|
Name |
Accession |
Description |
Interval |
E-value |
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
15-369 |
0e+00 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 563.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 15 GTSGITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAG--GRILIGDTDVTQLPPYKRGL 92
Cdd:TIGR03258 2 ACGGIRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGltGRIAIADRDLTHAPPHKRGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 93 AMVVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:TIGR03258 82 ALLFQNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 173 DEPLSALDAQIRHNMVEEIARLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGR 252
Cdd:TIGR03258 162 DEPLSALDANIRANMREEIAALHEELPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 253 ANILQATALKDSPEPGLVSVSCGGGLINAFSRGGLHGNNKLLCIRPQHMSLAPRSATSNRLNATLTSVHWQGDLTHLLCD 332
Cdd:TIGR03258 242 ANILPAIALGITEAPGLVDVSCGGAVIFAFGDGRHDGRDKLACIRPEHLALTPRPAGEGRFHATIASVEWHGAALHLLCD 321
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 490252226 333 V-AGEAVRIV---MTHVNPLPRAGDKLALYFEPGDAVLIEV 369
Cdd:TIGR03258 322 LdAACDEPMLvtmLRGRGPAPERGAKLALDCEADDAVLIEP 362
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
16-368 |
4.60e-162 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 457.64 E-value: 4.60e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 16 TSGITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMV 95
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 176 LSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRANI 255
Cdd:COG3842 163 LSALDAKLREEMREELRRLQREL-GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 256 LQATALKDSPEpglvSVSCGGGLINAFSRGGL-HGNNKLLCIRPQHMSLAPRSATsNRLNATLTSVHWQGDLTHLLCDVA 334
Cdd:COG3842 242 LPGTVLGDEGG----GVRTGGRTLEVPADAGLaAGGPVTVAIRPEDIRLSPEGPE-NGLPGTVEDVVFLGSHVRYRVRLG 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 490252226 335 -GEAVRIVMT-HVNPLPRAGDKLALYFEPGDAVLIE 368
Cdd:COG3842 317 dGQELVVRVPnRAALPLEPGDRVGLSWDPEDVVVLP 352
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
17-366 |
8.64e-145 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 413.70 E-value: 8.64e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 17 SGITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVV 96
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:COG3839 82 QSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 177 SALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLG--RAN 254
Cdd:COG3839 162 SNLDAKLRVEMRAEIKRLHRRL-GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGspPMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 255 ILQATALKDSPEPGLVSVSCGGGLinafsrGGLHGNNKLLCIRPQHMSLAPRSAtsNRLNATLTSVHWQGDLTHLLCDVA 334
Cdd:COG3839 241 LLPGTVEGGGVRLGGVRLPLPAAL------AAAAGGEVTLGIRPEHLRLADEGD--GGLEATVEVVEPLGSETLVHVRLG 312
|
330 340 350
....*....|....*....|....*....|..
gi 490252226 335 GEAVRIVMTHVNPLpRAGDKLALYFEPGDAVL 366
Cdd:COG3839 313 GQELVARVPGDTRL-RPGDTVRLAFDPERLHL 343
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
18-367 |
3.86e-121 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 353.68 E-value: 3.86e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 18 GITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDV-TQLPPYKRGLAMVV 96
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 177 SALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRANIL 256
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDEL-GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 257 QATALKDspepglvSVSCGGglINAFSRGGLHGNNKLLCIRPQHMSLAPRSATSNRLNATLTSVHWQGDLTHLLCDVAGE 336
Cdd:COG1118 241 RGRVIGG-------QLEADG--LTLPVAEPLPDGPAVAGVRPHDIEVSREPEGENTFPATVARVSELGPEVRVELKLEDG 311
|
330 340 350
....*....|....*....|....*....|.
gi 490252226 337 AVRIVMTHVNplPRAGDKLALyfEPGDAVLI 367
Cdd:COG1118 312 EGQPLEAEVT--KEAWAELGL--APGDPVYL 338
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
19-251 |
4.11e-114 |
|
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: 331.51 E-value: 4.11e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQN 98
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490252226 179 LDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLG 251
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKEL-GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
19-232 |
6.29e-110 |
|
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: 320.24 E-value: 6.29e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQN 98
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490252226 179 LDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03259 161 LDAKLREELREELKELQREL-GITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
19-262 |
8.97e-107 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 318.04 E-value: 8.97e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQN 98
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 179 LDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRANILQA 258
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKL-GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDA 253
|
....
gi 490252226 259 TALK 262
Cdd:PRK09452 254 TVIE 257
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
49-367 |
4.60e-101 |
|
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: 301.72 E-value: 4.60e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 49 LIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAER 128
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 129 VTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTH 208
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQL-GITFVFVTH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 209 DQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRANILQATaLKDSPEPGLVSVSCGGGLINAFSRGGLH 288
Cdd:TIGR01187 160 DQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEAT-VIERKSEQVVLAGVEGRRCDIYTDVPVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 289 GNNKL-LCIRPQHMSL--APRSATSNRLNATLTSVHWQGD--LTHLLCDVAGE---AVRIVMTHVNPLPRAGDKLALYFE 360
Cdd:TIGR01187 239 KDQPLhVVLRPEKIVIeeEDEANSSNAIIGHVIDITYLGMtlEVHVRLETGQKvlvSEFFNEDDPHMSPSIGDRVGLTWH 318
|
....*..
gi 490252226 361 PGDAVLI 367
Cdd:TIGR01187 319 PGSEVVL 325
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
19-226 |
2.67e-98 |
|
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: 290.70 E-value: 2.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQN 98
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490252226 179 LDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRL-GTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
33-368 |
5.88e-98 |
|
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: 295.02 E-value: 5.88e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQNYALFPHMKVEDNVA 112
Cdd:TIGR03265 19 ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYALFPNLTVADNIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 113 FGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIA 192
Cdd:TIGR03265 99 YGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 193 RLHRELPELTILyVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRANILQATALKDSP-EPGLVS 271
Cdd:TIGR03265 179 QLQRRLGVTTIM-VTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLPGTRGGGSRaRVGGLT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 272 VSCGGGLINAfsrgglhGNNKLLCIRPQHMSLAPRSATSNRLNATLTSVHWQGDLTHLLCDVAGEAVRIVMTHVnpLPRA 351
Cdd:TIGR03265 258 LACAPGLAQP-------GASVRLAVRPEDIRVSPAGNAANLLLARVEDMEFLGAFYRLRLRLEGLPGQALVADV--SASE 328
|
330
....*....|....*..
gi 490252226 352 GDKLALyfEPGDAVLIE 368
Cdd:TIGR03265 329 VERLGI--RAGQPIWIE 343
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
34-344 |
1.55e-95 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 288.51 E-value: 1.55e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQNYALFPHMKVEDNVAF 113
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 114 GLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIAR 193
Cdd:NF040840 96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 194 LHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRANILQATALKDSpepGLVSVS 273
Cdd:NF040840 176 WHREF-GFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVAEKGG---EGTILD 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 274 CGGGLINAF--SRGGLHgnnklLCIRPQHMSLA-PRSATS--NRLNATLTSVHWQGDLTHLLCDVaGEAVRIVMTH 344
Cdd:NF040840 252 TGNIKIELPeeKKGKVR-----IGIRPEDITIStEKVKTSarNEFKGKVEEIEDLGPLVKLTLDV-GIILVAFITR 321
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
17-363 |
1.64e-94 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 285.97 E-value: 1.64e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 17 SGITLDSLRVSYHGNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMV 95
Cdd:PRK11650 2 AGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIaVR-PRVLLLDE 174
Cdd:PRK11650 82 FQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI-VRePAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 175 PLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRA- 253
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRL-KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPa 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 254 -NILQATAlkdSPEPGLVSVSCGGGLINAFSRGGLHGNNKLLCIRPQHMSLAPRSAtsnRLNATLTSVHWQGDLTHLLCD 332
Cdd:PRK11650 240 mNLLDGRV---SADGAAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIALSSAEG---GVPLTVDTVELLGADNLAHGR 313
|
330 340 350
....*....|....*....|....*....|.
gi 490252226 333 VAGEAVRIVMTHvNPLPRAGDKLALYFEPGD 363
Cdd:PRK11650 314 WGGQPLVVRLPH-QERPAAGSTLWLHLPANQ 343
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
19-226 |
5.53e-93 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 278.90 E-value: 5.53e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYH----GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPykrGLAM 94
Cdd:COG1116 8 LELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---DRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490252226 175 PLSALDAQIRHNMVEEIARLHRELPeLTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:COG1116 165 PFGALDALTRERLQDELLRLWQETG-KTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-255 |
1.04e-90 |
|
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: 271.90 E-value: 1.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYhGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQN 98
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 179 LDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRANI 255
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEF-GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
31-361 |
2.82e-90 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 275.06 E-value: 2.82e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 31 NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQNYALFPHMKVEDN 110
Cdd:PRK11432 19 NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEE 190
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 191 IARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRANILQATALKDSPEPGLV 270
Cdd:PRK11432 179 IRELQQQF-NITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPATLSGDYVDIYGY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 271 SVScgggLINAFSRGGLHGNNkLLCIRPQHMSLAPRSATSNRlnATLTSVHWQGDLTHLLCDVAGEAvriVMTHVNPL-- 348
Cdd:PRK11432 258 RLP----RPAAFAFNLPDGEC-TVGVRPEAITLSEQGEESQR--CTIKHVAYMGPQYEVTVDWHGQE---LLLQVNATql 327
|
330
....*....|....
gi 490252226 349 -PRAGDKLALYFEP 361
Cdd:PRK11432 328 qPDLGEHYYLEIHP 341
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-294 |
2.66e-89 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 270.81 E-value: 2.66e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYK--RGLAMV 95
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGM--ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:COG1125 82 IQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 174 EPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRA 253
Cdd:COG1125 162 EPFGALDPITREQLQDELLRLQREL-GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490252226 254 NI---LQATALKDSPEPGLVSVSCGGGLINAFSRGGLHGNNKLL 294
Cdd:COG1125 241 RGlrrLSLLRVEDLMLPEPPTVSPDASLREALSLMLERGVDWLL 284
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
18-251 |
5.75e-89 |
|
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: 267.67 E-value: 5.75e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 18 GITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQ 97
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 NYALFPHMKVEDNVAFGLRAQKQ----PRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 174 EPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLG 251
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDEL-HVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
19-223 |
2.68e-88 |
|
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: 265.49 E-value: 2.68e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPykrGLAM 94
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490252226 175 PLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIM 223
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRET-GKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
19-256 |
1.75e-87 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 263.97 E-value: 1.75e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQN 98
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 179 LDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRANIL 256
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEV-HVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
23-275 |
3.61e-87 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 268.24 E-value: 3.61e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 23 SLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQNYALF 102
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 103 PHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:PRK11607 104 PHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 183 IRHNMVEEIARLhRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRANILQATaLK 262
Cdd:PRK11607 184 LRDRMQLEVVDI-LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFEGV-LK 261
|
250
....*....|...
gi 490252226 263 DSPEPGLVSVSCG 275
Cdd:PRK11607 262 ERQEDGLVIDSPG 274
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
17-357 |
5.38e-84 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 259.58 E-value: 5.38e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 17 SGITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVV 96
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 177 SALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLG--RAN 254
Cdd:PRK11000 162 SNLDAALRVQMRIEISRLHKRL-GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGspKMN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 255 ILQATALkdSPEPGLVSVSCGGGL---INAFSRGGLHGNNKLLCIRPQHmsLAPRSATSNRLNATLTSVHWQGDLTHLLC 331
Cdd:PRK11000 241 FLPVKVT--ATAIEQVQVELPNRQqvwLPVEGRGVQVGANMSLGIRPEH--LLPSDIADVTLEGEVQVVEQLGNETQIHI 316
|
330 340
....*....|....*....|....*....
gi 490252226 332 DVagEAVRIVMTHVNP---LPRAGDKLAL 357
Cdd:PRK11000 317 QI--PAIRQNLVYRQNdvvLVEEGATFAI 343
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
19-355 |
1.03e-81 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 253.47 E-value: 1.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQN 98
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVEDNVAFGL----RAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLtvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 175 PLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRAN 254
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEEL-KFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 255 ILQATAlkdspepglvsvsCG-----GGLINAFSRGGLHGNNKLLCIRPQHMSLAPRSATSNRLNATLTSVHWQGDLTHL 329
Cdd:PRK10851 242 RLQGTI-------------RGgqfhvGAHRWPLGYTPAYQGPVDLFLRPWEVDISRRTSLDSPLPVQVLEVSPKGHYWQL 308
|
330 340
....*....|....*....|....*....
gi 490252226 330 LCDVAG---EAVRIVMTHVNPLPRAGDKL 355
Cdd:PRK10851 309 VVQPLGwynEPLTVVMHGDIDAPQRGERL 337
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
19-252 |
2.10e-80 |
|
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: 246.06 E-value: 2.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYK--RGLAMV 95
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGM--ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 174 EPLSALDAQIRHNMVEEIARLHRELPElTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGR 252
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGK-TIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
38-365 |
7.28e-78 |
|
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: 243.47 E-value: 7.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDT---DVTQ---LPPYKRGLAMVVQNYALFPHMKVEDNV 111
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARgifLPPHRRRIGYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 112 AFGL-RAQKQPRGLIAERVTEALkivGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEE 190
Cdd:COG4148 99 LYGRkRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 191 IARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRANILQATALKDSPEPGLV 270
Cdd:COG4148 176 LERLRDEL-DIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAHDPDYGLT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 271 SVSCGGGLINAFSRGGLHGNNKLLCIRPQHMSLA--PRSATS--NRLNATLTSVHWQGDLTHLLC-DVAGEAV--RIVmt 343
Cdd:COG4148 255 RLALGGGRLWVPRLDLPPGTRVRVRIRARDVSLAlePPEGSSilNILPGRVVEIEPADGGQVLVRlDLGGQTLlaRIT-- 332
|
330 340
....*....|....*....|..
gi 490252226 344 hvnplPRAGDKLALyfEPGDAV 365
Cdd:COG4148 333 -----RRSADELGL--APGQTV 347
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
19-252 |
1.10e-76 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 236.19 E-value: 1.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGnvvlKPL--SLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVV 96
Cdd:COG3840 2 LRLDDLTYRYGD----FPLrfDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPHMKVEDNVAFGLR-------AQKQprgliaeRVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIaVRPR- 168
Cdd:COG3840 78 QENNLFPHLTVAQNIGLGLRpglkltaEQRA-------QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCL-VRKRp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 169 VLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAE 248
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRER-GLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAA 228
|
....
gi 490252226 249 FLGR 252
Cdd:COG3840 229 YLGI 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-252 |
6.54e-76 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 234.50 E-value: 6.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT----QLPPYKRGLAM 94
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFPHMKVEDNVAFGLR-AQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 174 EPLSALDAQirhnMVEEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLG 251
Cdd:COG1126 162 EPTSALDPE----LVGEVLDVMRDLAKegMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237
|
.
gi 490252226 252 R 252
Cdd:COG1126 238 K 238
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
19-239 |
1.89e-75 |
|
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: 233.33 E-value: 1.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP-----PYKRGLA 93
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekelyELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 MVVQNYALFPHMKVEDNVAFGLRAQ-KQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 173 DEPLSALDAQIRHNMVEEIARLHRELPeLTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYH 239
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDELG-LTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-239 |
3.41e-74 |
|
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: 229.53 E-value: 3.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYH-GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYK--RGLAMV 95
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQN--YALFpHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:COG1122 81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 174 EPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYH 239
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE--GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-241 |
1.44e-73 |
|
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: 237.11 E-value: 1.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN-----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP-----PY 88
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrslrEL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 89 KRGLAMVVQN--YALFPHMKVEDNVAFGLRAQKQ-PRGLIAERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIA 164
Cdd:COG1123 341 RRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 165 VRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQREL-GLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
38-249 |
2.53e-73 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 228.68 E-value: 2.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP------YKRGLAMVVQNYALFPHMKVEDNV 111
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelrelRRKKISMVFQSFALLPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 112 AFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEI 191
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDEL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 192 ARLHRELPElTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEF 249
Cdd:cd03294 204 LRLQAELQK-TIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-237 |
1.40e-70 |
|
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: 221.22 E-value: 1.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSY----HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGL 92
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkaFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 93 AMVVQNY--ALFPHMKVEDNVAFGLRAQKQPRglIAERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLPD--REERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 170 LLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREER-GLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
30-281 |
5.59e-70 |
|
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: 223.58 E-value: 5.59e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP------YKRGLAMVVQNYALFP 103
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 104 HMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:TIGR01186 85 HMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 184 RHNMVEEIARLHRELPElTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRANILQATALKD 263
Cdd:TIGR01186 165 RDSMQDELKKLQATLQK-TIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFDAER 243
|
250 260
....*....|....*....|.
gi 490252226 264 ---SPEPGLVSVSCGGGLINA 281
Cdd:TIGR01186 244 iaqRMNTGPITKTADKGPRSA 264
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
19-226 |
7.76e-69 |
|
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: 215.47 E-value: 7.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT----QLPPYKRGLAM 94
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFPHMKVEDNVAFGLR-AQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 174 EPLSALDAQirhnMVEEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:cd03262 161 EPTSALDPE----LVGEVLDVMKDLAEegMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
19-237 |
1.14e-68 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 215.70 E-value: 1.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP-YKRGLAMVVQ 97
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAeVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 NYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 178 ALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:COG1131 161 GLDPEARRELWELLRELAAE--GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
19-232 |
1.64e-68 |
|
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: 215.06 E-value: 1.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHG----NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP-----PYK 89
Cdd:cd03257 2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 90 RGLAMVVQNY--ALFPHMKVEDNVAFGLRAQKQPRG--LIAERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIA 164
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKkeARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 165 VRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEEL-GLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-237 |
4.86e-68 |
|
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: 213.90 E-value: 4.86e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYK-----RGLA 93
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 MVVQNYALFPHMKVEDNVAFGLRAQKQ-PRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 173 DEPLSALDAQIRHNMVEEIARLHRELPeLTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELG-LTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-266 |
9.92e-68 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 214.34 E-value: 9.92e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 17 SGITLDSLRVSYHGNV----VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQlPPYKRGL 92
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 93 amVVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:COG4525 81 --VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 173 DEPLSALDAQIRHNMVEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDGSL-IAHgeTHELyhyppnRFSAEFL- 250
Cdd:COG4525 159 DEPFGALDALTREQMQELLLDVWQR-TGKGVFLITHSVEEALFLATRLVVMSPGPGrIVE--RLEL------DFSRRFLa 229
|
250
....*....|....*.
gi 490252226 251 GRAnilqATALKDSPE 266
Cdd:COG4525 230 GED----ARAIKSDPA 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
19-230 |
2.63e-67 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 211.83 E-value: 2.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYH-GNV---VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRG--- 91
Cdd:COG1136 5 LELRNLTKSYGtGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 92 ---LAMVVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPR 168
Cdd:COG1136 85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490252226 169 VLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQtEALTLADKIGIMKDGSLIA 230
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNREL-GTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-251 |
3.36e-67 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 215.33 E-value: 3.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP-----YK 89
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelraAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 90 RGLAMVVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 170 LLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEF 249
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINREL-GLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
..
gi 490252226 250 LG 251
Cdd:COG1135 241 LP 242
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
19-228 |
3.74e-67 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 211.19 E-value: 3.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRG--- 91
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 92 ---LAMVVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPR 168
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 169 VLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALtLADKIGIMKDGSL 228
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEA-GTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
19-237 |
5.64e-67 |
|
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: 211.83 E-value: 5.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRG--LAMVV 96
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELArrIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPHMKVEDNVAFGLRAQKQPRGLIA----ERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRYPHLGLFGRPSaedrEAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 173 DEPLSALDaqIRH--NMVEEIARLHRELPeLTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:COG1120 162 DEPTSHLD--LAHqlEVLELLRRLARERG-RTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
19-226 |
2.79e-66 |
|
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: 207.42 E-value: 2.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT----QLPPYKRGLAM 94
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFPHMKVEDNVAFGlraqkqprgliaervtealkivgmadyatryphqLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490252226 175 PLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQL-GITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-272 |
1.40e-65 |
|
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: 216.31 E-value: 1.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHG--NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAG---GRILIGDTDVTQLPPYKRG-- 91
Cdd:COG1123 5 LEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 92 LAMVVQN--YALFPhMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 170 LLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYpPNRFSAEF 249
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRER-GTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA-PQALAAVP 241
|
250 260
....*....|....*....|...
gi 490252226 250 LGRANILQATALKDSPEPgLVSV 272
Cdd:COG1123 242 RLGAARGRAAPAAAAAEP-LLEV 263
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
21-226 |
9.20e-65 |
|
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: 204.62 E-value: 9.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 21 LDSLRVSYHG--NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGL--AMVV 96
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRkvGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QN--YALFPHMkVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:cd03225 82 QNpdDQFFGPT-VEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490252226 175 PLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAE--GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
19-237 |
1.45e-63 |
|
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: 202.41 E-value: 1.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFV-----QPAGGRILIGDTDVTQLPP----YK 89
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVdvleLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 90 RGLAMVVQNYALFPhMKVEDNVAFGLRAQ-KQPRGLIAERVTEALKIVGMADYATR--YPHQLSGGQQQRVAIARAIAVR 166
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHgIKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490252226 167 PRVLLLDEPLSALDAQIRHNMVEEIARLHRelpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKK---EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
43-232 |
1.95e-63 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 201.37 E-value: 1.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 43 PGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDT---DVTQ---LPPYKRGLAMVVQNYALFPHMKVEDNVAFGLR 116
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkinLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 117 aqKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHR 196
Cdd:cd03297 102 --RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 490252226 197 ELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03297 180 NL-NIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
19-210 |
2.42e-63 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 201.43 E-value: 2.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT-----QLPPYKRGL 92
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkrrEIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 93 AMVVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490252226 173 DEPLSALDAQirhnMVEEIARLHRELPEL--TILYVTHDQ 210
Cdd:COG2884 162 DEPTGNLDPE----TSWEIMELLEEINRRgtTVLIATHDL 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-253 |
2.48e-63 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 202.24 E-value: 2.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLppyKRGLAMVVQN 98
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---RRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YAL---FPhMKVEDNVAFGLRAQ----KQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:COG1121 84 AEVdwdFP-ITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 172 LDEPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGsLIAHGETHELyhyppnrFSAEFLG 251
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRRE--GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEV-------LTPENLS 232
|
..
