|
Name |
Accession |
Description |
Interval |
E-value |
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-333 |
4.82e-168 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 471.50 E-value: 4.82e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNT 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLS-FAvARKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEgLA-DRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 160 EPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTSN 239
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 240 VFDAGLAQKIC--------------------GMEGSYSLRPEHIRLDEGGDVQVQGVV-QAVQYQGAATRLELKLADGAR 298
Cdd:COG3842 241 LLPGTVLGDEGggvrtggrtlevpadaglaaGGPVTVAIRPEDIRLSPEGPENGLPGTvEDVVFLGSHVRYRVRLGDGQE 320
|
330 340 350
....*....|....*....|....*....|....*
gi 2673334298 299 LLVSQANlseaSPLSGIAPGQAVTASWSREAMIRL 333
Cdd:COG3842 321 LVVRVPN----RAALPLEPGDRVGLSWDPEDVVVL 351
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-330 |
1.67e-133 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 384.04 E-value: 1.67e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQ 83
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 DYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:COG3839 83 SYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 164 ALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTS--NVF 241
Cdd:COG3839 163 NLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPpmNLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 242 DA----------GLAQKICGMEGSYS-------LRPEHIRLDEGGDVQVQGVVQAVQYQGAATRLELKLaDGARLLVSqa 304
Cdd:COG3839 243 PGtvegggvrlgGVRLPLPAALAAAAggevtlgIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRL-GGQELVAR-- 319
|
330 340
....*....|....*....|....*.
gi 2673334298 305 nlseASPLSGIAPGQAVTASWSREAM 330
Cdd:COG3839 320 ----VPGDTRLRPGDTVRLAFDPERL 341
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-236 |
2.26e-131 |
|
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: 373.88 E-value: 2.26e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQD 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 YALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 165 LDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVG 236
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-325 |
6.36e-126 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 365.42 E-value: 6.36e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQD 84
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 YALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 165 LDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTSNVFDAG 244
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIFDAT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 245 LAQKI------CGMEGSYS-----------------LRPEHIRLDEGGDVQVQGVV----QAVQYQGAATRLELKLADGA 297
Cdd:PRK09452 255 VIERLdeqrvrANVEGRECniyvnfavepgqklhvlLRPEDLRVEEINDDEHAEGLigyvRERNYKGMTLDSVVELENGK 334
|
330 340
....*....|....*....|....*...
gi 2673334298 298 RLLVSQAnLSEASPLSGIAPGQAVTASW 325
Cdd:PRK09452 335 MVMVSEF-FNEDDPDFDHSLGQKVAVTW 361
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-328 |
5.15e-114 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 334.04 E-value: 5.15e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEA-SELPPWERDVNTVFQ 83
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 DYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLS-FAvARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEgLA-DRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 163 GALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTSNVFD 242
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 243 AGLAQKICGMEGSYS--------------LRPEHIRLDEGGDVQVQGVV--QAVQYQGAATRLELKLADGARLLVsQANL 306
Cdd:COG1118 242 GRVIGGQLEADGLTLpvaeplpdgpavagVRPHDIEVSREPEGENTFPAtvARVSELGPEVRVELKLEDGEGQPL-EAEV 320
|
330 340
....*....|....*....|...
gi 2673334298 307 S-EASPLSGIAPGQAVTASWSRE 328
Cdd:COG1118 321 TkEAWAELGLAPGDPVYLRPRPA 343
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
9-330 |
1.41e-110 |
|
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: 325.84 E-value: 1.41e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 9 NVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQDYALF 88
Cdd:TIGR03265 9 NIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 89 PHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSfAVARK-PSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:TIGR03265 89 PNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLP-GSERKyPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 168 KLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTSNVF----DA 243
Cdd:TIGR03265 168 RVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNWLpgtrGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 244 GLAQKICGME-------------GSYSLRPEHIRLDEGGDVQVQGVVQAVQY--QGAATRLELKLA--DGARLLVSQAnl 306
Cdd:TIGR03265 248 GSRARVGGLTlacapglaqpgasVRLAVRPEDIRVSPAGNAANLLLARVEDMefLGAFYRLRLRLEglPGQALVADVS-- 325
|
330 340
....*....|....*....|....
gi 2673334298 307 SEASPLSGIAPGQAVTASWSREAM 330
Cdd:TIGR03265 326 ASEVERLGIRAGQPIWIELPAERL 349
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-217 |
3.81e-109 |
|
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: 316.77 E-value: 3.81e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQD 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 YALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 165 LDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVD 217
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-325 |
3.05e-105 |
|
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: 311.35 E-value: 3.05e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 35 MLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQ 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 115 ARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHD 194
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 195 QGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTSNVFDA-------------GLAQKICGMEGSYS---- 257
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEAtvierkseqvvlaGVEGRRCDIYTDVPvekd 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 258 ------LRPEHIRLDE----GGDVQVQGVVQAVQYQGAATRLELKLADGARLLVSqANLSEASPLSGIAPGQAVTASW 325
Cdd:TIGR01187 241 qplhvvLRPEKIVIEEedeaNSSNAIIGHVIDITYLGMTLEVHVRLETGQKVLVS-EFFNEDDPHMSPSIGDRVGLTW 317
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-269 |
2.18e-99 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 297.14 E-value: 2.18e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLY-GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVF 82
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 83 QDYALFPHMSILDNVAYGLMVKGIDK---KKRHAQARDALEKVGLsfaVARKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRGMPKaeiEERVAEAARILELEPL---LDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 160 EPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTS- 238
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPa 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 239 -NVFDAGLAQKICGMEGSYS--------------------LRPEHIRLDEGG 269
Cdd:PRK11650 240 mNLLDGRVSADGAAFELAGGialplgggyrqyagrkltlgIRPEHIALSSAE 291
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-236 |
2.75e-99 |
|
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: 292.71 E-value: 2.75e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 3 YAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVF 82
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 83 QDYALFPHMSILDNVAYGLMVKGI----DKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 159 DEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVG 236
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-217 |
1.94e-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: 289.54 E-value: 1.94e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQD 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 YALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 165 LDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVD 217
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-231 |
8.34e-98 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 289.68 E-value: 8.34e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLY----GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPwerDVN 79
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---DRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG1116 84 VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 160 EPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNN--GRI---EQVDTPrdlymRPRTPFV 231
Cdd:COG1116 164 EPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIveeIDVDLP-----RPRDREL 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-213 |
1.52e-92 |
|
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: 274.73 E-value: 1.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGD----VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPwerDVNT 80
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP---DRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 161 PLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNN--GRI 213
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
5-240 |
5.72e-92 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 273.98 E-value: 5.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQD 84
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 YALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 165 LDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTSNV 240
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-270 |
1.29e-91 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 277.37 E-value: 1.29e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQD 84
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 YALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 165 LDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTSNVFDAG 244
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIFPAT 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2673334298 245 LAQKICGMEGsYSL-------------------RPEHIRLDEGGD 270
Cdd:PRK11432 247 LSGDYVDIYG-YRLprpaafafnlpdgectvgvRPEAITLSEQGE 290
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-240 |
2.10e-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: 269.98 E-value: 2.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRaVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQD 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 YALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 165 LDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTSNV 240
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-238 |
3.82e-90 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 271.96 E-value: 3.82e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGD-VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVNTVF 82
Cdd:COG1125 3 EFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 83 QDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGL---SFAvARKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpeEYR-DRYPHELSGGQQQRVGVARALAADPPILLMD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 160 EPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTS 238
Cdd:COG1125 162 EPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGAD 240
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-237 |
3.24e-85 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 261.50 E-value: 3.24e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQD 84
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 YALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 165 LDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGT 237
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGS 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-253 |
3.95e-84 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 258.09 E-value: 3.95e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQ 83
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 DYALFPHMSILDNVAYGLMV---------KGIDKKkrhaqARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVlprrerpnaAAIKAK-----VTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGF 234
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEF 236
|
250
....*....|....*....
gi 2673334298 235 VGTSNVFDAglaqKICGME 253
Cdd:PRK10851 237 MGEVNRLQG----TIRGGQ 251
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
5-248 |
4.21e-83 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 255.39 E-value: 4.21e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDgVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQD 84
Cdd:NF040840 2 IRIENLSKDWKEFKLRD-ISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 YALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:NF040840 81 YMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 165 LDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTSNVFDaG 244
Cdd:NF040840 161 LDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIE-G 239
|
....
gi 2673334298 245 LAQK 248
Cdd:NF040840 240 VAEK 243
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-236 |
4.42e-82 |
|
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: 249.14 E-value: 4.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVR-AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVNTV 81
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 FQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGL---SFAvARKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpaEFA-DRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 159 DEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVG 236
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-248 |
8.42e-82 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 253.22 E-value: 8.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNT 80
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 161 PLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTSNV 240
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
|
....*...
