LDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-226 |
6.25e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 151.42 E-value: 6.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRF---GGF-----EIIH---GANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEP 72
Cdd:COG4608 8 LEVRDLKKHFpvrGGLfgrtvGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 73 AD-----RGIAMVFQ-SYA-LYPHLTVEENLSFGLRMNG-NPKADTERRvshVADILQI----TELMKRRPKQLSGGQRQ 140
Cdd:COG4608 88 RElrplrRRMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGlASKAERRER---VAELLELvglrPEHADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 141 RVAIGRAIVREPEVFLFDEPLSNLDAELRVQ----MRveisRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVSIQAQvlnlLE----DLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250
....*....|
gi 1037261085 217 APLDLYDDPA 226
Cdd:COG4608 241 PRDELYARPL 250
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
7.55e-43 |
|
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: 146.81 E-value: 7.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 5 SLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG--IAMVFQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELArkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 syalyphltveenlsfglrmngnpkadterrvshVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 163 NLDaeLRVQMRV--EISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03214 127 HLD--IAHQIELleLLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-212 |
8.62e-43 |
|
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: 147.75 E-value: 8.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFQS 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMNGNPKADTERrvshVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1037261085 164 LDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-210 |
2.25e-42 |
|
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: 144.88 E-value: 2.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD---RGIAMV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FqsyalyphltveenlsfglrmngnpkadterrvshvadilqitelmkrrpkQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:cd03216 81 Y---------------------------------------------------QLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1037261085 161 LSNLDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-210 |
4.81e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 152.87 E-value: 4.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD---RGIAMV 80
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGLRMNGNP---KADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 158 DEPLSNLDAElrvqmrvEISRLHKQL------GTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:COG1129 165 DEPTASLTER-------EVERLFRIIrrlkaqGVAIIYISHRLDEVFEIADRVTVLRDG 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-226 |
1.56e-41 |
|
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: 145.12 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEP---ADRGI 77
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhriARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVFQSYALYPHLTVEENLSFGLRmNGNPKADTERRVSHVAD---ILQitELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAY-ARRDRAEVRADLERVYElfpRLK--ERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 155 FLFDEPLSNLdAELRVQ--MRVeISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPA 226
Cdd:COG0410 158 LLLDEPSLGL-APLIVEeiFEI-IRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-232 |
3.10e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 145.11 E-value: 3.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAE--LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD---- 74
Cdd:PRK10619 1 MSEnkLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 -----------RGIAMVFQSYALYPHLTVEEN-LSFGLRMNGNPKADTERRVSHVADILQITELMKRR-PKQLSGGQRQR 141
Cdd:PRK10619 81 vadknqlrllrTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 142 VAIGRAIVREPEVFLFDEPLSNLDAELrvqmRVEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPEL----VGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
250
....*....|....*...
gi 1037261085 219 LDLYDDPAN----QFVAG 232
Cdd:PRK10619 237 EQLFGNPQSprlqQFLKG 254
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-233 |
3.24e-41 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 149.03 E-value: 3.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD------RGI 77
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 158 DEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGF 233
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-221 |
1.44e-40 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 143.30 E-value: 1.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 5 SLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQ 82
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 SYALYPHLTVEENLSFGlRM---NGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:COG4604 83 ENHINSRLTVRELVAFG-RFpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 160 PLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:COG4604 162 PLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-212 |
3.89e-40 |
|
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: 140.97 E-value: 3.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRF----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGG-KVVNDVEPADRGIA 78
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 159 EPLSNLDAeLRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03266 162 EPTTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
2.69e-39 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 146.45 E-value: 2.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 2 AELSLTNIVKRF--GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGI 77
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVFQSyalyPHL---TVEENLSFglrmnGNPKAdTERRVSHVADILQITELMKRRPK-----------QLSGGQRQRVA 143
Cdd:COG4987 412 AVVPQR----PHLfdtTLRENLRL-----ARPDA-TDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 144 IGRAIVREPEVFLFDEPLSNLDAELRVQMrveISRLHKQL-GTTMIYVTHDQTeAMTLADRIVVLRAGNIEQIGAPLDLY 222
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALaGRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELL 557
|
....
gi 1037261085 223 DDPA 226
Cdd:COG4987 558 AQNG 561
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
23-224 |
1.15e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.97 E-value: 1.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVND--VEPADRGIAMVFQSyalyPH-----LTVEEN 95
Cdd:PRK13632 29 SFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKKIGIIFQN----PDnqfigATVEDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 96 LSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVE 175
Cdd:PRK13632 105 IAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1037261085 176 ISRLHKQLGTTMIYVTHDQTEAmTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13632 185 MVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-212 |
1.91e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 139.09 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVE-------PADRG 76
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 iamvfqsyaLYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:COG4152 82 ---------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 157 FDEPLSNLD---AELrvqMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG4152 153 LDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-228 |
2.12e-38 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 137.90 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGF---------EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVE 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 72 PAD-----RGIAMVFQSY--ALYPHLTVEENLSFGLR-MNGNPKADTERRVSHVADILQIT-ELMKRRPKQLSGGQRQRV 142
Cdd:PRK10419 81 RAQrkafrRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 143 AIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNI--EQIGAPLD 220
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDKL 240
|
....*...
gi 1037261085 221 LYDDPANQ 228
Cdd:PRK10419 241 TFSSPAGR 248
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-226 |
2.41e-38 |
|
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: 138.01 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRF--GGF-------EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD 74
Cdd:TIGR02769 3 LEVRDVTHTYrtGGLfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 -----RGIAMVFQ-SY-ALYPHLTVEENLSFGLR-MNGNPKADTERRVSHVADILQI-TELMKRRPKQLSGGQRQRVAIG 145
Cdd:TIGR02769 83 rrafrRDVQLVFQdSPsAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 146 RAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNI--EQIGAPLDLYD 223
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIveECDVAQLLSFK 242
|
...
gi 1037261085 224 DPA 226
Cdd:TIGR02769 243 HPA 245
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-210 |
2.94e-38 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 142.86 E-value: 2.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD---RGIAMV 80
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGL--RMNGNPKADTERRvshvadilQITELMKR---------RPKQLSGGQRQRVAIGRAIV 149
Cdd:COG3845 86 HQHFMLVPNLTVAENIVLGLepTKGGRLDRKAARA--------RIRELSERygldvdpdaKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 150 REPEVFLFDEPLSNLD----AELRVQMRveisRLhKQLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:COG3845 158 RGARILILDEPTAVLTpqeaDELFEILR----RL-AAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-218 |
3.36e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 137.84 E-value: 3.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVND--VEPADRGIAMVFQSyalyPH-----LT 91
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVRRQVGMVFQN----PDnqfvgAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 92 VEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQ 171
Cdd:PRK13635 99 VQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1037261085 172 MRVEISRLHKQLGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIGAP 218
Cdd:PRK13635 179 VLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-216 |
5.13e-38 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 139.24 E-value: 5.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 36 GPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVE------PADRGIAMVFQSYALYPHLTVEENLSFGLRMNGNPKAD 109
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclpPEKRRIGYVFQDARLFPHYKVRGNLRYGMAKSMVAQFD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 110 TerrvshVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIY 189
Cdd:PRK11144 111 K------IVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170 180
....*....|....*....|....*..
gi 1037261085 190 VTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:PRK11144 185 VSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-216 |
6.86e-38 |
|
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: 135.01 E-value: 6.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVfVGPSGCGKSTLLRMIAGLEDITSGELRI-GGKVVNDVEPADRGIAMVFQ 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGL-LGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 163 NLDAELRVQMRVEISRLHKqlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-222 |
2.11e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 135.95 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELriggkVVNDVEPADRGIAM---------VFQ--SYALYPHlT 91
Cdd:PRK13637 27 NIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI-----IIDGVDITDKKVKLsdirkkvglVFQypEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 92 VEENLSFGLRMNGNPKADTERRVSHVADI--LQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELR 169
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 170 VQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLY 222
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-226 |
3.40e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 135.53 E-value: 3.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN------DVEPADRGIAMVFQ--SYALYPHlTVEE 94
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQfpEHQLFEE-TVEK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 95 NLSFGlRMN-GNPKADTERRVSHVADILQITE-LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQM 172
Cdd:PRK13634 106 DICFG-PMNfGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 173 RVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPA 226
Cdd:PRK13634 185 MEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-231 |
9.01e-37 |
|
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: 132.65 E-value: 9.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEP---ADRGIAMV 80
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPherARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGLrmngNPKADTERRVshVADILQI----TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGL----AALPRRSRKI--PDEIYELfpvlKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 157 FDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVA 231
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-236 |
1.01e-36 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 135.70 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 6 LTNIVKRFGG----FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVV-----NDVEPADRG 76
Cdd:PRK11153 4 LKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalseKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 IAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 157 FDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFVGS 236
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQS 243
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-212 |
2.99e-36 |
|
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: 131.75 E-value: 2.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSG-ELRIGGKVVNDVEPAD--RGIAMV 80
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWElrKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 fqSYAL----YPHLTVEENL------SFGLRMNgnPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVR 150
Cdd:COG1119 84 --SPALqlrfPRDETVLDVVlsgffdSIGLYRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 151 EPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-234 |
3.14e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 131.96 E-value: 3.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGL-----EDITSGELRIGGKVV--NDVEPA 73
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfkMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 74 DRGIAMVFQSYALYPHLTVEENLSFGLRMN--GNPKADTERRVSHVADILQITELMKRR----PKQLSGGQRQRVAIGRA 147
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNrlVKSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 148 IVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLgtTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPAN 227
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
....*..
gi 1037261085 228 QFVAGFV 234
Cdd:PRK14247 239 ELTEKYV 245
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-212 |
3.90e-36 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 130.55 E-value: 3.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRF--GGFEII--HGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG--- 76
Cdd:TIGR02211 2 LKCENLGKRYqeGKLDTRvlKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 ---IAMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVshvADILQITELMKR---RPKQLSGGQRQRVAIGRAIVR 150
Cdd:TIGR02211 82 nkkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERA---YEMLEKVGLEHRinhRPSELSGGERQRVAIARALVN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 151 EPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLaDRIVVLRAGNI 212
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-221 |
4.70e-36 |
|
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: 130.81 E-value: 4.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 15 GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDV--EPADRGIAMVFQSYALYpHLTV 92
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtlDSLRRAIGVVPQDTVLF-NDTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 93 EENLSFglrmnGNPKAdTERRVSHVADILQITELMKRRPKQ-----------LSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:cd03253 92 GYNIRY-----GRPDA-TDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 162 SNLDAELRVQMRVEISRLHKqlGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIGAPLDL 221
Cdd:cd03253 166 SALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-225 |
1.35e-35 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 135.97 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 11 KRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGELRIGGKVVNDVEPAD-----RGIAMVFQS-Y 84
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 85 A-LYPHLTVEENLSFGLRMNGNPKADTERRvSHVADILQITEL----MKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:COG4172 373 GsLSPRMTVGQIIAEGLRVHGPGLSAAERR-ARVAEALEEVGLdpaaRHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 160 PLSNLDAELRVQMrVEI-SRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNI-EQiGAPLDLYDDP 225
Cdd:COG4172 452 PTSALDVSVQAQI-LDLlRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVvEQ-GPTEQVFDAP 517
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-212 |
1.91e-35 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 128.14 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAdRGIAMVFQS--YALYPHlT 91
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR-KSIGYVMQDvdYQLFTD-S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 92 VEENLSFGLRmngnPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAElrvQ 171
Cdd:cd03226 89 VREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK---N 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1037261085 172 MRvEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03226 162 ME-RVGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-234 |
3.04e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 129.19 E-value: 3.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 13 FGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDIT-----SGELRIGGKVV--NDVEPAD--RGIAMVFQS 83
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEvrREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMNG--NPKADTERRVSHVADILQITELMKRR----PKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 158 DEPLSNLDAELRVQMRVEISRLHKQLgtTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFV 234
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-226 |
3.52e-35 |
|
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: 128.43 E-value: 3.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEP---ADRGIAMV 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhkrARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 161 LSNLDAeLRVQmrvEISRLHKQLGTTMIYV---THDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPA 226
Cdd:cd03218 161 FAGVDP-IAVQ---DIQKIIKILKDRGIGVlitDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-228 |
3.75e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 129.00 E-value: 3.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 13 FGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGELRIGGKVVND--VEPAD--RGIAMVFQS 83
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDIYDpdVDVVElrRRVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHlTVEENLSFGLRMNG-NPKADTERRV----------SHVADILqitelmKRRPKQLSGGQRQRVAIGRAIVREP 152
Cdd:COG1117 101 PNPFPK-SIYDNVAYGLRLHGiKSKSELDEIVeeslrkaalwDEVKDRL------KKSALGLSGGQQQRLCIARALAVEP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 153 EVFLFDEPLSNLD--AElrvqMRVE--ISRLHKQLgtTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQ 228
Cdd:COG1117 174 EVLLMDEPTSALDpiST----AKIEelILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDK 247
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
26-222 |
3.85e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 129.85 E-value: 3.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 26 VKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVV--NDVEPADRGIAMVFQSyalyPH-----LTVEENLSF 98
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteENVWDIRHKIGMVFQN----PDnqfvgATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 99 GLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISR 178
Cdd:PRK13650 106 GLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1037261085 179 LHKQLGTTMIYVTHDQTEaMTLADRIVVLRAGNIEQIGAPLDLY 222
Cdd:PRK13650 186 IRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-212 |
4.72e-35 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 127.71 E-value: 4.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSyalyPHL---TVE 93
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQD----VTLfygTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 94 ENLSFGlrmngNPKADTERrVSHVADILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:cd03245 96 DNITLG-----APLADDER-ILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 163 NLD--AELRVqmrveISRLHKQLGT-TMIYVTHdQTEAMTLADRIVVLRAGNI 212
Cdd:cd03245 170 AMDmnSEERL-----KERLRQLLGDkTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-210 |
7.30e-35 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 127.01 E-value: 7.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVE-------PADRG 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 iamvfqsyaLYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:cd03269 81 ---------LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 157 FDEPLSNLDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-222 |
5.42e-34 |
|
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: 125.34 E-value: 5.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSYALYPhLTVEE 94
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 95 NLSFGLRmngNPKADTERRVSHVADILQ-ITELMKR-------RPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDA 166
Cdd:cd03249 96 NIRYGKP---DATDEEVEEAAKKANIHDfIMSLPDGydtlvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 167 --ELRVQMRVEisRLHKqlGTTMIYVTHDQTeamTL--ADRIVVLRAGNIEQIGAPLDLY 222
Cdd:cd03249 173 esEKLVQEALD--RAMK--GRTTIVIAHRLS---TIrnADLIAVLQNGQVVEQGTHDELM 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-207 |
5.72e-34 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 123.88 E-value: 5.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 12 RFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGkvvndvepaDRGIAMVFQSYAL---YP 88
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 89 hLTVEENLSFGL----RMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:NF040873 72 -LTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1037261085 165 DAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMtLADRIVVL 207
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVR-RADPCVLL 191
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-224 |
6.35e-34 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 125.04 E-value: 6.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSYALYpHLTVEEN 95
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGLVSQDVFLF-NDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 96 LSFGlrmngNPKAdTERRVSHVADILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:cd03251 96 IAYG-----RPGA-TREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 165 DAELRVQMRVEISRLHKqlGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:cd03251 170 DTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-212 |
8.11e-34 |
|
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: 123.82 E-value: 8.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNI---VKRF---GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELRIGGKVVNDVEP 72
Cdd:cd03213 1 GVTLSFRNLtvtVKSSpskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 73 ADRgIAMVFQSYALYPHLTVEENLSFGLRMngnpkadterrvshvadilqitelmkrrpKQLSGGQRQRVAIGRAIVREP 152
Cdd:cd03213 81 RKI-IGYVPQDDILHPTLTVRETLMFAAKL-----------------------------RGLSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 153 EVFLFDEPLSNLDAELRVQMRVEISRLHKQlGTTMIYVTHD-QTEAMTLADRIVVLRAGNI 212
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-224 |
9.27e-34 |
|
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: 124.75 E-value: 9.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 5 SLTNIVKR-FGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVvndvePADRG------I 77
Cdd:cd03267 22 SLKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-----PWKRRkkflrrI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVF-QSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:cd03267 97 GVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 157 FDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIeqigapldLYDD 224
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL--------LYDG 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-218 |
9.58e-34 |
|
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: 130.69 E-value: 9.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRF-----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGEL--RIGGKVVNDVEP---- 72
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDEWVDMTKPgpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 73 ---ADRGIAMVFQSYALYPHLTVEENL--SFGLRMngnPKADTERRVSHVADILQITE-----LMKRRPKQLSGGQRQRV 142
Cdd:TIGR03269 360 rgrAKRYIGILHQEYDLYPHRTVLDNLteAIGLEL---PDELARMKAVITLKMVGFDEekaeeILDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 143 AIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-218 |
3.40e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 124.07 E-value: 3.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVF 81
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 82 QSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAI------VREPEVF 155
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 156 LF-DEPLSNLDaeLRVQMRV-EISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:COG4559 162 LFlDEPTSALD--LAHQHAVlRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP 224
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-212 |
4.45e-33 |
|
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: 129.99 E-value: 4.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSYALYpHLTVEENL 96
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTLRDNI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 97 SFGlrmngNPKADtERRVSHVADILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:TIGR03375 560 ALG-----APYAD-DEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEPTSAMD 633
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1037261085 166 AelRVQMRVeISRLHKQL-GTTMIYVTHdQTEAMTLADRIVVLRAGNI 212
Cdd:TIGR03375 634 N--RSEERF-KDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGRI 677
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-218 |
4.41e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 121.03 E-value: 4.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVF 81
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 82 QSYAL-YPhLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVR------EPEV 154
Cdd:PRK13548 83 QHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 155 FLFDEPLSNLDaeLRVQMRVeiSRLHKQL----GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:PRK13548 162 LLLDEPTSALD--LAHQHHV--LRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-225 |
5.47e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 120.13 E-value: 5.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVeP----ADRG 76
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-PmhkrARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 I------AMVFQsyalypHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVR 150
Cdd:COG1137 80 IgylpqeASIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 151 EPEVFLFDEPLSNLD----AELRvQMrveISRL-HKQLGttmIYVT-HDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:COG1137 154 NPKFILLDEPFAGVDpiavADIQ-KI---IRHLkERGIG---VLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNN 226
|
.