gi 490252226 252 RA 253
Cdd:COG1121 233 RA 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
19-241 |
1.87e-62 |
|
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: 199.73 E-value: 1.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYK----- 89
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 90 RGLAMVVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490252226 170 LLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINREL-GLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-232 |
3.25e-61 |
|
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: 197.65 E-value: 3.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN--VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDV---TQLPPYKRGLA 93
Cdd:TIGR04520 1 IEVENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 MVVQNyalfPH-----MKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPR 168
Cdd:TIGR04520 81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490252226 169 VLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALtLADKIGIMKDGSLIAHG 232
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEE-GITVISITHDMEEAV-LADRVIVMNKGKIVAEG 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
19-237 |
3.50e-61 |
|
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: 196.62 E-value: 3.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP-YKRGLAMVVQ 97
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 NYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 178 ALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:COG4555 162 GLDVMARRLLREILRALKKE--GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
18-214 |
5.39e-60 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 192.70 E-value: 5.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 18 GITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQP---AGGRILIGDTDVTQLPPYKRGLAM 94
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFPHMKVEDNVAFGLRAqKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALPP-TIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490252226 175 PLSALDA----QIRHNMVEEIARlhRELPelTILyVTHDQTEAL 214
Cdd:COG4136 160 PFSKLDAalraQFREFVFEQIRQ--RGIP--ALL-VTHDEEDAP 198
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
19-250 |
6.44e-59 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 191.04 E-value: 6.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP-----YKRGL 92
Cdd:COG3638 3 LELRNLSKRYPGGTpALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrrLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 93 AMVVQNYALFPHMKVEDNVAFGLRAQK-QPRGLIA-------ERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIA 164
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRLGRTsTWRSLLGlfppedrERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 165 VRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGethelyhyPPNR 244
Cdd:COG3638 163 QEPKLILADEPVASLDPKTARQVMDLLRRIARED-GITVVVNLHQVDLARRYADRIIGLRDGRVVFDG--------PPAE 233
|
....*.
gi 490252226 245 FSAEFL 250
Cdd:COG3638 234 LTDAVL 239
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
19-228 |
3.38e-57 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 185.40 E-value: 3.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGLAMVV 96
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpeWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPhMKVEDNVAFGLRAQKQPrgLIAERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:COG4619 81 QEPALWG-GTVRDNLPFPFQLRERK--FDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490252226 176 LSALDAQIRHNMVEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAE-EGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
31-250 |
1.32e-56 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 184.91 E-value: 1.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 31 NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGL----AMVVQNYALFPHMK 106
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQFYLFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 107 VEDNVAFG-LRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRH 185
Cdd:PRK09493 94 ALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRH 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490252226 186 nmveEIARLHRELPE--LTILYVTHDqteaLTLADKIG---IMKDGSLIAH-GETHELYHYPPNRFSAEFL 250
Cdd:PRK09493 174 ----EVLKVMQDLAEegMTMVIVTHE----IGFAEKVAsrlIFIDKGRIAEdGDPQVLIKNPPSQRLQEFL 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
21-236 |
1.39e-56 |
|
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: 185.24 E-value: 1.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 21 LDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKR---GLAMVVQ 97
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlGIARTFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 NYALFPHMKVEDNVAFGLRAQKQPRGL---------------IAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARA 162
Cdd:COG0411 87 NPRLFPELTVLENVLVAAHARLGRGLLaallrlprarreereARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490252226 163 IAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHE 236
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPEETEELAELIRRLRDER-GITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-241 |
1.51e-56 |
|
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: 187.18 E-value: 1.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 24 LRVSYH---GNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQP---AGGRILIGDTDVTQLPP------YKR 90
Cdd:COG0444 7 LKVYFPtrrGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkelrkiRGR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 91 GLAMVVQN-Y-ALFPHMKVEDNVAFGLRA-QKQPRGLIAERVTEALKIVGM---ADYATRYPHQLSGGQQQRVAIARAIA 164
Cdd:COG0444 87 EIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 165 VRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:COG0444 167 LEPKLLIADEPTTALDVTIQAQILNLLKDLQREL-GLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENP 242
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-252 |
2.74e-56 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 184.57 E-value: 2.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 17 SGITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPY--KRGL-- 92
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqQKGLir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 93 ------AMVVQNYALFPHMKVEDNVAFG-LRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAV 165
Cdd:PRK11264 82 qlrqhvGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 166 RPRVLLLDEPLSALDAQirhnMVEEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPN 243
Cdd:PRK11264 162 RPEVILFDEPTSALDPE----LVGEVLNTIRQLAQekRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
....*....
gi 490252226 244 RFSAEFLGR 252
Cdd:PRK11264 238 PRTRQFLEK 246
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-236 |
2.96e-56 |
|
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: 183.79 E-value: 2.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 21 LDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKR---GLAMVVQ 97
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 NYALFPHMKVEDNVAFGLRAQKQPRGL----------IAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRP 167
Cdd:cd03219 83 IPRLFPELTVLENVMVAAQARTGSGLLlararreereARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 168 RVLLLDEPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHE 236
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELRER--GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-238 |
9.01e-56 |
|
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: 183.81 E-value: 9.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN-----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT-----QLPPY 88
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 89 KRGLAMVVQN--YALFpHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAV 165
Cdd:TIGR04521 81 RKKVGLVFQFpeHQLF-EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490252226 166 RPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELY 238
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEK-GLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
38-241 |
1.79e-55 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 184.55 E-value: 1.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP-----PYKRGLAMVVQN-YA-LFPHMKVEDN 110
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgrelrPLRRRMQMVFQDpYAsLNPRMTVGDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAFGLRAQKQ-PRGLIAERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD----AQIR 184
Cdd:COG4608 118 IAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQVL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490252226 185 hNMVEEiarLHRELpELTILYVTHDqteaLT----LADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:COG4608 198 -NLLED---LQDEL-GLTYLFISHD----LSvvrhISDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
19-252 |
2.37e-55 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 181.72 E-value: 2.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRA------------IAGFVQPAGGRILIGDTDVTQLp 86
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSlnrmndlvpgvrIEGKVLFDGQDIYDKKIDVVEL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 87 pyKRGLAMVVQNYALFPhMKVEDNVAFGLRAQK-QPRGLIAERVTEALKIVGM----ADYATRYPHQLSGGQQQRVAIAR 161
Cdd:TIGR00972 81 --RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGiKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 162 AIAVRPRVLLLDEPLSALDAQirhnMVEEIARLHRELPE-LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHY 240
Cdd:TIGR00972 158 ALAVEPEVLLLDEPTSALDPI----ATGKIEELIQELKKkYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTN 233
|
250
....*....|...
gi 490252226 241 PPNRFSAEFL-GR 252
Cdd:TIGR00972 234 PKEKRTEDYIsGR 246
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-232 |
1.18e-54 |
|
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: 178.88 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 21 LDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPpykRGLAMVVQNYA 100
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---KRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 101 L---FPhMKVEDNVAFGLRAQKQPRGLI----AERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:cd03235 79 IdrdFP-ISVRDVVLMGLYGHKGLFRRLskadKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 174 EPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIgIMKDGSLIAHG 232
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRRE--GMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
19-252 |
3.09e-54 |
|
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: 178.92 E-value: 3.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP-----YKRGL 92
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 93 AMVVQNYALFPHMKVEDNVAFGLRAQKQP-RGLIA-------ERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIA 164
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTwRSLFGlfpkeekQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 165 VRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGethelyhyPPNR 244
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREE-GITVIVSLHQVDLAREYADRIVGLKDGRIVFDG--------PPAE 231
|
....*...
gi 490252226 245 FSAEFLGR 252
Cdd:cd03256 232 LTDEVLDE 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-232 |
4.19e-54 |
|
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: 176.09 E-value: 4.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 20 TLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRglamvvqny 99
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 100 alfphmkvednvafglrAQKqpRGLiaerVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:cd03214 72 -----------------ARK--IAY----VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490252226 180 DAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03214 129 DIAHQIELLELLRRLARER-GKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-241 |
4.33e-54 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 181.54 E-value: 4.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP-----YK 89
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrkAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 90 RGLAMVVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490252226 170 LLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINREL-GLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-237 |
1.73e-53 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 177.15 E-value: 1.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 9 SSPSLAGTSGITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRA-------IAGF-VQpagGRILIGDT 80
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGArVE---GEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 81 DV--TQLPPYK--RGLAMVVQNYALFPhMKVEDNVAFGLRAQ-KQPRGLIAERVTEALKIVGMAD--------YATRyph 147
Cdd:COG1117 79 DIydPDVDVVElrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHgIKSKSELDEIVEESLRKAALWDevkdrlkkSALG--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 148 qLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD----AQIrhnmvEEiarLHREL-PELTILYVTHDQTEALTLADKIGI 222
Cdd:COG1117 155 -LSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistAKI-----EE---LILELkKDYTIVIVTHNMQQAARVSDYTAF 225
|
250
....*....|....*
gi 490252226 223 MKDGSLIAHGETHEL 237
Cdd:COG1117 226 FYLGELVEFGPTEQI 240
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
30-362 |
1.78e-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: 180.31 E-value: 1.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 30 GNVVLKpLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDV------TQLPPYKRGLAMVVQNYALFP 103
Cdd:TIGR02142 10 GDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkgIFLPPEKRRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 104 HMKVEDNVAFGL-RAQKQPRGLIAERVTEALKIVGMADyatRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:TIGR02142 89 HLSVRGNLRYGMkRARPSERRISFERVIELLGIGHLLG---RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 183 IRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHyPPNRFSAEFLGRANILQATALK 262
Cdd:TIGR02142 166 RKYEILPYLERLHAEF-GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA-SPDLPWLAREDQGSLIEGVVAE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 263 DSPEPGLVSVSCGGGLINAFSRGGLHGNNKLLCIRPQHMSLA--PRSATS--NRLNATLT-SVHWQGDLTHLLCDVAGEA 337
Cdd:TIGR02142 244 HDQHYGLTALRLGGGHLWVPENLGPTGARLRLRVPARDVSLAlqKPEATSirNILPARVVeIEDSDIGRVGVVLESGGKT 323
|
330 340
....*....|....*....|....*
gi 490252226 338 VRIVMThvnplPRAGDKLAlyFEPG 362
Cdd:TIGR02142 324 LWARIT-----RWARDELG--IAPG 341
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-232 |
4.68e-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: 174.60 E-value: 4.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVlkPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQN 98
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIaVRPR-VLLLDEPLS 177
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVL-VRDKpVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 178 ALDAQIRHNMVEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAE-TKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
19-217 |
1.02e-52 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 175.27 E-value: 1.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQlPPYKRGLamVVQN 98
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 490252226 179 LDAQIRHNMVEEIARLHRELPElTILYVTHDQTEALTLA 217
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGK-QVLLITHDIEEAVFMA 196
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
34-177 |
2.90e-52 |
|
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: 170.52 E-value: 2.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQ--LPPYKRGLAMVVQNYALFPHMKVEDNV 111
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 112 AFGLRAQKQPRGLIAERVTEALKIVGMADYATR----YPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
19-228 |
4.58e-52 |
|
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: 170.66 E-value: 4.58e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP-YKRGLAMVVQ 97
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEeVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 NYALFPHMKVEDNVafglraqkqprgliaervtealkivgmadyatryphQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490252226 178 ALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:cd03230 125 GLDPESRREFWELLRELKKE--GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-226 |
1.89e-51 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 172.17 E-value: 1.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 13 LAGTSgITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRgl 92
Cdd:PRK11247 8 NQGTP-LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 93 aMVVQNYALFPHMKVEDNVAFGLRAQKQPRGLiaervtEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:PRK11247 85 -LMFQDARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490252226 173 DEPLSALDAQIRHNMVEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQ-HGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
34-238 |
2.11e-51 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 172.51 E-value: 2.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPY--KRGLAMVVQNY-ALFPHMKVEDN 110
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWdvRRQVGMVFQNPdNQFVGATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEE 190
Cdd:PRK13635 103 VAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLET 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490252226 191 IARLHRELpELTILYVTHDQTEALTlADKIGIMKDGSLIAHGETHELY 238
Cdd:PRK13635 183 VRQLKEQK-GITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
19-234 |
4.20e-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: 169.66 E-value: 4.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHgnVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQN 98
Cdd:TIGR01277 1 LALDKVRYEYE--HLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIaVRPR-VLLLDEPLS 177
Cdd:TIGR01277 79 NNLFAHLTVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCL-VRPNpILLLDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 178 ALDAQIRHNMVEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGET 234
Cdd:TIGR01277 158 ALDPLLREEMLALVKQLCSE-RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
19-237 |
9.38e-51 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 169.38 E-value: 9.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGnvvlKPL--SLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVV 96
Cdd:PRK10771 2 LKLTDITWLYHH----LPMrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPHMKVEDNVAFGL-------RAQKQPRGLIAERvtealkiVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:PRK10771 78 QENNLFSHLTVAQNIGLGLnpglklnAAQREKLHAIARQ-------MGIEDLLARLPGQLSGGQRQRVALARCLVREQPI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 170 LLLDEPLSALDAQIRHNMVEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK10771 151 LLLDEPFSALDPALRQEMLTLVSQVCQE-RQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
34-241 |
9.86e-51 |
|
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: 177.57 E-value: 9.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVqPAGGRILIGDTDVTQLP-----PYKRGLAMVVQN-YA-LFPHMK 106
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrralrPLRRRMQVVFQDpFGsLSPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 107 VEDNVAFGLRAQ--KQPRGLIAERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:COG4172 381 VGQIIAEGLRVHgpGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 184 RHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:COG4172 461 QAQILDLLRDLQREH-GLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-213 |
1.29e-50 |
|
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: 168.04 E-value: 1.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP-YKRGLAMVVQ 97
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 NYALFPHMKVEDNVAFGLRAQKQPRGliAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 490252226 178 ALDAQIRHnMVEEIARLHRELpELTILYVTHDQTEA 213
Cdd:COG4133 161 ALDAAGVA-LLAELIAAHLAR-GGAVLLTTHQPLEL 194
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
34-226 |
1.88e-50 |
|
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: 168.80 E-value: 1.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKrglaMVV-QNYALFPHMKVEDNVA 112
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR----MVVfQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 113 FGLRA--QKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEE 190
Cdd:TIGR01184 77 LAVDRvlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 490252226 191 IARLHRElPELTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:TIGR01184 157 LMQIWEE-HRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-237 |
3.20e-50 |
|
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: 167.61 E-value: 3.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKR---GLAMV 95
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNYALFPHMKVEDNVAFGLRAQKQPRG-LIAERVTE---ALKivgmaDYATRYPHQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRkARLERVYElfpRLK-----ERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 172 LDEPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDE--GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-236 |
7.43e-50 |
|
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: 177.72 E-value: 7.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 11 PSLAGTsgITLDSLRVSYHGNV--VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP- 87
Cdd:COG2274 468 PRLKGD--IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPa 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 88 -YKRGLAMVVQNYALFpHMKVEDNVAFGlraqkqpRGLIA-ERVTEALKIVGMADYATRYPH-----------QLSGGQQ 154
Cdd:COG2274 546 sLRRQIGVVLQDVFLF-SGTIRENITLG-------DPDATdEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQR 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 155 QRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMveeIARLHRELPELTILYVTHDqTEALTLADKIGIMKDGSLIAHGeT 234
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAII---LENLRRLLKGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDG-T 692
|
..
gi 490252226 235 HE 236
Cdd:COG2274 693 HE 694
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
19-209 |
8.72e-50 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 167.67 E-value: 8.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGD---------------TDVT 83
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdgelvpADRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 84 QLPPYKRGLAMVVQNYALFPHMKVEDNVAFG-LRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARA 162
Cdd:COG4598 89 QLQRIRTRLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490252226 163 IAVRPRVLLLDEPLSALDAQirhnMVEEIARLHRELPE--LTILYVTHD 209
Cdd:COG4598 169 LAMEPEVMLFDEPTSALDPE----LVGEVLKVMRDLAEegRTMLVVTHE 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-237 |
1.02e-49 |
|
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: 166.70 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 20 TLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKR---GLAMVV 96
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPHMKVEDNVAFGLRAQKQPRGL--IAERVTE---ALKivgmaDYATRYPHQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:COG0410 85 EGRRIFPSLTVEENLLLGAYARRDRAEVraDLERVYElfpRLK-----ERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 172 LDEPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRLNRE--GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-239 |
2.48e-49 |
|
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: 174.18 E-value: 2.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 8 TSSPSLAGTSGITLDSLRVSYH-GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP 86
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 87 P--YKRGLAMVVQNYALFpHMKVEDNVAFGLRAqkqprgliA--ERVTEALKIVGMADYATRYPH-----------QLSG 151
Cdd:COG4988 406 PasWRRQIAWVPQNPYLF-AGTIRENLRLGRPD--------AsdEELEAALEAAGLDEFVAALPDgldtplgeggrGLSG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 152 GQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRelpELTILYVTHDqTEALTLADKIGIMKDGSLIAH 231
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK---GRTVILITHR-LALLAQADRILVLDDGRIVEQ 552
|
....*...
gi 490252226 232 GETHELYH 239
Cdd:COG4988 553 GTHEELLA 560
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
20-226 |
6.40e-49 |
|
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: 162.03 E-value: 6.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 20 TLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGLAMVvq 97
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeeLRRRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 nyalfphmkvednvafglraqkqprgliaervtealkivgmadyatrypHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:cd00267 79 -------------------------------------------------PQLSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490252226 178 ALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:cd00267 110 GLDPASRERLLELLRELAEE--GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-226 |
7.33e-49 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 163.96 E-value: 7.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT-----QLPPYKRGL 92
Cdd:TIGR02673 2 IEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNrlrgrQLPLLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 93 AMVVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 173 DEPLSALDAQirhnMVEEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDG 226
Cdd:TIGR02673 162 DEPTGNLDPD----LSERILDLLKRLNKrgTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
34-272 |
8.93e-49 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 169.44 E-value: 8.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP------YKRGLAMVVQNYALFPHMKV 107
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 108 EDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNM 187
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 188 VEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLGRANILQATALKDSPEP 267
Cdd:PRK10070 204 QDELVKLQAK-HQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQVFSAKDIARR 282
|
....*
gi 490252226 268 GLVSV 272
Cdd:PRK10070 283 TPNGL 287
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-236 |
2.35e-48 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 164.13 E-value: 2.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYK--RGLAMVV 96
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYAL-FPhMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIA-------VRPR 168
Cdd:COG4559 82 QHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 169 VLLLDEPLSALDaqIRH-NMVEEIAR-LHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHE 236
Cdd:COG4559 161 WLFLDEPTSALD--LAHqHAVLRLARqLARR--GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-250 |
2.42e-48 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 163.65 E-value: 2.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 18 GITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDT--DVTQLPPYKRGLA-- 93
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIRLlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 ----MVVQNYALFPHMKVEDN-VAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPR 168
Cdd:COG4161 82 qkvgMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 169 VLLLDEPLSALDAQIRHNMVEEIarlhRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGeTHELYHYPPNRFS 246
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEII----RELSQtgITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQPQTEAF 236
|
....
gi 490252226 247 AEFL 250
Cdd:COG4161 237 AHYL 240
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
19-238 |
5.87e-48 |
|
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: 162.47 E-value: 5.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQ-----LPPYKRGL 92
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgkkLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 93 AMVVQNYALFPHMKVEDNVAFG-LRAQKQPRGLIA-------ERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIA 164
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGrLGYKPTWRSLLGrfseedkERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490252226 165 VRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELY 238
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKED-GITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-236 |
5.00e-47 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 168.42 E-value: 5.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 18 GITLDSLRVSYHGNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGLAM 94
Cdd:COG1132 339 EIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLesLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFpHMKVEDNVAFG-LRAQKqprgliaERVTEALKIVGMADYATRYPH-----------QLSGGQQQRVAIARA 162
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYGrPDATD-------EEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 163 IAVRPRVLLLDEPLSALD----AQIRHNmveeiarLHRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHGeTHE 236
Cdd:COG1132 491 LLKDPPILILDEATSALDteteALIQEA-------LERLMKGRTTIVIAH-RLSTIRNADRILVLDDGRIVEQG-THE 559
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-226 |
8.12e-47 |
|
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: 157.16 E-value: 8.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN--VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGLAM 94
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLesLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFpHMKVEDNVafglraqkqprgliaervtealkivgmadyatryphqLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490252226 175 PLSALDAQIRHNMVEEIARLHRelpELTILYVTHDqTEALTLADKIGIMKDG 226
Cdd:cd03228 123 ATSALDPETEALILEALRALAK---GKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-232 |
1.23e-46 |
|
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: 158.52 E-value: 1.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSY--HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPY--KRGLAM 94
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFpHMKVEDNVAFGLRAQKQprgliaERVTEALKIVGMADYATRYPH-----------QLSGGQQQRVAIARAI 163
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLGAPLADD------ERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490252226 164 AVRPRVLLLDEPLSALDaqirhNMVEE--IARLHRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03245 156 LNDPPILLLDEPTSAMD-----MNSEErlKERLRQLLGDKTLIIITH-RPSLLDLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-238 |
1.61e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 159.90 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN---VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPY--KRGLA 93
Cdd:PRK13650 5 IEVKNLTFKYKEDqekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWdiRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 MVVQNY-ALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:PRK13650 85 MVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 173 DEPLSALDAQIRHNMVEEIARLhRELPELTILYVTHDQTEaLTLADKIGIMKDGSLIAHGETHELY 238
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGI-RDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-232 |
2.94e-46 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 158.40 E-value: 2.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYK--RGLAMVV 96
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYAL-FPhMKVEDNVAFGL----RAQKQPRGLIAervtEALKIVGMADYATRYPHQLSGGQQQRVAIARAIA------V 165
Cdd:PRK13548 83 QHSSLsFP-FTVEEVVAMGRaphgLSRAEDDALVA----AALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 166 RPRVLLLDEPLSALDaqIRHNmvEEIARLHRELPE---LTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:PRK13548 158 PPRWLLLDEPTSALD--LAHQ--HHVLRLARQLAHergLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
31-237 |
3.07e-46 |
|
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: 157.28 E-value: 3.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 31 NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDV-TQLPPYKRGLAMVVQNYALFPHMKVED 109
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYCPQFDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 110 NVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVE 189
Cdd:cd03263 95 HLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490252226 190 EIarlHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:cd03263 175 LI---LEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-238 |
4.00e-46 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 157.50 E-value: 4.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 17 SGITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKR---GLA 93
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 MVVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 174 EPLSALD--AqirhnmVEEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELY 238
Cdd:COG1137 162 EPFAGVDpiA------VADIQKIIRHLKErgIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-232 |
3.29e-45 |
|
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: 164.65 E-value: 3.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 4 KTTVTSSPSLAGtsGITLDSLRVSYHGNV--VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTD 81
Cdd:TIGR03375 451 GTRFLHRPRLQG--EIEFRNVSFAYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVD 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 82 VTQLPPY--KRGLAMVVQNYALFpHMKVEDNVAFGLRAqkqprgLIAERVTEALKIVGMADYATRYPH-----------Q 148
Cdd:TIGR03375 529 IRQIDPAdlRRNIGYVPQDPRLF-YGTLRDNIALGAPY------ADDEEILRAAELAGVTEFVRRHPDgldmqigergrS 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 149 LSGGQQQRVAIARAIAVRPRVLLLDEPLSALDaqirhNMVEE--IARLHRELPELTILYVTHdQTEALTLADKIGIMKDG 226
Cdd:TIGR03375 602 LSGGQRQAVALARALLRDPPILLLDEPTSAMD-----NRSEErfKDRLKRWLAGKTLVLVTH-RTSLLDLVDRIIVMDNG 675
|
....*.