gi 2673334298 241 FDAGLAQK 248
Cdd:PRK11607 256 FEGVLKER 263
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-214 |
6.50e-79 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 240.33 E-value: 6.50e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGD----VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER 76
Cdd:COG1136 1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 77 DV--NT----VFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALV 150
Cdd:COG1136 81 ARlrRRhigfVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 151 NEPRVLLLDEPLGALDLKLREQ-MQFeLKKLQQELGITFIFVTHDQgEALSMSDRVAVFNNGRIE 214
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEvLEL-LRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-213 |
3.28e-77 |
|
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: 235.85 E-value: 3.28e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGD----VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERD--- 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 ---VNTVFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQgEALSMSDRVAVFNNGRI 213
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-235 |
3.29e-77 |
|
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: 237.54 E-value: 3.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE------RDVNTVFQDYALF 88
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 89 PHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:cd03294 115 PHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 169 LREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFV 235
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
15-244 |
7.71e-77 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 240.78 E-value: 7.71e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE------RDVNTVFQDYALF 88
Cdd:COG4175 38 GQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 89 PHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLS-FAvARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:COG4175 118 PHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAgWE-DSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 168 KLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVG---TSNVFDAG 244
Cdd:COG4175 197 LIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEdvdRSKVLTAG 276
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-212 |
9.64e-76 |
|
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: 230.54 E-value: 9.64e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGK----EASELPPWERDVNT 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdltdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFPHMSILDNVAYGlmvkgidkkkrhaqardalekvglsfavarkpsqLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 161 PLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-229 |
2.46e-72 |
|
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: 232.87 E-value: 2.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY-----GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE---- 75
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 76 -RDVNTVFQD--YALFPHMSILDNVAYGLMVKGI-DKKKRHAQARDALEKVGLSFAVA-RKPSQLSGGQRQRVAIARALV 150
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLAdRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 151 NEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTP 229
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-229 |
4.12e-72 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 223.33 E-value: 4.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEaseLPPWERDVNT---- 80
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGED---LTDSKKDINKlrrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 ---VFQDYALFPHMSILDNVAYGLM-VKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:COG1126 79 vgmVFQQFNLFPHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 157 LLDEPLGALD-------LKLreqmqfeLKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTP 229
Cdd:COG1126 159 LFDEPTSALDpelvgevLDV-------MRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-217 |
2.12e-67 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 210.68 E-value: 2.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY-GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE-----RDV 78
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 79 NTVFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 159 DEPLGALDLKLREQ-MQFeLKKLQQeLGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVD 217
Cdd:COG2884 162 DEPTGNLDPETSWEiMEL-LEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-213 |
8.50e-67 |
|
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: 209.67 E-value: 8.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY----GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELP-----PWE 75
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 76 RDVNTVFQDY--ALFPHMSILDNVAYGLMVKGIDKKKRHAQAR--DALEKVGLSFAVA-RKPSQLSGGQRQRVAIARALV 150
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAvlLLLVGVGLPEEVLnRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 151 NEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-213 |
1.76e-66 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 209.72 E-value: 1.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYG----DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASElPPWERDVntV 81
Cdd:COG4525 5 TVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGV--V 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 FQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 162 LGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVF--NNGRI 213
Cdd:COG4525 162 FGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-222 |
2.45e-66 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 208.76 E-value: 2.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP-WERDVNTVFQ 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAeVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 DYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 164 ALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-230 |
9.45e-66 |
|
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: 207.35 E-value: 9.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYG----DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEAS--ELPPWERD 77
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTrrRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 VNTVFQDY--ALFPHMSILDNVAYGLMVKGIDKkkRHAQARDALEKVGLSFAVA-RKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPD--REERIAELLEQVGLPPSFLdRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPF 230
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-237 |
1.60e-65 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 206.53 E-value: 1.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGD--VRAvdgvTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQ 83
Cdd:COG3840 3 RLDDLTYRYGDfpLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 DYALFPHMSILDNVAYGLmvkgiDKKKR-----HAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGL-----RPGLKltaeqRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 159 DEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGT 237
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-228 |
4.46e-65 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 205.26 E-value: 4.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY-GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVNTV 81
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 FQ--DYALFpHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLS-FAvARKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:COG1122 81 FQnpDDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEhLA-DRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 159 DEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRT 228
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-238 |
1.78e-64 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 207.24 E-value: 1.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY----GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE----- 75
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 76 RDVNTVFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 156 LLLDEPLGALD-------LKLreqmqfeLKKLQQELGITFIFVTHDqgealsMS------DRVAVFNNGRIEQVDTPRDL 222
Cdd:COG1135 162 LLCDEATSALDpettrsiLDL-------LKDINRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDV 228
|
250
....*....|....*.
gi 2673334298 223 YMRPRTPFVAGFVGTS 238
Cdd:COG1135 229 FANPQSELTRRFLPTV 244
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-227 |
1.87e-63 |
|
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: 201.27 E-value: 1.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGD----VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE----- 75
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 76 RDVNTVFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 156 LLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPR 227
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-217 |
2.47e-63 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 200.21 E-value: 2.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 29 DGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFG------KEASELPPWERDVNTVFQDYALFPHMSILDNVAYGLm 102
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 103 vKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQ 182
Cdd:cd03297 101 -KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 2673334298 183 ELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVD 217
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-222 |
2.51e-63 |
|
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: 200.98 E-value: 2.51e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERD--- 77
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 --VNTVFQDYALFPHMSILDNVAYGL-MVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:COG1127 82 rrIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 155 VLLLDEPLGALD-------LKLreqmqfeLKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:COG1127 162 ILLYDEPTAGLDpitsaviDEL-------IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-213 |
3.44e-63 |
|
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: 199.68 E-value: 3.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEaseLPPWERDVNT---- 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLK---LTDDKKNINElrqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 ---VFQDYALFPHMSILDNVAYGLM-VKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:cd03262 78 vgmVFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 157 LLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
37-243 |
4.90e-61 |
|
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: 198.79 E-value: 4.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 37 GPSGSGKTTCLRLIAGFEQLSGGTISIFGK----EASE--LPPWERDVNTVFQDYALFPHMSILDNVAYGLmvKGIDKKK 110
Cdd:COG4148 32 GPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGifLPPHRRRIGYVFQEARLFPHLSVRGNLLYGR--KRAPRAE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 111 RHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIF 190
Cdd:COG4148 110 RRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILY 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 191 VTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTSNVFDA 243
Cdd:COG4148 190 VSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEA 242
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-222 |
1.14e-59 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 191.56 E-value: 1.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE-----RDVN 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPHMSILDNVAYGLMVKGIDKKKR-HAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 159 DEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-234 |
1.73e-59 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 191.07 E-value: 1.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDV----NT 80
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFPHMSILDNVAYG-LMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 160 EPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGF 234
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-213 |
8.21e-59 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 189.88 E-value: 8.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLY-GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP-----WERD 77
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrrLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 VNTVFQDYALFPHMSILDNVAYGL---------MVKGIDKKKRhAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARA 148
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGRlgrtstwrsLLGLFPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 149 LVNEPRVLLLDEPLGALDLKLREQ-MQFeLKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQvMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-222 |
9.96e-59 |
|
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: 188.93 E-value: 9.96e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQL-----SGGTISIFGKEASELPPWE---- 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 76 RDVNTVFQDYALFPhMSILDNVAYGLMVKGI-DKKKRHAQARDALEKVGLSFAVARK--PSQLSGGQRQRVAIARALVNE 152
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 153 PRVLLLDEPLGALDLKLREQMQFELKKLQQElgITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
15-229 |
2.66e-58 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 191.10 E-value: 2.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE-----RDVNTVFQD-YA-L 87
Cdd:COG4608 29 GVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYAsL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 88 FPHMSILDNVAYGLMVKGI-DKKKRHAQARDALEKVGLSFAVARK-PSQLSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:COG4608 109 NPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHADRyPHEFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 166 DLKLREQMQFELKKLQQELGITFIFVTHDqgeaLSM----SDRVAVFNNGRI-EQVDTpRDLYMRPRTP 229
Cdd:COG4608 189 DVSIQAQVLNLLEDLQDELGLTYLFISHD----LSVvrhiSDRVAVMYLGKIvEIAPR-DELYARPLHP 252
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-227 |
5.17e-58 |
|
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: 195.12 E-value: 5.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLY--GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAG---FEQLSGGTISIFGKEASELPPWE 75
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 76 R--DVNTVFQD--YALFPhMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVN 151
Cdd:COG1123 81 RgrRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 152 EPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPR 227
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
15-229 |
1.33e-57 |
|
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: 188.72 E-value: 1.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQ---LSGGTISIFGKEASELPPWE------RDVNTVFQD- 84
Cdd:COG0444 16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElrkirgREIQMIFQDp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 Y-ALFPHMSILDNVAYGLMV-KGIDKKKRHAQARDALEKVGLSFAVARK---PSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG0444 96 MtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQRVMIARALALEPKLLIAD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 160 EPLGALD-------LKLreqmqfeLKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDTpRDLYMRPRTP 229
Cdd:COG0444 176 EPTTALDvtiqaqiLNL-------LKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIvEEGPV-EELFENPRHP 245
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
9-202 |
3.23e-57 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 186.06 E-value: 3.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 9 NVSRL---YGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKeASELPPWERDVntVFQDY 85
Cdd:PRK11248 3 QISHLyadYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-PVEGPGAERGV--VFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 86 ALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 2673334298 166 DLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMS 202
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMA 196
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-229 |
4.15e-56 |
|
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: 190.67 E-value: 4.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 12 RLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTC----LRLIAgfeqlSGGTISIFGKE-----ASELPPWERDVNTVF 82
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDldglsRRALRPLRRRMQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 83 QD-YA-LFPHMSILDNVAYGLMVKGI--DKKKRHAQARDALEKVGLSFAVA-RKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:COG4172 369 QDpFGsLSPRMTVGQIIAEGLRVHGPglSAAERRARVAEALEEVGLDPAARhRYPHEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 158 LDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDTpRDLYMRPRTP 229
Cdd:COG4172 449 LDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVvEQGPT-EQVFDAPQHP 520
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-220 |
5.76e-56 |
|
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: 181.90 E-value: 5.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 20 VDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPwERDVntVFQDYALFPHMSILDNVAy 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DRMV--VFQNYSLLPWLTVRENIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 100 gLMVKGI----DKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQF 175
Cdd:TIGR01184 77 -LAVDRVlpdlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 176 ELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNN------GRIEQVDTPR 220
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNgpaaniGQILEVPFPR 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-212 |
9.33e-56 |
|
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: 180.74 E-value: 9.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGD--VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVNTV 81
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 FQ--DYALFpHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:cd03225 81 FQnpDDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 160 EPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
1.09e-55 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 181.44 E-value: 1.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASElpPWER---- 76
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR--ARRRigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 77 ----DVNtvfqdyALFPhMSILDNVAYGLMVK----GIDKKKRHAQARDALEKVGLSfAVARKP-SQLSGGQRQRVAIAR 147
Cdd:COG1121 81 pqraEVD------WDFP-ITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLE-DLADRPiGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 148 ALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI-----EQVDTPRDL 222
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVahgppEEVLTPENL 231
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-226 |
1.39e-55 |
|
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: 182.27 E-value: 1.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYG-----DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFG-----KEASELPPW 74
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrditaKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 75 ERDVNTVFQ--DYALFpHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVA-RKPSQLSGGQRQRVAIARALVN 151
Cdd:TIGR04521 81 RKKVGLVFQfpEHQLF-EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLeRSPFELSGGQMRRVAIAGVLAM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 152 EPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRP 226
Cdd:TIGR04521 160 EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-227 |
1.53e-54 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 179.10 E-value: 1.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 8 NNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTIsIFGkeASELPPWERDVNTVFQDYAL 87
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG--TAPLAEAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 88 FPHMSILDNVAYGLmvkgidKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:PRK11247 93 LPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 168 KLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIeQVDTPRDLyMRPR 227
Cdd:PRK11247 167 LTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI-GLDLTVDL-PRPR 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-213 |
2.26e-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: 178.15 E-value: 2.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGD-VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP-----WERDVN 79
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPHMSILDNVAYGL------------MVKGIDKKKrhaqARDALEKVGLSFAVARKPSQLSGGQRQRVAIAR 147
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGRlgrrstwrslfgLFPKEEKQR----ALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 148 ALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-206 |
1.32e-53 |
|
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: 175.13 E-value: 1.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY-GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEAS-----ELPPWERDV 78
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNrlrgrQLPLLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 79 NTVFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2673334298 159 DEPLGALDLKLREQMQFELKKLQQeLGITFIFVTHDqgeaLSMSDRVA 206
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHD----LSLVDRVA 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-222 |
1.89e-53 |
|
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: 175.82 E-value: 1.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP-WERDVNTVFQD 84
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPReARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 YALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 165 LDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:COG4555 163 LDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-222 |
2.89e-53 |
|
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: 175.62 E-value: 2.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVNTV 81
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 FQDYALFPHMSILDNVAYGLM----VKGIDKKKRHAQARDALEKVGLSfAVARKP-SQLSGGQRQRVAIARALVNEPRVL 156
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYphlgLFGRPSAEDREAVEEALERTGLE-HLADRPvDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 157 LLDEPLGALDLKlreqMQFE----LKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:COG1120 160 LLDEPTSHLDLA----HQLEvlelLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-213 |
3.68e-53 |
|
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: 175.23 E-value: 3.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERD--- 77
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 -VNTvFQDYALFPHMSILDNVAYGLMVKG---------------IDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQ 141
Cdd:COG0411 81 iART-FQNPRLFPELTVLENVLVAAHARLgrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 142 RVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-213 |
3.74e-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: 173.83 E-value: 3.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAirDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQD 84
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 YALFPHMSILDNVAYG----LMVKGIDKKKRHAqardALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:cd03298 79 NNLFAHLTVEQNVGLGlspgLKLTAEDRQAIEV----ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 161 PLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-213 |
1.09e-51 |
|
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: 168.73 E-value: 1.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP-WERDVNTVFQ 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEeVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 DYALFPHMSILDNVayglmvkgidkkkrhaqardalekvglsfavarkpsQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2673334298 164 ALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-213 |
4.78e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 168.46 E-value: 4.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVNTVFQ 83
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 DYALFPhMSILDNVAYGLMVKgiDKKKRHAQARDALEKVGLSFAVARKP-SQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:COG4619 82 EPALWG-GTVRDNLPFPFQLR--ERKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 163 GALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-216 |
4.39e-50 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 166.19 E-value: 4.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 25 IAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQDYALFPHMSILDNVAYG---- 100
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGlhpg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 101 LMVKGIDKKKRHAQARdaleKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKL 180
Cdd:TIGR01277 99 LKLNAEQQEKVVDAAQ----QVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 2673334298 181 QQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQV 216
Cdd:TIGR01277 175 CSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-213 |
5.37e-50 |
|
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: 166.46 E-value: 5.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 9 NVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP---WERDVNTVFQDY 85
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGRTFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 86 ALFPHMSILDNVAYG---------LMVKGIDKKKRH-AQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:cd03219 85 RLFPELTVLENVMVAaqartgsglLLARARREEREArERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 156 LLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-219 |
7.02e-50 |
|
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: 166.07 E-value: 7.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGD----VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEaseLPPWERD-- 77
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD---LFALDEDar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 -------VNTVFQDYALFPHMSILDNVAYGLMVKGidKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALV 150
Cdd:COG4181 85 arlrarhVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 151 NEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEAlSMSDRVAVFNNGRIEQVDTP 219
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAA 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-211 |
1.53e-49 |
|
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: 164.63 E-value: 1.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELP------PWERDVN 79
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyvPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TvfqdyaLFPhMSILDNVAYGL-----MVKGIDKKKRHAqARDALEKVGLSfAVARKP-SQLSGGQRQRVAIARALVNEP 153
Cdd:cd03235 81 R------DFP-ISVRDVVLMGLyghkgLFRRLSKADKAK-VDEALERVGLS-ELADRQiGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 154 RVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNG 211
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-232 |
3.74e-49 |
|
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: 167.98 E-value: 3.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 35 MLGPSGSGKTTCLRLIAGFEQLSGGTISIFG------KEASELPPWERDVNTVFQDYALFPHMSILDNVAYGLmvKGIDK 108
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsRKGIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYGM--KRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 109 KKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITF 188
Cdd:TIGR02142 106 SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2673334298 189 IFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVA 232
Cdd:TIGR02142 186 LYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-223 |
1.07e-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: 163.62 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYG-DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKE-----ASELPPWERDV 78
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitklrGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 79 NTVFQDYALFPHMSILDNVAYGL--------MVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALV 150
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 151 NEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-238 |
1.11e-48 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 163.82 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 2 TYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKE-------ASELPPW 74
Cdd:COG4598 6 PPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEirlkpdrDGELVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 75 ERD--------VNTVFQDYALFPHMSILDNVAYG-LMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAI 145
Cdd:COG4598 86 DRRqlqrirtrLGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 146 ARALVNEPRVLLLDEPLGALD-------LKLreqMQfelkKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDT 218
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDpelvgevLKV---MR----DLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237
|
250 260
....*....|....*....|
gi 2673334298 219 PRDLYMRPRTPFVAGFVGTS 238
Cdd:COG4598 238 PAEVFGNPKSERLRQFLSSS 257
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-202 |
1.25e-48 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 162.27 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGF--EQLSG-GTISIFGKEASELPPWERDVNTVF 82
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSAsGEVLLNGRRLTALPAEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 83 QDYALFPHMSILDNVAYGLmVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:COG4136 83 QDDLLFPHLSVGENLAFAL-PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2673334298 163 GALDLKLREQM-QFELKKLQQeLGITFIFVTHDQGEALSMS 202
Cdd:COG4136 162 SKLDAALRAQFrEFVFEQIRQ-RGIPALLVTHDEEDAPAAG 201
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-234 |
1.42e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 160.56 E-value: 1.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFG-----------KEASELp 72
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKAIREL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 73 pwERDVNTVFQDYALFPHMSILDNVAYGLM-VKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVN 151
Cdd:PRK11124 81 --RRNVGMVFQQYNLWPHLTVQQNLIEAPCrVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 152 EPRVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDtpRDLYMRPRTPF 230
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIvEQGD--ASCFTQPQTEA 235
|
....