gi 1037261085 225 P 225
Cdd:COG1137 227 P 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-212 |
1.58e-31 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 116.93 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFE--IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG--IAM 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 80 VFQSYALYPHlTVEENLsfglrmngnpkadterrvshvadilqitelmkrrpkqLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 160 PLSNLDAELRVQMRVEISRLHKQlGTTMIYVTHdQTEAMTLADRIVVLRAGNI 212
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-214 |
1.66e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 118.76 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPA------DRGIAMVFQSYALYPHL 90
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelrNQKLGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 91 TVEENLSFGLRMNGNPKADTERRVShvaDILQITELMKR---RPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:PRK11629 103 TALENVAMPLLIGKKKPAEINSRAL---EMLAAVGLEHRanhRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1037261085 168 LRVQMRVEISRLHKQLGTTMIYVTHDqteaMTLADRI---VVLRAGNIEQ 214
Cdd:PRK11629 180 NADSIFQLLGELNRLQGTAFLVVTHD----LQLAKRMsrqLEMRDGRLTA 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-216 |
2.95e-31 |
|
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: 117.63 E-value: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 10 VKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVndvepadrgiAMVFQSYALYPH 89
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS----------SLLGLGGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 90 LTVEENLSFGLRMNGNPKADTERRvshVADILQITEL---MKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDA 166
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEIDEK---IDEIIEFSELgdfIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1037261085 167 ELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03220 176 AFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-221 |
4.28e-31 |
|
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: 117.71 E-value: 4.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSYALYPHlTVEEN 95
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 96 LSFglrmnGNPKAdTERRVSHVADILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:cd03254 97 IRL-----GRPNA-TDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 165 D--AELRVQMRVEisRLHKqlGTTMIYVTHDQTeamTL--ADRIVVLRAGNIEQIGAPLDL 221
Cdd:cd03254 171 DteTEKLIQEALE--KLMK--GRTSIIIAHRLS---TIknADKILVLDDGKIIEEGTHDEL 224
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
18-227 |
6.48e-31 |
|
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: 117.08 E-value: 6.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGELRIGGKVVNDVEPADRGIAMVFQS--YALYPHLT 91
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 92 VEENLSFGLRMNGNPKADTERRVSHV---ADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEAleaVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 169 RVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPAN 227
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-222 |
7.60e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 117.10 E-value: 7.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 11 KRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEpadrgIAMVFQsyalyPHL 90
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLE-----LGAGFH-----PEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 91 TVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRV 170
Cdd:COG1134 104 TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 171 QMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP---LDLY 222
Cdd:COG1134 184 KCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPeevIAAY 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-238 |
1.17e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 117.91 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN------DVEPADRGIAMVFQ--SYALYPHlTVEE 94
Cdd:PRK13643 26 DLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQfpESQLFEE-TVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 95 NLSFGLRMNGNPKADTERRVSHVADILQIT-ELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMR 173
Cdd:PRK13643 105 DVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 174 VEISRLHkQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDpANQFVAGFVGSPK 238
Cdd:PRK13643 185 QLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE-VDFLKAHELGVPK 247
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-212 |
1.17e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 116.13 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 13 FGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD-----RGIAMVFQSYALY 87
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 88 PHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:PRK10908 92 MDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1037261085 168 LrvqmRVEISRLHKQ---LGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:PRK10908 172 L----SEGILRLFEEfnrVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-212 |
1.66e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 116.72 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFG-GF----EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG-- 76
Cdd:COG1101 2 LELKNLSKTFNpGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 IAMVFQSYAL--YPHLTVEENLS--------FGLRMnGNPKADTErrvsHVADILQITEL-----MKRRPKQLSGGQRQR 141
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRR-GLTKKRRE----LFRELLATLGLglenrLDTKVGLLSGGQRQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 142 VAIGRAIVREPEVFLFDEPLSNLD---AELRVQMRVEISRLHKqLGTTMiyVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDpktAALVLELTEKIVEENN-LTTLM--VTHNMEQALDYGNRLIMMHEGRI 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-207 |
1.90e-30 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 121.62 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 3 ELSLTNIVKRFGG-FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAM 79
Cdd:TIGR02857 321 SLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 80 VFQSYALYPHlTVEENLSFGLRmngNPKADTERRVSHVADILQITE--------LMKRRPKQLSGGQRQRVAIGRAIVRE 151
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARP---DASDAEIREALERAGLDEFVAalpqgldtPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 152 PEVFLFDEPLSNLDAELRVQMRVEISRLHKqlGTTMIYVTHDqTEAMTLADRIVVL 207
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-223 |
2.60e-30 |
|
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: 115.33 E-value: 2.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 24 LEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKvvnDVEPADRGIAMVFQSYAL---YPHLTVEENLSFGL 100
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFPISVAHTVMSGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 101 RMNG---NPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD---AELRVQMRV 174
Cdd:TIGR03771 78 GHIGwlrRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDmptQELLTELFI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1037261085 175 EISrlhkQLGTTMIYVTHDQTEAMTLADRIVVLRaGNIEQIGAPLDLYD 223
Cdd:TIGR03771 158 ELA----GAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQD 201
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-222 |
3.10e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 116.73 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGK--VVNDVEPADRGIAMVFQSY-ALYPHLTVEEN 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEllTAENVWNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 96 LSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVE 175
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1037261085 176 ISRLHKQLGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIGAPLDLY 222
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-225 |
5.49e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 116.99 E-value: 5.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 10 VKRFGG--FEIIHGANLEVkdgefvvfVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD-----RGIAMVFQ 82
Cdd:PRK11308 28 VKALDGvsFTLERGKTLAV--------VGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 S-YA-LYPHLTVEENLSFGLRMNGNPKAdTERRvSHVADILQI----TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:PRK11308 100 NpYGsLNPRKKVGQILEEPLLINTSLSA-AERR-EKALAMMAKvglrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 157 FDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK11308 178 ADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-214 |
6.39e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 114.49 E-value: 6.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG------IAMVFQSYALYPHLT 91
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 92 VEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQ 171
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1037261085 172 MRVEISRLHKQLGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQ 214
Cdd:PRK10584 185 IADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-225 |
7.89e-30 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 116.73 E-value: 7.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 21 GANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADR-----GIAMVFQS--YALYPHLTVE 93
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 94 ENLSFGLRMNgNPKADTERRVSHVADILQ----ITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELR 169
Cdd:PRK15079 119 EIIAEPLRTY-HPKLSRQEVKDRVKAMMLkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 170 VQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK15079 198 AQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-217 |
9.70e-30 |
|
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: 119.85 E-value: 9.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 2 AELSLTNIVKRFGGFE--IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG--I 77
Cdd:COG4618 329 GRLSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVFQSYALYPHlTVEENLSfglRMngnPKADTErRVSHVADILQITELMKRRPK-----------QLSGGQRQRVAIGR 146
Cdd:COG4618 409 GYLPQDVELFDG-TIAENIA---RF---GDADPE-KVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 147 AIVREPEVFLFDEPLSNLDAELRVQMRVEISRLhKQLGTTMIYVTHDQTeAMTLADRIVVLRAGNIEQIGA 217
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGP 549
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-202 |
9.97e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 114.88 E-value: 9.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 7 TNIVKRFGGFEIIHGANLEVKD-------GEFVVFVGPSGCGKSTLLRMIAGLEDITSGeLRIGGKVV--------NDVE 71
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNvwldipkNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTfhgknlyaPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 72 PAD--RGIAMVFQSYALYPHlTVEENLSFGLRMNGNpKAD----TERRVSHVADILQITELMKRRPKQLSGGQRQRVAIG 145
Cdd:PRK14243 86 PVEvrRRIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDmdelVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 146 RAIVREPEVFLFDEPLSNLD--AELRVQmrveisRLHKQLGT--TMIYVTHDQTEAMTLAD 202
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDpiSTLRIE------ELMHELKEqyTIIIVTHNMQQAARVSD 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-233 |
1.49e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 119.44 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 2 AELSLTNIVKRF----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGI 77
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 ------AMVFQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVRE 151
Cdd:PRK10535 83 lrrehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 152 PEVFLFDEPLSNLDAelrvQMRVEISRLHKQL---GTTMIYVTHDQTEAMTlADRIVVLRAGNI----------EQIGAP 218
Cdd:PRK10535 163 GQVILADEPTGALDS----HSGEEVMAILHQLrdrGHTVIIVTHDPQVAAQ-AERVIEIRDGEIvrnppaqekvNVAGGT 237
|
250
....*....|....*..
gi 1037261085 219 LDLYDDPA--NQFVAGF 233
Cdd:PRK10535 238 EPVVNTASgwRQFVSGF 254
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-224 |
2.24e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 114.72 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 16 FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGG-------KVVNDVEPADRGIAMVFQ--SYAL 86
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVKRLRKEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 87 YPHlTVEENLSFGLRMNGNPKADTERRVSHVADILQI-TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:PRK13645 104 FQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 166 AELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-218 |
2.29e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.57 E-value: 2.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVepADRGIAmvfQSYALYP--HLT---- 91
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML--SSRQLA---RRLALLPqhHLTpegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 92 -VEENLSFG----LRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDa 166
Cdd:PRK11231 92 tVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD- 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 167 elrVQMRVEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:PRK11231 171 ---INHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-306 |
7.63e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 115.32 E-value: 7.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN--DVEPADRGIA 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVFQSYALYPHLTVEENLSFGL-----RMNGNPKADtERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPE 153
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRtphrsRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 154 VFLFDEPLSNLDAELRVQMrVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP-------A 226
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRT-LELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADtlraafdA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 227 NQFVAG--FVGSPKMNFLTAVVVEAQPGRAVIAL--ESNPETRLpvpIAEPVEAGTKVTLGIRPEhfadagaGDADLTVA 302
Cdd:PRK09536 239 RTAVGTdpATGAPTVTPLPDPDRTEAAADTRVHVvgGGQPAARA---VSRLVAAGASVSVGPVPE-------GDTAAETA 308
|
....
gi 1037261085 303 IDVA 306
Cdd:PRK09536 309 ARVG 312
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-210 |
2.52e-28 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 115.01 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVV---NDVEPADRGI 77
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVFQSYALYPHLTVEENL-------SFGLRMNGNPKADTERRVSHVA-DILQITELmkrrpKQLSGGQRQRVAIGRAIV 149
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLylgqlphKGGIVNRRLLNYEAREQLEHLGvDIDPDTPL-----KYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 150 REPEVFLFDEPLSNLDA-ELRVQMRVeISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:PRK11288 157 RNARVIAFDEPTSSLSArEIEQLFRV-IRELRAE-GRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-230 |
5.48e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.46 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVND---VEPADRGIAMVFQS-YALYPHLTVEENLSF 98
Cdd:PRK13644 22 NLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfskLQGIRKLVGIVFQNpETQFVGRTVEEDLAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 99 GLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISR 178
Cdd:PRK13644 102 GPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 179 LHKQlGTTMIYVTHDqTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFV 230
Cdd:PRK13644 182 LHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-224 |
6.05e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.60 E-value: 6.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 21 GANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN------DVEPADRGIAMVFQsyalYPHL---- 90
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPESqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 91 -TVEENLSFGLRMNGNPKADTERRVSHVADILQITE-LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:PRK13649 101 eTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 169 RVQMRVEISRLHkQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13649 181 RKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-233 |
7.09e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 111.33 E-value: 7.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 5 SLTNIVKRfgGFEIIH---GANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVvndvePAD------R 75
Cdd:COG4586 23 ALKGLFRR--EYREVEavdDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKrrkefaR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 76 GIAMVF-QSYALYPHLTVEEnlSFGL--RMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREP 152
Cdd:COG4586 96 RIGVVFgQRSQLWWDLPAID--SFRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 153 EVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIeqigapldLYDDPANQFVAG 232
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI--------IYDGSLEELKER 245
|
.