gi 490252226 227 SLIAHG 232
Cdd:TIGR03375 676 RIVADG 681
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-238 |
3.47e-45 |
|
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: 155.01 E-value: 3.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKR---GLAMV 95
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 176 LSALDAQIrhnmVEEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELY 238
Cdd:cd03218 161 FAGVDPIA----VQDIQKIIKILKDrgIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-250 |
2.69e-44 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 152.86 E-value: 2.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDT--DVTQLPPYKRGLA--- 93
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAIRElrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 ---MVVQNYALFPHMKVEDNVafgLRAQKQPRGLI-AERVTEALKIVG---MADYATRYPHQLSGGQQQRVAIARAIAVR 166
Cdd:PRK11124 83 nvgMVFQQYNLWPHLTVQQNL---IEAPCRVLGLSkDQALARAEKLLErlrLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 167 PRVLLLDEPLSALDAQIRHNMVEEIarlhRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGeTHELYHYPPNR 244
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSII----RELAEtgITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCFTQPQTE 234
|
....*.
gi 490252226 245 FSAEFL 250
Cdd:PRK11124 235 AFKNYL 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
19-230 |
4.03e-44 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 152.20 E-value: 4.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPpyKRGLA- 93
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD--EDARAr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 -------MVVQNYALFPHMKVEDNVAFG--LRAQKQPRgliaERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIA 164
Cdd:COG4181 87 lrarhvgFVFQSFQLLPTLTALENVMLPleLAGRRDAR----ARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 165 VRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALtLADKIGIMKDGSLIA 230
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRER-GTTLVLVTHDPALAA-RCDRVLRLRAGRLVE 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-242 |
1.07e-43 |
|
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: 159.16 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 9 SSPSLAGTSGITLDSLRVSYHGNV--VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP 86
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 87 P--YKRGLAMVVQNYALFpHMKVEDNVafglraqkqprgLIA------ERVTEALKIVGMADYATRYPH----------- 147
Cdd:COG4987 404 EddLRRRIAVVPQRPHLF-DTTLRENL------------RLArpdatdEELWAALERVGLGDWLAALPDgldtwlgeggr 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 148 QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMveeIARLHRELPELTILYVTHDQTeALTLADKIGIMKDGS 227
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALAGRTVLLITHRLA-GLERMDRILVLEDGR 546
|
250
....*....|....*
gi 490252226 228 LIAHGETHELYHYPP 242
Cdd:COG4987 547 IVEQGTHEELLAQNG 561
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-237 |
1.11e-43 |
|
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: 151.14 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 20 TLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKR---GLAMVV 96
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTE---ALKivgmaDYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYElfpVLK-----EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 174 EPLSAldaqIRHNMVEEIARLHRELPE---LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:TIGR03410 157 EPTEG----IQPSIIKDIGRVIRRLRAeggMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
21-220 |
1.63e-43 |
|
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: 149.69 E-value: 1.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 21 LDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP------YKRGLAM 94
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSkkaskfRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490252226 175 PLSALDAQIRHnmveEIARLHRELPE--LTILYVTHDqTEALTLADKI 220
Cdd:TIGR03608 161 PTGSLDPKNRD----EVLDLLLELNDegKTIIIVTHD-PEVAKQADRV 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-241 |
1.87e-43 |
|
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: 157.92 E-value: 1.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKT----TVLRAIAGFVQPAGGRILIGDTDVTQLPPYK- 89
Cdd:COG4172 7 LSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 90 ---RG--LAMVVQN--YALFPHMKVEDNVAFGLRAQKQPRGLIA-ERVTEALKIVGMADYATR---YPHQLSGGQQQRVA 158
Cdd:COG4172 87 rriRGnrIAMIFQEpmTSLNPLHTIGKQIAEVLRLHRGLSGAAArARALELLERVGIPDPERRldaYPHQLSGGQRQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 159 IARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDqteaLTL----ADKIGIMKDGSLIAHGET 234
Cdd:COG4172 167 IAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQREL-GMALLLITHD----LGVvrrfADRVAVMRQGEIVEQGPT 241
|
....*..
gi 490252226 235 HELYHYP 241
Cdd:COG4172 242 AELFAAP 248
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
19-237 |
2.03e-43 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 151.00 E-value: 2.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGLAMVV 96
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSreLAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPHMKVEDNVAFG--------LRAQKQprgliaERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPR 168
Cdd:COG4604 82 QENHINSRLTVRELVAFGrfpyskgrLTAEDR------EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490252226 169 VLLLDEPLSALDaqIRHnMVEEIARLHRELPEL--TILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:COG4604 156 YVLLDEPLNNLD--MKH-SVQMMKLLRRLADELgkTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
19-237 |
3.01e-43 |
|
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: 149.44 E-value: 3.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP-PYKRGLAMVVQ 97
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPrEVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 NYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 178 ALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEF-GMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
32-238 |
8.97e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 150.20 E-value: 8.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT----QLPPYKRGLAMVVQ--NYALFPHM 105
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIRKKVGLVFQypEYQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 106 kVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMA--DYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:PRK13637 101 -IEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 184 RHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELY 238
Cdd:PRK13637 180 RDEILNKIKELHKEY-NMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-265 |
1.10e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 149.76 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 16 TSGITLDSLRVSYHG--NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQ--LPPYKRG 91
Cdd:PRK13632 5 SVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 92 LAMVVQNY-ALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVL 170
Cdd:PRK13632 85 IGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 171 LLDEPLSALDAQIRHNMVEEIARLHRELPElTILYVTHDQTEALtLADKIGIMKDGSLIAHGETHELYHyppnrfSAEFL 250
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKK-TLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILN------NKEIL 236
|
250
....*....|....*
gi 490252226 251 GRANIlqatalkDSP 265
Cdd:PRK13632 237 EKAKI-------DSP 244
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
29-209 |
1.47e-42 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 147.55 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 29 HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT-----QLPPYKRGLAMVVQNYALFP 103
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgrAIPYLRRKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 104 HMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQi 183
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD- 170
|
170 180
....*....|....*....|....*...
gi 490252226 184 rhnMVEEIARLHRELPE--LTILYVTHD 209
Cdd:cd03292 171 ---TTWEIMNLLKKINKagTTVVVATHA 195
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-237 |
1.95e-42 |
|
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: 148.31 E-value: 1.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPA-GGRILI-----GDTDVTQLppyKRGL 92
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLfgerrGGEDVWEL---RKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 93 AMV---VQNYaLFPHMKVEDNVAFGLRAQ----KQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAV 165
Cdd:COG1119 81 GLVspaLQLR-FPRDETVLDVVLSGFFDSiglyREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490252226 166 RPRVLLLDEPLSALDAQIRHNMVEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAE-GAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-237 |
2.04e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 154.41 E-value: 2.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP---YKRGLAMV 95
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNYALFPHMKVEDNVAFGLRAQKqpRGLI-----AERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVL 170
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGREPRR--GGLIdwramRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490252226 171 LLDEPLSALDAQirhnmveEIARLH---RELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:COG1129 163 ILDEPTASLTER-------EVERLFriiRRLKAqgVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
19-232 |
9.91e-42 |
|
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: 145.41 E-value: 9.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGeVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRG-LAMVVQ 97
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 NYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 178 ALDaqirhnmVEEIARLHRELPEL----TILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03264 160 GLD-------PEERIRFRNLLSELgedrIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
34-241 |
1.30e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 147.47 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT------QLPPYKRGLAMVVQnyalFPHMK- 106
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPLRKKVGIVFQ----FPEHQl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 107 ----VEDNVAFGLRAQKQPRGLIAERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDA 181
Cdd:PRK13634 99 feetVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 182 QIRHNMVEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:PRK13634 179 KGRKEMMEMFYKLHKE-KGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-232 |
4.11e-41 |
|
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: 144.05 E-value: 4.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP-PYKRGLA 93
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 MVVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 174 EPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRAL--GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
33-228 |
4.68e-41 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 143.71 E-value: 4.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPpYKRGLAM-------VVQNYALFPHM 105
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLS-YSQKIILrreligyIFQSFNLIPHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 106 KVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRH 185
Cdd:NF038007 99 SIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490252226 186 NMVEEIARLHRElpELTILYVTHDQtEALTLADKIGIMKDGSL 228
Cdd:NF038007 179 AVLQQLKYINQK--GTTIIMVTHSD-EASTYGNRIINMKDGKL 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-229 |
6.80e-41 |
|
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: 142.78 E-value: 6.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 20 TLDSLRVSYHGNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGlAMVVQN 98
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSI-GYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 --YALFphmkvEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:cd03226 80 vdYQLF-----TDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 177 SALDaqiRHNMvEEIARLHRELPEL--TILYVTHDQTEALTLADKIGIMKDGSLI 229
Cdd:cd03226 155 SGLD---YKNM-ERVGELIRELAAQgkAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-241 |
9.78e-41 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 146.56 E-value: 9.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 30 GNVVLKpLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDT---DVTQ---LPPYKRGLAMVVQNYALFP 103
Cdd:PRK11144 11 GDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgicLPPEKRRIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 104 HMKVEDNVAFGLRAQKQPRgliAERVTEALkivGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:PRK11144 90 HYKVRGNLRYGMAKSMVAQ---FDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 184 RHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:PRK11144 164 KRELLPYLERLAREI-NIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-244 |
1.51e-40 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 143.38 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAI------------AGFVQPAGGRILIGDTDVTQLp 86
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNIYSPRTDTVDL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 87 pyKRGLAMVVQNYALFPhMKVEDNVAFGLR-AQKQPRGLIAERVTEALKIVGMADYATRYPHQ----LSGGQQQRVAIAR 161
Cdd:PRK14239 85 --RKEIGMVFQQPNPFP-MSIYENVVYGLRlKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 162 AIAVRPRVLLLDEPLSALDAqIRHNMVEEIarLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDP-ISAGKIEET--LLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
...
gi 490252226 242 PNR 244
Cdd:PRK14239 239 KHK 241
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
24-238 |
2.91e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 143.29 E-value: 2.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 24 LRVSY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIG----DTDVTQLPPYKRGLAMVVQN 98
Cdd:PRK13639 7 LKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepiKYDKKSLLEVRKTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 Y--ALFPHmKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:PRK13639 87 PddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490252226 177 SALDAQirhnMVEEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELY 238
Cdd:PRK13639 166 SGLDPM----GASQIMKLLYDLNKegITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
33-241 |
2.96e-40 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 143.05 E-value: 2.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVtQLPPYK---RGLAMVVQ--NYALFPHMKV 107
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-EYGDYKyrcKHIRMIFQdpNTSLNPRLNI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 108 EDNVAFGLR------AQKQprgliAERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:COG4167 107 GQILEEPLRlntdltAEER-----EERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490252226 181 AQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:COG4167 182 MSVRSQIINLMLELQEKL-GISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-231 |
1.80e-39 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 137.56 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPY---KRGLAMV 95
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdarRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 vqnyalfphmkvednvafglraqkqprgliaervtealkivgmadyatrypHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:cd03216 81 ---------------------------------------------------YQLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 176 LSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAH 231
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ--GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-237 |
2.53e-39 |
|
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: 139.67 E-value: 2.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYH-GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT--QLPPYKRGLAMV 95
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNYALFpHMKVEDNVAFG-LRAQKqprgliaERVTEALKIVGMADYATRYPHQ-----------LSGGQQQRVAIARAI 163
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYGrPDATD-------EEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 164 AVRPRVLLLDEPLSALDAQIRHNMVEEIARL--HRelpelTILYVTHDQTEALTlADKIGIMKDGSLIAHGETHEL 237
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVskGR-----TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-273 |
1.46e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 139.47 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYK-------RG 91
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeeRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 92 lamvvqnyaLFPHMKVEDNVAF-----GLRAQKqprglIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVR 166
Cdd:COG4152 82 ---------LYPKMKVGEQLVYlarlkGLSKAE-----AKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 167 PRVLLLDEPLSALD---AQIrhnMVEEIARLHRElpELTILYVTH--DQTEAltLADKIGIMKDGSLIAHGETHELYH-Y 240
Cdd:COG4152 148 PELLILDEPFSGLDpvnVEL---LKDVIRELAAK--GTTVIFSSHqmELVEE--LCDRIVIINKGRKVLSGSVDEIRRqF 220
|
250 260 270
....*....|....*....|....*....|...
gi 490252226 241 PPNRFSAEFLGRANILQAtalkdspEPGLVSVS 273
Cdd:COG4152 221 GRNTLRLEADGDAGWLRA-------LPGVTVVE 246
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
30-262 |
1.59e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 138.71 E-value: 1.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPY----KRGLAMVVQNYALFPhM 105
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvrsKVGLVFQDPDDQVFS-S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 106 KVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRH 185
Cdd:PRK13647 96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 186 NMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGEThelyhyppnrfsaEFLGRANILQATALK 262
Cdd:PRK13647 176 TLMEILDRLHNQ--GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-------------SLLTDEDIVEQAGLR 237
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-238 |
2.32e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 138.35 E-value: 2.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN--VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQ--LPPYKRGLAM 94
Cdd:PRK13648 8 IVFKNVSFQYQSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdnFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQN-YALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:PRK13648 88 VFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 174 EPLSALDAQIRHNMVEEIARLHRElPELTILYVTHDQTEALTlADKIGIMKDGSLIAHGETHELY 238
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVKSE-HNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-236 |
3.21e-38 |
|
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: 136.59 E-value: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSY--HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT--QLPPYKRGLAM 94
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFpHMKVEDNVAFGLraqkqpRGLIAERVTEALKIVGMADYATRYPH-----------QLSGGQQQRVAIARAI 163
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGR------PGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 164 AVRPRVLLLDEPLSALDAQIRHNMVEEIARL--HRelpelTILYVTHDQTeALTLADKIGIMKDGSLIAHGeTHE 236
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLmkNR-----TTFVIAHRLS-TIENADRIVVLEDGKIVERG-THE 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
19-232 |
3.40e-38 |
|
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: 135.81 E-value: 3.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVVQN 98
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVEDNVAFGLRAqkqpRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:cd03268 81 PGFYPNLTARENLRLLARL----LGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490252226 179 LDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ--GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
30-236 |
3.44e-38 |
|
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: 143.74 E-value: 3.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRG-----LAmvvQNYALFPH 104
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhigyLP---QDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 105 mKVEDNVA-FGlraqkqprGLIAERVTEALKIVGMAD--------YATRY---PHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:COG4618 421 -TIAENIArFG--------DADPEKVVAAAKLAGVHEmilrlpdgYDTRIgegGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490252226 173 DEPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTeALTLADKIGIMKDGSLIAHGETHE 236
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKAR--GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-250 |
2.09e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 135.35 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRA------------IAGFVQPAGGRILIGDTDVTQLp 86
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearVEGEVRLFGRNIYSPDVDPIEV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 87 pyKRGLAMVVQNYALFPHMKVEDNVAFGLRAQK--QPRGLIAERVTEALKIVGM----ADYATRYPHQLSGGQQQRVAIA 160
Cdd:PRK14267 84 --RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 161 RAIAVRPRVLLLDEPLSALDAqIRHNMVEEIarLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHY 240
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDP-VGTAKIEEL--LFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
250
....*....|
gi 490252226 241 PPNRFSAEFL 250
Cdd:PRK14267 239 PEHELTEKYV 248
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
32-238 |
5.97e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 134.83 E-value: 5.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT---QLPPYKRGLAMVVQNyalfPHMK-- 106
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeeNLWDIRNKAGMVFQN----PDNQiv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 107 ---VEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:PRK13633 100 atiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 184 RHNMVEEIARLHRELpELTILYVTHDQTEALTlADKIGIMKDGSLIAHGETHELY 238
Cdd:PRK13633 180 RREVVNTIKELNKKY-GITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
33-238 |
7.06e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 134.54 E-value: 7.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQP---AGGRILIGDTDVTQLPPY--KRGLAMVVQNY-ALFPHMK 106
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWdiREKVGIVFQNPdNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 107 VEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHN 186
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490252226 187 MVEEIARLHRElPELTILYVTHDQTEAlTLADKIGIMKDGSLIAHGETHELY 238
Cdd:PRK13640 182 ILKLIRKLKKK-NNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIF 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
19-232 |
8.28e-37 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 132.40 E-value: 8.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP-------PYKRG 91
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 92 LamvvqnyalFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:cd03269 81 L---------YPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490252226 172 LDEPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARA--GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
37-244 |
9.78e-37 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 134.12 E-value: 9.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 37 LSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDV-----TQLPPYKRGLAMVVQNYALFPHMKVEDNV 111
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 112 AFGLRAQKQ-PRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEE 190
Cdd:PRK11831 106 AYPLREHTQlPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490252226 191 IARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNR 244
Cdd:PRK11831 186 ISELNSAL-GVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
34-238 |
1.10e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 134.06 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPY--KRGLAMVVQNY-ALFPHMKVEDN 110
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWnlRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRhnmvEE 190
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR----QE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490252226 191 IARLHRELPE---LTILYVTHDQTEALTlADKIGIMKDGSLIAHGETHELY 238
Cdd:PRK13642 179 IMRVIHEIKEkyqLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-238 |
3.78e-36 |
|
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: 131.51 E-value: 3.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSY---HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGLA 93
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrwLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 MVVQNYALFPhMKVEDNVAFGLRAQKQprgliaERVTEALKIVGMADYATRYPH-----------QLSGGQQQRVAIARA 162
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYGKPDATD------EEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 163 IAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRelpELTILYVTHDQTeALTLADKIGIMKDGSLIAHGeTH-ELY 238
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMK---GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQG-THdELM 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-220 |
8.92e-36 |
|
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: 136.65 E-value: 8.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 17 SGITLDSLRVSYHG-NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGLA 93
Cdd:TIGR02857 320 SSLEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAdsWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 MVVQNYALFPHmKVEDNVAFGLRAQKqprgliAERVTEALKIVGMADYATRYP-----------HQLSGGQQQRVAIARA 162
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDAS------DAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 163 IAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRelpELTILYVTHDqTEALTLADKI 220
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ---GRTVLLVTHR-LALAALADRI 526
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-232 |
1.07e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 130.62 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 3 MKTTVTSSPSLAgtsgitLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDV 82
Cdd:COG4674 1 MSLDTMHGPILY------VEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 83 TQLPPYKRGLAMVV---QNYALFPHMKVEDNVAFGLRAQKQPRGLI--------AERVTEALKIVGMADYATRYPHQLSG 151
Cdd:COG4674 75 TGLDEHEIARLGIGrkfQKPTVFEELTVFENLELALKGDRGVFASLfarltaeeRDRIEEVLETIGLTDKADRLAGLLSH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 152 GQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVE---EIARLHrelpelTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:COG4674 155 GQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAEllkSLAGKH------SVVVVEHDMEFVRQIARKVTVLHQGSV 228
|
....
gi 490252226 229 IAHG 232
Cdd:COG4674 229 LAEG 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-250 |
1.34e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 130.47 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 24 LRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT---------------QLPPY 88
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadknQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 89 KRGLAMVVQNYALFPHMKVEDNVafgLRAQKQPRGL----IAERVTEALKIVGMADYAT-RYPHQLSGGQQQRVAIARAI 163
Cdd:PRK10619 91 RTRLTMVFQHFNLWSHMTVLENV---MEAPIQVLGLskqeARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 164 AVRPRVLLLDEPLSALDAQirhnMVEEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPE----LVGEVLRIMQQLAEegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
....*....