gi 2673334298 231 VAGF 234
Cdd:PRK11124 236 FKNY 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-213 |
2.46e-47 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 159.11 E-value: 2.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY-GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASEL-----PPWERDV 78
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgraiPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 79 NTVFQDYALFPHMSILDNVAYGLMVkgIDKKKRHAQAR--DALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEV--TGVPPREIRKRvpAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 157 LLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-225 |
2.89e-47 |
|
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: 160.67 E-value: 2.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY--GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFG---KEASELppWE--RD 77
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtLDEENL--WEirKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 VNTVFQDyalfPhmsilDN----------VAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIAR 147
Cdd:TIGR04520 79 VGMVFQN----P-----DNqfvgatveddVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 148 ALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALsMSDRVAVFNNGRIEQVDTPRDLYMR 225
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-243 |
3.48e-47 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 164.05 E-value: 3.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 19 AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE------RDVNTVFQDYALFPHMS 92
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 93 ILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQ 172
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 173 MQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGF---VGTSNVFDA 243
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFfrgVDISQVFSA 276
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-218 |
3.82e-47 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 165.96 E-value: 3.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP---WERD 77
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 VNTVFQDYALFPHMSILDNVAYGLMVKG---IDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 155 VLLLDEPLGALDLKLREQMqFEL-KKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIeqVDT 218
Cdd:COG1129 161 VLILDEPTASLTEREVERL-FRIiRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-222 |
4.48e-47 |
|
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: 158.69 E-value: 4.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFG----KEASELppwERDVNT 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPREV---RRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 161 PLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
16-213 |
5.91e-47 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 158.28 E-value: 5.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 16 DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER------DVNTVFQDYALFP 89
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKLGFIYQFHHLLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 90 HMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKL 169
Cdd:TIGR02211 97 DFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2673334298 170 REQMqFEL-KKLQQELGITFIFVTHDQGEALSMsDRVAVFNNGRI 213
Cdd:TIGR02211 177 AKII-FDLmLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-227 |
7.54e-47 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 159.05 E-value: 7.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLR-------LIAGFEqlSGGTISIFGKE--ASEL 71
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDiyDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 72 PPWE--RDVNTVFQDYALFPhMSILDNVAYGLMVKGI-DKKKRHAQARDALEKVGL---------SFAVArkpsqLSGGQ 139
Cdd:COG1117 86 DVVElrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevkdrlkKSALG-----LSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 140 RQRVAIARALVNEPRVLLLDEPLGALD----LKLREQMQfELKKlqqelGITFIFVTHDQGEALSMSDRVAVFNNGRIEQ 215
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELIL-ELKK-----DYTIVIVTHNMQQAARVSDYTAFFYLGELVE 233
|
250
....*....|..
gi 2673334298 216 VDTPRDLYMRPR 227
Cdd:COG1117 234 FGPTEQIFTNPK 245
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-213 |
2.97e-46 |
|
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: 154.90 E-value: 2.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVNTVFQ 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 dyalfphmsildnvayglmvkgidkkkrhaqardALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 164 ALDLKlreqMQFE----LKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03214 127 HLDIA----HQIEllelLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-213 |
3.78e-46 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 156.67 E-value: 3.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 24 TIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQDYALFPHMSILDNVAYGLMV 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 104 KGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQE 183
Cdd:PRK10771 99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178
|
170 180 190
....*....|....*....|....*....|
gi 2673334298 184 LGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK10771 179 RQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-205 |
4.41e-46 |
|
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: 155.47 E-value: 4.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 9 NVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEAseLPPWERDVNT-------- 80
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQET--PPLNSKKASKfrreklgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2673334298 161 PLGALDLKLREQMQFELKKLQQElGITFIFVTHDQgEALSMSDRV 205
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRV 203
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-229 |
8.09e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 158.81 E-value: 8.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY----GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE----- 75
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 76 RDVNTVFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 156 LLLDEPLGALD-------LKLreqmqfeLKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRT 228
Cdd:PRK11153 162 LLCDEATSALDpattrsiLEL-------LKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKH 234
|
.
gi 2673334298 229 P 229
Cdd:PRK11153 235 P 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-237 |
4.72e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 154.14 E-value: 4.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISI----------FGKEASELPP 73
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarsLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 74 WERDVNTVFQDYALFPHMSILDNVAYG-LMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNE 152
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 153 PRVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTP--- 229
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPrtr 241
|
....*....
gi 2673334298 230 -FVAGFVGT 237
Cdd:PRK11264 242 qFLEKFLLQ 250
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-234 |
4.88e-45 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 154.02 E-value: 4.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFG-----------KEASELp 72
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpseKAIRLL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 73 pwERDVNTVFQDYALFPHMSILDN-VAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVN 151
Cdd:COG4161 81 --RQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 152 EPRVLLLDEPLGALDLKLREQMQFELKKLQQeLGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDTprDLYMRPRTPF 230
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIiEQGDA--SHFTQPQTEA 235
|
....
gi 2673334298 231 VAGF 234
Cdd:COG4161 236 FAHY 239
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-212 |
4.93e-45 |
|
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: 151.24 E-value: 4.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERdvntvfqdy 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 86 alfphmsildnvayglmvkgidkkkrhaqardaLEKVGLSFavarkpsQLSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:cd00267 72 ---------------------------------RRRIGYVP-------QLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2673334298 166 DLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:cd00267 112 DPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-225 |
6.82e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 154.89 E-value: 6.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVR---AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE-- 75
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 76 RDVNTVFQDY-ALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK13650 81 HKIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEaLSMSDRVAVFNNGRIEQVDTPRDLYMR 225
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-213 |
8.92e-45 |
|
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: 152.35 E-value: 8.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 9 NVSRLYGDVRAVDGVTIAIRDGeFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERD-VNTVFQDYAL 87
Cdd:cd03264 5 NLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQEFGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 88 FPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDl 167
Cdd:cd03264 84 YPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2673334298 168 kLREQMQFelKKLQQELG--ITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03264 163 -PEERIRF--RNLLSELGedRIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-161 |
1.32e-43 |
|
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: 147.02 E-value: 1.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 20 VDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKE--ASELPPWERDVNTVFQDYALFPHMSILDNV 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 98 AYGLMVKGIDKKKRHAQARDALEKVGLSFAVARK----PSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
20-225 |
1.37e-43 |
|
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: 151.11 E-value: 1.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 20 VDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP-----WERDVNTVFQDY--ALFPHMS 92
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRkqrraFRRDVQLVFQDSpsAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 93 ILDNVAYGLM-VKGIDKKKRHAQARDALEKVGLSFAVARK-PSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLR 170
Cdd:TIGR02769 107 VRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQ 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 171 EQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDTPRDLYMR 225
Cdd:TIGR02769 187 AVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIvEECDVAQLLSFK 242
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-213 |
1.10e-42 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 148.68 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 20 VDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELP-----PWERDVNTVFQDY--ALFPHMS 92
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkAFRRDIQMVFQDSisAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 93 ILDNVAYGLM-VKGIDKKKRHAQARDALEKVGLSFAVA-RKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLR 170
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLdKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2673334298 171 EQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-222 |
1.21e-42 |
|
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: 156.53 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVS-RLYGDVRAV-DGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP--WERDVN 79
Cdd:COG2274 473 DIELENVSfRYPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPasLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFpHMSILDNVAYGLmvKGIDKkkrhAQARDALEKVGLSFAVARKP-----------SQLSGGQRQRVAIARA 148
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLGD--PDATD----EEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 149 LVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQelGITFIFVTHDQgEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-222 |
1.30e-42 |
|
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: 146.81 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER---DVNTVF 82
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 83 QDYALFPHMSILDNVAYGLMVKGIDKKKRhaqardALEKVglsFAV--------ARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:cd03224 82 EGRRIFPELTVEENLLLGAYARRRAKRKA------RLERV---YELfprlkerrKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-213 |
2.23e-41 |
|
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: 143.51 E-value: 2.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQD 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 YALFPHMSILDNVAYGLMVKGIdKKKRHAQardALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGI-RKKRIDE---VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2673334298 165 LDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-222 |
2.51e-41 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 143.41 E-value: 2.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVR--AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKE-ASELPPWERDVNTV 81
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSiRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 FQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 162 LGALDLKLREQMQFELKKLQQELgiTFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-212 |
4.47e-41 |
|
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: 141.37 E-value: 4.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGD--VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP--WERDVNT 80
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLesLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFpHMSILDNVayglmvkgidkkkrhaqardalekvglsfavarkpsqLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 161 PLGALDLKLREQMQFELKKLQQelGITFIFVTHDQgEALSMSDRVAVFNNGR 212
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-223 |
1.86e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 143.26 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 18 RAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFG----KEASELPPWERDVNTVFQ--DYALFPHm 91
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditDKKVKLSDIRKKVGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 92 SILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVA--RKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKL 169
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYkdKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 170 REQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-229 |
6.09e-40 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 147.14 E-value: 6.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVRAVDGVTIAIRDGEFFSMLGPSGSGKT----TCLRLIAGFEQLSGGTISIFGKEASELPPWE------RDVNTVFQD 84
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 --YALFPHMSILDNVAYGLMV-KGIDKKKRHAQARDALEKVGL---SFAVARKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:COG4172 101 pmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 159 DEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI-EQVDTpRDLYMRPRTP 229