gi 1037261085 233 F 233
Cdd:COG4586 246 F 246
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-214 |
1.43e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.88 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVF 81
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 82 QSYALYPHlTVEENLSFGLRMNGnpKADTERRVshVADILQI---TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:PRK10247 88 QTPTLFGD-TVYDNLIFPWQIRN--QQPDPAIF--LDDLERFalpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 159 EPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEaMTLADRIVVL--RAGNIEQ 214
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLqpHAGEMQE 219
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-216 |
1.91e-27 |
|
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: 112.83 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG--IAMVFQSYALYPHlTVEEN 95
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIGYLPQDVELFPG-TVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 96 LSfglRMNGNPKAdteRRVSHVADILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:TIGR01842 412 IA---RFGENADP---EKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 165 DAELRVQMRVEISRLHKQlGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:TIGR01842 486 DEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFG 535
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
29-224 |
2.44e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 108.69 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSyalyPH-----LTVEENLSFGLR 101
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQN----PDnqfvgSIVKYDVAFGLE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 102 MNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHK 181
Cdd:PRK13648 111 NHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKS 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1037261085 182 QLGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13648 191 EHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-228 |
3.05e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 107.94 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGELRIGGKVV----NDVEPAD 74
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIysprTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 RGIAMVFQSYALYPhLTVEENLSFGLRMNG-NPKADTERRVSHVADILQITELMKRRPKQ----LSGGQRQRVAIGRAIV 149
Cdd:PRK14239 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGiKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 150 REPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLgtTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQ 228
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHK 241
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-210 |
3.21e-27 |
|
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: 106.40 E-value: 3.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGkvvndvepadrGIAMVFQSyalyPHL---TVEE 94
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQE----PWIqngTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 95 NLSFGLRMNgnpkadtERRVSHVADILQITELMKRRPKQ-----------LSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03250 85 NILFGKPFD-------EERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1037261085 164 LDAELRVQMRVEISRLHKQLGTTMIYVTHdQTEAMTLADRIVVLRAG 210
Cdd:cd03250 158 VDAHVGRHIFENCILGLLLNNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-224 |
4.65e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 107.90 E-value: 4.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 15 GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN-DVEPADRG-IAMVFQSyalyPH--- 89
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaENEKWVRSkVGLVFQD----PDdqv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 90 --LTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:PRK13647 93 fsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 168 LRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13647 173 GQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-212 |
7.53e-27 |
|
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: 106.20 E-value: 7.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED---ITSGELRIGGKVVNDVEPADRgIAMVFQSYALYPHLTVEE 94
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 95 NLSFGLRM-NGNPKADTERRV-------SHVADilqiTELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDA 166
Cdd:cd03234 101 TLTYTAILrLPRKSSDAIRKKrvedvllRDLAL----TRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1037261085 167 ELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-225 |
9.48e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.09 E-value: 9.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 15 GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN----DVEPADRGIAMVFQS-----YA 85
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkkSLLEVRKTVGIVFQNpddqlFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 86 lyPhlTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:PRK13639 94 --P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 166 AELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK13639 170 PMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-218 |
9.67e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 106.99 E-value: 9.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 13 FGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSYALYPHL 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 91 TVEENLSFGlRMNGNP-----KADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:PRK10253 97 TVQELVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 166 AELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
1.32e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 105.73 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD---RGI 77
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVFQSYALYPHLTVEENLSFGLRMngNPKADTERRVSHVADIL-QITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFF--AERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 157 FDEPLSNLDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNI--EQIGAPL 219
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVvlEDTGDAL 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-226 |
1.36e-26 |
|
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: 110.54 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGG----FEIIHGANLEVKDGEFVVFVGPSGCGKS----TLLRMIAGLEDITSGELRIGGKVVNDVEPAD- 74
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 ---RG--IAMVFQ--SYALYPHLTVEENLSFGLRM-NGNPKADTERRVSHVADILQITE---LMKRRPKQLSGGQRQRVA 143
Cdd:COG4172 87 rriRGnrIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 144 IGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYD 223
Cdd:COG4172 167 IAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFA 246
|
...
gi 1037261085 224 DPA 226
Cdd:COG4172 247 APQ 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-224 |
1.45e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 110.14 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADR---GIAMV 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAhqlGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGLrmngnPK-ADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGL-----PKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 160 PLSNLDAelrvqmrVEISRLHKQL------GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK15439 167 PTASLTP-------AETERLFSRIrellaqGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
11-229 |
1.80e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 106.25 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 11 KRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGL--EDITSGE--------LRIGGKVVNDVEPADRGIAMV 80
Cdd:PRK09984 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGShiellgrtVQREGRLARDIRKSRANTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGlRMNGNPKADT---------ERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVRE 151
Cdd:PRK09984 92 FQQFNLVNRLSVLENVLIG-ALGSTPFWRTcfswftreqKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 152 PEVFLFDEPLSNLDAE-LRVQMRVeISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIeqigapldLYDDPANQF 229
Cdd:PRK09984 171 AKVILADEPIASLDPEsARIVMDT-LRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV--------FYDGSSQQF 240
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
23-225 |
1.90e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.42 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGL--------EDITSGELRIGGKVVNDVEpaDRgIAMVFQSyalyPH----- 89
Cdd:PRK13640 27 SFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITLTAKTVWDIR--EK-VGIVFQN----PDnqfvg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 90 LTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELR 169
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 170 VQMRVEISRLHKQLGTTMIYVTHDQTEAmTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-224 |
1.94e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 106.33 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGG---KVVNDVEPADRGIAMVFQSyalyPH-----LTVEE 94
Cdd:PRK13633 30 NLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PDnqivaTIVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 95 NLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRV 174
Cdd:PRK13633 106 DVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVN 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1037261085 175 EISRLHKQLGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13633 186 TIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-214 |
2.75e-26 |
|
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: 109.91 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSYALYpHLTVEE 94
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 95 NLSFglrmnGNPKAdTERRVSHVADILQITELMKRRPKQ-----------LSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:COG5265 451 NIAY-----GRPDA-SEEEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 164 LD--------AELRvqmrvEISRlhkqlGTTMIYVTH------DqteamtlADRIVVLRAGNI-EQ 214
Cdd:COG5265 525 LDsrteraiqAALR-----EVAR-----GRTTLVIAHrlstivD-------ADEILVLEAGRIvER 573
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-237 |
4.65e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 105.23 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVV-----NDVEPADRGIAMVFQSYALYP 88
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 89 HLTVEENLSFGLRMNGN-PKAdterrvshvadILQITELMKRR-----------PKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:PRK11831 98 DMNVFDNVAYPLREHTQlPAP-----------LLHSTVMMKLEavglrgaaklmPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 157 FDEPLSNLDAelrVQMRV---EISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP---ANQFV 230
Cdd:PRK11831 167 FDEPFVGQDP---ITMGVlvkLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPdprVRQFL 243
|
....*..
gi 1037261085 231 AGFVGSP 237
Cdd:PRK11831 244 DGIADGP 250
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-193 |
5.12e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.61 E-value: 5.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 6 LTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVndvepadrgIAMVFQSYA 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR---------IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 86 LYPHLTVEENLSFGL--------RMN------GNPKADTER------------------RVSHVADILQITELMKRRP-K 132
Cdd:COG0488 72 LDDDLTVLDTVLDGDaelraleaELEeleaklAEPDEDLERlaelqeefealggweaeaRAEEILSGLGFPEEDLDRPvS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 133 QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAElrvqmrvEISRLHKQLGT---TMIYVTHD 193
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE-------SIEWLEEFLKNypgTVLVVSHD 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-234 |
5.73e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 104.73 E-value: 5.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDItSGELRIGGKV-----------VNdVEPADRGIAMVFQSYA 85
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRVeffnqniyerrVN-LNRLRRQVSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 86 LYPhLTVEENLSFGLRMNG-NPKADTERRVSHV---ADIL-QITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:PRK14258 99 LFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESAlkdADLWdEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 161 LSNLD--AELRVQMRVEISRLHKQLgtTMIYVTHDQTEAMTLADRIVVL-----RAGNIEQIGAPLDLYDDPANQFVAGF 233
Cdd:PRK14258 178 CFGLDpiASMKVESLIQSLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGLTKKIFNSPHDSRTREY 255
|
.
gi 1037261085 234 V 234
Cdd:PRK14258 256 V 256
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-229 |
7.24e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 105.17 E-value: 7.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 8 NIVKRFGG-----FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGEL---------------------- 60
Cdd:PRK13651 7 NIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvlek 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 61 ----RIGGKVVNDVEPADRGIAMVFQ--SYALYPHlTVEENLSFGLRMNGNPKADTERRVshvADILQITEL----MKRR 130
Cdd:PRK13651 87 lviqKTRFKKIKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRA---AKYIELVGLdesyLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 131 PKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
250
....*....|....*....
gi 1037261085 211 NIEQIGAPLDLYDDpaNQF 229
Cdd:PRK13651 242 KIIKDGDTYDILSD--NKF 258
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-210 |
9.48e-26 |
|
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: 103.28 E-value: 9.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRF-----GGFEI--IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRI--GGKVVNDVEPAD 74
Cdd:COG4778 5 LEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 RGIAMVFQSYALY--------PHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITE-LMKRRPKQLSGGQRQRVAIG 145
Cdd:COG4778 85 REILALRRRTIGYvsqflrviPRVSALDVVAEPLLERGVDREEARARARELLARLNLPErLWDLPPATFSGGEQQRVNIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 146 RAIVREPEVFLFDEPLSNLDAELRvqmRVEISRLH--KQLGTTMIYVTHDqTEAM-TLADRIVVLRAG 210
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAANR---AVVVELIEeaKARGTAIIGIFHD-EEVReAVADRVVDVTPF 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-234 |
9.55e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.97 E-value: 9.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVV---NDVEPAD-----RGIAMVFQSYALYPH 89
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDaiklrKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 90 LTVEENLSFGLRMNG-----NPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:PRK14246 105 LSIYDNIAYPLKSHGikekrEIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 165 DAELRVQMRVEISRLHKQLgtTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGFV 234
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-224 |
1.13e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.48 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 16 FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVND------VEPADRGIAMVFQsyalYPH 89
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 90 L-----TVEENLSFGLRmngNPKADTERRVSHVADILQ----ITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:PRK13646 96 SqlfedTVEREIIFGPK---NFKMNLDEVKNYAHRLLMdlgfSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 161 LSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
3.84e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.35 E-value: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 2 AELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEP-ADRGIAMV 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARhARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 161 LSNLDAELRVQMrveISRLHKQL--GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYD 223
Cdd:PRK13537 166 TTGLDPQARHLM---WERLRSLLarGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-225 |
6.43e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 102.19 E-value: 6.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN--DVEPADRGIAMVFQS---YALYP 88
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFVGLVFQNpddQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 89 hlTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:PRK13652 95 --TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 169 RVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-225 |
6.75e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.21 E-value: 6.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN------DVEPADRGIAMVFQsyalYPHL-----T 91
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQ----FPEAqlfenT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 92 VEENLSFGLRMNGnpKADTERRVSHVADILQI---TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:PRK13641 103 VLKDVEFGPKNFG--FSEDEAKEKALKWLKKVglsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 169 RVQMrVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK13641 181 RKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-216 |
1.12e-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: 100.64 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPA--DRGIAMVFQSYALYpHLTVEE 94
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 95 NLSFGlrmngNPKADTER--RVSHVAD----ILQITE----LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:cd03252 95 NIALA-----DPGMSMERviEAAKLAGahdfISELPEgydtIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 165 DAElrvQMRVEISRLHKQL-GTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIG 216
Cdd:cd03252 170 DYE---SEHAIMRNMHDICaGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-225 |
1.36e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.19 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPA--DRGIAMVFQSYALYPHlTVEEN 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 96 LSFGLRMNGNPKADTERRVSHVADIlqITELMK-------RRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEl 168
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANAHDF--IMEFPNgydtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE- 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 169 rVQMRVEISRlhKQLGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:TIGR00958 652 -CEQLLQESR--SRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-192 |
1.43e-24 |
|
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: 98.97 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPA-DRGIAMVFQ 82
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 SYALYPHLTVEENLSFGLRMNGnpkaDTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|
gi 1037261085 163 NLDAElRVQMRVEISRLHKQLGTTMIYVTH 192
Cdd:TIGR01189 157 ALDKA-GVALLAGLLRAHLARGGIVLLTTH 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-206 |
2.00e-24 |
|
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: 104.48 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGF--EIIHGanlEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGE----LRIGGK---VVNDVEpad 74
Cdd:COG1245 342 VEYPDLTKSYGGFslEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEvdedLKISYKpqyISPDYD--- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 rgiamvfqsyalyphLTVEENLsfglRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:COG1245 416 ---------------GTVEEFL----RSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 155 FLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVV 206
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-224 |
2.11e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.83 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRI-GGKVVNDVEPADRGIAMVFQ 82
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 163 NLDAELRvQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13536 202 GLDPHAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
35-226 |
2.58e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.47 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 35 VGPSGCGKSTLLRMIAGL----------EDITSGELRIGGKVVNDVEPAD--------RGIAMVFQ--SYALYPHlTVEE 94
Cdd:PRK13631 58 IGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELITNPYSKKiknfkelrRRVSMVFQfpEYQLFKD-TIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 95 NLSFGLRMNGNPKADTERRVSHVADILQITE-LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMr 173
Cdd:PRK13631 137 DIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM- 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 174 VEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPA 226
Cdd:PRK13631 216 MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-212 |
2.96e-24 |
|
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: 98.49 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIV----KRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGledITSGELRIGGKVVNDVEPADrG 76
Cdd:cd03233 1 ASTLSWRNISfttgKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIHYNGIPYK-E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 IAMVFQSYALY--------PHLTVEENLSFGLRMNGNpkadterrvshvaDILqitelmkrrpKQLSGGQRQRVAIGRAI 148
Cdd:cd03233 77 FAEKYPGEIIYvseedvhfPTLTVRETLDFALRCKGN-------------EFV----------RGISGGERKRVSIAEAL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 149 VREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLG-TTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKtTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-225 |
3.52e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.68 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN---DVEPADRGIAMV 80
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFG--LRMNGN--------P---KADTE--RRVSHVADILQITELMKRRPKQLSGGQRQRVAIG 145
Cdd:PRK11300 86 FQHVRLFREMTVIENLLVAqhQQLKTGlfsgllktPafrRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 146 RAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-212 |
3.95e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.17 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 10 VKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD---RGIAMV---FQS 83
Cdd:COG1129 259 VEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVpedRKG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFG----LRMNG--NPKAdtERRVS-HVADILQI-TELMKRRPKQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:COG1129 339 EGLVLDLSIRENITLAsldrLSRGGllDRRR--ERALAeEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 156 LFDEPLSNLDaelrVQMRVEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG1129 417 ILDEPTRGID----VGAKAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-212 |
4.11e-24 |
|
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: 97.50 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADR---GIAMV---FQSYALYPHLTV 92
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYVpedRKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 93 EENLSFGLrmngnpkadterrvshvadilqitelmkrrpkQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQM 172
Cdd:cd03215 96 AENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1037261085 173 RVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:cd03215 144 YRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-223 |
5.41e-24 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 102.87 E-value: 5.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEI--IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAM 79
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 80 VFQSYALYPHlTVEENLSFGlRMNGNPKADTERrvshVADILQITELMKRRPK-----------QLSGGQRQRVAIGRAI 148
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG-RTEQADRAEIER----ALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 149 VREPEVFLFDEPLSNLDAELRVQMRVEISRLHKqlGTTMIYVTHDQTeAMTLADRIVVLRAGNIEQIGAPLDLYD 223
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
9-206 |
5.69e-24 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 98.63 E-value: 5.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 9 IVKRFGGF--EIIHGanlEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELrigGKVVNDVEPADRGIAMVFQSyal 86
Cdd:cd03237 6 MKKTLGEFtlEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKPQYIKADYEG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 87 yphlTVEENLSFGLRMNGN-PKADTErrvshVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:cd03237 77 ----TVRDLLSSITKDFYThPYFKTE-----IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1037261085 166 AELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVV 206
Cdd:cd03237 148 VEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
6.45e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 102.57 E-value: 6.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDI--TSGEL-----------------RIGG 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 65 K-----------VVNDVEPAD-------RGIAMVFQ-SYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITE 125
Cdd:TIGR03269 81 PcpvcggtlepeEVDFWNLSDklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 126 LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHdQTEAMT-LADRI 204
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH-WPEVIEdLSDKA 239
|
250
....*....|....*..