gi 490252226 242 PNRFSAEFL 250
Cdd:PRK10619 244 QSPRLQQFL 252
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
27-218 |
1.38e-35 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 128.51 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 27 SYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTdvtqlppykRGLAMVVQNYAL---FP 103
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------ARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 104 hMKVEDNVAFGLRAQKQP-RGLIAE---RVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:NF040873 72 -LTVRDLVAMGRWARRGLwRRLTRDdraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 490252226 180 DAQIRHNMVEEIARLHRElpELTILYVTHDQtEALTLAD 218
Cdd:NF040873 151 DAESRERIIALLAEEHAR--GATVVVVTHDL-ELVRRAD 186
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
38-241 |
1.49e-35 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 130.50 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYK---RGLAMVVQNYALFPHMKVEDNVafg 114
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVRTFQHVRLFREMTVIENL--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 115 LRAQKQP------RGLIA------------ERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:PRK11300 102 LVAQHQQlktglfSGLLKtpafrraesealDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 177 SALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:PRK11300 182 AGLNPKETKELDELIAELRNEH-NVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-237 |
2.06e-35 |
|
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: 129.53 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN--VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGLAM 94
Cdd:cd03252 1 ITFEHVRFRYKPDgpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFpHMKVEDNVAFGlraqkqPRGLIAERVTEALKIVGMADYATRYPH-----------QLSGGQQQRVAIARAI 163
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALA------DPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490252226 164 AVRPRVLLLDEPLSALDAQIRHNMveeIARLHRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAI---MRNMHDICAGRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-226 |
2.83e-35 |
|
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: 126.95 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN--VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGLAM 94
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPneLGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFPhmkvednvafglraqkqprGLIAERVtealkivgmadyatryphqLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:cd03246 81 LPQDDELFS-------------------GSIAENI-------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490252226 175 PLSALDAQIRHNMVEEIARLhrELPELTILYVTHdQTEALTLADKIGIMKDG 226
Cdd:cd03246 123 PNSHLDVEGERALNQAIAAL--KAAGATRIVIAH-RPETLASADRILVLEDG 171
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-208 |
3.55e-35 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 135.32 E-value: 3.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 17 SGITLDSLRV-SYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRIligdtdvtQLPPYKRglamv 95
Cdd:COG4178 361 GALALEDLTLrTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR----- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 vqnyALF----PHMKVEDnvafgLRAQ----KQPRGLIAERVTEALKIVGMADYATRY------PHQLSGGQQQRVAIAR 161
Cdd:COG4178 428 ----VLFlpqrPYLPLGT-----LREAllypATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFAR 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490252226 162 AIAVRPRVLLLDEPLSALDAQIRHNMveeIARLHRELPELTILYVTH 208
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAAL---YQLLREELPGTTVISVGH 542
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
19-237 |
7.54e-35 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 134.44 E-value: 7.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN---VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGLA 93
Cdd:TIGR02204 338 IEFEQVNFAYPARpdqPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPaeLRARMA 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 MVVQNYALFPHmKVEDNVAFGLRAQKQPRGLIAERVTEALKIV-----GMADYATRYPHQLSGGQQQRVAIARAIAVRPR 168
Cdd:TIGR02204 418 LVPQDPVLFAA-SVMENIRYGRPDATDEEVEAAARAAHAHEFIsalpeGYDTYLGERGVTLSGGQRQRIAIARAILKDAP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 169 VLLLDEPLSALDAQIRHNMVEEIARLhreLPELTILYVTHDQTEALTlADKIGIMKDGSLIAHGETHEL 237
Cdd:TIGR02204 497 ILLLDEATSALDAESEQLVQQALETL---MKGRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAEL 561
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
33-238 |
1.45e-34 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 134.85 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGLAMVVQNYALFPHmKVEDN 110
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHhyLHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAFGLRAQKQprgliaERVTEALKIVGMADYATRYPH-----------QLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:TIGR00958 575 IAYGLTDTPD------EEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 180 DAQIRHNMVEEiarlhRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETHELY 238
Cdd:TIGR00958 649 DAECEQLLQES-----RSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLM 701
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-251 |
1.71e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 128.29 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 9 SSPSLAGTSgitldsLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRA-------IAGFVQPA----GGRILI 77
Cdd:PRK14271 18 AAPAMAAVN------LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRYSGdvllGGRSIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 78 GDTDVTQlppYKRGLAMVVQNYALFPhMKVEDNVAFGLRA-----QKQPRGLIAERVTEALKIVGMADYATRYPHQLSGG 152
Cdd:PRK14271 92 NYRDVLE---FRRRVGMLFQRPNPFP-MSIMDNVLAGVRAhklvpRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 153 QQQRVAIARAIAVRPRVLLLDEPLSALDAqirhNMVEEIARLHRELPE-LTILYVTHDQTEALTLADKIGIMKDGSLIAH 231
Cdd:PRK14271 168 QQQLLCLARTLAVNPEVLLLDEPTSALDP----TTTEKIEEFIRSLADrLTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
250 260
....*....|....*....|
gi 490252226 232 GETHELYHYPPNRFSAEFLG 251
Cdd:PRK14271 244 GPTEQLFSSPKHAETARYVA 263
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
38-241 |
1.92e-34 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 129.44 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKR-----GLAMVVQN--YALFPHMKVEDN 110
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAFGLRA--QKQPRGLIAERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNM 187
Cdd:PRK15079 121 IAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490252226 188 VEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:PRK15079 201 VNLLQQLQREM-GLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
37-237 |
5.32e-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: 131.46 E-value: 5.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 37 LSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGR--ILIGD--TDVTQLPPYKRG-----LAMVVQNYALFPHMKV 107
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDewVDMTKPGPDGRGrakryIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 108 EDNV--AFGLraqKQPRGLIAERVTEALKIVGMAD-YAT----RYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:TIGR03269 383 LDNLteAIGL---ELPDELARMKAVITLKMVGFDEeKAEeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 181 AQIRHNMVEEIARLHRELPElTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:TIGR03269 460 PITKVDVTHSILKAREEMEQ-TFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-252 |
6.94e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 125.93 E-value: 6.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQ------PAGGRILIGDTDVTQLPPYK--RGLAMVVQNYALFPH 104
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKlrKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 105 MKVEDNVAFGLRAQ--KQPRGlIAERVTEALKIVGM----ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:PRK14246 105 LSIYDNIAYPLKSHgiKEKRE-IKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 179 LDAQIRHNMVEEIARLHRelpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEF-LGR 252
Cdd:PRK14246 184 IDIVNSQAIEKLITELKN---EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYvIGR 255
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
27-241 |
8.10e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 126.46 E-value: 8.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 27 SYHGNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQ--LPPYKRGLAMVVQNY--AL 101
Cdd:PRK13652 12 SYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenIREVRKFVGLVFQNPddQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 102 FPhMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDA 181
Cdd:PRK13652 92 FS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490252226 182 QirhnMVEEIARLHRELPE---LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:PRK13652 171 Q----GVKELIDFLNDLPEtygMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-229 |
1.75e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 125.20 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 31 NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRG--LAMVVQNYAL--FPHMK 106
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAkyIGRVFQDPMMgtAPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 107 VEDNVAFGLRaQKQPRGLI-------AERVTEALKIVGMA-----DYATRYphqLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:COG1101 99 IEENLALAYR-RGKRRGLRrgltkkrRELFRELLATLGLGlenrlDTKVGL---LSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 175 PLSALD---AQIRHNMVEEIARLHRelpeLTILYVTHDQTEALTLADKIGIMKDGSLI 229
Cdd:COG1101 175 HTAALDpktAALVLELTEKIVEENN----LTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-209 |
2.46e-33 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 123.45 E-value: 2.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQL-----PPYKRGLAMVVQNYALFPH 104
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 105 MKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIR 184
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180
....*....|....*....|....*..
gi 490252226 185 hnmvEEIARLHRELPE--LTILYVTHD 209
Cdd:PRK10908 174 ----EGILRLFEEFNRvgVTVLMATHD 196
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-246 |
4.44e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 124.33 E-value: 4.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIG--DT-DVTQLPPYKRGLAM 94
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgiDTgDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQN-YALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490252226 174 EPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDqTEALTLADKIGIMKDGSLIAHGEthelyhyPPNRFS 246
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEK--GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGE-------PENVLS 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-236 |
4.53e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 123.59 E-value: 4.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGLAMVV 96
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrqLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPHMKVEDNVAFG----------LRAQKQprgliaERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVR 166
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGrspwlslwgrLSAEDN------ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490252226 167 PRVLLLDEPLSALDaqIRHNMveEIARLHRELPEL--TILYVTHDQTEALTLADKIGIMKDGSLIAHGETHE 236
Cdd:PRK11231 157 TPVVLLDEPTTYLD--INHQV--ELMRLMRELNTQgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
33-229 |
5.75e-33 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 123.76 E-value: 5.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP-----YKRGLAMVVQNY--ALFPHM 105
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrraFRRDVQLVFQDSpsAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 106 KVEDNVAFGLR--------AQKqprgliaERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:TIGR02769 106 TVRQIIGEPLRhltsldesEQK-------ARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490252226 177 SALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLI 229
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAF-GTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
38-241 |
6.43e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 125.08 E-value: 6.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLA-----MVVQN-YA-LFPHMKVEDN 110
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqkiqIVFQNpYGsLNPRKKVGQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAFGL-------RAQKqprgliAERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:PRK11308 115 LEEPLlintslsAAER------REKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 183 IRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:PRK11308 189 VQAQVLNLMMDLQQEL-GLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
30-220 |
3.30e-32 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 120.59 E-value: 3.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGLAMVVQNYALFPHmKV 107
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiYRQQVSYCAQTPTLFGD-TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 108 EDNVAF--GLRAQK-QPRGLIAErvteaLKIVGMADYATRYP-HQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:PRK10247 98 YDNLIFpwQIRNQQpDPAIFLDD-----LERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 490252226 184 RHNMVEEIARLHRElPELTILYVTHDQTEaLTLADKI 220
Cdd:PRK10247 173 KHNVNEIIHRYVRE-QNIAVLWVTHDKDE-INHADKV 207
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-237 |
3.85e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 126.88 E-value: 3.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 26 VSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVqPAGGRILIGDTDVTQLPP--YKRGLAMVVQNYALFp 103
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPesWRKHLSWVGQNPQLP- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 104 HMKVEDNVAFGlRAQKQPrgliaERVTEALKIVGMADYATRYPH-----------QLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:PRK11174 436 HGTLRDNVLLG-NPDASD-----EQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 173 DEPLSALDAQIRHNMVEEIARLHRelpELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAASR---RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
33-228 |
4.74e-32 |
|
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: 118.69 E-value: 4.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPY---KRGLAMVV---QNYALFPHMK 106
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaiRAGIAYVPedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 107 VEDNVAFglraqkqprgliaervtealkivgmadyatryPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD--Aqir 184
Cdd:cd03215 95 VAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDvgA--- 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490252226 185 hnmVEEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:cd03215 140 ---KAEIYRLIRELADagKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
27-237 |
6.54e-32 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 120.02 E-value: 6.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 27 SY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP--PYKRGLAMVVQNYALFP 103
Cdd:cd03254 11 SYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkSLRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 104 HmKVEDNVAFG-LRAQKqprgliaERVTEALKIVGMADYATRYP-----------HQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:cd03254 91 G-TIMENIRLGrPNATD-------EEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 172 LDEPLSALDaqirhnmVEEIARLHRELPEL----TILYVTHdQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:cd03254 163 LDEATSNID-------TETEKLIQEALEKLmkgrTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
38-236 |
7.75e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.14 E-value: 7.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP---YKRGLAMVVQNYALFPHMKVEDNVAFG 114
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrdaIALGIGMVHQHFMLVPNLTVAENIVLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 115 L---RAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQirhnmveEI 191
Cdd:COG3845 105 LeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQ-------EA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490252226 192 ARLHRELPEL-----TILYVTHDQTEALTLADKIGIMKDGSLIAHGETHE 236
Cdd:COG3845 178 DELFEILRRLaaegkSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
33-228 |
1.43e-31 |
|
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: 119.11 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIgdtDVTQLPPYK-----RGLAMVVQNYALFPHmKV 107
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL---DGKPISQYEhkylhSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 108 EDNVAFGLraqkqpRGLIAERVTEALKIVGMADYATRYPH-----------QLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:cd03248 105 QDNIAYGL------QSCSFECVKEAAQKAHAHSFISELASgydtevgekgsQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490252226 177 SALDAQIRHnMVEEiarLHRELPELTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:cd03248 179 SALDAESEQ-QVQQ---ALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-250 |
3.74e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.48 E-value: 3.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQ-----PAGGRILIGDTDVTQLP--PYKRG 91
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDviELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 92 LAMVVQNYALFPHMKVEDNVAFGLRAQK--QPRGLIAERVTEALKIVGMADYATRY----PHQLSGGQQQRVAIARAIAV 165
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 166 RPRVLLLDEPLSALDAQirhnMVEEIARLHREL-PELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNR 244
Cdd:PRK14247 164 QPEVLLADEPTANLDPE----NTAKIESLFLELkKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHE 239
|
....*.
gi 490252226 245 FSAEFL 250
Cdd:PRK14247 240 LTEKYV 245
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
34-236 |
5.66e-31 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 118.02 E-value: 5.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVqPAGGRILIGDTDVTQLPPYK--RGLAMVVQNYALFPHMKVEDNV 111
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 112 AFGLRAQKQP---RGLIAErVTEALKIvgmADYATRYPHQLSGGQQQRVAIARAIA-VRPRV------LLLDEPLSALDa 181
Cdd:COG4138 91 ALHQPAGASSeavEQLLAQ-LAEALGL---EDKLSRPLTQLSGGEWQRVRLAAVLLqVWPTInpegqlLLLDEPMNSLD- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 182 qIRHnmveEIA--RLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHE 236
Cdd:COG4138 166 -VAQ----QAAldRLLRELCQqgITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
33-236 |
1.02e-30 |
|
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: 122.90 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQ--LPPYKRGLAMVVQNYALFPHmKVEDN 110
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytLASLRRQVALVSQDVVLFND-TIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAFGlraqkQPRGLIAERVTEALKIVGMADYATRYP---HQ--------LSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:TIGR02203 426 IAYG-----RTEQADRAEIERALAAAYAQDFVDKLPlglDTpigengvlLSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 180 DAQiRHNMVEeiARLHRELPELTILYVTHDQTeALTLADKIGIMKDGSLIAHGeTHE 236
Cdd:TIGR02203 501 DNE-SERLVQ--AALERLMQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERG-THN 552
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
32-227 |
1.41e-30 |
|
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: 116.38 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILI----GDTDVTQLPPY------KRGLAMVVQNYAL 101
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPReilalrRRTIGYVSQFLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 102 FPHMKVEDNVAFGLRAQKQPRGLIAERVTEALkivgmadyaTR----------YPHQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:COG4778 105 IPRVSALDVVAEPLLERGVDREEARARARELL---------ARlnlperlwdlPPATFSGGEQQRVNIARGFIADPPLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 172 LDEPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGS 227
Cdd:COG4778 176 LDEPTASLDAANRAVVVELIEEAKAR--GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-237 |
1.41e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 116.92 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPY---KRGLAMV 95
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNYALFPHMKVEDNVAFGLRAQK----QPRGLIAERVTEALKIVGMADyatRYPHQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDdlsaEQREDRANELMEEFHIEHLRD---SMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 172 LDEPLSALDAQirhnMVEEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK10895 161 LDEPFAGVDPI----SVIDIKRIIEHLRDsgLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-232 |
2.66e-30 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 115.93 E-value: 2.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 24 LRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGF--VQPAGGRILIGDTDVTQLPPYKR---GLAMVVQN 98
Cdd:COG0396 6 LHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERaraGIFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVED--NVAFGLRAQKQPRGLIA-ERVTEALKIVGM-ADYATRYPHQ-LSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:COG0396 86 PVEIPGVSVSNflRTALNARRGEELSAREFlKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490252226 174 EPLSALDA---QIrhnMVEEIARLHRelPELTILYVTHdQTEALTL--ADKIGIMKDGSLIAHG 232
Cdd:COG0396 166 ETDSGLDIdalRI---VAEGVNKLRS--PDRGILIITH-YQRILDYikPDFVHVLVDGRIVKSG 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-252 |
2.74e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 116.42 E-value: 2.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 22 DSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRA-------IAGFvqPAGGRILIGDTDV--TQLPP--YKR 90
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGF--RVEGKVTFHGKNLyaPDVDPveVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 91 GLAMVVQNYALFPHmKVEDNVAFGLRAQKQpRGLIAERVTEALKIVGMADYATRYPHQ----LSGGQQQRVAIARAIAVR 166
Cdd:PRK14243 92 RIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 167 PRVLLLDEPLSALDAqIRHNMVEEiarLHRELPE-LTILYVTHDQTEALTLADKIGIM---------KDGSLIAHGETHE 236
Cdd:PRK14243 170 PEVILMDEPCSALDP-ISTLRIEE---LMHELKEqYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEK 245
|
250
....*....|....*..
gi 490252226 237 LYHYPPNRFSAEFL-GR 252
Cdd:PRK14243 246 IFNSPQQQATRDYVsGR 262
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-238 |
4.71e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 116.65 E-value: 4.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 16 TSGITLDSLRVSYHGNV-----VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGD-------TDVT 83
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 84 QLPPYKRGLAMVVQ--NYALFPHMkVEDNVAFG---LRAQKQPrglIAERVTEALKIVGMA-DYATRYPHQLSGGQQQRV 157
Cdd:PRK13645 84 EVKRLRKEIGLVFQfpEYQLFQET-IEKDIAFGpvnLGENKQE---AYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 158 AIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELPElTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKK-RIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
.
gi 490252226 238 Y 238
Cdd:PRK13645 239 F 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
33-232 |
5.39e-30 |
|
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: 113.80 E-value: 5.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAG--GRILIGDTDVTQLPPYKRgLAMVVQNYALFPHMKVEDN 110
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAFglraqkqprgliaervteALKIVGmadyatryphqLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVE- 189
Cdd:cd03213 103 LMF------------------AAKLRG-----------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSl 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490252226 190 --EIARLHRelpelTILYVTHD-QTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03213 154 lrRLADTGR-----TIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-182 |
8.54e-30 |
|
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: 113.22 E-value: 8.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDV-TQLPPYKRGLAMVVQ 97
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 NYALFPHMKVEDNVAFgLRAQKQPRGLIAErvtEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:TIGR01189 81 LPGLKPELSALENLHF-WAAIHGGAQRTIE---DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
....*
gi 490252226 178 ALDAQ 182
Cdd:TIGR01189 157 ALDKA 161
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
16-237 |
1.06e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 116.06 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 16 TSGITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMV 95
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNY-ALFPHMKVEDNVA-----FGLRAQKqprglIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRV 169
Cdd:PRK13537 85 VPQFdNLDPDFTVRENLLvfgryFGLSAAA-----ARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 170 LLLDEPLSALDAQIRHNMVEeiaRLHRELPE-LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWE---RLRSLLARgKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
33-236 |
1.07e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 115.95 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRI-----------------LIGDTDVTQLPPYK------ 89
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekeKVLEKLVIQKTRFKkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 90 ---RGLAMVVQ--NYALFpHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAI 163
Cdd:PRK13651 102 eirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490252226 164 AVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHE 236
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ--GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-250 |
1.23e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 114.75 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 18 GITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRA------------IAGFVQPAGGRILIGDTDVTQL 85
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKClnrmnelesevrVEGRVEFFNQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 86 ppyKRGLAMVVQNYALFPhMKVEDNVAFGLRAQK-QPRGLIAERVTEALKIVGMADYATRYPHQ----LSGGQQQRVAIA 160
Cdd:PRK14258 87 ---RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 161 RAIAVRPRVLLLDEPLSALDAqIRHNMVEEIARLHRELPELTILYVTHDQTEALTLADKIGIMKD-----GSLIAHGETH 235
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDP-IASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTK 241
|
250
....*....|....*
gi 490252226 236 ELYHYPPNRFSAEFL 250
Cdd:PRK14258 242 KIFNSPHDSRTREYV 256
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-237 |
1.48e-29 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 114.50 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 17 SGITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQL--PPYKRGLAM 94
Cdd:PRK10575 10 TTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWssKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFPHMKVEDNVAFGLRAQKQPRGLIA----ERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVL 170
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAIGRYPWHGALGRFGaadrEKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 171 LLDEPLSALDaqIRHNmVEEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK10575 170 LLDEPTSALD--IAHQ-VDVLALVHRLSQErgLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
32-238 |
2.07e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 114.88 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQ------LPPYKRGLAMVVQnyalFPHM 105
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyIRPVRKRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 106 KV-EDNVA----FGLRAQKQPRGLIAERVTEALKIVGMA-DYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:PRK13646 97 QLfEDTVEreiiFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 180 DAQIRHNMVEEIARLHRELPElTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELY 238
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQTDENK-TIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
33-231 |
2.49e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 113.37 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRG------LAMVVQNYALFPHMK 106
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 107 VEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHN 186
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490252226 187 MVEEIARLHRElPELTILYVTHDqteaLTLADKIGI---MKDGSLIAH 231
Cdd:PRK11629 184 IFQLLGELNRL-QGTAFLVVTHD----LQLAKRMSRqleMRDGRLTAE 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
34-241 |
3.41e-29 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 113.73 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRG--LAMVVQN--YALFPHMKVED 109
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrIRMIFQDpsTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 110 NVAFGLRAQKQPRGLIAE-RVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRhnm 187
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREkQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR--- 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 188 vEEIARLHRELPE---LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:PRK15112 186 -SQLINLMLELQEkqgISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-250 |
3.53e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 118.27 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 31 NVVLKPLSLTIEPGEVLALIGPSGSGKTT----VLRAIAgfvqpAGGRILIGDT-----DVTQLPPYKRGLAMVVQ--NY 99
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQplhnlNRRQLLPVRHRIQVVFQdpNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 100 ALFPHMKVEDNVAFGLRAQkQPRGLIAER---VTEALKIVGMaDYATR--YPHQLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLRVH-QPTLSAAQReqqVIAVMEEVGL-DPETRhrYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 175 PLSALD----AQIRhNMVEEIARLHRelpeLTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFL 250
Cdd:PRK15134 452 PTSSLDktvqAQIL-ALLKSLQQKHQ----LAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
33-230 |
5.03e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.43 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPY---KRGLAMVVQN---YALFPHMK 106
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdaiRAGIAYVPEDrkgEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 107 VEDNVAFGLRAQKQPRGLI--------AERVTEALKIVgmadyaTRYPHQ----LSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:COG1129 347 IRENITLASLDRLSRGGLLdrrreralAEEYIKRLRIK------TPSPEQpvgnLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490252226 175 PLSALDaqirhnmV---EEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIA 230
Cdd:COG1129 421 PTRGID-------VgakAEIYRLIRELAAegKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
33-209 |
7.00e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 112.86 E-value: 7.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP-----PYKRGLAMVVQNY--ALFPHM 105
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkAFRRDIQMVFQDSisAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 106 KVEDNVAFGLR----AQKQPRgliAERVTEALKIVGMAD-YATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK10419 107 TVREIIREPLRhllsLDKAER---LARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180
....*....|....*....|....*....