Cdd:COG4172 181 DEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIvEQGPT-AELFAAPQHP 251
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-213 |
1.00e-39 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 139.38 E-value: 1.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRA----VDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKE---ASE--LPPW 74
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLrkqvLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQElhgASKkqLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 75 ERDVNTVFQDYALFPHMSILDNVAYGL-MVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEP 153
Cdd:TIGR02982 81 RRRIGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 154 RVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQgEALSMSDRVAVFNNGRI 213
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDN-RILDVADRILQMEDGKL 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-226 |
1.80e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 140.71 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVR--AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGF---EQLSGGTISIFGKEASELPPWE-RD 77
Cdd:PRK13640 5 IVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDiRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 -VNTVFQDY-ALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK13640 85 kVGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 156 LLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEAlSMSDRVAVFNNGRIEQVDTPRDLYMRP 226
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-213 |
2.01e-39 |
|
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: 138.18 E-value: 2.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELP-------PWERd 77
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEER- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 vntvfqdyALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:cd03269 80 --------GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 158 LDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-213 |
2.21e-39 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 138.47 E-value: 2.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY-GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEAS-----ELPPWERDV 78
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 79 NTVFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 159 DEPLGALDLKLREQMqFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK10908 162 DEPTGNLDDALSEGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-213 |
3.19e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 140.24 E-value: 3.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELP-------PWER 76
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 77 dvntvfqdyALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:COG4152 81 ---------GLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 157 LLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
14-238 |
4.67e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 138.95 E-value: 4.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 14 YGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEAS---------------ELPPWERDV 78
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadknQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 79 NTVFQDYALFPHMSILDNVAYG-LMVKGIDKKKRHAQARDALEKVGLS-FAVARKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDeRAQGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 157 LLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVG 236
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
..
gi 2673334298 237 TS 238
Cdd:PRK10619 254 GS 255
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-213 |
4.93e-39 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 146.02 E-value: 4.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLY----GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE- 75
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 76 -----RDVNTVFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALV 150
Cdd:PRK10535 81 aqlrrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 151 NEPRVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEAlSMSDRVAVFNNGRI 213
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEI 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-223 |
5.52e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 139.38 E-value: 5.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 19 AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVNTVFQDY-ALFPHMSILD 95
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGMVFQNPdNQFVGATVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 96 NVAYGLMVKGIDKKKRHAQARDALEKVGL-SFAvARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQ 174
Cdd:PRK13635 102 DVAFGLENIGVPREEMVERVDQALRQVGMeDFL-NREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2673334298 175 FELKKLQQELGITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:PRK13635 181 ETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-223 |
6.59e-39 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 144.90 E-value: 6.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGD-VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP--WERDVNT 80
Cdd:COG4988 336 SIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPasWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFpHMSILDNVAYGlmvkgidkkKRHA---QARDALEKVGLSFAVARKP-----------SQLSGGQRQRVAIA 146
Cdd:COG4988 416 VPQNPYLF-AGTIRENLRLG---------RPDAsdeELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 147 RALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQelGITFIFVTHDQgEALSMSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-213 |
8.16e-39 |
|
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: 137.91 E-value: 8.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFE-QLSGGTISIFGKEASELPPWE-RD---- 77
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRGGEDVWElRKrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 VNTVFQDYaLFPHMSILDNVAYGLM-VKGIDKK---KRHAQARDALEKVGLSfAVARKP-SQLSGGQRQRVAIARALVNE 152
Cdd:COG1119 83 VSPALQLR-FPRDETVLDVVLSGFFdSIGLYREptdEQRERARELLELLGLA-HLADRPfGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 153 PRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-222 |
1.21e-38 |
|
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: 143.40 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 9 NVSRLY-----GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISI-FGKE---ASELPPWERD-- 77
Cdd:TIGR03269 284 NVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEwvdMTKPGPDGRGra 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 ---VNTVFQDYALFPHMSILDNVA-----------------YGLMVKGIDKKKrhaqARDALEKVglsfavarkPSQLSG 137
Cdd:TIGR03269 364 kryIGILHQEYDLYPHRTVLDNLTeaiglelpdelarmkavITLKMVGFDEEK----AEEILDKY---------PDELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 138 GQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVD 217
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
....*
gi 2673334298 218 TPRDL 222
Cdd:TIGR03269 511 DPEEI 515
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-222 |
1.86e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 143.77 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLY-GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP--WERDVNT 80
Cdd:COG1132 339 EIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLesLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFpHMSILDNVAYGLmvKGIDkkkrHAQARDALEKVGLSFAVARKP-----------SQLSGGQRQRVAIARAL 149
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYGR--PDAT----DEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 150 VNEPRVLLLDEPLGALDLKLREQMQFELKKLQQelGITFIFVTHDqgeaLS---MSDRVAVFNNGRIEQVDTPRDL 222
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHR----LStirNADRILVLDDGRIVEQGTHEEL 561
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-226 |
3.64e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 137.46 E-value: 3.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 18 RAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISI------FGKEASELPPWERDVNTVFQ--DYALFP 89
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKPLRKKVGIVFQfpEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 90 HmSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAV-ARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:PRK13634 101 E-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 169 LREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRP 226
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
4-221 |
3.74e-38 |
|
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: 143.85 E-value: 3.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLY-GDVR-AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVN 79
Cdd:TIGR03375 463 EIEFRNVSFAYpGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFpHMSILDNVAYGlmvkgidkkkrHAQARD-----ALEKVGLSFAVARKPS-----------QLSGGQRQRV 143
Cdd:TIGR03375 543 YVPQDPRLF-YGTLRDNIALG-----------APYADDeeilrAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAV 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 144 AIARALVNEPRVLLLDEPLGALDlkLREQMQFeLKKLQQEL-GITFIFVTHdQGEALSMSDRVAVFNNGRIeQVDTPRD 221
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMD--NRSEERF-KDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGRI-VADGPKD 684
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-194 |
5.06e-38 |
|
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: 134.53 E-value: 5.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP-WERDVNTVFQ 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 DYALFPHMSILDNVAYGLMVKGIDKkkRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRA--DREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2673334298 164 ALDLK----LREQMQFELKKlqqelGITFIFVTHD 194
Cdd:COG4133 161 ALDAAgvalLAELIAAHLAR-----GGAVLLTTHQ 190
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-213 |
5.07e-38 |
|
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: 135.02 E-value: 5.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGD--VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVN 79
Cdd:cd03245 2 RIEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFpHMSILDNVAYG------------LMVKGIDK-KKRHAQardalekvGLSFAVARKPSQLSGGQRQRVAIA 146
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLGapladderilraAELAGVTDfVNKHPN--------GLDLQIGERGRGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 147 RALVNEPRVLLLDEPLGALDLKLREQMqfeLKKLQQEL-GITFIFVTHDQgEALSMSDRVAVFNNGRI 213
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERL---KERLRQLLgDKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
6.80e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 135.74 E-value: 6.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSG-----GTISIFGKE--ASELPP 73
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNiySPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 74 WE--RDVNTVFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARD--ALEKVGLSFAVARK----PSQLSGGQRQRVAI 145
Cdd:PRK14267 81 IEvrREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVewALKKAALWDEVKDRlndyPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 146 ARALVNEPRVLLLDEPLGALD---LKLREQMQFELKKlqqelGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-----EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
....*
gi 2673334298 223 YMRPR 227
Cdd:PRK14267 236 FENPE 240
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-230 |
1.03e-37 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 137.14 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 18 RAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER-----DVNTVFQD--YALFPH 90
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 91 MSILDNVAYGLMV--KGIDKKKRHAQARDALEKVGL-SFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:PRK15079 115 MTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 168 KLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPF 230
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPY 257
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-213 |
1.15e-37 |
|
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: 134.03 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVR----AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELP-PWERDVN 79
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 160 EPLGALDLkLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03266 162 EPTTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-230 |
1.29e-37 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 137.31 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 37 GPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASE------LPPWERDVNTVFQDYALFPHMSILDNVAYGLmvkgidKKK 110
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKRRIGYVFQDARLFPHYKVRGNLRYGM------AKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 111 RHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL-KLREQMQFeLKKLQQELGITFI 189
Cdd:PRK11144 105 MVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLpRKRELLPY-LERLAREINIPIL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2673334298 190 FVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLY----MRPRTPF 230
Cdd:PRK11144 184 YVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWassaMRPWLPK 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-222 |
1.34e-37 |
|
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: 134.34 E-value: 1.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER---DVNTVF 82
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 83 QDYALFPHMSILDNvaygLMVkGIDKKKRHAQARDALEKVglsFAV--------ARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:COG0410 85 EGRRIFPSLTVEEN----LLL-GAYARRDRAEVRADLERV---YELfprlkerrRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 155 VLLLDEP-LGaLDLKLREQMqFE-LKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:COG0410 157 LLLLDEPsLG-LAPLIVEEI-FEiIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-223 |
1.35e-37 |
|
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: 134.20 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY---GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASEL-PPWERD-VN 79
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLnLRWLRSqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPhMSILDNVAYGL---MVKGIDKKKRHAQARDALEKV--GLSFAVARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYGKpdaTDEEVEEAAKKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQelGITFIFVTHdQGEALSMSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-235 |
3.28e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 133.88 E-value: 3.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRL------------IAGFEQLSGGtiSIFGKEASELp 72
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLDGQ--DIFKMDVIEL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 73 pwERDVNTVFQDYALFPHMSILDNVAYGLMVKGIDKKKRHAQAR--DALEKVGLSFAVARK----PSQLSGGQRQRVAIA 146
Cdd:PRK14247 81 --RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQERvrWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 147 RALVNEPRVLLLDEPLGALD----LKLrEQMQFELKKlqqelGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDpentAKI-ESLFLELKK-----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
250
....*....|...