gi 1037261085 205 VVLRAGNIEQIGAPLDL 221
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEV 256
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-216 |
1.20e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 102.23 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITsGELRIGGKVVNDVEPAD--RGIAMVFQSYALyPHLTVEENLSFGl 100
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLLG- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 101 rmngNPKAdTERRVSHVADILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDA--E 167
Cdd:PRK11174 447 ----NPDA-SDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAhsE 521
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 168 LRVQMRV-EISRlhkqlGTTMIYVTH--DQTEAMtlaDRIVVLRAGNIEQIG 216
Cdd:PRK11174 522 QLVMQALnAASR-----RQTTLMVTHqlEDLAQW---DQIWVMQDGQIVQQG 565
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-218 |
1.30e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.83 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELRIGGKVVNDVEPADR---GIA 78
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVFQsyalYPhltVE----ENLSFgLRMNGNPKADTE-------RRVSHVADILQITELMKRRP--KQLSGGQRQRVAIG 145
Cdd:COG0396 81 LAFQ----YP---VEipgvSVSNF-LRTALNARRGEElsareflKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 146 RAIVREPEVFLFDEPLSNLDAE-LRVqMRVEISRLHKQlGTTMIYVTHDQteamTL-----ADRIVVLRAGNIEQIGAP 218
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLDIDaLRI-VAEGVNKLRSP-DRGILIITHYQ----RIldyikPDFVHVLVDGRIVKSGGK 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-224 |
1.65e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.38 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 15 GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN----DVEPADRGIAMVFQS--YALYP 88
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkGLMKLRESVGMVFQDpdNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 89 hLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:PRK13636 98 -ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 169 RVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
17-216 |
1.75e-23 |
|
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: 101.74 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPA--DRGIAMVFQSYALYPHlTVEE 94
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIRD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 95 NLSFGlrmngNPKADTERrVSHVADILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:TIGR01846 550 NIALC-----NPGAPFEH-VIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEATSA 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 164 LDAE----LRVQMRvEISRlhkqlGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:TIGR01846 624 LDYEsealIMRNMR-EICR-----GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESG 673
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-213 |
1.80e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVndvepadrgIAMVFQS 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK---------IGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YA-LYPHLTVEENLSfglrmNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:COG0488 387 QEeLDPDKTVLDELR-----DGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 163 NLDAELRvqmrvEIsrLHKQLGT---TMIYVTHDQTEAMTLADRIVVLRAGNIE 213
Cdd:COG0488 462 HLDIETL-----EA--LEEALDDfpgTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-224 |
1.81e-23 |
|
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: 96.06 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELRIGGKVVNDVEPADR---GIA 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVFQSYALYPHLTVEENLsfglrmngnpkadteRRVShvadilqitelmkrrpKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:cd03217 81 LAFQYPPEIPGVKNADFL---------------RYVN----------------EGFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 159 EPLSNLDAE-LRVQMRVeISRLHKQlGTTMIYVTHDQTEAMTL-ADRIVVLRAGNIEQIGaPLDLYDD 224
Cdd:cd03217 130 EPDSGLDIDaLRLVAEV-INKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-210 |
2.42e-23 |
|
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: 94.05 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVvndvepadrgiamvfqs 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 yalyphltveenlsfglrmngnpkadterRVSHVAdilqitelmkrrpkQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:cd03221 64 -----------------------------KIGYFE--------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1037261085 164 LDAELRVQMRVEISRLHKqlgtTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-210 |
2.43e-23 |
|
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: 100.67 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLE-------DITSGELRIGGKVVNDVEPAdrG 76
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgtwdgEIYWSGSPLKASNIRDTERA--G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 IAMVFQSYALYPHLTVEENLSFG--LRMNGNPKADTE--RRVSHVADILQITELMKRRP-KQLSGGQRQRVAIGRAIVRE 151
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGneITLPGGRMAYNAmyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 152 PEVFLFDEPLSNLdAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:TIGR02633 160 ARLLILDEPSSSL-TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-206 |
5.11e-23 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 100.27 E-value: 5.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGF--EIIHGanlEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGE----LRIGGK---VVNDVEpad 74
Cdd:PRK13409 341 VEYPDLTKKLGDFslEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEvdpeLKISYKpqyIKPDYD--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 75 rgiamvfqsyalyphLTVEENLSfglrmNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:PRK13409 415 ---------------GTVEDLLR-----SITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 155 FLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVV 206
Cdd:PRK13409 475 YLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-192 |
5.75e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.94 E-value: 5.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRgIAMVFQS 83
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMNGNPkadtERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PRK13539 82 NAMKPALTVAENLEFWAAFLGGE----ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*....
gi 1037261085 164 LDAElRVQMRVEISRLHKQLGTTMIYVTH 192
Cdd:PRK13539 158 LDAA-AVALFAELIRAHLAQGGIVIAATH 185
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-222 |
6.75e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.61 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNdvePADRG------- 76
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD---YSKRGllalrqq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 IAMVFQSYALYPHLT-VEENLSFGLRMNGNPKADTERRVSHVADILQiTELMKRRPKQ-LSGGQRQRVAIGRAIVREPEV 154
Cdd:PRK13638 79 VATVFQDPEQQIFYTdIDSDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 155 FLFDEPLSNLDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLY 222
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
18-221 |
6.75e-23 |
|
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: 100.03 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN--DVEPADRGIAMVFQSYALYPHlTVEEN 95
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLGVVLQNGRLMSG-SIFEN 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 96 LSFGLRMNGNPKADTERRVSHVADIlqitelmKRRPKQ-----------LSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:TIGR03797 547 IAGGAPLTLDEAWEAARMAGLAEDI-------RAMPMGmhtvisegggtLSGGQRQRLLIARALVRKPRILLFDEATSAL 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 165 DAelRVQMRVEISRlhKQLGTTMIYVTHDQTEAMTlADRIVVLRAGNIEQIGAPLDL 221
Cdd:TIGR03797 620 DN--RTQAIVSESL--ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDEL 671
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-212 |
9.05e-23 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 94.85 E-value: 9.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPA--DRGIAMVFQSYALYPHlTVEEN 95
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 96 LSFGLRMNGNPKADTERRVSHVADILQITEL-----MKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRV 170
Cdd:cd03248 108 IAYGLQSCSFECVKEAAQKAHAHSFISELASgydteVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1037261085 171 QMRVEISRLHKQlgTTMIYVTHdQTEAMTLADRIVVLRAGNI 212
Cdd:cd03248 188 QVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-210 |
1.17e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 99.11 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIggkvvndvePADRGIAMVFQ-SY--------AL-Y 87
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQrPYlplgtlreALlY 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 88 PHLtveenlsfglrmngnPKADTERRVSHVADILQITELMKR------RPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:COG4178 449 PAT---------------AEAFSDAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1037261085 162 SNLDAELRVQMrveISRLHKQL-GTTMIYVTHdQTEAMTLADRIVVLRAG 210
Cdd:COG4178 514 SALDEENEAAL---YQLLREELpGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-210 |
1.87e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.08 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAE--LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGL--EDITSGELRIGGKV-----VNDVE 71
Cdd:PRK13549 1 MMEylLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEElqasnIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 72 PAdrGIAMVFQSYALYPHLTVEENLSFG--LRMNGnpkadterRVSHVADILQITELMKR---------RPKQLSGGQRQ 140
Cdd:PRK13549 81 RA--GIAIIHQELALVKELSVLENIFLGneITPGG--------IMDYDAMYLRAQKLLAQlkldinpatPVGNLGLGQQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 141 RVAIGRAIVREPEVFLFDEPLSNL-DAELRVQMrvEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLtESETAVLL--DIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-253 |
1.98e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.39 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN-----DVEPADRGIAMVFQS-YA-LYPHLTVEENLSFGLR 101
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspgKLQALRRDIQFIFQDpYAsLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 102 MNGNPKADTERRvsHVADILQITELMK----RRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEIS 177
Cdd:PRK10261 430 VHGLLPGKAAAA--RVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 178 RLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANqfvagfvgsPKMNFLTAVVVEAQPGR 253
Cdd:PRK10261 508 DLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQH---------PYTRKLMAAVPVADPSR 574
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-216 |
2.77e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 92.38 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG-IAMVFQSyalyPHL---TVE 93
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVLNQR----PYLfdtTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 94 ENLSfglrmngnpkadterrvshvadilqitelmkrrpKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMr 173
Cdd:cd03247 93 NNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1037261085 174 veISRLHKQL-GTTMIYVTHDQTeAMTLADRIVVLRAGNIEQIG 216
Cdd:cd03247 138 --LSLIFEVLkDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-216 |
6.48e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.95 E-value: 6.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSYALYPHlTVEENL 96
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAVVFQDAGLFNR-SIEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 97 SFGlrmngnpKAD-TERRVSHVADILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:PRK13657 430 RVG-------RPDaTDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 165 DAELRVQMRVEISRLHKqlGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:PRK13657 503 DVETEAKVKAALDELMK--GRTTFIIAH-RLSTVRNADRILVFDNGRVVESG 551
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-210 |
7.18e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.39 E-value: 7.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEP---ADRGIAMV 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGL----RMNGNPKADTERRVSHVADILQITELmKRRPKQ----LSGGQRQRVAIGRAIVREP 152
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRhltkKVCGVNIIDWREMRVRAAMMLLRVGL-KVDLDEkvanLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 153 EVFLFDEPLSNLDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-223 |
1.08e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 96.35 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 15 GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVepaDRGIAMVFQSY-ALYPHL--- 90
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFINYlPQEPYIfsg 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 91 TVEENLSFGlrmnGNPKAdTERRVSHVADILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:TIGR01193 563 SILENLLLG----AKENV-SQDEIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 160 PLSNLDAELRVQMrveISRLHKQLGTTMIYVTHDQTEAmTLADRIVVLRAGNIEQIGAPLDLYD 223
Cdd:TIGR01193 638 STSNLDTITEKKI---VNNLLNLQDKTIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLD 697
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
18-216 |
1.16e-21 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 96.55 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPA--DRGIAMVFQSYALYPHlTVEEN 95
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREvlANSVAMVDQDIFLFEG-TVRDN 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 96 LSfgLRMNGNPKADTERRVSHVAdilqITELMKRRP-----------KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNL 164
Cdd:TIGR03796 573 LT--LWDPTIPDADLVRACKDAA----IHDVITSRPggydaelaeggANLSGGQRQRLEIARALVRNPSILILDEATSAL 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 165 DAELRVQmrveISRLHKQLGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:TIGR03796 647 DPETEKI----IDDNLRRRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRG 693
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-229 |
2.49e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.16 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 29 GEFVVFVGPSGCGKST----LLRMIAglediTSGELRIGGKVVNDVE-----PADRGIAMVFQ--SYALYPHLTVEENLS 97
Cdd:PRK15134 312 GETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNrrqllPVRHRIQVVFQdpNSSLNPRLNVLQIIE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 98 FGLRMNgNPKADTERRVSHVADILQIT----ELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMR 173
Cdd:PRK15134 387 EGLRVH-QPTLSAAQREQQVIAVMEEVgldpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 174 VEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQF 229
Cdd:PRK15134 466 ALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
26-225 |
2.81e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 91.77 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 26 VKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN--DVEPADRGIAMVFQ--SYALYPHLTVEENLSFGLR 101
Cdd:PRK15112 36 LREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 102 MNgnPKADTERRVSHVADILQITELMKRR----PKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEIS 177
Cdd:PRK15112 116 LN--TDLEPEQREKQIIETLRQVGLLPDHasyyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLML 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1037261085 178 RLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDP 225
Cdd:PRK15112 194 ELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-224 |
4.86e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 90.72 E-value: 4.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDV---EPADRGI 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVFQSYALYPHLTVEENLSFGLRMNGNPKADT-ERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 157 FDEPLSNLDAELRVQMRVEISRLhKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDD 224
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-214 |
5.21e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.12 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 2 AELSLTNIVKRF--GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDV-EPADR-GI 77
Cdd:PRK11160 337 VSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYsEAALRqAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVFQSYALYPHlTVEENLSFglrmnGNPKADTERrvshVADILQITELMK----------------RrpkQLSGGQRQR 141
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLL-----AAPNASDEA----LIEVLQQVGLEKlleddkglnawlgeggR---QLSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 142 VAIGRAIVREPEVFLFDEPLSNLDAELRVQMrVEISRLHKQlGTTMIYVTHDQTeAMTLADRIVVLRAGNI-EQ 214
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQI-LELLAEHAQ-NKTVLMITHRLT-GLEQFDRICVMDNGQIiEQ 554
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-218 |
6.33e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.96 E-value: 6.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLediTSGELRIGGKVVNDVEPAD----RGI-AMVFQSYALYPHLT 91
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR---SPKGVKGSGSVLLNGMPIDakemRAIsAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 92 VEENLSFG--LRMNGNPKADTerRVSHVADILQITELMK---------RRPKQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:TIGR00955 116 VREHLMFQahLRMPRRVTKKE--KRERVDEVLQALGLRKcantrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 161 LSNLDAeLRVQMRVEISRLHKQLGTTMIYVTHDQT-EAMTLADRIVVLRAGNIEQIGAP 218
Cdd:TIGR00955 194 TSGLDS-FMAYSVVQVLKGLAQKGKTIICTIHQPSsELFELFDKIILMAEGRVAYLGSP 251
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-221 |
7.49e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 94.04 E-value: 7.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 8 NIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVV--NDVEpADRGIAMVFQSYA 85
Cdd:NF033858 271 GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIA-TRRRVGYMSQAFS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 86 LYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:NF033858 350 LYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 166 AELR---VQMRVEISRlhkQLGTTmIYV-THDQTEAMtLADRIVVLRAGNIEQIGAPLDL 221
Cdd:NF033858 430 PVARdmfWRLLIELSR---EDGVT-IFIsTHFMNEAE-RCDRISLMHAGRVLASDTPAAL 484
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-225 |
1.49e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.60 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGEL--RIGGKVVNDV----EPADRGI 77
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyRMRDGQLRDLyalsEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 78 AMVFQSYalyphltVEENLSFGLRMNGNPKADTERR-----VSHVADI-------LQITELMKRR----PKQLSGGQRQR 141
Cdd:PRK11701 87 LRTEWGF-------VHQHPRDGLRMQVSAGGNIGERlmavgARHYGDIratagdwLERVEIDAARiddlPTTFSGGMQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 142 VAIGRAIVREPEVFLFDEPLSNLDaeLRVQMRV--EISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPL 219
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLD--VSVQARLldLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTD 237
|
....*.