gi 490252226 181 AQIRHNMVEEIARLHRELpELTILYVTHD 209
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQF-GTACLFITHD 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-238 |
7.60e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.02 E-value: 7.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 26 VSYH---GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIG----DTDVTQLPPYKRGLAMVVQ- 97
Cdd:PRK13636 11 LNYNysdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpiDYSRKGLMKLRESVGMVFQd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 -NYALFPHMKVEDnVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:PRK13636 91 pDNQLFSASVYQD-VSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490252226 177 SALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELY 238
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKEL-GLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-260 |
7.80e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 117.90 E-value: 7.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 21 LDSLRVSYHGN----VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP------YKR 90
Cdd:PRK10535 7 LKDIRRSYPSGeeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaqlRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 91 GLAMVVQNYALFPHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVL 170
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 171 LLDEPLSALDAqirHNMVEEIARLHrELPEL--TILYVTHDQTEAlTLADKIGIMKDGSLIAHgethelyhyPPNRFSAE 248
Cdd:PRK10535 167 LADEPTGALDS---HSGEEVMAILH-QLRDRghTVIIVTHDPQVA-AQAERVIEIRDGEIVRN---------PPAQEKVN 232
|
250
....*....|..
gi 490252226 249 FLGRANILQATA 260
Cdd:PRK10535 233 VAGGTEPVVNTA 244
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-209 |
1.59e-28 |
|
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: 116.31 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 8 TSSPSLAGTSGITLDSLRVSYHG-NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP 86
Cdd:TIGR02868 324 AAGAVGLGKPTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 87 --PYKRGLAMVVQNYALFpHMKVEDNVAFGlRAQKQPrgliaERVTEALKIVGMADYATRYPH-----------QLSGGQ 153
Cdd:TIGR02868 404 qdEVRRRVSVCAQDAHLF-DTTVRENLRLA-RPDATD-----EELWAALERVGLADWLRALPDgldtvlgeggaRLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 154 QQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLhreLPELTILYVTHD 209
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA---LSGRTVVLITHH 529
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
33-229 |
2.06e-28 |
|
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: 110.44 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAG---GRILIgdtDVTQLPPY--KRGLAMVVQNYALFPHMKV 107
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILF---NGQPRKPDqfQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 108 EDNVAFG--LRAQ-KQPRGLIAERV-TEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:cd03234 99 RETLTYTaiLRLPrKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490252226 184 RHNMVEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLI 229
Cdd:cd03234 179 ALNLVSTLSQLARR-NRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-307 |
2.32e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 116.49 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 37 LSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYK-----RGLAMVVQN-YA-LFPHMKVED 109
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 110 NVAFGLRAQKQPRGLIA-ERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNM 187
Cdd:PRK10261 423 SIMEPLRVHGLLPGKAAaARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 188 VEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFLgrANILQATALKDSPEP 267
Cdd:PRK10261 503 INLLLDLQRDF-GIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM--AAVPVADPSRQRPQR 579
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490252226 268 GLVSVSCGGgliNAFSRGGLHGNNKLLCIRPQHMSLAPRS 307
Cdd:PRK10261 580 VLLSDDLPS---NIHLRGEEVAAVSLQCVGPGHYVAQPQS 616
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
32-237 |
5.71e-28 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 114.75 E-value: 5.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRG--LAMVVQNYALFPHmKVED 109
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIGYLPQDVELFPG-TVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 110 NVA-FGLRAQkqprgliAERVTEALKIVGMADYATRYPH-----------QLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:TIGR01842 411 NIArFGENAD-------PEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 178 ALDAQIRHNMVEEIARLhrELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:TIGR01842 484 NLDEEGEQALANAIKAL--KARGITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
26-227 |
6.48e-28 |
|
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: 108.33 E-value: 6.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 26 VSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTdvtqlppykrgLAMVVQNYALFPhM 105
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQEPWIQN-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 106 KVEDNVAFGLRAQKQpRgliAERVTEA------LKIVGMADyatryphQ---------LSGGQQQRVAIARAIAVRPRVL 170
Cdd:cd03250 81 TIRENILFGKPFDEE-R---YEKVIKAcalepdLEILPDGD-------LteigekginLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490252226 171 LLDEPLSALDAQIRHNMVEE----IARLHRelpelTILYVTHdQTEALTLADKIGIMKDGS 227
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFENcilgLLLNNK-----TRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
19-232 |
8.97e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 112.63 E-value: 8.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYK--RGLAMVV 96
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPHMKVEDNVAFGL---RAQKQPRGLIAER-VTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMGRtphRSRFDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490252226 173 DEPLSALDA--QIRhnMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:PRK09536 164 DEPTASLDInhQVR--TLELVRRLVDD--GKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-269 |
1.10e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 109.71 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 28 YHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTdvtQLPPYKRGLAMVVQNYA------- 100
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYSKRGLLALRQQVAtvfqdpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 101 --LFpHMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGmadyATRYPHQ----LSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:PRK13638 88 qqIF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD----AQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 175 PLSALDAQIRHNMVEEIARLHRELPELTIlyVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHyppnrfSAEFLGRAN 254
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVII--SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA------CTEAMEQAG 234
|
250
....*....|....*
gi 490252226 255 ILQATALKDSPEPGL 269
Cdd:PRK13638 235 LTQPWLVKLHTQLGL 249
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-266 |
1.88e-27 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 109.20 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 16 TSGITLDSLRVSY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQlpPYKRGL-A 93
Cdd:PRK15056 4 QAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ--ALQKNLvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 MVVQNYAL---FPHMkVEDNVAFGLRAQ----KQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVR 166
Cdd:PRK15056 82 YVPQSEEVdwsFPVL-VEDVVMMGRYGHmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 167 PRVLLLDEPLSALDAQIRhnmvEEIARLHRELPE--LTILYVTHDQTEALTLADKIgIMKDGSLIAHGETHelyhyppNR 244
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTE----ARIISLLRELRDegKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTE-------TT 228
|
250 260
....*....|....*....|....
gi 490252226 245 FSAEFLGRA--NILQATALKDSPE 266
Cdd:PRK15056 229 FTAENLELAfsGVLRHVALNGSEE 252
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-237 |
2.15e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 112.84 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 3 MKTTVTSSPSLAGTSGItldslRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDV 82
Cdd:PRK15439 1 MQTSDTTAPPLLCARSI-----SKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 83 TQLPP---YKRGLAMVVQNYALFPHMKVEDNVAFGLRAQKQPrgliAERVTEALKIVGMADYATRYPHQLSGGQQQRVAI 159
Cdd:PRK15439 76 ARLTPakaHQLGIYLVPQEPLLFPNLSVKENILFGLPKRQAS----MQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 160 ARAIAVRPRVLLLDEPLSALDAQirhnmveEIARLHRELPELT-----ILYVTHDQTEALTLADKIGIMKDGSLIAHGET 234
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLTPA-------ETERLFSRIRELLaqgvgIVFISHKLPEIRQLADRISVMRDGTIALSGKT 224
|
...
gi 490252226 235 HEL 237
Cdd:PRK15439 225 ADL 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-238 |
2.44e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 109.06 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 18 GITLDSLRVSYHGNV-----VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT------QLP 86
Cdd:PRK13649 2 GINLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 87 PYKRGLAMVVQnyalFPHMK-----VEDNVAFGlraqKQPRGLI---AERVT-EALKIVGMA-DYATRYPHQLSGGQQQR 156
Cdd:PRK13649 82 QIRKKVGLVFQ----FPESQlfeetVLKDVAFG----PQNFGVSqeeAEALArEKLALVGISeSLFEKNPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 157 VAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHE 236
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS--GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKD 231
|
..
gi 490252226 237 LY 238
Cdd:PRK13649 232 IF 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-237 |
2.53e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.43 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 6 TVTSSPSLAGTSGITLDSLRV-SYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQ 84
Cdd:COG3845 245 RVEKAPAEPGEVVLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 85 LPPYKR---GLAMVV---QNYALFPHMKVEDNVAFGL--RAQKQPRGLI----AERVTEALkivgMADYATRYPH----- 147
Cdd:COG3845 325 LSPRERrrlGVAYIPedrLGRGLVPDMSVAENLILGRyrRPPFSRGGFLdrkaIRAFAEEL----IEEFDVRTPGpdtpa 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 148 -QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDaqirhnmVEEIARLHRELPEL-----TILYVTHDQTEALTLADKIG 221
Cdd:COG3845 401 rSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD-------VGAIEFIHQRLLELrdagaAVLLISEDLDEILALSDRIA 473
|
250
....*....|....*.
gi 490252226 222 IMKDGSLIAHGETHEL 237
Cdd:COG3845 474 VMYEGRIVGEVPAAEA 489
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
30-197 |
3.47e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 106.50 E-value: 3.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTqLPPYKRGLAMVVQNYALFPHMKVED 109
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID-DPDVAEACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 110 NVAFGLRAQKQPRGLIAervtEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRhNMVE 189
Cdd:PRK13539 93 NLEFWAAFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV-ALFA 167
|
....*...
gi 490252226 190 EIARLHRE 197
Cdd:PRK13539 168 ELIRAHLA 175
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-245 |
3.75e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.18 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFV---QPAGGRI-LIGDTdVTQLPPYKRGL-- 92
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIeLLGRT-VQREGRLARDIrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 93 -----AMVVQNYALFPHMKVEDNVAFGL---------------RAQKQprgliaeRVTEALKIVGMADYATRYPHQLSGG 152
Cdd:PRK09984 84 srantGYIFQQFNLVNRLSVLENVLIGAlgstpfwrtcfswftREQKQ-------RALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 153 QQQRVAIARAIAVRPRVLLLDEPLSALDAQiRHNMVEEIARLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPE-SARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
250
....*....|...
gi 490252226 233 ETHelyHYPPNRF 245
Cdd:PRK09984 236 SSQ---QFDNERF 245
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
37-239 |
4.54e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 108.67 E-value: 4.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 37 LSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT------QLPPYKRGLAMVVQ--NYALFPHMKVE 108
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQfpESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 109 DnVAFGLRAQKQPRGLIAERVTEALKIVGMA-DYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNM 187
Cdd:PRK13643 105 D-VAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490252226 188 VEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYH 239
Cdd:PRK13643 184 MQLFESIHQS--GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
37-241 |
5.64e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 109.06 E-value: 5.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 37 LSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAG----GRILIGDTDVTQLPPYKR------GLAMVVQN--YALFPH 104
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 105 MKVEDNVAFGLRA-QKQPRGLIAERVTEALKIVGMADYATR---YPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK11022 106 YTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490252226 181 AQIRHNMVEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:PRK11022 186 VTIQAQIIELLLELQQK-ENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
32-238 |
7.06e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 108.78 E-value: 7.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGD----------TDVTQLPPYK--------RGLA 93
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhELITNPYSKKiknfkelrRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 MVVQ--NYALFPHMkVEDNVAFGLRAQKQPRGLIAERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAVRPRVL 170
Cdd:PRK13631 120 MVFQfpEYQLFKDT-IEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 171 LLDEPLSALDAQIRHNMVEEIarLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELY 238
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLI--LDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
11-236 |
1.09e-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: 111.45 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 11 PSLAGTSG-ITLDSLRVSYHGN-VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP- 87
Cdd:COG5265 349 PPLVVGGGeVRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQa 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 88 -YKRGLAMVVQNYALFpHMKVEDNVAFGlRAqkqprGLIAERVTEALKIVGMADYATRYPHQ-----------LSGGQQQ 155
Cdd:COG5265 429 sLRAAIGIVPQDTVLF-NDTIAYNIAYG-RP-----DASEEEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQ 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 156 RVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELPELTILY----VTHdqtealtlADKIGIMKDGSLIAH 231
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHrlstIVD--------ADEILVLEAGRIVER 573
|
....*
gi 490252226 232 GeTHE 236
Cdd:COG5265 574 G-THA 577
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-237 |
1.67e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.99 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 7 VTSSPSLAGTSGITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDV-TQL 85
Cdd:PRK13536 30 KASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 86 PPYKRGLAMVVQNYALFPHMKVEDNVA-----FGLRAQKqprglIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIA 160
Cdd:PRK13536 110 RLARARIGVVPQFDNLDLEFTVRENLLvfgryFGMSTRE-----IEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 161 RAIAVRPRVLLLDEPLSALDAQIRHNMVEeiaRLHRELPE-LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWE---RLRSLLARgKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-232 |
2.03e-26 |
|
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: 104.53 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 24 LRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGF--VQPAGGRILIGDTDVTQLPPYKR---GLAMVVQN 98
Cdd:cd03217 6 LHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERarlGIFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVED-----NVAFglraqkqprgliaervtealkivgmadyatryphqlSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:cd03217 86 PPEIPGVKNADflryvNEGF------------------------------------SGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 174 EPLSALDAQIRHNMVEEIARLHRelPELTILYVTHDQTEALTL-ADKIGIMKDGSLIAHG 232
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLRE--EGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
19-241 |
1.22e-25 |
|
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: 103.76 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILI-----GDTDVTQLPPYKRGLA 93
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 MVVQnYALfphmkVEDNVAFGLRAQKQPRGLIAERvteaLKIVGMADY-----------------ATRY---PHQLSGGQ 153
Cdd:TIGR02323 84 MRTE-WGF-----VHQNPRDGLRMRVSAGANIGER----LMAIGARHYgnirataqdwleeveidPTRIddlPRAFSGGM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 154 QQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGE 233
Cdd:TIGR02323 154 QQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDL-GLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGL 232
|
....*...
gi 490252226 234 THELYHYP 241
Cdd:TIGR02323 233 TDQVLDDP 240
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
33-213 |
1.23e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 102.93 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRG------LAMVVQNYALFPHMK 106
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 107 VEDNVAFG--LRAQ--KQPRgliaERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:PRK10584 105 ALENVELPalLRGEssRQSR----NGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190
....*....|....*....|....*....|.
gi 490252226 183 IRHNMVEEIARLHRELPELTILyVTHDQTEA 213
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLIL-VTHDLQLA 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
33-250 |
1.60e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 107.48 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKT----TVLRAIAG--FVQPAGGRILIGDTDVTQLPPYKRGL-----AMVVQN--Y 99
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppVVYPSGDIRFHGESLLHASEQTLRGVrgnkiAMIFQEpmV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 100 ALFPHMKVEDNVAFGLRAQKQPRGLIAE-RVTEALKIVGMADYATR---YPHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:PRK15134 104 SLNPLHTLEKQLYEVLSLHRGMRREAARgEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEP 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 176 LSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFL 250
Cdd:PRK15134 184 TTALDVSVQAQILQLLRELQQEL-NMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
34-267 |
1.65e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 108.02 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGR---------------ILIGDTDVTQLPpYKRG--LAMVV 96
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdkmllrrrsrqvIELSEQSAAQMR-HVRGadMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QN--YALFPHMKVEDNVAFGLR----AQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVL 170
Cdd:PRK10261 111 QEpmTSLNPVFTVGEQIAESIRlhqgASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 171 LLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSAEFL 250
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEM-SMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALL 269
|
250
....*....|....*..
gi 490252226 251 grANILQATALKDSPEP 267
Cdd:PRK10261 270 --AAVPQLGAMKGLDYP 284
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-237 |
2.19e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 103.53 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 22 DSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYK--RGLAMVVQNY 99
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 100 ALFPHMKVEDNVAFGlRAQKQP-----RGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDE 174
Cdd:PRK10253 91 TTPGDITVQELVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490252226 175 PLSALDAQIRHNMVEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNRE-KGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
25-229 |
2.19e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 102.65 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 25 RVSYH-GNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP---YKRGLAMVVQNY 99
Cdd:PRK11614 10 KVSAHyGKIqALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakiMREAVAIVPEGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 100 ALFPHMKVEDNVA----FGLRAQKQPRgliAERVTEALKivGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:PRK11614 90 RVFSRMTVEENLAmggfFAERDQFQER---IKWVYELFP--RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490252226 176 LSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLI 229
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQ--GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
34-249 |
2.71e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.76 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT------QLPPYKRGLAMVVQ--NYALFPHM 105
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 106 KVEDnVAFGLR----AQKQPRgliaERVTEALKIVGMA-DYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK13641 103 VLKD-VEFGPKnfgfSEDEAK----EKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 181 AQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELY--------HY----PPNRFSAE 248
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA--GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFsdkewlkkHYldepATSRFASK 255
|
.
gi 490252226 249 F 249
Cdd:PRK13641 256 L 256
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-237 |
2.73e-25 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 103.37 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAG----FVQPAG----GRILIGDTDVTQLPPYKR 90
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRGarvtGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 91 GLAMVV---QNYALFPhMKVEDNVAFGLRAQKQPRGLIAER----VTEALKIVGMADYATRYPHQLSGGQQQRVAIARAI 163
Cdd:PRK13547 82 ARLRAVlpqAAQPAFA-FSAREIVLLGRYPHARRAGALTHRdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 164 A---------VRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGET 234
Cdd:PRK13547 161 AqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDW-NLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
...
gi 490252226 235 HEL 237
Cdd:PRK13547 240 ADV 242
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-182 |
2.94e-25 |
|
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: 101.42 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 22 DSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILI-GDTDVTQLPPYKRGLAMVVQNYA 100
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnGGPLDFQRDSIARGLLYLGHAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 101 LFPHMKVEDNVAFGLRAQKQprgliaERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:cd03231 84 IKTTLSVLENLRFWHADHSD------EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
..
gi 490252226 181 AQ 182
Cdd:cd03231 158 KA 159
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-234 |
4.52e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 102.31 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 22 DSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAmvvQNYAL 101
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEA---ERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 102 fphMK-----VEDNVAFGLRAQKQPRGLIAERvteaLKIVGMADY------ATRY--------------PHQLSGGQQQR 156
Cdd:PRK11701 87 ---LRtewgfVHQHPRDGLRMQVSAGGNIGER----LMAVGARHYgdiratAGDWlerveidaariddlPTTFSGGMQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 157 VAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGET 234
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVREL-GLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLT 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-231 |
4.99e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 105.76 E-value: 4.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 21 LDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTqlppYKR-------GLA 93
Cdd:PRK11288 7 FDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR----FASttaalaaGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 MVVQNYALFPHMKVEDNVAFGLRAQKQ---PRGLIAERVTEALKIVGMA-DYATRYPHqLSGGQQQRVAIARAIAVRPRV 169
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLYLGQLPHKGgivNRRLLNYEAREQLEHLGVDiDPDTPLKY-LSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 170 LLLDEPLSALDAQirhnmveEIARLHRELPEL-----TILYVTHDQTEALTLADKIGIMKDGSLIAH 231
Cdd:PRK11288 162 IAFDEPTSSLSAR-------EIEQLFRVIRELraegrVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
10-241 |
9.46e-25 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 101.31 E-value: 9.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 10 SPSLAGTSGITLDSLRVSYHGnvvlkpLSLTIEPGEVLALIGPSGSGKTTVLRAIAGfVQPAG-----GRILIGDTDVTQ 84
Cdd:PRK10418 1 MPQQIELRNIALQAAQPLVHG------VSLTLQRGRVLALVGGSGSGKSLTCAAALG-ILPAGvrqtaGRVLLDGKPVAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 85 LPPYKRGLAMVVQN--YALFPHMKVEDNVAFGLRAQKQPRGliAERVTEALKIVGMADYAT---RYPHQLSGGQQQRVAI 159
Cdd:PRK10418 74 CALRGRKIATIMQNprSAFNPLHTMHTHARETCLALGKPAD--DATLTAALEAVGLENAARvlkLYPFEMSGGMLQRMMI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 160 ARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYH 239
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQK-RALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
..
gi 490252226 240 YP 241
Cdd:PRK10418 231 AP 232
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-246 |
3.36e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 101.34 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 1 MLMKTTVTSSPSLagtsgiTLDSLRVSYH---GNVV-LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAG---G 73
Cdd:PRK09473 1 TVPLAQQQADALL------DVKDLRVTFStpdGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 74 RILIGDTDVTQLPPYK------RGLAMVVQN--YALFPHMKVEDNVAFGLRAQK----------QPRGLIAERVTEALKI 135
Cdd:PRK09473 75 SATFNGREILNLPEKElnklraEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKgmskaeafeeSVRMLDAVKMPEARKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 136 VGMadyatrYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALT 215
Cdd:PRK09473 155 MKM------YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREF-NTAIIMITHDLGVVAG 227
|
250 260 270
....*....|....*....|....*....|.