gi 2673334298 223 YMRPRTPFVAGFV 235
Cdd:PRK14247 233 FTNPRHELTEKYV 245
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-230 |
8.49e-37 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 134.71 E-value: 8.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 17 VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE-----RDVNTVFQD-YA-LFP 89
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 90 HMSILDNVAYGLMVK-GIDKKKRHAQARDALEKVGL--SFAvARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:PRK11308 108 RKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLrpEHY-DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 167 LKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPF 230
Cdd:PRK11308 187 VSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPY 250
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-221 |
8.79e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 132.93 E-value: 8.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 8 NNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE----RDVntVFQ 83
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElarrRAV--LPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 DYAL-FPhMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALV-------NEPRV 155
Cdd:COG4559 83 HSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 156 LLLDEPLGALDlkLREQMQF--ELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRD 221
Cdd:COG4559 162 LFLDEPTSALD--LAHQHAVlrLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-213 |
1.67e-36 |
|
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: 129.09 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWErdvntvfqd 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 yalfphmsildnvayglmvkgidkkkrhaqARDAleKVGLSFavarkpsQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03216 72 ------------------------------ARRA--GIAMVY-------QLSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2673334298 165 LDLKLREQMqFE-LKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03216 113 LTPAEVERL-FKvIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
2.66e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.04 E-value: 2.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVR--AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASE--LPPWERDVN 79
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQ--DYAlFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:PRK13632 87 IIFQnpDNQ-FIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 158 LDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALsMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-218 |
2.67e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 136.70 E-value: 2.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPweRD--- 77
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSP--RDaia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 --VNTVFQDYALFPHMSILDNVAYGLMVKG---IDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNE 152
Cdd:COG3845 80 lgIGMVHQHFMLVPNLTVAENIVLGLEPTKggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 153 PRVLLLDEPLGALDLKLREQMqFE-LKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGR-IEQVDT 218
Cdd:COG3845 160 ARILILDEPTAVLTPQEADEL-FEiLRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKvVGTVDT 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-235 |
6.80e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 130.55 E-value: 6.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 9 NVSRLY---GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISI------FGKEASELPP--WERD 77
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkvlyFGKDIFQIDAikLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 VNTVFQDYALFPHMSILDNVAYGLMVKGI-DKKKRHAQARDALEKVGLSFAVARK----PSQLSGGQRQRVAIARALVNE 152
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIAYPLKSHGIkEKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 153 PRVLLLDEPLGALDLKLREQMQFELKKLQQElgITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVA 232
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
...
gi 2673334298 233 GFV 235
Cdd:PRK14246 250 KYV 252
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-223 |
8.56e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 131.10 E-value: 8.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYG-----DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEAS------ELP 72
Cdd:PRK13641 2 SIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 73 PWERDVNTVFQ--DYALFPHmSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARK-PSQLSGGQRQRVAIARAL 149
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKsPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 150 VNEPRVLLLDEPLGALDLKLREQMqFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-205 |
2.86e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 128.01 E-value: 2.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 23 VTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPW------ERDVNTVFQDYALFPHMSILDN 96
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaelrNQKLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 97 VAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFE 176
Cdd:PRK11629 108 VAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQL 187
|
170 180
....*....|....*....|....*....
gi 2673334298 177 LKKLQQELGITFIFVTHDQGEALSMSDRV 205
Cdd:PRK11629 188 LGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-244 |
4.51e-35 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 134.60 E-value: 4.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 7 FNNVSRlygDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKE-----ASELPPWERDVNTV 81
Cdd:PRK10261 330 LNRVTR---EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidtlsPGKLQALRRDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 FQD-YA-LFPHMSILDNVAYGLMVKGIDKKKRhAQARDA--LEKVGLSFAVA-RKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:PRK10261 407 FQDpYAsLDPRQTVGDSIMEPLRVHGLLPGKA-AAARVAwlLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 157 LLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVG 236
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMA 565
|
....*...
gi 2673334298 237 TSNVFDAG 244
Cdd:PRK10261 566 AVPVADPS 573
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-213 |
6.08e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 128.28 E-value: 6.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 17 VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER--DVNTVFQDYAL--FPHMS 92
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakYIGRVFQDPMMgtAPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 93 ILDNVA--------YGLmVKGIDKKKRhAQARDALEKVGLSFAvAR---KPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:COG1101 99 IEENLAlayrrgkrRGL-RRGLTKKRR-ELFRELLATLGLGLE-NRldtKVGLLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 162 LGALDLKlREQMQFEL-KKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG1101 176 TAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-227 |
8.69e-35 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 127.41 E-value: 8.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE---RDVNTVF 82
Cdd:PRK11300 7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarMGVVRTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 83 QDYALFPHMSILDN--VAYGLMVK-----------GIDKKKRHAQARDA--LEKVGLSFAVARKPSQLSGGQRQRVAIAR 147
Cdd:PRK11300 87 QHVRLFREMTVIENllVAQHQQLKtglfsgllktpAFRRAESEALDRAAtwLERVGLLEHANRQAGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 148 ALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPR 227
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-221 |
1.25e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 127.20 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 8 NNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE----RDVntVFQ 83
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarrRAV--LPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 DYAL-FPhMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALV------NEPRVL 156
Cdd:PRK13548 84 HSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 157 LLDEPLGALDlkLREQ---MQFeLKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRD 221
Cdd:PRK13548 163 LLDEPTSALD--LAHQhhvLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-226 |
1.52e-34 |
|
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: 132.58 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 3 YAVEFNNVSRLY--GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP--WERDV 78
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEddLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 79 NTVFQDYALFpHMSILDNVAYGlmvkgiDKKKRHAQARDALEKVGLSFAVARKP-----------SQLSGGQRQRVAIAR 147
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLRLA------RPDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 148 ALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQelGITFIFVTHDQgEALSMSDRVAVFNNGRIEQVDTPRDLYMRP 226
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-213 |
3.21e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 125.35 E-value: 3.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 9 NVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER---DVNTVFQDY 85
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 86 ALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:cd03218 85 SIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2673334298 166 DLKLREQMQFELKKLqQELGITfIFVT-HDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03218 165 DPIAVQDIQKIIKIL-KDRGIG-VLITdHNVRETLSITDRAYIIYEGKV 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-225 |
7.49e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 130.60 E-value: 7.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 12 RLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTC----LRLIAgfeqlSGGTISIFGK-----EASELPPWERDVNTVF 82
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQplhnlNRRQLLPVRHRIQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 83 QD--YALFPHMSILDNVAYGLMV--KGIDKKKRHAQARDALEKVGLSFAV-ARKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:PRK15134 369 QDpnSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 158 LDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGR-IEQVD------TPRDLYMR 225
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEvVEQGDcervfaAPQQEYTR 523
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-194 |
7.64e-34 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 124.12 E-value: 7.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 22 GVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER------DVNTVFQDYALFPHMSILD 95
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 96 NVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQF 175
Cdd:PRK10584 108 NVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170
....*....|....*....