gi 1037261085 220 DLYDDP 225
Cdd:PRK11701 238 QVLDDP 243
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-238 |
2.35e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.38 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSG-----ELRIGGKVV---NDVEPADR 75
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyRDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 76 GIAMVFQSYALYPhLTVEENLSFGLRMNG-NPKAD----TERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVR 150
Cdd:PRK14271 102 RVGMLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEfrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 151 EPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLgtTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPAN--- 227
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHaet 258
|
250
....*....|..
gi 1037261085 228 -QFVAGFVGSPK 238
Cdd:PRK14271 259 aRYVAGLSGDVK 270
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-167 |
4.65e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.78 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 20 HGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAdrgiamvFQSYALY--------PHLT 91
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------YHQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 92 VEENLSFGLRMNGNPKADTerrvshVADILQITELMKRR--P-KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDEA------LWEALAQVGLAGFEdvPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
4-212 |
6.67e-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: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIV--KRFGGFeiihgaNLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGELRIGGKVVNDVEPAD--RGIAM 79
Cdd:COG4138 1 LQLNDVAvaGRLGPI------SAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 80 VFQSYALYPHLTVEENLSFGLRMNGNPKAdTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVR-------EP 152
Cdd:COG4138 74 LSQQQSPPFAMPVFQYLALHQPAGASSEA-VEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 153 EVFLFDEPLSNLD-----AELRVqmrveISRLHkQLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG4138 153 QLLLLDEPMNSLDvaqqaALDRL-----LRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-233 |
8.90e-20 |
|
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: 91.23 E-value: 8.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 8 NIVKRF--GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGK-VVNDVEPADRGIAMVFQSY 84
Cdd:TIGR01257 933 NLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdIETNLDAVRQSLGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 85 ALYPHLTVEENLSFGLRMNGnpKADTERRVSHVAdILQITELMKRRPKQ---LSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:TIGR01257 1013 ILFHHLTVAEHILFYAQLKG--RSWEEAQLEMEA-MLEDTGLHHKRNEEaqdLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 162 SNLDAELRVQMRVEIsrLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLyddpANQFVAGF 233
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-214 |
2.58e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.99 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 17 EIIHGANLEVKDGEFVVFVGPSGCGKS----TLLRMIAGLEDI-TSGELRIGGK-VVNDVEPADRG-----IAMVFQS-- 83
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGEsLLHASEQTLRGvrgnkIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMNGNPKADTERrvshvADILQITELM-----KRR----PKQLSGGQRQRVAIGRAIVREPEV 154
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLHRGMRREAAR-----GEILNCLDRVgirqaAKRltdyPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 155 FLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGN-IEQ 214
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRcVEQ 238
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-221 |
5.09e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.61 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 5 SLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN--DVEPADRGIAMVFQ 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 SYALYPHLTVEENLSFGlRMN-----GNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:PRK10575 93 QLPAAEGMTVRELVAIG-RYPwhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 158 DEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-218 |
5.83e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.98 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGELRIGGKVVNDVEPAD----RG---------IAM-VFQSYALYp 88
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMpVFQYLTLH- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 89 hltveenlsfglRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRV-------AIGRAIVREPEVFLFDEPL 161
Cdd:PRK03695 94 ------------QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVrlaavvlQVWPDINPAGQLLLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 162 SNLDAELRVQMRVEISRLhKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:PRK03695 162 NSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-236 |
6.06e-19 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 84.88 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIggkvvndvEPADRGIAMVFQ- 82
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATY--------IMRSGAELELYQl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 SYALYPHLT------VEENLSFGLRMNGNPKADTERR-----VSHVADI-------LQITELMKRR----PKQLSGGQRQ 140
Cdd:TIGR02323 76 SEAERRRLMrtewgfVHQNPRDGLRMRVSAGANIGERlmaigARHYGNIrataqdwLEEVEIDPTRiddlPRAFSGGMQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 141 RVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLD 220
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQ 235
|
250
....*....|....*.
gi 1037261085 221 LYDDPANQFVAGFVGS 236
Cdd:TIGR02323 236 VLDDPQHPYTQLLVSS 251
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-193 |
9.35e-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: 87.42 E-value: 9.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRGIAMVFqsYALYPHL--- 90
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV--CAQDAHLfdt 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 91 TVEENLSFGlrmngNPKAdTERRVSHVADILQITELMKRRP-----------KQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:TIGR02868 424 TVRENLRLA-----RPDA-TDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....*
gi 1037261085 160 PLSNLDAELRVQMrveISRLHKQL-GTTMIYVTHD 193
Cdd:TIGR02868 498 PTEHLDAETADEL---LEDLLAALsGRTVVLITHH 529
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-212 |
1.42e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 22 ANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD---RGIAMV---FQSYALYPHLTVEEN 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairAGIMLCpedRKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 96 LS---------FGLRMNGNPKADTERRvshvadilQITELMKRRP------KQLSGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:PRK11288 352 INisarrhhlrAGCLINNRWEAENADR--------FIRSLNIKTPsreqliMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 161 LSNLDaelrVQMRVEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:PRK11288 424 TRGID----VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-192 |
1.47e-18 |
|
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: 82.93 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPA-DRGIAMVFQSYALYPHLTV 92
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 93 EENLSFGLRMNGNPKadterrVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAElRVQM 172
Cdd:cd03231 91 LENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA-GVAR 163
|
170 180
....*....|....*....|
gi 1037261085 173 RVEISRLHKQLGTTMIYVTH 192
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-229 |
1.66e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.83 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKS----TLLRMI--AGLEdITSGEL---RIGGKVVNDVEPAD------RG--IAMVFQS-- 83
Cdd:PRK10261 36 SFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGL-VQCDKMllrRRSRQVIELSEQSAaqmrhvRGadMAMIFQEpm 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPHLTVEENLSFGLRMN-GNPKADTERRVSHVADILQITE---LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:PRK10261 115 TSLNPVFTVGEQIAESIRLHqGASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADE 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 160 PLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQF 229
Cdd:PRK10261 195 PTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPY 264
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-297 |
2.06e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 87.14 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRiggkvvndvepADRGIAMVFQSyALYPHLTVEENL 96
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 97 SFGLRMNGNPKADTERRVSHVADILQI-----TELmKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL--R 169
Cdd:PTZ00243 742 LFFDEEDAARLADAVRVSQLEADLAQLgggleTEI-GEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeR 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 170 VQMRVEISRLHkqlGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIGAPLDlyddpanqfvagFVGSPKMNFLTAVVVEA 249
Cdd:PTZ00243 821 VVEECFLGALA---GKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSAD------------FMRTSLYATLAAELKEN 884
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1037261085 250 QPGRAVIALESnpETRLPVPIAEPVEAGTKVTLGIRPEHFADAGAGDA 297
Cdd:PTZ00243 885 KDSKEGDADAE--VAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAALDA 930
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-210 |
2.84e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADR---GIAMV 80
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSqeaGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYPHLTVEENLSFGLRMNGNPKADTERRVSHVADILqITEL-MKRRPKQLSG----GQRQRVAIGRAIVREPEVF 155
Cdd:PRK10762 85 HQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKL-LARLnLRFSSDKLVGelsiGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 156 LFDEPLSNL-DAELRVQMRVeISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:PRK10762 164 IMDEPTDALtDTETESLFRV-IRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-223 |
2.99e-18 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 86.54 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVvndvepadrgiAMVFQSyALYPHLTVEENLSF 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV-----------AYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 99 GLRMNGNPKADTERRVSHVADiLQI------TELmKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQM 172
Cdd:TIGR00957 722 GKALNEKYYQQVLEACALLPD-LEIlpsgdrTEI-GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 173 RVEISRLHKQL-GTTMIYVTHDQTeAMTLADRIVVLRAGNIEQIGAPLDLYD 223
Cdd:TIGR00957 800 FEHVIGPEGVLkNKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-215 |
4.03e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 26 VKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD---RGIAMVFQSY---ALYPHLTVEENLSFG 99
Cdd:PRK09700 286 VCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdnGFFPNFSIAQNMAIS 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 100 --LRMNG--------NPKadTERRVSHVA-DILQIT-ELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDae 167
Cdd:PRK09700 366 rsLKDGGykgamglfHEV--DEQRTAENQrELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGID-- 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 168 lrVQMRVEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQI 215
Cdd:PRK09700 442 --VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
23-267 |
4.44e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 84.01 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGL---EDITSGELRIGGK-VVNDVEPA-----DRGIAMVFQS--YALYPHLT 91
Cdd:PRK09473 36 NFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGReILNLPEKElnklrAEQISMIFQDpmTSLNPYMR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 92 VEENLSFGLRMN-GNPKADTERRVSHVADILQITELMKRR---PKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:PRK09473 116 VGEQLMEVLMLHkGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 168 LRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGfvgspkmnFLTAVVV 247
Cdd:PRK09473 196 VQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIG--------LLNAVPR 267
|
250 260
....*....|....*....|..
gi 1037261085 248 EAQPGRAVIALESNPET--RLP 267
Cdd:PRK09473 268 LDAEGESLLTIPGNPPNllRLP 289
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-216 |
4.79e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 85.15 E-value: 4.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD-RG-IAMVFQSYALYPHlTVEEN 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSrLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 96 LSFGlrmngNPKAdTERRVSHVA-------DILQI-----TELmKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PRK10789 409 IALG-----RPDA-TQQEIEHVArlasvhdDILRLpqgydTEV-GERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 164 LDAELRVQMRVEISRLHKqlGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:PRK10789 482 VDGRTEHQILHNLRQWGE--GRTVIISAH-RLSALTEASEILVMQHGHIAQRG 531
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-195 |
2.42e-17 |
|
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: 78.35 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIggkvvndvePADRGIAMVFQ-SYalyphltveenLSFG-L 100
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQrPY-----------LPLGtL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 101 RmngnpkadterrvshvaDILqitelmkRRP--KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRveisR 178
Cdd:cd03223 81 R-----------------EQL-------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY----Q 132
|
170
....*....|....*..
gi 1037261085 179 LHKQLGTTMIYVTHDQT 195
Cdd:cd03223 133 LLKELGITVISVGHRPS 149
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-212 |
2.85e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 82.74 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD---RGIAMVFQSY---ALYPHLTV 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 93 EENLSF-GLR----MNGNPKADTERR-VSHVADILQI-TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:PRK10762 348 KENMSLtALRyfsrAGGSLKHADEQQaVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1037261085 166 aelrVQMRVEISRL---HKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:PRK10762 428 ----VGAKKEIYQLinqFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-210 |
7.08e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 81.70 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 6 LTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN---DVEPADRGIAMVFQ 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 SYALYPHLTVEENLSFGLRMNGNPKADTE---RRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGMFVDQDkmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 160 PLSNLdAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAG 210
Cdd:PRK10982 161 PTSSL-TEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-226 |
1.18e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.59 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 17 EIIHGANLEVKDGEFVVFVGPSGCGKStlLRMIAGLEDITSGELRIGGKVVND---VEPAD---RGIAMVFQS--YALYP 88
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDgkpVAPCAlrgRKIATIMQNprSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 89 HLTVEENLSFGLRMNGNPKAD-TERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDae 167
Cdd:PRK10418 95 LHTMHTHARETCLALGKPADDaTLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD-- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 168 LRVQMRV--EISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPA 226
Cdd:PRK10418 173 VVAQARIldLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-194 |
1.33e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.69 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 16 FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGElrigGKVVNDVEPADRGIAMVFQSYALYPHLTVEEN 95
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA----GCVDVPDNQFGREASLIDAIGRKGDFKDAVEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 96 LS-FGLrmNGNPkadterrvshvadilqiteLMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRV 174
Cdd:COG2401 119 LNaVGL--SDAV-------------------LWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180
....*....|....*....|
gi 1037261085 175 EISRLHKQLGTTMIYVTHDQ 194
Cdd:COG2401 178 NLQKLARRAGITLVVATHHY 197
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-225 |
1.66e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.40 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGG----FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGELRIGGKVVNDVEP 72
Cdd:PRK11022 1 MALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 73 ADR------GIAMVFQS--YALYPHLTVEENLSFGLRMN--GNPKADTERRVshvaDILQ---ITELMKR---RPKQLSG 136
Cdd:PRK11022 81 KERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHqgGNKKTRRQRAI----DLLNqvgIPDPASRldvYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 137 GQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
....*....