gi 490252226 216 LADKIGIMKDGSLIAHGETHELYHYPPNRFS 246
Cdd:PRK09473 228 ICDKVLVMYAGRTMEYGNARDVFYQPSHPYS 258
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-229 |
3.89e-24 |
|
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: 98.72 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSY--HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYK--RGLAM 94
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQnyalfphmkveDNVAFG--LRAQKQPRGLIA-ERVTEALKIVGMADYATRYPHQL-----------SGGQQQRVAIA 160
Cdd:cd03244 83 IPQ-----------DPVLFSgtIRSNLDPFGEYSdEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 161 RAIAVRPRVLLLDEPLSALDAQIRHNMVEEIarlHRELPELTILYVTHdQTEALTLADKIGIMKDGSLI 229
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTI---REAFKDCTVLTIAH-RLDTIIDSDRILVLDKGRVV 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-232 |
4.49e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 98.94 E-value: 4.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 14 AGTSGITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDtdvtqLPPYKR--- 90
Cdd:cd03267 17 PGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVPWKRrkk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 91 -----GLAM-----------VVQNYALFPHMKVEDNVAFGLRaqkqprgliAERVTEALKIVGMADYATRyphQLSGGQQ 154
Cdd:cd03267 92 flrriGVVFgqktqlwwdlpVIDSFYLLAAIYDLPPARFKKR---------LDELSELLDLEELLDTPVR---QLSLGQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 155 QRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRE-RGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
33-232 |
6.86e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 97.99 E-value: 6.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRIlIGDTDVTQLppykrgLAMvvqNYALFPHMKVEDNVA 112
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-TVRGRVSSL------LGL---GGGFNPELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 113 FGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIA 192
Cdd:cd03220 107 LNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLR 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490252226 193 RLHRELPelTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03220 187 ELLKQGK--TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-237 |
8.82e-24 |
|
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: 102.90 E-value: 8.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPY--KRGLAMV 95
Cdd:TIGR01193 474 IVINDVSYSYgYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNYALFPHmKVEDNVAFGLRaqkqpRGLIAERVTEALKIVGMAD--------YATRYPHQ---LSGGQQQRVAIARAIA 164
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAK-----ENVSQDEIWAACEIAEIKDdienmplgYQTELSEEgssISGGQKQRIALARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490252226 165 VRPRVLLLDEPLSALDAQIRHNMVEEIARLHrelpELTILYVTHDQTEAlTLADKIGIMKDGSLIAHGETHEL 237
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQ----DKTIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
29-241 |
1.05e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 99.98 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 29 HGNV-VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQP----AGGRILIGDTDVTQLPPYKR------GLAMVVQ 97
Cdd:COG4170 17 QGRVkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 N--YALFPHMKVEDNVAFGLRAQK------QPRGLIAERVTEALKIVGMADYA---TRYPHQLSGGQQQRVAIARAIAVR 166
Cdd:COG4170 97 EpsSCLDPSAKIGDQLIEAIPSWTfkgkwwQRFKWRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 167 PRVLLLDEPLSALDAQIRHNMVEEIARLHReLPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQ-LQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
34-236 |
1.50e-23 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 97.70 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGfVQPAGGRILIGDTDVTQLPPYK--RGLAMVVQNYALFPHMKVEDNV 111
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAElaRHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 112 AFGLRAQKQPRGLIA--ERVTEALKIvgmADYATRYPHQLSGGQQQRVAIARAI-----AVRP--RVLLLDEPLSALD-A 181
Cdd:PRK03695 91 TLHQPDKTRTEAVASalNEVAEALGL---DDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDvA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 182 QirhnmveEIA--RLHRELPEL--TILYVTHDQTEALTLADKIGIMKDGSLIAHGETHE 236
Cdd:PRK03695 168 Q-------QAAldRLLSELCQQgiAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
37-182 |
1.57e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 96.80 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 37 LSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP-YKRGLAMVVQNYALFPHMKVEDNVAFGL 115
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeYHQDLLYLGHQPGIKTELTALENLRFYQ 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 116 RAQKQPRgliAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:PRK13538 100 RLHGPGD---DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
19-226 |
1.61e-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: 94.82 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTdvtqlppykrglamvvqn 98
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 yalfphmkvednvafglraqkqprgliaervteaLKIVgmadyatrYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:cd03221 63 ----------------------------------VKIG--------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490252226 179 LDaqirhnmVEEIARLHRELPEL--TILYVTHDQTEALTLADKIGIMKDG 226
Cdd:cd03221 101 LD-------LESIEALEEALKEYpgTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-211 |
3.23e-23 |
|
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: 94.53 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRV-SYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIgdtdvtqlpPYKRGLAMVVQ 97
Cdd:cd03223 1 IELENLSLaTPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 NyalfPHMkvednvafglraqkqPRGLIAERVTealkivgmadyatrYP--HQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:cd03223 72 R----PYL---------------PLGTLREQLI--------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190
....*....|....*....|....*....|....*...
gi 490252226 176 LSALDAQirhnmVEeiARLHRELPEL--TILYVTHDQT 211
Cdd:cd03223 119 TSALDEE-----SE--DRLYQLLKELgiTVISVGHRPS 149
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-232 |
3.84e-23 |
|
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: 94.69 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN--VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVV 96
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPHMKVEDNVafGLRaqkqprgliaervtealkivgmadyatryphqLSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:cd03247 81 NQRPYLFDTTLRNNL--GRR--------------------------------FSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 177 SALDAQIRHNMVEEIArlhRELPELTILYVTHDQTeALTLADKIGIMKDGSLIAHG 232
Cdd:cd03247 127 VGLDPITERQLLSLIF---EVLKDKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-237 |
1.35e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 98.70 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP---YKRGLAMV 95
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNYALFPHMKVEDNVAFGLRAQKQPRGL-------IAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPR 168
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKVCGVniidwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 169 VLLLDEPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKE--GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
11-240 |
3.26e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 97.86 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 11 PSLAGTSGITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT--QLPPY 88
Cdd:PRK10789 308 PEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklQLDSW 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 89 KRGLAMVVQNYALFPHmKVEDNVAFGLRAQKQprgliaERVTEALKIVGMADYATRYPH-----------QLSGGQQQRV 157
Cdd:PRK10789 388 RSRLAVVSQTPFLFSD-TVANNIALGRPDATQ------QEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRI 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 158 AIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRelpELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK10789 461 SIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE---GRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQL 536
|
250
....*....|...
gi 490252226 238 ----------YHY 240
Cdd:PRK10789 537 aqqsgwyrdmYRY 549
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-209 |
3.39e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 21 LDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRIligdtdvtQLPPYKRgLAMVVQNYA 100
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLR-IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 101 LFPHMKVEDNVAFGLRAQKQprgLIAE-----------------------------------RVTEALKIVGM-ADYATR 144
Cdd:COG0488 72 LDDDLTVLDTVLDGDAELRA---LEAEleeleaklaepdedlerlaelqeefealggweaeaRAEEILSGLGFpEEDLDR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 145 YPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAqirhnmvEEIARLHRELPEL--TILYVTHD 209
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-------ESIEWLEEFLKNYpgTVLVVSHD 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-237 |
3.83e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 97.59 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGN--VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP--PYKRGLAM 94
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeaALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFPHmKVEDNVAFglrAQKQPRGliaERVTEALKIVGMADYATRYP----------HQLSGGQQQRVAIARAIA 164
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNLLL---AAPNASD---EALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490252226 165 VRPRVLLLDEPLSALDAQIRHnmveEIARLHRELPE-LTILYVTHDQTeALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETER----QILELLAEHAQnKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
32-236 |
4.93e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.61 E-value: 4.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLppykrGLAMVVQnyalfPHMKVEDNV 111
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL-----ELGAGFH-----PELTGRENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 112 AFGLRAQKQPRGLIAERVTEalkIV---GMADYATRyP-HQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNM 187
Cdd:COG1134 110 YLNGRLLGLSRKEIDEKFDE---IVefaELGDFIDQ-PvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKC 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490252226 188 VEEIARLHRELPelTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHE 236
Cdd:COG1134 186 LARIRELRESGR--TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-229 |
2.47e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTdvtqlppykrglamVVQN 98
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET--------------VKIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 Y------ALFPHMKVEDNVAfglraqkqpRGLIAERVTEALKIVGM----ADYATRYPHQLSGGQQQRVAIARAIAVRPR 168
Cdd:COG0488 382 YfdqhqeELDPDKTVLDELR---------DGAPGGTEQEVRGYLGRflfsGDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 169 VLLLDEPLSALDAQIRhNMVEEIarlhrelpeL-----TILYVTHDQtEAL-TLADKIGIMKDGSLI 229
Cdd:COG0488 453 VLLLDEPTNHLDIETL-EALEEA---------LddfpgTVLLVSHDR-YFLdRVATRILEFEDGGVR 508
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-232 |
4.49e-21 |
|
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: 90.16 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNV--VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP--PYKRGLAM 94
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFphmkvednvAFGLRAQKQPRGLIAER-VTEALKIVGMADyatryphQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:cd03369 87 IPQDPTLF---------SGTIRSNLDPFDEYSDEeIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 174 EPLSALDAQIRHNMVEEIarlHRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03369 151 EATASIDYATDALIQKTI---REEFTNSTILTIAH-RLRTIIDYDKILVMDAGEVKEYD 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-237 |
6.35e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 94.10 E-value: 6.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTT---VLRAIAGFvQPAGGRIL-------------IGDTDV 82
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVlmhVLRGMDQY-EPTSGRIIyhvalcekcgyveRPSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 83 TQLP------------------PYKRGLA-----MVVQNYALFPHMKVEDNVafgLRAQKQPRGLIAERVTEALKIVGMA 139
Cdd:TIGR03269 80 EPCPvcggtlepeevdfwnlsdKLRRRIRkriaiMLQRTFALYGDDTVLDNV---LEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 140 DYATRYPH---QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD---AQIRHNMVEEIARLHrelpELTILYVTHdQTEA 213
Cdd:TIGR03269 157 QLSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHNALEEAVKAS----GISMVLTSH-WPEV 231
|
250 260
....*....|....*....|....*
gi 490252226 214 LT-LADKIGIMKDGSLIAHGETHEL 237
Cdd:TIGR03269 232 IEdLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-194 |
8.37e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 93.79 E-value: 8.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAG--GRILIGDTDVTQlpPYKRGLAMVVQNYALFPHMKVEDN 110
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK--QILKRTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAFG--LR----AQKQPRGLIAERVTEALKIVGMAD--YATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQ 182
Cdd:PLN03211 161 LVFCslLRlpksLTKQEKILVAESVISELGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170
....*....|..
gi 490252226 183 IRHNMVEEIARL 194
Cdd:PLN03211 241 AAYRLVLTLGSL 252
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
38-230 |
5.18e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.14 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPGEVLALIGPSGSGKTTVLRAIAGfVQPAG---GRIL----------IGDTDvtqlppyKRGLAMVVQNYALFPH 104
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIfegeelqasnIRDTE-------RAGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 105 MKVEDNVAFGlrAQKQPRGLIA-----ERVTEALKIVGMA-DYATRYPHqLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:PRK13549 97 LSVLENIFLG--NEITPGGIMDydamyLRAQKLLAQLKLDiNPATPVGN-LGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 179 LDAQirhnmveEIARLHRELPEL-----TILYVTHDQTEALTLADKIGIMKDGSLIA 230
Cdd:PRK13549 174 LTES-------ETAVLLDIIRDLkahgiACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
37-237 |
5.95e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.18 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 37 LSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQ--LPPYKRGLAMVVQNYALFpHMKVEDNVAFG 114
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvtRASLRRNIAVVFQDAGLF-NRSIEDNIRVG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 115 lraqkQPRGLIAErVTEALKIVGMADYATRYPH-----------QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDaqi 183
Cdd:PRK13657 433 -----RPDATDEE-MRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILDEATSALD--- 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490252226 184 rhnmVEEIARLHRELPEltilyVTHDQTE---ALTL-----ADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK13657 504 ----VETEAKVKAALDE-----LMKGRTTfiiAHRLstvrnADRILVFDNGRVVESGSFDEL 556
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
34-237 |
6.93e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.85 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVT--QLPPYKRGLAMVVQNYALFpHMKVEDNV 111
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVALVSQNVHLF-NDTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 112 AFGlRAQKQPRgliaERVTEALKIVGMADYATRYPH-----------QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK11176 438 AYA-RTEQYSR----EQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490252226 181 AQirhnmvEEIArLHRELPEL----TILYVTHdQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK11176 513 TE------SERA-IQAALDELqknrTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-232 |
8.13e-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: 91.61 E-value: 8.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 37 LSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDV-TQLPPYKRGLAMVVQNYALFPHMKVEDNVAF-- 113
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHILFya 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 114 GLRAQKQPRgliAERVTEA-LKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIA 192
Cdd:TIGR01257 1029 QLKGRSWEE---AQLEMEAmLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490252226 193 RLHRelpELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:TIGR01257 1106 KYRS---GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
34-250 |
1.43e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.11 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAgFVQPAG----GRILIGDTDVTqLPPYKRGLAMVVQNYALFPHMKVED 109
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGvkgsGSVLLNGMPID-AKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 110 NVAFG--LR-----AQKQPRgliaERVTEALKIVGMADYA-TR--YPHQ---LSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:TIGR00955 119 HLMFQahLRmprrvTKKEKR----ERVDEVLQALGLRKCAnTRigVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 177 SALDAQIRHNMVEEIARLHRElpELTILYVTHDQT-EALTLADKIGIMKDGSLIAHGETHEL--------YHYPPNRFSA 247
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQK--GKTIICTIHQPSsELFELFDKIILMAEGRVAYLGSPDQAvpffsdlgHPCPENYNPA 272
|
...
gi 490252226 248 EFL 250
Cdd:TIGR00955 273 DFY 275
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
33-210 |
1.83e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.78 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFV--QPAGGRILIGDTDVTQLPPykrglamvvqnyalfphmkVEDN 110
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREAS-------------------LIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAfglraqkqPRGLIAErVTEALKIVGMADYAT--RYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMV 188
Cdd:COG2401 106 IG--------RKGDFKD-AVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180
....*....|....*....|..
gi 490252226 189 EEIARLHRELpELTILYVTHDQ 210
Cdd:COG2401 177 RNLQKLARRA-GITLVVATHHY 197
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
34-232 |
4.17e-19 |
|
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: 84.24 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAG---GRILIGDTDVTQ-LPPYKRGLAMVVQNYALFPHMKVED 109
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEfAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 110 NVAFGLRAQkqprgliaervtealkivgmadyATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVE 189
Cdd:cd03233 103 TLDFALRCK-----------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490252226 190 EIARLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHG 232
Cdd:cd03233 160 CIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
34-230 |
7.62e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 87.57 E-value: 7.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGfVQPAG---GRIL----------IGDTDvtqlppyKRGLAMVVQNYA 100
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYwsgsplkasnIRDTE-------RAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 101 LFPHMKVEDNVAFG----LRAQKQPRGLIAERVTEALKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:TIGR02633 89 LVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 176 LSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIA 230
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKAH--GVACVYISHKLNEVKAVCDTICVIRDGQHVA 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
24-232 |
1.04e-18 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 84.31 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 24 LRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGfvQPA----GGRILIGDTDVTQLPPYKR---GLAMVV 96
Cdd:CHL00131 13 LHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERahlGIFLAF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPHMKVEDNVAFGLRAQKQPRGL-------IAERVTEALKIVGM-ADYATRYPHQ-LSGGQQQRVAIARAIAVRP 167
Cdd:CHL00131 91 QYPIEIPGVSNADFLRLAYNSKRKFQGLpeldpleFLEIINEKLKLVGMdPSFLSRNVNEgFSGGEKKRNEILQMALLDS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 168 RVLLLDEPLSALDAQIRHNMVEEIARLHRelPELTILYVTHDQtEAL--TLADKIGIMKDGSLIAHG 232
Cdd:CHL00131 171 ELAILDETDSGLDIDALKIIAEGINKLMT--SENSIILITHYQ-RLLdyIKPDYVHVMQNGKIIKTG 234
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
5-250 |
1.26e-18 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 87.86 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 5 TTVTSSPSLAGTSGITLdsLRVSYHGNVV--LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIA----GFVQPAGGRILIG 78
Cdd:TIGR00956 48 PTFPNALLKILTRGFRK--LKKFRDTKTFdiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 79 DTDVTQLPPYKRG-LAMVVQNYALFPHMKVEDNVAFGLR---AQKQPRGLIAERVTEALKIVGMADYATRYPHQ------ 148
Cdd:TIGR00956 126 GITPEEIKKHYRGdVVYNAETDVHFPHLTVGETLDFAARcktPQNRPDGVSREEYAKHIADVYMATYGLSHTRNtkvgnd 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 149 ----LSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMV---EEIARLHRELPELTILYVTHDqteALTLADKIG 221
Cdd:TIGR00956 206 fvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIralKTSANILDTTPLVAIYQCSQD---AYELFDKVI 282
|
250 260 270
....*....|....*....|....*....|....*..
gi 490252226 222 IMKDGSLIAHGETHELYHY--------PPNRFSAEFL 250
Cdd:TIGR00956 283 VLYEGYQIYFGPADKAKQYfekmgfkcPDRQTTADFL 319
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-180 |
2.24e-18 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 82.59 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 3 MKTTVTSSPSLAGTSGITLdslrvSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIgDTDV 82
Cdd:PRK13543 1 MIEPLHTAPPLLAAHALAF-----SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 83 TQLPPYKRGLAMVVQNYALFPHMKVEDNVAF-----GLRAQKQPrgliaervTEALKIVGMADYATRYPHQLSGGQQQRV 157
Cdd:PRK13543 75 ATRGDRSRFMAYLGHLPGLKADLSTLENLHFlcglhGRRAKQMP--------GSALAIVGLAGYEDTLVRQLSAGQKKRL 146
|
170 180
....*....|....*....|...
gi 490252226 158 AIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK13543 147 ALARLWLSPAPLWLLDEPYANLD 169
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-209 |
5.62e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.47 E-value: 5.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRIligdtdvtQLPPYKRgLAMVVQN 98
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR-IGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVEDNVAFGLRAqkqprGLIAERVTEALKIVgMADYATRYPHQ-LSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:PRK09544 76 LYLDTTLPLTVNRFLRLRP-----GTKKEDILPALKRV-QAGHLIDAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190
....*....|....*....|....*....|..