gi 2673334298 176 ELKKLQQELGITFIFVTHD 194
Cdd:PRK10584 188 LLFSLNREHGTTLILVTHD 206
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-213 |
9.75e-34 |
|
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: 124.12 E-value: 9.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY---GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEAS--ELPPWERDVN 79
Cdd:cd03248 12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPHmSILDNVAYGLMVKGIDKKKRHAQARDA------LEKvGLSFAVARKPSQLSGGQRQRVAIARALVNEP 153
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYGLQSCSFECVKEAAQKAHAhsfiseLAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 154 RVLLLDEPLGALDLKLREQMQfelKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQ---QALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-213 |
1.39e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 125.58 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 18 RAVDGVTIAIRDGEFFSMLGPSGSGKTTclrLIAGFEQL---SGGTISIF-----GKEASELPPWE-------------- 75
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTT---FIEHLNALllpDTGTIEWIfkdekNKKKTKEKEKVleklviqktrfkki 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 76 -------RDVNTVFQ--DYALFpHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGL--SFaVARKPSQLSGGQRQRVA 144
Cdd:PRK13651 98 kkikeirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdeSY-LQRSPFELSGGQKRRVA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 145 IARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-226 |
1.72e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 124.12 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAV-EFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLS-----GGTISIFGK-------E 67
Cdd:PRK14239 1 MTEPIlQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHniysprtD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 68 ASELppwERDVNTVFQDYALFPhMSILDNVAYGLMVKGIDKKKRHAQA--------------RDALEKVGLSfavarkps 133
Cdd:PRK14239 81 TVDL---RKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAvekslkgasiwdevKDRLHDSALG-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 134 qLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELgiTFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK14239 149 -LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDL 225
|
250
....*....|...
gi 2673334298 214 EQVDTPRDLYMRP 226
Cdd:PRK14239 226 IEYNDTKQMFMNP 238
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-213 |
9.08e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 122.54 E-value: 9.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGD-VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEAS-ELPPWERD- 77
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaENEKWVRSk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 VNTVFQDY--ALFPhMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK13647 81 VGLVFQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 156 LLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-222 |
2.58e-32 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 119.96 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 30 GEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASelpPWERDVNTVFQ------DYALFPHMSILDNVAYGLMV 103
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPG---KGWRHIGYVPQrhefawDFPISVAHTVMSGRTGHIGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 104 KGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQE 183
Cdd:TIGR03771 83 LRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELAGA 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 2673334298 184 lGITFIFVTHDQGEALSMSDRVAVFnNGRIEQVDTPRDL 222
Cdd:TIGR03771 163 -GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQL 199
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-223 |
2.93e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 121.39 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYG-----DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEAS------ELP 72
Cdd:PRK13649 2 GINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 73 PWERDVNTVFQdyalFPHM-----SILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAV-ARKPSQLSGGQRQRVAIA 146
Cdd:PRK13649 82 QIRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 147 RALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
15-218 |
4.57e-32 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 120.71 E-value: 4.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGK--EASELPPWERDVNTVFQD--YALFPH 90
Cdd:COG4167 24 QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHklEYGDYKYRCKHIRMIFQDpnTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 91 M---SILD-----NVAYglmvkgiDKKKRHAQARDALEKVGL-----SFavarKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:COG4167 104 LnigQILEeplrlNTDL-------TAEEREERIFATLRLVGLlpehaNF----YPHMLSSGQKQRVALARALILQPKIII 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 158 LDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGR-IEQVDT 218
Cdd:COG4167 173 ADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEvVEYGKT 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-209 |
5.17e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 120.27 E-value: 5.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 2 TYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLR-------LIAGFEqlSGGTISIFGKE--ASELP 72
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNlyAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 73 PWE--RDVNTVFQDYALFPHmSILDNVAYGLMVKG--------IDKKKRHA----QARDALEKVGLSfavarkpsqLSGG 138
Cdd:PRK14243 86 PVEvrRRIGMVFQKPNPFPK-SIYDNIAYGARINGykgdmdelVERSLRQAalwdEVKDKLKQSGLS---------LSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 139 QRQRVAIARALVNEPRVLLLDEPLGALD----LKLREQMQfELKKlqqelGITFIFVTHDQGEALSMSDRVAVFN 209
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDpistLRIEELMH-ELKE-----QYTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-228 |
8.17e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.18 E-value: 8.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGD-VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKE----ASELPPWERDVN 79
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikydKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQ--DYALFPHmSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:PRK13639 82 IVFQnpDDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 158 LDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRT 228
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-223 |
9.66e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 119.86 E-value: 9.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY-GDVR-AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTIsIFGKE---ASELPPWERDVN 79
Cdd:PRK13648 8 IVFKNVSFQYqSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQaitDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQD-YALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:PRK13648 87 IVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 159 DEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-222 |
2.33e-31 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 117.71 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVR-AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELP--PWERDVNTV 81
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 FQDYALFPHmSILDNVAYG---LMVKGIDKKKRHAQARDALEKV--GLSFAVARKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGrpnATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 157 LLDEPLGALDLKLREQMQFELKKLQQelGITFIFVTHdqgeALSM---SDRVAVFNNGRIEQVDTPRDL 222
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH----RLSTiknADKILVLDDGKIIEEGTHDEL 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
14-213 |
2.73e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 117.82 E-value: 2.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 14 YGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER---DVNTVFQDYALFPH 90
Cdd:COG1137 13 YGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarlGIGYLPQEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 91 MSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSfAVARKP-SQLSGGQRQRVAIARALVNEPRVLLLDE------PLG 163
Cdd:COG1137 93 LTVEDNILAVLELRKLSKKEREERLEELLEEFGIT-HLRKSKaYSLSGGERRRVEIARALATNPKFILLDEpfagvdPIA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 164 ALDLKlreQMQFELKklqqELGITfIFVT-HDQGEALSMSDRVAVFNNGRI 213
Cdd:COG1137 172 VADIQ---KIIRHLK----ERGIG-VLITdHNVRETLGICDRAYIISEGKV 214
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-222 |
3.01e-31 |
|
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: 123.29 E-value: 3.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYG--DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASE--LPPWERDVNT 80
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFPHmSILDNVAYGLMVKGIDKK-KRHAQARDALEKV-----GLSFAVARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGRTEQADRAEiERALAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQelGITFIFVTHdqgeALSM---SDRVAVFNNGRIEQVDTPRDL 222
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH----RLSTiekADRIVVMDDGRIVERGTHNEL 554
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-223 |
3.42e-31 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 117.33 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGD--VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASE--LPPWERDVNT 80
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFpHMSILDNVAYGLMVKGIDKKKRHAQARDALEKV-----GLSFAVARKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGRPGATREEVEEAARAANAHEFImelpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 156 LLLDEPLGALDLKLREQMQFELKKLQQelGITFIFVTHdqgeALSM---SDRVAVFNNGRIEQVDTPRDLY 223
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMK--NRTTFVIAH----RLSTienADRIVVLEDGKIVERGTHEELL 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
15-233 |
7.10e-31 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 119.06 E-value: 7.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGF---EQLSGGTISIFGKEASELPpwERDVN--------TVFQ 83
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLP--EKELNklraeqisMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 D--YALFPHMSILDNVAYGLMV-KGIDKKKRHAQARDALEKVGLSfaVARK-----PSQLSGGQRQRVAIARALVNEPRV 155
Cdd:PRK09473 105 DpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMP--EARKrmkmyPHEFSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 156 LLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAG 233
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIG 260
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-226 |
8.00e-31 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 116.31 E-value: 8.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 19 AVDGVTIAIRDGEFFSMLGPSGSGKT-TCLRLI----AGFEQLSGgTISIFGKEASELPPWERDVNTVFQD--YALFPHM 91
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSlTCLAILgllpPGLTQTSG-EILLDGRPLLPLSIRGRHIATIMQNprTAFNPLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 92 SILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFA---VARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:TIGR02770 80 TMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPeevLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 169 LREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRP 226
Cdd:TIGR02770 160 NQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNP 217
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-213 |
1.24e-30 |
|
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: 115.70 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER---DVNTVF 82
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 83 QDYALFPHMSILDNVAYGLMVKGIDKKKRHAQARD---ALEKVglsfaVARKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYElfpVLKEM-----LGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 160 EPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-222 |
1.45e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 117.60 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERD-VN 79
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPHMSILDNvaygLMVKGIDKKKRHAQARDALEKVgLSFA-----VARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK13537 84 VVPQFDNLDPDFTVREN----LLVFGRYFGLSAAAARALVPPL-LEFAklenkADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-223 |
1.90e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.80 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYG-----DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEAS------ELPP 73
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 74 WERDVNTVFQdyalFPHMSIL-DNVA----YGLMVKGIDKKKRHAQARDALEKVGLSFAVARK-PSQLSGGQRQRVAIAR 147
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFeDTVEreiiFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 148 ALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-226 |
2.05e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 121.75 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY---GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP--WERDVN 79