gi 1037261085 217 APLDLYDDP 225
Cdd:PRK11022 237 KAHDIFRAP 245
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-216 |
3.10e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 77.37 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLE--DITSGELRIGGKVVNDVEPADR---GIA 78
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERahlGIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVFQsyalYPhltVE----ENLSFgLRM--------NGNPKADTerrVSHVADILQITELMKRRPKQL--------SGGQ 138
Cdd:CHL00131 88 LAFQ----YP---IEipgvSNADF-LRLaynskrkfQGLPELDP---LEFLEIINEKLKLVGMDPSFLsrnvnegfSGGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 139 RQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLhKQLGTTMIYVTHDQteamTLADRIV-----VLRAGNIE 213
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQ----RLLDYIKpdyvhVMQNGKII 231
|
...
gi 1037261085 214 QIG 216
Cdd:CHL00131 232 KTG 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-212 |
3.19e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 3.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNI-VKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADR---GIAM 79
Cdd:COG3845 258 LEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 80 V---FQSYALYPHLTVEENLSFGL----RMNGNPKADTERRVSHVAdilqitELMKR---RP-------KQLSGGQRQRV 142
Cdd:COG3845 338 IpedRLGRGLVPDMSVAENLILGRyrrpPFSRGGFLDRKAIRAFAE------ELIEEfdvRTpgpdtpaRSLSGGNQQKV 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 143 AIGRAIVREPEVFLFDEPLSNLD--AelrvqmrveISRLHKQL------GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDvgA---------IEFIHQRLlelrdaGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
18-214 |
4.36e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 79.38 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPA--DRGIAMVFQ-----SYALYPHL 90
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQdpvvlADTFLANV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 91 TVEENLSfglrmngnpkadtERRVSHVADILQITELMKRRPK-----------QLSGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:PRK10790 436 TLGRDIS-------------EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 160 PLSNLDA--ELRVQMRVEISRLHkqlgTTMIYVTHdQTEAMTLADRIVVLRAGN-IEQ 214
Cdd:PRK10790 503 ATANIDSgtEQAIQQALAAVREH----TTLVVIAH-RLSTIVEADTILVLHRGQaVEQ 555
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-210 |
5.75e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.15 E-value: 5.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLediTSGELRIGGKVVNDVEPAD---RGIAMVFQSYALYPHLTVEE 94
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGR---IQGNNFTGTILANNRKPTKqilKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 95 NLSFG--LRMngnPKADTERRVSHVADILqITELMKRRPKQ----------LSGGQRQRVAIGRAIVREPEVFLFDEPLS 162
Cdd:PLN03211 160 TLVFCslLRL---PKSLTKQEKILVAESV-ISELGLTKCENtiignsfirgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1037261085 163 NLDAELRVQMRVEISRLhKQLGTTMIYVTHD-QTEAMTLADRIVVLRAG 210
Cdd:PLN03211 236 GLDATAAYRLVLTLGSL-AQKGKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-210 |
1.59e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 74.67 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRG------IAMVFQSYALYpHLTVEENL 96
Cdd:cd03290 21 NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrysVAYAAQKPWLL-NATVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 97 SFGLRMNGNPKADTERRVSHVADI--------LQITElmkrRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:cd03290 100 TFGSPFNKQRYKAVTDACSLQPDIdllpfgdqTEIGE----RGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1037261085 169 RVQ-MRVEISRLHKQLGTTMIYVTHdQTEAMTLADRIVVLRAG 210
Cdd:cd03290 176 SDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-207 |
2.60e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRiggkvvndvEPADRGIAMVFQS 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLRIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YALYPH--LTVEEnlsFGLRMNGNPKADTERRVSHVadilQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:PRK09544 76 LYLDTTlpLTVNR---FLRLRPGTKKEDILPALKRV----QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1037261085 162 SNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVL 207
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-208 |
3.63e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.53 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 15 GFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADRgIAMVFQSYAL---YPHLt 91
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-VAYVPQSEEVdwsFPVL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 92 VEENLSFG----LRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDae 167
Cdd:PRK15056 97 VEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD-- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1037261085 168 lrVQMRVEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLR 208
Cdd:PRK15056 175 --VKTEARIISLLRELrdeGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
23-207 |
4.06e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.34 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAdRGIAMVFQSYALYPHLTVEENLSFglrM 102
Cdd:PRK13543 31 DFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS-RFMAYLGHLPGLKADLSTLENLHF---L 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 103 NGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE-LRVQMRVEISRLHK 181
Cdd:PRK13543 107 CGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEgITLVNRMISAHLRG 186
|
170 180
....*....|....*....|....*.
gi 1037261085 182 QLGTtmIYVTHDQTEAMTLADRIVVL 207
Cdd:PRK13543 187 GGAA--LVTTHGAYAAPPVRTRMLTL 210
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-216 |
5.57e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 76.70 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLR-MIAGLEDITSGELRIGGKVvndvepadrgiAMVFQSYALYpHLTVEENLSFGLR 101
Cdd:PLN03130 637 NLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTV-----------AYVPQVSWIF-NATVRDNILFGSP 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 102 MNgnpkADTERRVSHVA------------DILQITElmkrRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAElr 169
Cdd:PLN03130 705 FD----PERYERAIDVTalqhdldllpggDLTEIGE----RGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH-- 774
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1037261085 170 VQMRVEISRLHKQL-GTTMIYVThDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:PLN03130 775 VGRQVFDKCIKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEG 821
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-218 |
5.61e-15 |
|
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: 73.30 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKST----LLRMIagleDITSGELRIGGKVVNDVEPAD--RGIAMVFQSyalyPHL- 90
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQD----PVLf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 91 --TVEENL-SFGLRmngnpkadTERRVSHVADILQITELMKRRPKQL-----------SGGQRQRVAIGRAIVREPEVFL 156
Cdd:cd03244 91 sgTIRSNLdPFGEY--------SDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 157 FDEPLSNLDAELRVQMRVEISRLHKqlGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:cd03244 163 LDEATASVDPETDALIQKTIREAFK--DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-169 |
6.47e-15 |
|
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: 75.74 E-value: 6.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 8 NIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVndvepadrgIAMVFQSY-AL 86
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK---------LAYVDQSRdAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 87 YPHLTVEENLSFGLrmngnpkadterrvshvaDILQI--TELMKR---------------RPKQLSGGQRQRVAIGRAIV 149
Cdd:TIGR03719 398 DPNKTVWEEISGGL------------------DIIKLgkREIPSRayvgrfnfkgsdqqkKVGQLSGGERNRVHLAKTLK 459
|
170 180
....*....|....*....|.
gi 1037261085 150 REPEVFLFDEPLSNLDAE-LR 169
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVEtLR 480
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-207 |
7.42e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 75.59 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 3 ELSlTNIVKRFG--GFEIIhgaNLEV-KDGEFVVFVGPSGCGKSTLLRMIAG---------------------------- 51
Cdd:COG1245 74 ELE-EDPVHRYGenGFRLY---GLPVpKKGKVTGILGPNGIGKSTALKILSGelkpnlgdydeepswdevlkrfrgtelq 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 52 --LEDITSGELriggKVVNDVEPADRgIAMVFQSyalyphlTVEENLSfglrmngnpKADTERRVSHVADILQITELMKR 129
Cdd:COG1245 150 dyFKKLANGEI----KVAHKPQYVDL-IPKVFKG-------TVRELLE---------KVDERGKLDELAEKLGLENILDR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 130 RPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDaelrVQMRVEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVV 206
Cdd:COG1245 209 DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD----IYQRLNVARLIRELaeeGKYVLVVEHDLAILDYLADYVHI 284
|
.
gi 1037261085 207 L 207
Cdd:COG1245 285 L 285
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-207 |
1.39e-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: 72.78 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 26 VKDGEFVVFVGPSGCGKSTLLRMIAG------------------------------LEDITSGELriggKVVNDVEPADR 75
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdwdeildefrgselqnyFTKLLEGDV----KVIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 76 gIAMVFQSyalyphlTVEENLSfglrmngnpKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:cd03236 99 -IPKAVKG-------KVGELLK---------KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 156 LFDEPLSNLDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVL 207
Cdd:cd03236 162 FFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-215 |
1.55e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 74.62 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 3 ELSLTNIVKRFG--GFEIiHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIA 78
Cdd:PRK10522 322 TLELRNVTFAYQdnGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVFQSYALYPHLTVEENLSfglrmngnpkADTERrvshVADILQITElMKRRPK---------QLSGGQRQRVAIGRAIV 149
Cdd:PRK10522 401 AVFTDFHLFDQLLGPEGKP----------ANPAL----VEKWLERLK-MAHKLEledgrisnlKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 150 REPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQtEAMTLADRIVVLRAGNIEQI 215
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLSEL 530
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
9-207 |
1.61e-14 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 71.06 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 9 IVKRFGGFEIIHGANlEVKDGEFVVFVGPSGCGKSTLLRMIAGLEditsgelriggkvvndvEPADrgiamvfqsyalyp 88
Cdd:cd03222 6 CVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQL-----------------IPNG-------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 89 hltveENLSFGLrmngnpkadterrvshvadilqITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:cd03222 54 -----DNDEWDG----------------------ITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQ 106
|
170 180 190
....*....|....*....|....*....|....*....
gi 1037261085 169 RVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVL 207
Cdd:cd03222 107 RLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-207 |
1.89e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.46 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 26 VKDGEFVVFVGPSGCGKSTLLRMIAG------------------------------LEDITSGELRiggkVVNDVEPADR 75
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGelipnlgdyeeepswdevlkrfrgtelqnyFKKLYNGEIK----VVHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 76 gIAMVFQSyalyphlTVEENLSfglrmngnpKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:PRK13409 172 -IPKVFKG-------KVRELLK---------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 156 LFDEPLSNLDaelrVQMRVEISRLHKQL--GTTMIYVTHDQTEAMTLADRIVVL 207
Cdd:PRK13409 235 FFDEPTSYLD----IRQRLNVARLIRELaeGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-218 |
2.05e-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: 71.29 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 3 ELSLTNIVKRFGGF--EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIA 78
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVFQSYALYPHlTVEENLsfglrmngnpkaDTERRVS--HVADILQITElmkrRPKQLSGGQRQRVAIGRAIVREPEVFL 156
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNL------------DPFDEYSdeEIYGALRVSE----GGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 157 FDEPLSNL----DAELRVQMRVEISrlhkqlGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIGAP 218
Cdd:cd03369 149 LDEATASIdyatDALIQKTIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
23-221 |
2.30e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 74.28 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSYALYpHLTVEENLSFGl 100
Cdd:PRK11176 363 NFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVALVSQNVHLF-NDTIANNIAYA- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 101 RMNGNPKADTER--RVSHVADILQITE-----LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMR 173
Cdd:PRK11176 441 RTEQYSREQIEEaaRMAYAMDFINKMDngldtVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQ 520
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1037261085 174 VEISRLHKQlgTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:PRK11176 521 AALDELQKN--RTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-222 |
3.65e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.86 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGleditsgelriggkvvnDVEPADRGIAMVFQSYALYPHL------TVEENL 96
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVVIRGSVAYVPQVswifnaTVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 97 SFGLRMNGNP--KADTERRVSHVADIL---QITELmKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAElrVQ 171
Cdd:PLN03232 700 LFGSDFESERywRAIDVTALQHDLDLLpgrDLTEI-GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH--VA 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 172 MRVEISRLHKQL-GTTMIYVThDQTEAMTLADRIVVLRAGNIEQIGAPLDLY 222
Cdd:PLN03232 777 HQVFDSCMKDELkGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-215 |
5.46e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.86 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGELRIGGKVVNDVEPADR------GIAMVFQ--SYALYPHL 90
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQepSSCLDPSA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 91 TVEENL-------SFGLRMNGNPKADTERRVS--HVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:COG4170 107 KIGDQLieaipswTFKGKWWQRFKWRKKRAIEllHRVGIKDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPT 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 162 SNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVL------RAGNIEQI 215
Cdd:COG4170 187 NAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLycgqtvESGPTEQI 246
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-210 |
7.98e-14 |
|
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: 71.04 E-value: 7.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKvvndvepadrgIAMVFQSYALYPHlTVEENLSFGLRM 102
Cdd:cd03291 57 NLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIFGVSY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 103 NgnpkadtERRVSHVADILQITELMKRRPKQ-----------LSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDaeLRVQ 171
Cdd:cd03291 125 D-------EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD--VFTE 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1037261085 172 MRVEISRLHKQLGT-TMIYVThDQTEAMTLADRIVVLRAG 210
Cdd:cd03291 196 KEIFESCVCKLMANkTRILVT-SKMEHLKKADKILILHEG 234
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-165 |
1.39e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.82 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELRIGGKVVNDVEPADR---GIA 78
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVFQsyalYPhltVE-ENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQL---------------SGGQRQRV 142
Cdd:PRK09580 82 MAFQ----YP---VEiPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRN 154
|
170 180
....*....|....*....|...