gi 490252226 178 ALDAQIRHNMVEEIARLHRELpELTILYVTHD 209
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRREL-DCAVLMVSHD 180
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
37-241 |
1.28e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 82.54 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 37 LSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQP----AGGRILIGDTDVTQLPPYKR------GLAMVVQ--NYALFPH 104
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERrklvghNVSMIFQepQSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 105 MKVEDNVAFGLRAQK------QPRGLIAERVTEALKIVGMADYA---TRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:PRK15093 106 ERVGRQLMQNIPGWTykgrwwQRFGWRKRRAIELLHRVGIKDHKdamRSFPYELTEGECQKVMIAIALANQPRLLIADEP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 176 LSALDAQIRHNMVEEIARLHRElPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELY---HYP 241
Cdd:PRK15093 186 TNAMEPTTQAQIFRLLTRLNQN-NNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVttpHHP 253
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
37-228 |
1.47e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 37 LSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKRGLAMVV------QNYALFPHMKVEDN 110
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 V--------AFGLRAQKQPRglIAERVTEALKI-VGMADYATRyphQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDA 181
Cdd:PRK15439 362 VcalthnrrGFWIKPARENA--VLERYRRALNIkFNHAEQAAR---TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490252226 182 QIRHnmveEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:PRK15439 437 SARN----DIYQLIRSIAAqnVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
27-251 |
1.63e-17 |
|
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: 81.83 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 27 SYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRIligdtdvtqlpPYKRGLAMVVQNYALFPHmK 106
Cdd:cd03291 46 CLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHSGRISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 107 VEDNVAFGLRAQKQprgliaeRVTEALKIVGMADYATRYPHQ-----------LSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:cd03291 114 IKENIIFGVSYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 176 LSALDAQIRHNMVEEIarLHRELPELTILYVThDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNrFSAEFLG 251
Cdd:cd03291 187 FGYLDVFTEKEIFESC--VCKLMANKTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSLRPD-FSSKLMG 258
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
27-251 |
1.83e-17 |
|
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: 84.19 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 27 SYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRIligdtdvtqlpPYKRGLAMVVQNYALFPHMk 106
Cdd:TIGR01271 435 SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KHSGRISFSPQTSWIMPGT- 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 107 VEDNVAFGLRAQKQprgliaeRVTEALKIVGMADYATRYPHQ-----------LSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:TIGR01271 503 IKDNIIFGLSYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 176 LSALDAQIRHNMVEEIarLHRELPELTILYVThDQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNrFSAEFLG 251
Cdd:TIGR01271 576 FTHLDVVTEKEIFESC--LCKLMSNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPD-FSSLLLG 647
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
38-248 |
1.94e-17 |
|
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: 80.92 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPG-----EVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPY-KRGLAMVVQNyalFPHMKVEDnv 111
Cdd:cd03237 14 TLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYiKADYEGTVRD---LLSSITKD-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 112 aFGLRAQKQprgliaervTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRhNMVEEI 191
Cdd:cd03237 89 -FYTHPYFK---------TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR-LMASKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490252226 192 ARLHRELPELTILYVTHDQTEALTLADKIgIMKDGSLIAHGETHelyhyPP-------NRFSAE 248
Cdd:cd03237 158 IRRFAENNEKTAFVVEHDIIMIDYLADRL-IVFEGEPSVNGVAN-----PPqslrsgmNRFLKN 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
34-248 |
2.68e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 81.67 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDvtqlpPYKR--------GLAM----------- 94
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKRrkefarriGVVFgqrsqlwwdlp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 95 VVQNYALFPHM-KVEDNVAfglraqkqprgliAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:COG4586 113 AIDSFRLLKAIyRIPDAEY-------------KKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 174 EPLSALDAQIRHNMVEEIARLHRELpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELyhypPNRFSAE 248
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRER-GTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL----KERFGPY 249
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
35-228 |
3.20e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.91 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 35 KPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPY---KRGLAMVVQNY---ALFPHMKVE 108
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdavKKGMAYITESRrdnGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 109 DNVAFgLRAQKQPR-----GLI----------AERVTEALKIVGMADYATryphQLSGGQQQRVAIARAIAVRPRVLLLD 173
Cdd:PRK09700 360 QNMAI-SRSLKDGGykgamGLFhevdeqrtaeNQRELLALKCHSVNQNIT----ELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 174 EPLSALDAQIRhnmvEEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:PRK09700 435 EPTRGIDVGAK----AEIYKVMRQLADdgKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
36-236 |
6.68e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.88 E-value: 6.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 36 PLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP---YKRGLAMVVQNY---ALFPHMKVED 109
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrdaIRAGIMLCPEDRkaeGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 110 NVAFGLRAQKQPRGLI---------AERVTEALKIvgmadyATRYPHQ----LSGGQQQRVAIARAIAVRPRVLLLDEPL 176
Cdd:PRK11288 351 NINISARRHHLRAGCLinnrweaenADRFIRSLNI------KTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 177 SALDAQIRHnmveEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSL---IAHGETHE 236
Cdd:PRK11288 425 RGIDVGAKH----EIYNVIYELAAqgVAVLFVSSDLPEVLGVADRIVVMREGRIageLAREQATE 485
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
42-223 |
8.50e-17 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 78.95 E-value: 8.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 42 EPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRiLIGDTDVTQLPPYKRGLAMvvQNYalFPHMKvEDNVAFGLRAQ--- 118
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEILDEFRGSEL--QNY--FTKLL-EGDVKVIVKPQyvd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 119 ---KQPRGLIAE------------RVTEALKIVGMADyatRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:cd03236 98 lipKAVKGKVGEllkkkdergkldELVDQLELRHVLD---RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490252226 184 RHNMveeiARLHREL--PELTILYVTHDQTEALTLADKIGIM 223
Cdd:cd03236 175 RLNA----ARLIRELaeDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-236 |
9.96e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.69 E-value: 9.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 16 TSG-ITLDSLRVSY-HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP--PYKRG 91
Cdd:PRK10790 337 QSGrIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 92 LAMVVQNYALFPHmKVEDNVAFGlraqkqpRGLIAERVTEALKIVGMADYATRYP-----------HQLSGGQQQRVAIA 160
Cdd:PRK10790 417 VAMVQQDPVVLAD-TFLANVTLG-------RDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 161 RAIAVRPRVLLLDEPLSALDAQIRhnmvEEIARLHRELPELTILYVTHDQTEALTLADKIGIMKDGSLIAHGeTHE 236
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTE----QAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQG-THQ 559
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-237 |
1.61e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.79 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 23 SLR-VSYH---GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP--YKRGLAMVV 96
Cdd:PRK10522 324 ELRnVTFAyqdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPedYRKLFSAVF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 97 QNYALFPHMkvednvafgLRAQKQPRGliAERVTEALKIVGMADYATRYPH-----QLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:PRK10522 404 TDFHLFDQL---------LGPEGKPAN--PALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 172 LDEPLSALDAQIRHNMVEEIARLHRELPElTILYVTHDQtEALTLADKIGIMKDGSLIA-HGETHEL 237
Cdd:PRK10522 473 LDEWAADQDPHFRREFYQVLLPLLQEMGK-TIFAISHDD-HYFIHADRLLEMRNGQLSElTGEERDA 537
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
34-227 |
3.27e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 76.60 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRI-----LIGDTDVTQLPPYKRGLAMVVQNYALFPHMKVE 108
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 109 DNVAFGLRAQKQPRgliaERVTEALKIVGMADYatrYPH-----------QLSGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:cd03290 97 ENITFGSPFNKQRY----KAVTDACSLQPDIDL---LPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490252226 178 ALDAQIR-HNMVEEIARLHRElPELTILYVTHdQTEALTLADKIGIMKDGS 227
Cdd:cd03290 170 ALDIHLSdHLMQEGILKFLQD-DKRTLVLVTH-KLQYLPHADWIIAMKDGS 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-209 |
6.02e-16 |
|
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: 79.21 E-value: 6.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 20 TLDSLRVSYHGN-VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGdtdvtqlPPYKRGlaMVVQN 98
Cdd:TIGR03719 6 TMNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-------PGIKVG--YLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YALFPHMKVEDNVAFGLRAQKQ--------------PRG----LIAE--RVTEALKIVG---------MADYATRYP--- 146
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVAEIKDaldrfneisakyaePDAdfdkLAAEqaELQEIIDAADawdldsqleIAMDALRCPpwd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 147 ---HQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAqirhnmvEEIARLHRELPEL--TILYVTHD 209
Cdd:TIGR03719 157 advTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA-------ESVAWLERHLQEYpgTVVAVTHD 217
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-180 |
2.38e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.83 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 23 SLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQ-LPPYKRGLAMVVQNYAL 101
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 102 FPHMKVEDNVAFGLRAQKQPRGliaerVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK13540 86 NPYLTLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-237 |
2.76e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.71 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQ--LPPYKRGLAMVVQNYALFphmkvEDN 110
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLF-----SGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAFGLR--AQKQPRGLiaervTEALKIVGMADYATRYPHQL-----------SGGQQQRVAIARAIAVRPRVLLLDEPLS 177
Cdd:PLN03232 1326 VRFNIDpfSEHNDADL-----WEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 178 ALDAQIrHNMVEEIARlhRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PLN03232 1401 SVDVRT-DSLIQRTIR--EEFKSCTMLVIAH-RLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
8-209 |
3.70e-15 |
|
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: 76.76 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 8 TSSPSLAGTSGITLDSLRVSYHG-----NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDV 82
Cdd:COG4615 317 AAPPAPADFQTLELRGVTYRYPGedgdeGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 83 T--QLPPYKRGLAMVVQNYALFPHMkvednvaFGLRAQKQPrgliaERVTEALKIVGMAD--------YATRyphQLSGG 152
Cdd:COG4615 397 TadNREAYRQLFSAVFSDFHLFDRL-------LGLDGEADP-----ARARELLERLELDHkvsvedgrFSTT---DLSQG 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490252226 153 QQQRVAIARAIAV-RPrVLLLDEPLSALDAQIRHNMVEEIarlhreLPEL-----TILYVTHD 209
Cdd:COG4615 462 QRKRLALLVALLEdRP-ILVFDEWAADQDPEFRRVFYTEL------LPELkargkTVIAISHD 517
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
19-180 |
1.35e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 72.52 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGF--VQPAGGRILIGDTDVTQLPPYKR---GLA 93
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRageGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 94 MVVQNYALFPHMKVEDNVAFGLRAQKQPRGL-------IAERVTEALKIVGM-ADYATRYPHQ-LSGGQQQRVAIARAIA 164
Cdd:PRK09580 82 MAFQYPVEIPGVSNQFFLQTALNAVRSYRGQepldrfdFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAV 161
|
170
....*....|....*.
gi 490252226 165 VRPRVLLLDEPLSALD 180
Cdd:PRK09580 162 LEPELCILDESDSGLD 177
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-237 |
1.37e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 75.44 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 37 LSLTIEPGEVLALIGPSGSGKTTVLRaiagfvqpaggrILIGDTDVTQLPPYKRG------LAMVVQNYALFPHMKVEDN 110
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFK------------MLTGDTTVTSGDATVAGksiltnISDVHQNMGYCPQFDAIDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAFG---LRAQKQPRGLIAERVTE----ALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:TIGR01257 2026 LLTGrehLYLYARLRGVPAEEIEKvanwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490252226 184 RHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:TIGR01257 2106 RRMLWNTIVSIIRE--GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
34-242 |
1.74e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.16 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQP-AGGRILIgdtdvtqlppykRG-LAMVVQNYALFpHMKVEDNV 111
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVI------------RGtVAYVPQVSWIF-NATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 112 AFGLRAQkqprgliAERVTEALKIVGMADYATRYPH-----------QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PLN03130 700 LFGSPFD-------PERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490252226 181 AQIRHNMVEEIarLHRELPELTILYVThDQTEALTLADKIGIMKDGSLIAHGETHELYHYPP 242
Cdd:PLN03130 773 AHVGRQVFDKC--IKDELRGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGP 831
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-237 |
3.31e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 27 SYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP---YKRGLAMVVQNYALFP 103
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAGIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 104 HMKVEDNVAFGlRAQKQPRGLI--AERVTEA---LKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:PRK10762 93 QLTIAENIFLG-REFVNRFGRIdwKKMYAEAdklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490252226 179 L-DAQirhnmVEEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK10762 172 LtDTE-----TESLFRVIRELKSqgRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-238 |
8.62e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.09 E-value: 8.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 11 PSLAGTSGITLDSLRVSYHG---NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGgriligDTDVTqlpp 87
Cdd:PLN03232 607 PLQPGAPAISIKNGYFSWDSktsKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE------TSSVV---- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 88 yKRGLAMVVQNYALFPHMKVEDNVAFGLRAQkqprgliAERVTEALKIVGMADYATRYPHQ-----------LSGGQQQR 156
Cdd:PLN03232 677 -IRGSVAYVPQVSWIFNATVRENILFGSDFE-------SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQR 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 157 VAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARlhRELPELTILYVThDQTEALTLADKIGIMKDGSLIAHGETHE 236
Cdd:PLN03232 749 VSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK--DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAE 825
|
..
gi 490252226 237 LY 238
Cdd:PLN03232 826 LS 827
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
38-229 |
9.06e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.13 E-value: 9.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPGEVLALIGPSGSGKTTVLRAIAGfVQPAG---GRIL----------IGDTDvtqlppyKRGLAMVVQNYALFPH 104
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHGsyeGEILfdgevcrfkdIRDSE-------ALGIVIIHQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 105 MKVEDNVAFGLRAQKqpRGLI-----AERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:NF040905 93 LSIAENIFLGNERAK--RGVIdwnetNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490252226 180 DAQIRHNMVEeiarLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLI 229
Cdd:NF040905 171 NEEDSAALLD----LLLELKAqgITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
43-220 |
1.02e-13 |
|
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: 67.78 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 43 PGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDtdvtqlppykrglamvvqnyalfphmkvednvafglraqkqpr 122
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 123 gliAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELPE-- 200
Cdd:smart00382 38 ---GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKse 114
|
170 180
....*....|....*....|..
gi 490252226 201 --LTILYVTHDQTEALTLADKI 220
Cdd:smart00382 115 knLTVILTTNDEKDLGPALLRR 136
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-180 |
1.72e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.50 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVtqlppykrgLAMVVQN 98
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK---------LAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 Y-ALFPHMKVEDNVAFGL------RAQKQPRGLIAE---RVTEALKIVGmadyatryphQLSGGQQQRVAIARAIAVRPR 168
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLdiiklgKREIPSRAYVGRfnfKGSDQQKKVG----------QLSGGERNRVHLAKTLKSGGN 463
|
170
....*....|..
gi 490252226 169 VLLLDEPLSALD 180
Cdd:TIGR03719 464 VLLLDEPTNDLD 475
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
34-264 |
3.13e-13 |
|
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: 71.13 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIgdtdvtqlppyKRGLAMVVQNyALFPHMKVEDNVAF 113
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-----------KGSVAYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 114 GlRAQKQPRgliAERVTEA------LKIVGMADyATRYPHQ---LSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIR 184
Cdd:TIGR00957 722 G-KALNEKY---YQQVLEAcallpdLEILPSGD-RTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 185 HNMVEEIARLHRELPELTILYVTHDQTeALTLADKIGIMKDGSLIAHGETHELYHYppNRFSAEFL-GRANILQATALKD 263
Cdd:TIGR00957 797 KHIFEHVIGPEGVLKNKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLQR--DGAFAEFLrTYAPDEQQGHLED 873
|
.
gi 490252226 264 S 264
Cdd:TIGR00957 874 S 874
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-241 |
3.43e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.96 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIgdtdvtqlppyKRGLAMVVQNyALFPHMKVEDNV 111
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-----------ERSIAYVPQQ-AWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 112 AFgLRAQKQPRGLIAERVTE-----ALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHN 186
Cdd:PTZ00243 742 LF-FDEEDAARLADAVRVSQleadlAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 187 MVEEIARLHreLPELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETHELYHYP 241
Cdd:PTZ00243 821 VVEECFLGA--LAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
31-184 |
3.83e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 67.59 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 31 NVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLP-PYkrgLAMVVQNYALFPHMKVED 109
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPY---CTYIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 110 NVAFGLRAQKQprgliAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIR 184
Cdd:PRK13541 90 NLKFWSEIYNS-----AETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-230 |
6.75e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.76 E-value: 6.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 27 SYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDV---TQLPPYKRGLAMVVQNYALFP 103
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 104 HMKVEDNVAFGLRAQKqprGLIAE-----RVTEA------LKIVGMADYATryphqLSGGQQQRVAIARAIAVRPRVLLL 172
Cdd:PRK10982 87 QRSVMDNMWLGRYPTK---GMFVDqdkmyRDTKAifdeldIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 173 DEPLSALDAQirhnMVEEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIA 230
Cdd:PRK10982 159 DEPTSSLTEK----EVNHLFTIIRKLKErgCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
8-248 |
6.97e-13 |
|
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: 68.01 E-value: 6.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 8 TSSPSLAGTSG-ITLDSLRVSYHGNV--VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQ 84
Cdd:cd03288 8 SSNSGLVGLGGeIKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 85 LPPY--KRGLAMVVQNYALFphmkvEDNVAFGLRAQKQprgLIAERVTEALKIVGMADYATRYPHQL-----------SG 151
Cdd:cd03288 88 LPLHtlRSRLSIILQDPILF-----SGSIRFNLDPECK---CTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 152 GQQQRVAIARAIAVRPRVLLLDEPLSALDAQIrHNMVEEIarLHRELPELTILYVTHDQTEALTlADKIGIMKDGSLIAh 231
Cdd:cd03288 160 GQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENILQKV--VMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVE- 234
|
250
....*....|....*..
gi 490252226 232 gethelYHYPPNRFSAE 248
Cdd:cd03288 235 ------CDTPENLLAQE 245
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
19-238 |
7.95e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.54 E-value: 7.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRIligdtdvtqlppykrglamvvqn 98
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------------------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 yalfphmKVEDNVAFGLRAQ-------------------KQPRGliaervtEALKIVGM-------ADYATRYPHQLSGG 152
Cdd:PRK15064 377 -------KWSENANIGYYAQdhaydfendltlfdwmsqwRQEGD-------DEQAVRGTlgrllfsQDDIKKSVKVLSGG 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 153 QQQRVAIARAIAVRPRVLLLDEPLSALDaqirhnmVEEIARLHR--ELPELTILYVTHDQTEALTLADKIGIMKDGSLIA 230
Cdd:PRK15064 443 EKGRMLFGKLMMQKPNVLVMDEPTNHMD-------MESIESLNMalEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVD 515
|
....*...
gi 490252226 231 HGETHELY 238
Cdd:PRK15064 516 FSGTYEEY 523
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
73-236 |
1.28e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.29 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 73 GRILIGDTDVT--QLPPYKRGLAMVVQNYALFpHMKVEDNVAFGLRAQKQprgliaERVTEALKIVGMADYATRYPHQ-- 148
Cdd:PTZ00265 1277 GKILLDGVDICdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDATR------EDVKRACKFAAIDEFIESLPNKyd 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 149 ---------LSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQiRHNMVEEIARLHRELPELTILYVTHdQTEALTLADK 219
Cdd:PTZ00265 1350 tnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
170 180
....*....|....*....|.
gi 490252226 220 IGIM----KDGSLIAHGETHE 236
Cdd:PTZ00265 1428 IVVFnnpdRTGSFVQAHGTHE 1448
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
37-236 |
1.67e-12 |
|
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: 68.31 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 37 LSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPA-GGRILIGDTDVTQLPPYK---RGLAMVVQN---YALFPHMKVED 109
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 110 NVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPH------QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQI 183
Cdd:TIGR02633 359 NITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 184 RHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDG----SLIAHGETHE 236
Cdd:TIGR02633 439 KYEIYKLINQLAQE--GVAIIVVSSELAEVLGLSDRVLVIGEGklkgDFVNHALTQE 493
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
33-204 |
1.77e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.90 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDT----DVtQLPPYKRGLAMVVQNYALFPHmKVE 108
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkDI-NLKWWRSKIGVVSQDPLLFSN-SIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 109 DNVAFGLRAQKQ-----------------------------------------PRGLIAER----------VTEALKIVG 137
Cdd:PTZ00265 478 NNIKYSLYSLKDlealsnyynedgndsqenknkrnscrakcagdlndmsnttdSNELIEMRknyqtikdseVVDVSKKVL 557
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 138 MADYATRYP-----------HQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELPELTIL 204
Cdd:PTZ00265 558 IHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITII 635
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
41-194 |
2.25e-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: 64.96 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 41 IEPGEVLALIGPSGSGKTTVL-----RAIAGFVqpaGGRILIgdtDVTQLPP-YKRGLAMVVQNYALFPHMKVEDNVAFG 114
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLdvlagRKTAGVI---TGEILI---NGRPLDKnFQRSTGYVEQQDVHSPNLTVREALRFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 115 --LRAqkqprgliaervtealkivgmadyatryphqLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIA 192
Cdd:cd03232 104 alLRG-------------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
..
gi 490252226 193 RL 194
Cdd:cd03232 153 KL 154
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-259 |
1.03e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.80 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPP---YKRGLAMVVQNY---ALFPHMKVEDNV 111
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqdgLANGIVYISEDRkrdGLVLGMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 112 AF-GLRAQKQPRGLI--AERVTEALKIVGMADYATRYPHQ----LSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIR 184
Cdd:PRK10762 352 SLtALRYFSRAGGSLkhADEQQAVSDFIRLFNIKTPSMEQaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAK 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 185 HNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGsliahgethelyhyppnRFSAEFlgraNILQAT 259
Cdd:PRK10762 432 KEIYQLINQFKAE--GLSIILVSSEMPEVLGMSDRILVMHEG-----------------RISGEF----TREQAT 483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
38-209 |
1.10e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPG-----EVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIgDTDVTQLPPYkrglamVVQNYalfpHMKVEDNva 112
Cdd:PRK13409 354 SLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKISYKPQY------IKPDY----DGTVEDL-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 113 fgLRAqkqprglIAERV------TEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHN 186
Cdd:PRK13409 421 --LRS-------ITDDLgssyykSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180
....*....|....*....|...
gi 490252226 187 MVEEIARLHRElPELTILYVTHD 209
Cdd:PRK13409 492 VAKAIRRIAEE-REATALVVDHD 513
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
40-223 |
1.12e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.96 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 40 TIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRIligDTDV-----------TQLPPYKRGL-------AMVVQNYAL 101
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPswdevlkrfrgTELQDYFKKLangeikvAHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 102 FPhmKVEDNVAFGLRAQKQPRGLIAErVTEALKIVGMADyatRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDA 181
Cdd:COG1245 172 IP--KVFKGTVRELLEKVDERGKLDE-LAEKLGLENILD---RDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490252226 182 QIRHNMveeiARLHRELPEL--TILYVTHDqteaLT----LADKIGIM 223
Cdd:COG1245 246 YQRLNV----ARLIRELAEEgkYVLVVEHD----LAildyLADYVHIL 285
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
39-209 |
1.31e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 39 LTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIgDTDVT-----QLPP----------YKRGLAMVVQ---NYA 100
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDLIvarlqQDPPrnvegtvydfVAEGIEEQAEylkRYH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 101 LFPHMKVED------NVAFGLRAQKQPRGL--IAERVTEALKIVGMAdyatryPHQ----LSGGQQQRVAIARAIAVRPR 168
Cdd:PRK11147 103 DISHLVETDpseknlNELAKLQEQLDHHNLwqLENRINEVLAQLGLD------PDAalssLSGGWLRKAALGRALVSNPD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490252226 169 VLLLDEPLSALDaqirhnmVEEIARLHRELPEL--TILYVTHD 209
Cdd:PRK11147 177 VLLLDEPTNHLD-------IETIEWLEGFLKTFqgSIIFISHD 212
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-182 |
2.56e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.13 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVqpAGGRILIGDTDVTQLP---PYKRGLAMVVQNYALFPHMKVE 108
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLVNGRPldsSFQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 109 DNVAFGLRAqKQPRGL-IAER---VTEALKIVGMADYATRY---PHQ-LSGGQQQRVAIARAIAVRPRVLL-LDEPLSAL 179
Cdd:TIGR00956 855 ESLRFSAYL-RQPKSVsKSEKmeyVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
...
gi 490252226 180 DAQ 182
Cdd:TIGR00956 934 DSQ 936
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-209 |
2.57e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGriligdtDVTQLPPYKRGLAMvvQNYALFPHMKVEDNV 111
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------EARPAPGIKVGYLP--QEPQLDPEKTVRENV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 112 AFGLRAQKQ--------------PRG----LIAE--RVTEALKIVG---------MADYATRYPH------QLSGGQQQR 156
Cdd:PRK11819 92 EEGVAEVKAaldrfneiyaayaePDAdfdaLAAEqgELQEIIDAADawdldsqleIAMDALRCPPwdakvtKLSGGERRR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 157 VAIARAIAVRPRVLLLDEPLSALDAqirhnmvEEIARLHRELPEL--TILYVTHD 209
Cdd:PRK11819 172 VALCRLLLEKPDMLLLDEPTNHLDA-------ESVAWLEQFLHDYpgTVVAVTHD 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-219 |
3.35e-11 |
|
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: 64.97 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 23 SLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLppykrGLAMVVQNYALF 102
Cdd:TIGR00957 1291 CLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI-----GLHDLRFKITII 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 103 PhmkvEDNVAFG--LRAQKQPRGLIA-ERVTEALKIVGMADYATRYP----HQ-------LSGGQQQRVAIARAIAVRPR 168
Cdd:TIGR00957 1366 P----QDPVLFSgsLRMNLDPFSQYSdEEVWWALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 169 VLLLDEPLSALDAQIrHNMVEEIARLHRElpELTILYVTH------DQTEALTLaDK 219
Cdd:TIGR00957 1442 ILVLDEATAAVDLET-DNLIQSTIRTQFE--DCTVLTIAHrlntimDYTRVIVL-DK 1494
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-237 |
3.84e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.76 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLppykrGLAMVVQNYALFPHMKV--EDN 110
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF-----GLMDLRKVLGIIPQAPVlfSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAFGL----------------RA------QKQPRGLIAErVTEAlkivgmadyatryPHQLSGGQQQRVAIARAIAVRPR 168
Cdd:PLN03130 1329 VRFNLdpfnehndadlwesleRAhlkdviRRNSLGLDAE-VSEA-------------GENFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490252226 169 VLLLDEPLSAL----DAQIRHNMVEeiarlhrELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PLN03130 1395 ILVLDEATAAVdvrtDALIQKTIRE-------EFKSCTMLIIAH-RLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
38-236 |
4.41e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.18 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPA-GGRILIGDTDVTQLPP---YKRGLAMVVQN---YALFPHMKVEDN 110
Cdd:PRK13549 282 SFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNPqqaIAQGIAMVPEDrkrDGIVPVMGVGKN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 111 VAFGLRAQKQPRGLI--AERVTEALKIVGMADYATRYPHQ----LSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIR 184
Cdd:PRK13549 362 ITLAALDRFTGGSRIddAAELKTILESIQRLKVKTASPELaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAK 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 185 HnmveEIARLHRELPE--LTILYVTHDQTEALTLADKIGIMKDG----SLIAHGETHE 236
Cdd:PRK13549 442 Y----EIYKLINQLVQqgVAIIVISSELPEVLGLSDRVLVMHEGklkgDLINHNLTQE 495
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-180 |
5.75e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTdVTqlppykrgLAMVVQN 98
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET-VK--------LAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 Y-ALFPHMKVEDNV---------------------AFGLRAQKQPrgliaervtealKIVGmadyatryphQLSGGQQQR 156
Cdd:PRK11819 396 RdALDPNKTVWEEIsggldiikvgnreipsrayvgRFNFKGGDQQ------------KKVG----------VLSGGERNR 453
|
170 180
....*....|....*....|....