gi 1037261085 143 AIGRAIVREPEVFLFDEPLSNLD 165
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLD 177
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-242 |
2.38e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 71.58 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 26 VKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGK-VVNDVEPADRGIAMVFQSYALYPHLTVEENLSFGLRMNG 104
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 105 NPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQlG 184
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-G 2120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 185 TTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQFVAGF-VGSPKMNFL 242
Cdd:TIGR01257 2121 RAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMkIKSPKDDLL 2179
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-235 |
5.09e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.82 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITS--GELRIGGKVV-----NDVEpaDRG 76
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCrfkdiRDSE--ALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 IAMVFQSYALYPHLTVEENLSFglrmnGNPKA--------DTERRVshvadilqiTELMKR---------RPKQLSGGQR 139
Cdd:NF040905 80 IVIIHQELALIPYLSIAENIFL-----GNERAkrgvidwnETNRRA---------RELLAKvgldespdtLVTDIGVGKQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 140 QRVAIGRAIVREPEVFLFDEP-----------LSNLDAELRVQmrveisrlhkqlGTTMIYVTHDQTEAMTLADRIVVLR 208
Cdd:NF040905 146 QLVEIAKALSKDVKLLILDEPtaalneedsaaLLDLLLELKAQ------------GITSIIISHKLNEIRRVADSITVLR 213
|
250 260 270
....*....|....*....|....*....|
gi 1037261085 209 AGN-IEQigapLDLYDDPANQ--FVAGFVG 235
Cdd:NF040905 214 DGRtIET----LDCRADEVTEdrIIRGMVG 239
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-210 |
7.72e-13 |
|
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: 69.94 E-value: 7.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKvvndvepadrgIAMVFQSYALYPHlTVEENLSFGLRM 102
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNIIFGLSY 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 103 NgnpkadtERRVSHVADILQITELMKRRPKQ-----------LSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDaelrVQ 171
Cdd:TIGR01271 514 D-------EYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD----VV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1037261085 172 MRVEI--SRLHKQLGT-TMIYVThDQTEAMTLADRIVVLRAG 210
Cdd:TIGR01271 583 TEKEIfeSCLCKLMSNkTRILVT-SKLEHLKKADKILLLHEG 623
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-269 |
8.67e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.75 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 16 FEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGELRIGGKVVNDVEPADRG-IAMVFQSYALYPHL 90
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYRGdVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 91 TVEENLSFGLRMNG---NPKA-DTERRVSHVADI------LQITELMK---RRPKQLSGGQRQRVAIGRAIVREPEVFLF 157
Cdd:TIGR00956 154 TVGETLDFAARCKTpqnRPDGvSREEYAKHIADVymatygLSHTRNTKvgnDFVRGVSGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 158 DEPLSNLDAELRVQ-MRV--EISRLHKQLGTTMIYvtHDQTEAMTLADRIVVLRAGNIEQIGAPldlydDPANQFVA--G 232
Cdd:TIGR00956 234 DNATRGLDSATALEfIRAlkTSANILDTTPLVAIY--QCSQDAYELFDKVIVLYEGYQIYFGPA-----DKAKQYFEkmG 306
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1037261085 233 FVGSPKM---NFLTAVvveaqpgravialeSNPETRLPVP 269
Cdd:TIGR00956 307 FKCPDRQttaDFLTSL--------------TSPAERQIKP 332
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-160 |
8.93e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.38 E-value: 8.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 5 SLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRI-GGkvvnDVepADRG------- 76
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlGG----DM--ADARhrravcp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 77 -IAMVFQSYA--LYPHLTVEENLSFGLRMNGNPKADTERRvshVADILQITEL--MKRRP-KQLSGGQRQRVAIGRAIVR 150
Cdd:NF033858 77 rIAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRR---IDELLRATGLapFADRPaGKLSGGMKQKLGLCCALIH 153
|
170
....*....|
gi 1037261085 151 EPEVFLFDEP 160
Cdd:NF033858 154 DPDLLILDEP 163
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-169 |
1.82e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.22 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 8 NIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVndvepadrgIAMVFQSY-AL 86
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVK---------LAYVDQSRdAL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 87 YPHLTVEENLSFGLrmngnpkadterrvshvaDILQI--TELMKR---------------RPKQLSGGQRQRVAIGRAIV 149
Cdd:PRK11819 400 DPNKTVWEEISGGL------------------DIIKVgnREIPSRayvgrfnfkggdqqkKVGVLSGGERNRLHLAKTLK 461
|
170 180
....*....|....*....|.
gi 1037261085 150 REPEVFLFDEPLSNLDAE-LR 169
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVEtLR 482
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-215 |
2.09e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVND---VEPADRGIAMVFQ---SYALYPHLTV 92
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaNEAINHGFALVTEerrSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 93 EENL----------SFGLRMNGNPKADTErrvsHVADILQI-TELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPL 161
Cdd:PRK10982 344 GFNSlisnirnyknKVGLLDNSRMKSDTQ----WVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1037261085 162 SNLDaelrVQMRVEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIEQI 215
Cdd:PRK10982 420 RGID----VGAKFEIYQLIAELakkDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
36-192 |
2.16e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.36 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 36 GPSGCGKSTLLRMIAGLEDITSGELRIGGKVVN-DVEPADRGIAMVFQSYALYPHLTVEENLSFGLRMngnpkADTERRV 114
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHF-----SPGAVGI 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 115 SHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDaELRVQMRVEISRLHKQLGTTMIYVTH 192
Cdd:PRK13540 109 TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD-ELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
35-193 |
2.68e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.65 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 35 VGPSGCGKSTLLRMIAGLEDITSGELRIGgkvvndvepADRGIAMVFQSYALYPHLTVEENLSFGL--------RMN--- 103
Cdd:TIGR03719 37 LGLNGAGKSTLLRIMAGVDKDFNGEARPQ---------PGIKVGYLPQEPQLDPTKTVRENVEEGVaeikdaldRFNeis 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 104 ---GNPKADT----------------------ERRVSHVADILqitelmkRRP------KQLSGGQRQRVAIGRAIVREP 152
Cdd:TIGR03719 108 akyAEPDADFdklaaeqaelqeiidaadawdlDSQLEIAMDAL-------RCPpwdadvTKLSGGERRRVALCRLLLSKP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1037261085 153 EVFLFDEPLSNLDAElrvqmrvEISRLHKQLGT---TMIYVTHD 193
Cdd:TIGR03719 181 DMLLLDEPTNHLDAE-------SVAWLERHLQEypgTVVAVTHD 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-207 |
2.79e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELriggkVVNDVEPAD--------RGIAMVFQ------ 82
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-----IINDSHNLKdinlkwwrSKIGVVSQdpllfs 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 83 -------SYALYPhLTVEENLSFGLRMNGN-PKADTERRVSHVA-------DILQIT---ELMKRRPK------------ 132
Cdd:PTZ00265 474 nsiknniKYSLYS-LKDLEALSNYYNEDGNdSQENKNKRNSCRAkcagdlnDMSNTTdsnELIEMRKNyqtikdsevvdv 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 133 --------------------------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTT 186
Cdd:PTZ00265 553 skkvlihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 632
|
250 260
....*....|....*....|.
gi 1037261085 187 MIYVTHdQTEAMTLADRIVVL 207
Cdd:PTZ00265 633 TIIIAH-RLSTIRYANTIFVL 652
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-212 |
5.99e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.90 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAG---LEDitsGELRIGGKVV---------N 68
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDD---GRIIYEQDLIvarlqqdppR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 69 DVEPA-----DRGIAMVFQSYALYPHLT--VEENLSfglRMNGNPKADTERRVSH---------VADILQITELMKRRP- 131
Cdd:PRK11147 78 NVEGTvydfvAEGIEEQAEYLKRYHDIShlVETDPS---EKNLNELAKLQEQLDHhnlwqlenrINEVLAQLGLDPDAAl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 132 KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAElrvqmrvEISRLHKQLGT---TMIYVTHDQTEAMTLADRIVVLR 208
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-------TIEWLEGFLKTfqgSIIFISHDRSFIRNMATRIVDLD 227
|
....
gi 1037261085 209 AGNI 212
Cdd:PRK11147 228 RGKL 231
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-167 |
6.39e-12 |
|
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: 63.80 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELRIGGKVVNDVEPadRGIAMVFQSYALYPHLTVEE 94
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQ--RSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 95 NLSFGLRMNGnpkadterrvshvadilqitelmkrrpkqLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:cd03232 99 ALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-218 |
6.71e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 66.36 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEfVVF-VGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD-RG-IAMVFQSYALYPHLtveenlsfg 99
Cdd:COG4615 352 DLTIRRGE-LVFiVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyRQlFSAVFSDFHLFDRL--------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 100 lrMNGNPKADTER------------RVSHVADILQITElmkrrpkqLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAE 167
Cdd:COG4615 422 --LGLDGEADPARarellerleldhKVSVEDGRFSTTD--------LSQGQRKRLALLVALLEDRPILVFDEWAADQDPE 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1037261085 168 LR-VQMRVEISRLhKQLGTTMIYVTHDQTeAMTLADRIVVLRAGNIEQIGAP 218
Cdd:COG4615 492 FRrVFYTELLPEL-KARGKTVIAISHDDR-YFDLADRVLKMDYGKLVELTGP 541
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-214 |
9.25e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 9.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 57 SGELRIGGKVVNDVEPAD-RGIAMVFQSYALYPHLTVEENLSFGlrmngnpKADTERR-VSHVADILQITELMKRRP--- 131
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG-------KEDATREdVKRACKFAAIDEFIESLPnky 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 132 --------KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHdQTEAMTLADR 203
Cdd:PTZ00265 1349 dtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
170
....*....|....*
gi 1037261085 204 IVVL----RAGNIEQ 214
Cdd:PTZ00265 1428 IVVFnnpdRTGSFVQ 1442
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-207 |
9.29e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.81 E-value: 9.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRiggkvvNDvepadrgiamv 80
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ------SQ----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 81 FQSYALYP-----HLTVEENLSFGLRMNGNPKADTERRVSHV--------------ADILQITELMKRRPKQLSGGQRQR 141
Cdd:PRK10938 64 FSHITRLSfeqlqKLVSDEWQRNNTDMLSPGEDDTGRTTAEIiqdevkdparceqlAQQFGITALLDRRFKYLSTGETRK 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037261085 142 VAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVL 207
Cdd:PRK10938 144 TLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-193 |
9.81e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 9.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 8 NIVKRFggfeiihgaNLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKvvndVEPAdrgiamVFQSY--A 85
Cdd:PRK11147 333 QLVKDF---------SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVA------YFDQHraE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 86 LYPHLTVEENLSFG---LRMNGNPKadterrvsHVADILQ---ITELMKRRP-KQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:PRK11147 394 LDPEKTVMDNLAEGkqeVMVNGRPR--------HVLGYLQdflFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLILD 465
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1037261085 159 EPLSNLDaelrvqmrVEISRLHKQL-----GTTMIyVTHD 193
Cdd:PRK11147 466 EPTNDLD--------VETLELLEELldsyqGTVLL-VSHD 496
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-210 |
1.45e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.90 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 26 VKDGEFVVFVGPSGCGKSTLLRMIAGLED---ITSGELRIGGKVVNdvEPADRGIAMVFQSYALYPHLTVEENLSFGLRM 102
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLD--SSFQRSIGYVQQQDLHLPTSTVRESLRFSAYL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 103 ---NGNPKADTERRVSHVADILQITE----LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLF-DEPLSNLDAelrvQMRV 174
Cdd:TIGR00956 864 rqpKSVSKSEKMEYVEEVIKLLEMESyadaVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDS----QTAW 939
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1037261085 175 EISRLHKQL---GTTMIYVTHdQTEAMTLA--DRIVVLRAG 210
Cdd:TIGR00956 940 SICKLMRKLadhGQAILCTIH-QPSAILFEefDRLLLLQKG 979
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-169 |
3.60e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.81 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 36 GPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVepADRGIAMVFQSYALYPHLTVEENLSFGLRMngnpkADTERRVS 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI--AKPYCTYIGHNLGLKLEMTVFENLKFWSEI-----YNSAETLY 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 116 HVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELR 169
Cdd:PRK13541 106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-221 |
5.74e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAG--LEDITSGELRIGGKVVNDVEP---------ADRGIAMVFQSYAL 86
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDVTLNGEPlaaidaprlARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 87 YPhLTVEENLSFGLRMNGNPKADTERRVSHVAD----ILQITELMKRRPKQLSGGQRQRVAIGRAI---------VREPE 153
Cdd:PRK13547 96 FA-FSAREIVLLGRYPHARRAGALTHRDGEIAWqalaLAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 154 VFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-193 |
5.96e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 35 VGPSGCGKSTLLRMIAGLEDITSGELRI--GGKVvndvepadrGIAMvfQSYALYPHLTVEENLSFGL--------RMN- 103
Cdd:PRK11819 39 LGLNGAGKSTLLRIMAGVDKEFEGEARPapGIKV---------GYLP--QEPQLDPEKTVRENVEEGVaevkaaldRFNe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 104 -----GNPKADT----------------------ERRVSHVADILqitelmkRRP------KQLSGGQRQRVAIGRAIVR 150
Cdd:PRK11819 108 iyaayAEPDADFdalaaeqgelqeiidaadawdlDSQLEIAMDAL-------RCPpwdakvTKLSGGERRRVALCRLLLE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1037261085 151 EPEVFLFDEPLSNLDAElrvqmrvEISRLHKQLGT---TMIYVTHD 193
Cdd:PRK11819 181 KPDMLLLDEPTNHLDAE-------SVAWLEQFLHDypgTVVAVTHD 219
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-225 |
1.95e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.36 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 1 MAELSLTNIVKRF----GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGledITSGELRIGGK--VVNDVE--- 71
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG---VTKDNWRVTADrmRFDDIDllr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 72 --PADR------GIAMVFQSyalyPHLTVEENLSFGLRMNGNPKADT------------ERR---VSHVADILQITELMK 128
Cdd:PRK15093 78 lsPRERrklvghNVSMIFQE----PQSCLDPSERVGRQLMQNIPGWTykgrwwqrfgwrKRRaieLLHRVGIKDHKDAMR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 129 RRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLR 208
Cdd:PRK15093 154 SFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLY 233
|
250
....*....|....*..
gi 1037261085 209 AGNIEQIGAPLDLYDDP 225
Cdd:PRK15093 234 CGQTVETAPSKELVTTP 250
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-221 |
3.93e-10 |
|
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: 61.50 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSYALYphltveenlSFGL 100
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrFKITIIPQDPVLF---------SGSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 101 RMNGNPKAD-TERRVSHVADILQITELMKRRP-----------KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAEL 168
Cdd:TIGR00957 1377 RMNLDPFSQySDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 169 RVQMRveiSRLHKQLGT-TMIYVTHDQTEAMTLAdRIVVLRAGNIEQIGAPLDL 221
Cdd:TIGR00957 1457 DNLIQ---STIRTQFEDcTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
235-289 |
4.23e-10 |
|
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK transport protein.