gi 490252226 157 VAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
38-209 |
6.96e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.65 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPG-----EVLALIGPSGSGKTTVLRAIAGFVQPAGGRIlIGDTDVTQLPPYkrglamVVQNYalfpHMKVEDNVa 112
Cdd:COG1245 355 SLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKISYKPQY------ISPDY----DGTVEEFL- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 113 FGLRAQKQPRGLIAERVTEALKIVGMADyatRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIA 192
Cdd:COG1245 423 RSANTDDFGSSYYKTEIIKPLGLEKLLD---KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170
....*....|....*..
gi 490252226 193 RLHRElPELTILYVTHD 209
Cdd:COG1245 500 RFAEN-RGKTAMVVDHD 515
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
40-223 |
7.02e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 40 TIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRiLIGDTDVTQLPPYKRGLAMvvQNYalFPhmKVEDNvafGLRAQK 119
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD-YEEEPSWDEVLKRFRGTEL--QNY--FK--KLYNG---EIKVVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 120 QPR--GLIAE----RVTEALKIV---GMADYAT----------RYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK13409 165 KPQyvDLIPKvfkgKVRELLKKVderGKLDEVVerlglenildRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490252226 181 AQIRHNMveeiARLHREL-PELTILYVTHDqteaLT----LADKIGIM 223
Cdd:PRK13409 245 IRQRLNV----ARLIRELaEGKYVLVVEHD----LAvldyLADNVHIA 284
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
128-237 |
1.30e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.06 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 128 RVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRElpELTILYVT 207
Cdd:NF000106 124 RADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD--GATVLLTT 201
|
90 100 110
....*....|....*....|....*....|
gi 490252226 208 HDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:NF000106 202 QYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-237 |
1.31e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.83 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQlppyKRGLAMVVQN 98
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD----ARHRRAVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 99 YA---------LFPHMKVEDNVAF-----GLRAQKQPRgliaeRVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIA 164
Cdd:NF033858 78 IAympqglgknLYPTLSVFENLDFfgrlfGQDAAERRR-----RIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490252226 165 VRPRVLLLDEPLSALDAQIRHNMVEEIARLHRELPELTILYVTHDQTEALTLaDKIGIMKDGSLIAHGETHEL 237
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAEL 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-209 |
2.25e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 26 VSYH--GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGdtdvTQLPpykrgLAMVVQNYA-LF 102
Cdd:PRK11147 325 VNYQidGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLE-----VAYFDQHRAeLD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 103 PHMKVEDNVAFGlraqKQprgliaeRVTealkIVGMADYATRY-------PHQ-------LSGGQQQRVAIARaIAVRPR 168
Cdd:PRK11147 396 PEKTVMDNLAEG----KQ-------EVM----VNGRPRHVLGYlqdflfhPKRamtpvkaLSGGERNRLLLAR-LFLKPS 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490252226 169 VLL-LDEPLSALDaqirhnmVEEIARLHRELPEL--TILYVTHD 209
Cdd:PRK11147 460 NLLiLDEPTNDLD-------VETLELLEELLDSYqgTVLLVSHD 496
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
19-180 |
3.35e-10 |
|
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: 60.25 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSY--HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDT-DVTQLPPYKRGLAMV 95
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSwNSVPLQKWRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNYALFphmkvednvAFGLRAQKQPRGLIAE----RVTEAlkiVGMADYATRYPHQ-----------LSGGQQQRVAIA 160
Cdd:cd03289 83 PQKVFIF---------SGTFRKNLDPYGKWSDeeiwKVAEE---VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLA 150
|
170 180
....*....|....*....|
gi 490252226 161 RAIAVRPRVLLLDEPLSALD 180
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLD 170
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-236 |
7.61e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.64 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 30 GNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRIL--------------IGDTDVTQLPpykrgLAMV 95
Cdd:PLN03073 521 GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDLSSNP-----LLYM 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNYALFPHMKvednvafgLRAQKQPRGliaerVTEALKIVGMadyatrypHQLSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:PLN03073 596 MRCFPGVPEQK--------LRAHLGSFG-----VTGNLALQPM--------YTLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490252226 176 LSALDAQIRHNMVEEIArlhreLPELTILYVTHDQTEALTLADKIGIMKDGSLIA-HGETHE 236
Cdd:PLN03073 655 SNHLDLDAVEALIQGLV-----LFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPfHGTFHD 711
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-228 |
9.33e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.18 E-value: 9.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 21 LDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRIligdtdvtqlppykrGLAMVVQnYA 100
Cdd:PRK10636 315 MEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---------------GLAKGIK-LG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 101 LFPHMKVEdnvafGLRAQKQP---RGLIAERVTEA-----LKIVGM-ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLL 171
Cdd:PRK10636 379 YFAQHQLE-----FLRADESPlqhLARLAPQELEQklrdyLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490252226 172 LDEPLSALDAQIRHNMVEEIARLhrelpELTILYVTHDQTEALTLADKIGIMKDGSL 228
Cdd:PRK10636 454 LDEPTNHLDLDMRQALTEALIDF-----EGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-180 |
1.31e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.92 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSY--HGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDT-DVTQLPPYKRGLAMV 95
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSwNSVTLQTWRKAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 96 VQNYALF---------PHMKVEDNVAFglraqkqprgliaeRVTEAlkiVGMADYATRYPHQ-----------LSGGQQQ 155
Cdd:TIGR01271 1298 PQKVFIFsgtfrknldPYEQWSDEEIW--------------KVAEE---VGLKSVIEQFPDKldfvlvdggyvLSNGHKQ 1360
|
170 180
....*....|....*....|....*
gi 490252226 156 RVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-180 |
2.01e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 26 VSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAG------------FVQPAGGriliGDT--DVtqlppyKRG 91
Cdd:PRK10938 268 VSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltlFGRRRGS----GETiwDI------KKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 92 LAMVVQNYalfpHM--KVEDNV----------AFGLRAQKQPRglIAERVTEALKIVGMADYATRYP-HQLSGGQQQRVA 158
Cdd:PRK10938 338 IGYVSSSL----HLdyRVSTSVrnvilsgffdSIGIYQAVSDR--QQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLAL 411
|
170 180
....*....|....*....|..
gi 490252226 159 IARAIAVRPRVLLLDEPLSALD 180
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLD 433
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-182 |
2.09e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.47 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGfvQPAGGRILiGDTDVTQLPPYKRGLAMVV----QNYALFPHMKVE 108
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKKQETFARISgyceQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 109 DNVAFG--LR----AQKQPRGLIAERVTEALKIVGMADYATRYP--HQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PLN03140 972 ESLIYSafLRlpkeVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
..
gi 490252226 181 AQ 182
Cdd:PLN03140 1052 AR 1053
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
294-367 |
2.34e-09 |
|
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: 53.39 E-value: 2.34e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490252226 294 LCIRPQHMSLaprSATSNRLNATLTSVHWQGDLTHLLCDVAGEAVRIVMTHVN--PLPRAGDKLALYFEPGDAVLI 367
Cdd:pfam08402 1 LAIRPEKIRL---AAAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRVPNAhaRPPAPGDRVGLGWDPEDAHVL 73
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
32-224 |
3.37e-09 |
|
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: 55.44 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAgfvqpaggriligdtdvtqlppykrglamvvqnyalfphmkvednV 111
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------------------------------------L 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 112 AFGLRAQKQ-PRGLIAERVTEAlkivgmADYATRYP--HQLSGGQQQRVAIARAIA---VRPRVL-LLDEPLSALDAQIR 184
Cdd:cd03227 44 ALGGAQSATrRRSGVKAGCIVA------AVSAELIFtrLQLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDG 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490252226 185 HNMVEEIarLHRELPELTILYVTHDQTEALtLADKIGIMK 224
Cdd:cd03227 118 QALAEAI--LEHLVKGAQVIVITHLPELAE-LADKLIHIK 154
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
38-237 |
4.65e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPGEVLALIGPSGSGKTTVLRAIAG------------FVQPAggRI-------LIGD------TDVtqLPPYK--- 89
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGelpllsgerqsqFSHIT--RLsfeqlqkLVSDewqrnnTDM--LSPGEddt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 90 -RGLAMVVQNYalfphmkVEDNvafglraqkqprgliaERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPR 168
Cdd:PRK10938 99 gRTTAEIIQDE-------VKDP----------------ARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490252226 169 VLLLDEPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHEL 237
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQS--GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
41-220 |
4.79e-09 |
|
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: 55.27 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 41 IEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQLPPYKrglamvvqnyalfphmkvednvafglraqkq 120
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 121 prgliaervtealkivgmadyatryphQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHRElPE 200
Cdd:cd03222 71 ---------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE-GK 122
|
170 180
....*....|....*....|
gi 490252226 201 LTILYVTHDQTEALTLADKI 220
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRI 142
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
34-240 |
7.40e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.98 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRI-LIGDTDVTQLppykrglamvvqNYALFPHMKVEDNVA 112
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSVIAI------------SAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 113 FGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIA 192
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIY 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490252226 193 RLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHE-LYHY 240
Cdd:PRK13546 188 EFKEQ--NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDvLPKY 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
34-236 |
2.67e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDV---TQLPPYKRGLAMVVQ---NYALFPHMKV 107
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnhNANEAINHGFALVTEerrSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 108 EDN-VAFGLRAQKQPRGLIAER--------VTEALKiVGMADYATRYpHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSA 178
Cdd:PRK10982 344 GFNsLISNIRNYKNKVGLLDNSrmksdtqwVIDSMR-VKTPGHRTQI-GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 179 LDAQIRHNMVEEIARLHRElpELTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHE 236
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKK--DKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKT 477
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
38-223 |
3.48e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 38 SLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILI-------GDTDVTQLPPYkrglaM-----------VVQNY 99
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvdaGDIATRRRVGY-----MsqafslygeltVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 100 ALfpHMKVednvaFGLraqkqPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSAL 179
Cdd:NF033858 361 EL--HARL-----FHL-----PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490252226 180 DAQIRHNMVEEIARLHRElPELTILYVTHDQTEALtLADKIGIM 223
Cdd:NF033858 429 DPVARDMFWRLLIELSRE-DGVTIFISTHFMNEAE-RCDRISLM 470
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-208 |
6.67e-08 |
|
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: 54.37 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 17 SGITLDSLR-VSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGF--------VQPAGGRILIgdtdVTQLPP 87
Cdd:TIGR00954 450 NGIKFENIPlVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY----VPQRPY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 88 YKRGlamVVQNYALFPhMKVEDNVAFGLRAQKQPRGLIAERVTEALKIVGMADYATRYPHQLSGGQQQRVAIARAIAVRP 167
Cdd:TIGR00954 526 MTLG---TLRDQIIYP-DSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKP 601
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490252226 168 RVLLLDEPLSAldaqIRHNMVEEIARLHRELpELTILYVTH 208
Cdd:TIGR00954 602 QFAILDECTSA----VSVDVEGYMYRLCREF-GITLFSVSH 637
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-263 |
1.08e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 33 VLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPA---GGRILIGDTDVTQLPPYKRGlAMVVQNYALFPHMKVED 109
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTS-AYISQNDVHVGVMTVKE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 110 NVAFGLRAQ---------------KQPRGLIAER------------------VTE-ALKIVGM--------ADYATRyph 147
Cdd:PLN03140 259 TLDFSARCQgvgtrydllselarrEKDAGIFPEAevdlfmkatamegvksslITDyTLKILGLdickdtivGDEMIR--- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 148 QLSGGQQQRVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVEEIARLHReLPELTILY-VTHDQTEALTLADKIGIMKDG 226
Cdd:PLN03140 336 GISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVH-LTEATVLMsLLQPAPETFDLFDDIILLSEG 414
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490252226 227 SLIAHG-ETHEL-------YHYPPNRFSAEFLgraniLQATALKD 263
Cdd:PLN03140 415 QIVYQGpRDHILeffescgFKCPERKGTADFL-----QEVTSKKD 454
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
48-220 |
1.47e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.45 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 48 ALIGPSGSGKTTVLRAIagFVqpaggrILIGDtdvtqLPPYKRGLAMVvqnyalfPHM------KVEDNVAFGLRAQKQp 121
Cdd:cd03240 26 LIVGQNGAGKTTIIEAL--KY------ALTGE-----LPPNSKGGAHD-------PKLiregevRAQVKLAFENANGKK- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 122 rgLIAERVTEALKIV------GMADYATRYPHQLSGGQQQ------RVAIARAIAVRPRVLLLDEPLSALDAQIRHNMVE 189
Cdd:cd03240 85 --YTITRSLAILENVifchqgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLA 162
|
170 180 190
....*....|....*....|....*....|.
gi 490252226 190 EIARLHRELPELTILYVTHDQtEALTLADKI 220
Cdd:cd03240 163 EIIEERKSQKNFQLIVITHDE-ELVDAADHI 192
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-180 |
5.22e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 19 ITLDSLRVSYHGNVVLKPLSLTIEPGEVLALIGPSGSGKTTVLR-----AIAGFvqPAGGRIL------IGDtDVTQL-- 85
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGI--PKNCQILhveqevVGD-DTTALqc 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 86 ---PPYKRGLAMVVQNYALFPHMKVEDNVAFGLRAQKQPRGL----IAERVTEALK-----------------IVGM--- 138
Cdd:PLN03073 255 vlnTDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVdkdaVSQRLEEIYKrlelidaytaearaasiLAGLsft 334
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490252226 139 ADYATRYPHQLSGGQQQRVAIARAIAVRPRVLLLDEPLSALD 180
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
28-240 |
1.04e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.27 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 28 YHgnVVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIgdtdvtqlppyKRGLAMVVQNYALFPHMKV 107
Cdd:PRK13545 36 YH--YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-----------KGSAALIAISSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 108 EDNVAF-GLRAqkqprGLIAERVTEAL-KIVGMADYAtRYPHQ----LSGGQQQRVAIARAIAVRPRVLLLDEPLSALDA 181
Cdd:PRK13545 103 IENIELkGLMM-----GLTKEKIKEIIpEIIEFADIG-KFIYQpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490252226 182 QIRHNMVEEIarlhRELPE--LTILYVTHDQTEALTLADKIGIMKDGSLIAHGETHELY-HY 240
Cdd:PRK13545 177 TFTKKCLDKM----NEFKEqgKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVdHY 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-252 |
1.81e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 32 VVLKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDVTQ--LPPYKRGLAMVVQNYALFPHmKVED 109
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG-TVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 110 NVAFGLRAQkqprgliAERVTEALKIVGMADYATRYPHQL-----------SGGQQQRVAIARAIAVRPR-VLLLDEPLS 177
Cdd:PTZ00243 1403 NVDPFLEAS-------SAEVWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARALLKKGSgFILMDEATA 1475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 178 ----ALDAQIRhnmveeiARLHRELPELTILYVTHdQTEALTLADKIGIMKDGSLIAHGETHELYHYPPNRFSA--EFLG 251
Cdd:PTZ00243 1476 nidpALDRQIQ-------ATVMSAFSAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSmvEALG 1547
|
.
gi 490252226 252 R 252
Cdd:PTZ00243 1548 R 1548
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
34-220 |
2.70e-05 |
|
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: 44.24 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 34 LKPLSLTIEPGEVLALIGPSGSGKTTVLRAIAgfvqpaggriligdtdvtqlppYKRGLAMVVQNYALFPHMKVednVAF 113
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----------------------YASGKARLISFLPKFSRNKL---IFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 114 GlraqkQPRGLIAervtealkiVGMAdYAT--RYPHQLSGGQQQRVAIARAIAVRPR--VLLLDEPLSALDAQIRHNMVE 189
Cdd:cd03238 66 D-----QLQFLID---------VGLG-YLTlgQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE 130
|
170 180 190
....*....|....*....|....*....|.
gi 490252226 190 EIARLHRElpELTILYVTHDQTeALTLADKI 220
Cdd:cd03238 131 VIKGLIDL--GNTVILIEHNLD-VLSSADWI 158
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
149-262 |
6.93e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 149 LSGGQQQRVAIARAIAVRPR--VLLLDEPLSALDAQIRHNMVEEIARLHRElpELTILYVTHDQtEALTLADKIGIMKDG 226
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQ--GNTVLLVEHDE-QMISLADRIIDIGPG 553
|
90 100 110
....*....|....*....|....*....|....*.
gi 490252226 227 SLIAHGETheLYHYPPnrfsAEFLGRANILQATALK 262
Cdd:PRK00635 554 AGIFGGEV--LFNGSP----REFLAKSDSLTAKYLR 583
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
98-220 |
6.32e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 98 NYALFPHMKVEDNVAFGLRAQKQPRG-LIAERV----TEALKI---VGMaDYAT--RYPHQLSGGQQQRVAIARAIAVR- 166
Cdd:TIGR00630 429 SIADVSELSIREAHEFFNQLTLTPEEkKIAEEVlkeiRERLGFlidVGL-DYLSlsRAAGTLSGGEAQRIRLATQIGSGl 507
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 490252226 167 PRVL-LLDEPLSALDAQIRHNMVEEIARLhRELPElTILYVTHDQtEALTLADKI 220
Cdd:TIGR00630 508 TGVLyVLDEPSIGLHQRDNRRLINTLKRL-RDLGN-TLIVVEHDE-DTIRAADYV 559
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
47-77 |
1.07e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 39.05 E-value: 1.07e-03
10 20 30
....*....|....*....|....*....|.
gi 490252226 47 LALIGPSGSGKTTVLRAIAGFVQPAGGRILI 77
Cdd:cd00009 22 LLLYGPPGTGKTTLARAIANELFRPGAPFLY 52
|
|
| VirB11 |
COG0630 |
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ... |
20-86 |
1.27e-03 |
|
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440395 [Multi-domain] Cd Length: 462 Bit Score: 40.45 E-value: 1.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 20 TLDSLRVSYhgnvvlkpLSLTIEPGEVLALIGPSGSGKTTVLRAIAGFVqPAGGRIL-IGDTDVTQLP 86
Cdd:COG0630 274 TLSPELAAY--------LWLLLENGKSVLVAGGTASGKTTLLNALLSFI-PPDAKIVtIEDTRELNLP 332
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
148-220 |
1.45e-03 |
|
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: 39.94 E-value: 1.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490252226 148 QLSGGQQQRVAIARAIAVRpRV-----LLLDEPLSALDAQIRHNmveeIARLHRELPELTILYVTHDQTEALTLADKI 220
Cdd:cd03272 158 QLSGGQKSLVALALIFAIQ-KCdpapfYLFDEIDAALDAQYRTA----VANMIKELSDGAQFITTTFRPELLEVADKF 230
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
38-75 |
2.89e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.21 E-value: 2.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 490252226 38 SLTIE---PGEVLALIGPSGSGKTTVLRAIAGFVQPAGGRI 75
Cdd:COG3950 16 DLEIDfdnPPRLTVLVGENGSGKTTLLEAIALALSGLLSRL 56
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
38-65 |
4.68e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 4.68e-03
10 20
....*....|....*....|....*...
gi 490252226 38 SLTIEPGEVLALIGPSGSGKTTVLRAIA 65
Cdd:pfam13555 16 TIPIDPRGNTLLTGPSGSGKSTLLDAIQ 43
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
149-175 |
7.08e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.23 E-value: 7.08e-03
10 20
....*....|....*....|....*..
gi 490252226 149 LSGGQQQRVAIARAIAVRPRVLLLDEP 175
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
44-174 |
7.41e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 37.10 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490252226 44 GEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTDvtQLPPYkRGLAMVVQNYALFphmkvednVAFGLRAQKQPRG 123
Cdd:pfam13191 24 PPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCD--ENLPY-SPLLEALTREGLL--------RQLLDELESSLLE 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 490252226 124 LIAERVTEALKIVG--MADYATRYPHQLsggqqQRVAIARAIAVRPRVLLLDE 174
Cdd:pfam13191 93 AWRAALLEALAPVPelPGDLAERLLDLL-----LRLLDLLARGERPLVLVLDD 140
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
44-81 |
8.43e-03 |
|
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];
Pssm-ID: 443264 [Multi-domain] Cd Length: 179 Bit Score: 37.01 E-value: 8.43e-03
10 20 30
....*....|....*....|....*....|....*...
gi 490252226 44 GEVLALIGPSGSGKTTVLRAIAGFVQPAGGRILIGDTD 81
Cdd:COG4088 4 PMLLILTGPPGSGKTTFAKALAQRLYAEGIAVALLHSD 41
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
34-76 |
9.66e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 37.67 E-value: 9.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 490252226 34 LKPLSLTIEPGeVLALIGPSGSGKTTVLRAIAGFVQPAGGRIL 76
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKF 55
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