Pssm-ID: 465563 [Multi-domain] Cd Length: 53 Bit Score: 54.90 E-value: 4.23e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037261085 235 GSPKMNFLTAVVVEAQpgraviALESNPETRLPVP----IAEPVEAGTKVTLGIRPEHF 289
Cdd:pfam17912 1 GSPPMNFLPATVVEDG------LLVLGGGVTLPLPegqvLALKLYVGKEVILGIRPEHI 53
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-197 |
6.91e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 6 LTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAG------LEDIT-SGELRIGGKVVNDVEpadRGIA 78
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgySNDLTlFGRRRGSGETIWDIK---KHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVfqSYALYPHLTVEENL----------SFGLRmngnpKADTERR---VSHVADILQITELMKRRP-KQLSGGQRQRVAI 144
Cdd:PRK10938 340 YV--SSSLHLDYRVSTSVrnvilsgffdSIGIY-----QAVSDRQqklAQQWLDILGIDKRTADAPfHSLSWGQQRLALI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1037261085 145 GRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLHKQLGTTMIYVTHDQTEA 197
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-192 |
9.25e-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: 60.15 E-value: 9.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIggkvvndvePADRGIAMVFQSyalyPHLTVEE-------- 94
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQR----PYMTLGTlrdqiiyp 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 95 NLSFGLRMNGNPKADTERrvshVADILQITELMKRR---------PKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSnld 165
Cdd:TIGR00954 539 DSSEDMKRRGLSDKDLEQ----ILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTS--- 611
|
170 180
....*....|....*....|....*..
gi 1037261085 166 aELRVQMRVEISRLHKQLGTTMIYVTH 192
Cdd:TIGR00954 612 -AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-250 |
1.10e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSYALYPHlTVEEN 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFSG-TVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 96 LS-FGLRMNGNPKADTERrvSHVADILqitelmKRRP-----------KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSN 163
Cdd:PLN03232 1330 IDpFSEHNDADLWEALER--AHIKDVI------DRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 164 LDAELRVQMRVEISRLHKQlgTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDPANQF--VAGFVGSPKMNF 241
Cdd:PLN03232 1402 VDVRTDSLIQRTIREEFKS--CTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFfrMVHSTGPANAQY 1478
|
....*....
gi 1037261085 242 LTAVVVEAQ 250
Cdd:PLN03232 1479 LSNLVFERR 1487
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-212 |
1.42e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.14 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 4 LSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGElriggkvVNDVEPADRGiamvfqs 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-------VKWSENANIG------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 84 YalYPHLTVEEnlsFGLRMN--------GNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:PRK15064 386 Y--YAQDHAYD---FENDLTlfdwmsqwRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 156 LFDEPLSNLDAElrvqmrvEISRLHKQLGT---TMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:PRK15064 461 VMDEPTNHMDME-------SIESLNMALEKyegTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
9-212 |
2.25e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.21 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 9 IVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCG--KSTLLRMIAGLE--------DITSGELRIGGKVVNDVEPADRGIA 78
Cdd:NF000106 19 LVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrrpwrf*TWCANRRALRRTIG*HRPVR*GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVFQSyalyphltvEENLSFGLRMNGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFD 158
Cdd:NF000106 99 ESFSG---------RENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 159 EPLSNLDAELRVQMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-212 |
1.45e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 17 EIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGL-EDITSGELRIGGKVVNDVEPAD---RGIAMVFQS---YALYPH 89
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 90 LTVEEN--------LSFGLRMNGNPKADTERRvshvadilQITELMKRRP------KQLSGGQRQRVAIGRAIVREPEVF 155
Cdd:PRK13549 356 MGVGKNitlaaldrFTGGSRIDDAAELKTILE--------SIQRLKVKTAspelaiARLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 156 LFDEPLSNLDaelrVQMRVEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:PRK13549 428 ILDEPTRGID----VGAKYEIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-213 |
1.83e-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: 55.99 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 26 VKDGEFVVFVGPSGCGKSTLLRMIAGL-EDITSGELRIGGKVVNDVEPAD---RGIAMVFQS---YALYPHLTVEENLSF 98
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILGVGKNITL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 99 GL--RMNGNPKADTERRVSHVADILQITELMKRRP----KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDaelrVQM 172
Cdd:TIGR02633 363 SVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD----VGA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1037261085 173 RVEISRLHKQL---GTTMIYVTHDQTEAMTLADRIVVLRAGNIE 213
Cdd:TIGR02633 439 KYEIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-233 |
4.07e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVvndvepadrgiAMVFQSYALYPHLTVEENLSFGLRM 102
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------ALIAISSGLNGQLTGIENIELKGLM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 103 NGNPKADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLhKQ 182
Cdd:PRK13545 113 MGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF-KE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 183 LGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQIGAPLDLYDDpANQFVAGF 233
Cdd:PRK13545 192 QGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH-YDEFLKKY 241
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-219 |
1.02e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGELriggkvvndvepadrgiamvfqsyalyphltveenlsfgLRMNGNPKA 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV---------------------------------------IYIDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 109 DTERRVSHVadilqitELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEIS-----RLHKQL 183
Cdd:smart00382 43 EEVLDQLLL-------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEK 115
|
170 180 190
....*....|....*....|....*....|....*.
gi 1037261085 184 GTTMIYVTHDQTeamTLADRIVVLRAGNIEQIGAPL 219
Cdd:smart00382 116 NLTVILTTNDEK---DLGPALLRRRFDRRIVLLLIL 148
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
28-216 |
1.27e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 28 DGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVvndvepadrgiAMVFQSYALYPHLTVEENLSFGLRMNGNPK 107
Cdd:PRK13546 49 EGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV-----------SVIAISAGLSGQLTGIENIEFKMLCMGFKR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 108 ADTERRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRVQMRVEISRLhKQLGTTM 187
Cdd:PRK13546 118 KEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-KEQNKTI 196
|
170 180
....*....|....*....|....*....
gi 1037261085 188 IYVTHDQTEAMTLADRIVVLRAGNIEQIG 216
Cdd:PRK13546 197 FFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-212 |
1.28e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPADR-GIAMVF-----QSYALYPHLTVEENL 96
Cdd:PRK15439 283 SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWNV 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 97 SfGLRMNG-----NPKADTeRRVSHVADILQITELMKRRP-KQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDAELRV 170
Cdd:PRK15439 363 C-ALTHNRrgfwiKPAREN-AVLERYRRALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1037261085 171 QMRVEISRLHKQlGTTMIYVTHDQTEAMTLADRIVVLRAGNI 212
Cdd:PRK15439 441 DIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-165 |
9.18e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 32 VVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVvndvepadrGIAMVFQSYALYPHLTVEENLSFglrMNGNPKADTE 111
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV---------RMAVFSQHHVDGLDLSSNPLLYM---MRCFPGVPEQ 605
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 112 RRVSHVADILQITELMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:PLN03073 606 KLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-205 |
1.35e-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: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 19 IHGANLEVKDGEFVVFVGPSGCGKSTLLRmiAGLEdiTSGELRIGGKVVNdvePADRGIAMVFQsyalyphltveenLSF 98
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--ASGKARLISFLPK---FSRNKLIFIDQ-------------LQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 99 GLRMNgnpkadterrvshvadilqITELMKRRPKQ-LSGGQRQRVAIGRAIVREPE--VFLFDEPLSNLDAELRVQMRVE 175
Cdd:cd03238 71 LIDVG-------------------LGYLTLGQKLStLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEV 131
|
170 180 190
....*....|....*....|....*....|
gi 1037261085 176 ISRLhKQLGTTMIYVTHDQTeAMTLADRIV 205
Cdd:cd03238 132 IKGL-IDLGNTVILIEHNLD-VLSSADWII 159
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-166 |
1.49e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.23 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 29 GEFVVFVGPSGCGKSTLLRMIAGLED--ITSGELRIGGKVVNDvEPADRGIAMVFQSYALYPHLTVEENLSFG--LRMng 104
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKKQ-ETFARISGYCEQNDIHSPQVTVRESLIYSafLRL-- 982
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 105 nPK-ADTERRVSHVADILQITELMKRRPK--------QLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLDA 166
Cdd:PLN03140 983 -PKeVSKEEKMMFVDEVMELVELDNLKDAivglpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-214 |
4.55e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.54 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 3 ELSLTNIVKRF--GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGELRIGGKVVNDV--EPADRGIA 78
Cdd:cd03289 2 QMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVplQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 79 MVFQSYALYphltveenlSFGLRMNGNPKAD-TERRVSHVADILQITELMKRRPKQ-----------LSGGQRQRVAIGR 146
Cdd:cd03289 81 VIPQKVFIF---------SGTFRKNLDPYGKwSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037261085 147 AIVREPEVFLFDEPLSNLDAelrVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQ 214
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDP---ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-165 |
5.41e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 3 ELSLTNIVKRFGGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIA--GLEDITSG--ELRIGGKVVNDVEPA----- 73
Cdd:PLN03073 177 DIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhAIDGIPKNcqILHVEQEVVGDDTTAlqcvl 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 74 ----DRGIAMVFQSYALYPHLTVEENLSFG---LRMNGNPKADT--------------------ERRVSHVADILQIT-E 125
Cdd:PLN03073 257 ntdiERTQLLEEEAQLVAQQRELEFETETGkgkGANKDGVDKDAvsqrleeiykrlelidaytaEARAASILAGLSFTpE 336
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1037261085 126 LMKRRPKQLSGGQRQRVAIGRAIVREPEVFLFDEPLSNLD 165
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
23-221 |
1.14e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 46.44 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDV--EPADRGIAMVFQSYALYphltveenlSFGL 100
Cdd:cd03288 41 KAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplHTLRSRLSIILQDPILF---------SGSI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 101 RMNGNPKAD-TERRVSHVADILQITELMKRRPKQL-----------SGGQRQRVAIGRAIVREPEVFLFDEPLSNLD-AE 167
Cdd:cd03288 112 RFNLDPECKcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDmAT 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 168 LRVQMRVEISRLHKQLGTTMIYVTHDQTEamtlADRIVVLRAGNIEQIGAPLDL 221
Cdd:cd03288 192 ENILQKVVMTAFADRTVVTIAHRVSTILD----ADLVLVLSRGILVECDTPENL 241
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-221 |
1.40e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 18 IIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELRIGGKVVNDVEPAD--RGIAMVFQSYALYPHlTVEEN 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLGIIPQAPVLFSG-TVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 96 LSfglRMNGNPKADT----ERrvSHVADILqitelmKRRPKQL-----------SGGQRQRVAIGRAIVREPEVFLFDEP 160
Cdd:PLN03130 1333 LD---PFNEHNDADLweslER--AHLKDVI------RRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEA 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1037261085 161 LSNLDAELRVQMRVEISRLHKqlGTTMIYVTHdQTEAMTLADRIVVLRAGNIEQIGAPLDL 221
Cdd:PLN03130 1402 TAAVDVRTDALIQKTIREEFK--SCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-214 |
1.58e-05 |
|
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: 46.83 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 14 GGFEIIHGANLEVKDGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGELRIGGKVVNDV--EPADRGIAMVFQSYALyphlt 91
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVtlQTWRKAFGVIPQKVFI----- 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 92 veenLSFGLRMNGNPKAD-TERRVSHVADILQITELMKRRPKQL-----------SGGQRQRVAIGRAIVREPEVFLFDE 159
Cdd:TIGR01271 1304 ----FSGTFRKNLDPYEQwSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDE 1379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1037261085 160 PLSNLDAelrVQMRVEISRLHKQLGTTMIYVTHDQTEAMTLADRIVVLRAGNIEQ 214
Cdd:TIGR01271 1380 PSAHLDP---VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
28-205 |
2.82e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.52 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 28 DGEFVVFVGPSGCGKSTLlrmIAGLEDITSGELR---IGGKVVNDV--EPADRG-IAMVFQS-----YALYPHLTVEENL 96
Cdd:cd03240 21 FSPLTLIVGQNGAGKTTI---IEALKYALTGELPpnsKGGAHDPKLirEGEVRAqVKLAFENangkkYTITRSLAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 97 SFglrmngnpkadterrvSHVADILQITELMkrrPKQLSGGQRQ------RVAIGRAIVREPEVFLFDEPLSNLDAELRV 170
Cdd:cd03240 98 IF----------------CHQGESNWPLLDM---RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIE 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1037261085 171 QMRVEISRLHK-QLGTTMIYVTHDQtEAMTLADRIV 205
Cdd:cd03240 159 ESLAEIIEERKsQKNFQLIVITHDE-ELVDAADHIY 193
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-205 |
1.32e-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: 41.96 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 14 GGFEIIHGAN-LEVKDGEFVVFVGPSGCGKSTLLRMIAgleditsgelriggkvvndvepadrgiamvfqsyalyphltv 92
Cdd:cd03227 5 GRFPSYFVPNdVTFGEGSLTIITGPNGSGKSTILDAIG------------------------------------------ 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 93 eenLSFGLRMNGNPKADTERRVSHVADIlqITELMKRRPkQLSGGQRQRVAI-----GRAIVREPeVFLFDEPLSNLDAE 167
Cdd:cd03227 43 ---LALGGAQSATRRRSGVKAGCIVAAV--SAELIFTRL-QLSGGEKELSALalilaLASLKPRP-LYILDEIDRGLDPR 115
|
170 180 190
....*....|....*....|....*....|....*...
gi 1037261085 168 lRVQMRVEISRLHKQLGTTMIYVTHDQtEAMTLADRIV 205
Cdd:cd03227 116 -DGQALAEAILEHLVKGAQVIVITHLP-ELAELADKLI 151
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
122-204 |
1.72e-04 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 42.63 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 122 QITEL------MKRRPKQLSGGQRQRVAIGR--AIVR-EPEVF-LFDEPLSNLDAelrvQMRVEISRLHKQL-GTTMIYV 190
Cdd:cd03272 141 KINSLtnmkqdEQQEMQQLSGGQKSLVALALifAIQKcDPAPFyLFDEIDAALDA----QYRTAVANMIKELsDGAQFIT 216
|
90
....*....|....
gi 1037261085 191 THDQTEAMTLADRI 204
Cdd:cd03272 217 TTFRPELLEVADKF 230
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
23-205 |
2.80e-04 |
|
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: 41.86 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 23 NLEVKDGEFVVFVGPSGCGKSTL----------LRMIAGLEdiTSGELRIGGKVVNDVEPADrgiamvfqsyALYPHLTV 92
Cdd:cd03270 15 DVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLS--AYARQFLGQMDKPDVDSIE----------GLSPAIAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037261085 93 EENlsfglRMNGNPKAD----TE---------RRVSHVADILQITEL------MKRRPKQLSGGQRQRVAIGRAIVREPE 153
Cdd:cd03270 83 DQK-----TTSRNPRSTvgtvTEiydylrllfARVGIRERLGFLVDVglgyltLSRSAPTLSGGEAQRIRLATQIGSGLT 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 154 --VFLFDEPLSNLDAELRVQMRVEISRLhKQLGTTMIYVTHDQtEAMTLADRIV 205
Cdd:cd03270 158 gvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHVI 209
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
29-61 |
5.52e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.84 E-value: 5.52e-04
10 20 30
....*....|....*....|....*....|...
gi 1037261085 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGELR 61
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
282-352 |
5.61e-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: 37.98 E-value: 5.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037261085 282 LGIRPEHFADAGAGDAdLTVAIDVAEHLGNTSYIYAAIGSEQLIIERPESRTAGNR---ETLTVGLPARHTFLF 352
Cdd:pfam08402 1 LAIRPEKIRLAAAANG-LSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAHARPPapgDRVGLGWDPEDAHVL 73
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
36-62 |
4.98e-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: 37.08 E-value: 4.98e-03
10 20 30
....*....|....*....|....*....|
gi 1037261085 36 GPSGCGKSTLLRMIA---GLEDITSGELRI 62
Cdd:cd02020 6 GPAGSGKSTVAKLLAkklGLPYLDTGGIRT 35
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
28-61 |
6.59e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.14 E-value: 6.59e-03
10 20 30
....*....|....*....|....*....|....
gi 1037261085 28 DGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELR 61
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEIS 138
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
26-61 |
9.26e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 37.61 E-value: 9.26e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1037261085 26 VKDGEFVVFVGPSGCGKSTLLRMIAGLEDITSGELR 61
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVR 227
|
|
| |