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHhyLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPHmSILDNVAYGLMVKGIDKKKRHAQARDALEKV-----GLSFAVARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFImefpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 155 VLLLDEPLGALDLKLrEQMQFELKKLQqelGITFIFVTHDqgeaLSM---SDRVAVFNNGRIEQVDTPRDLYMRP 226
Cdd:TIGR00958 638 VLILDEATSALDAEC-EQLLQESRSRA---SRTVLLIAHR----LSTverADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
9-222 |
4.03e-30 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 114.68 E-value: 4.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 9 NVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER---DVNTVFQDY 85
Cdd:TIGR04406 6 NLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERarlGIGYLPQEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 86 ALFPHMSILDNVAYGL-MVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:TIGR04406 86 SIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 165 LDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:TIGR04406 166 VDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
4-222 |
9.80e-30 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 119.68 E-value: 9.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGD--VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVN 79
Cdd:TIGR03797 451 AIEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAvrRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPHmSILDNVAYGLMVKgidkkkrHAQARDALEKVGLSFAVARKP-----------SQLSGGQRQRVAIARA 148
Cdd:TIGR03797 531 VVLQNGRLMSG-SIFENIAGGAPLT-------LDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARA 602
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 149 LVNEPRVLLLDEPLGALDLKLREQMQFELKKLQqelgITFIFVTHdqgeALSM---SDRVAVFNNGRIEQVDTPRDL 222
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAH----RLSTirnADRIYVLDAGRVVQQGTYDEL 671
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-222 |
1.38e-29 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 113.09 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAV-DGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASE--LPPWERDVNTV 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVlKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 FQDYALFpHMSILDNVAYGLMVKGIDKKKRHAQARDALEKV-----GLSFAVARKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKImrfpdGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 157 LLDEPLGALDLKLREQMQFELKKLQQelGITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDTPRDL 222
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-213 |
1.53e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 111.15 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGDVRA--VDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP--WERDVNTV 81
Cdd:cd03246 2 EVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPneLGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 FQDYALFPHmSILDNVayglmvkgidkkkrhaqardalekvglsfavarkpsqLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:cd03246 82 PQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 162 LGALDLKlREQMQFELKKLQQELGITFIFVTHdQGEALSMSDRVAVFNNGRI 213
Cdd:cd03246 124 NSHLDVE-GERALNQAIAALKAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-220 |
1.86e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 113.57 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGF----------EQLSGGTISIFGKEASE 70
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 71 LPPWERDVNTVFQDYALFPHMSILDNVAYGLM---------VKGIDKKKRHaQARDALEKVGLSFAVARKPSQLSGGQRQ 141
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQ-RALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 142 RVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVA------VFNNGRIEQ 215
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIValrqghVFYDGSSQQ 239
|
....*
gi 2673334298 216 VDTPR 220
Cdd:PRK09984 240 FDNER 244
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-223 |
2.01e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.17 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 3 YAVEFNNVSRLYGD-VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGK----EASELPPWERD 77
Cdd:PRK13636 4 YILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidySRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 VNTVFQ--DYALFPhMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSfAVARKPSQ-LSGGQRQRVAIARALVNEPR 154
Cdd:PRK13636 84 VGMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIE-HLKDKPTHcLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-213 |
3.11e-29 |
|
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: 111.19 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 9 NVSRLYGDV-RAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEAselPPWER--DVNTVFQD- 84
Cdd:cd03226 4 NISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERrkSIGYVMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 -YALFPHmSILDNVAYGLMvkgiDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:cd03226 81 dYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2673334298 164 ALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-223 |
3.43e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 113.68 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 18 RAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISI------FGKEASELPPWERDVNTVFQ--DYALFP 89
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsSTSKQKEIKPVRKKVGVVFQfpESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 90 HmSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARK-PSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:PRK13643 100 E-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 169 LREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:PRK13643 179 ARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-226 |
3.93e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 112.48 E-value: 3.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPwerdvntvfQD 84
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS---------RE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 YALfpHMSIL--DN-VAYGLMV------------KGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARAL 149
Cdd:COG4604 73 LAK--RLAILrqENhINSRLTVrelvafgrfpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 150 VNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLyMRP 226
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI-ITP 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
16-223 |
3.95e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 113.26 E-value: 3.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 16 DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPW--ERDVNTVFQDY-ALFPHMS 92
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWnlRRKIGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 93 ILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQ 172
Cdd:PRK13642 99 VEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 173 MQFELKKLQQELGITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-243 |
5.10e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 115.32 E-value: 5.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVNTVF 82
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 83 QDYAL--------------FPHMSILDnvayglmvkGIDKKKRHAqARDALEKVGLSFAVARKPSQLSGGQRQRVAIARA 148
Cdd:PRK09536 84 QDTSLsfefdvrqvvemgrTPHRSRFD---------TWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 149 LVNEPRVLLLDEPLGALDLKlREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRP-- 226
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDIN-HQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADtl 232
|
250
....*....|....*...
gi 2673334298 227 RTPFVA-GFVGTSNVFDA 243
Cdd:PRK09536 233 RAAFDArTAVGTDPATGA 250
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-194 |
5.11e-29 |
|
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: 116.62 E-value: 5.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVR-AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP--WERDVNT 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAdsWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFPHmSILDNVAYGLMVKGIDKKKRHAQARDALEKV-----GLSFAVARKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190
....*....|....*....|....*....|....*....
gi 2673334298 156 LLLDEPLGALDLKLREQMQFELKKLQQelGITFIFVTHD 194
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR 516
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-223 |
6.70e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.49 E-value: 6.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVR------AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP- 73
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 74 WE--RDVNTVFQDyalfPHMSIL-----DNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIA 146
Cdd:PRK13633 81 WDirNKAGMVFQN----PDNQIVativeEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 147 RALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-216 |
9.95e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 111.67 E-value: 9.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSG-----GTISIFGKEASE----LPPW 74
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrvnLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 75 ERDVNTVFQDYALFPhMSILDNVAYGLMVKGIDKK-KRHAQARDALEKVGLSFAVARK----PSQLSGGQRQRVAIARAL 149
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 150 VNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVF--NNGRIEQV 216
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQL 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-213 |
2.45e-28 |
|
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: 109.73 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 10 VSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGkeaseLPPWERDVNTVFQDYALFP 89
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVPWKRRKKFLRRIGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 90 H-------MSILDNVAYGLMVKGIDK---KKRHAQARDALEKVGLSFAVARkpsQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:cd03267 102 QktqlwwdLPVIDSFYLLAAIYDLPParfKKRLDELSELLDLEELLDTPVR---QLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 160 EPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-223 |
3.62e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 110.02 E-value: 3.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 8 NNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEAS-----ELPPWER------ 76
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdlyALSEAERrrllrt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 77 DVNTVFQDYA--LFPHMSILDNVAYGLMVKGidkkKRH-----AQARDALEKVGLsfAVAR---KPSQLSGGQRQRVAIA 146
Cdd:PRK11701 90 EWGFVHQHPRdgLRMQVSAGGNIGERLMAVG----ARHygdirATAGDWLERVEI--DAARiddLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 147 RALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI------EQV-DTP 219
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVvesgltDQVlDDP 243
|
....
gi 2673334298 220 RDLY 223
Cdd:PRK11701 244 QHPY 247
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-236 |
1.32e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 112.70 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKE---ASELPPWERD 77
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 VNTVFQDYALFPHMSILDNVAYG-LMVKG--IDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGqLPHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRieQVDTPRDLYMRPRTPFVAGF 234
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGR--YVATFDDMAQVDRDQLVQAM 237
|
..
gi 2673334298 235 VG 236
Cdd:PRK11288 238 VG 239
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-236 |
1.48e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 109.03 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 9 NVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGF-EQLSG---------GTISIFGKEasELPPWERDV 78
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSGyrysgdvllGGRSIFNYR--DVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 79 NTVFQDYALFPhMSILDNVAYGLMV-KGIDKKKRHAQARDALEKVGLSFAVARK----PSQLSGGQRQRVAIARALVNEP 153
Cdd:PRK14271 104 GMLFQRPNPFP-MSIMDNVLAGVRAhKLVPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 154 RVLLLDEPLGALDLKLREQMQFELKKLQQELgiTFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPR----TP 229
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKhaetAR 260
|
....*..
gi 2673334298 230 FVAGFVG 236
Cdd:PRK14271 261 YVAGLSG 267
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-214 |
3.72e-27 |
|
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: 106.46 E-value: 3.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 14 YGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELppwerDVNTVFQdyalfPHMSI 93
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN-----PELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 94 LDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQM 173
Cdd:cd03220 102 RENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2673334298 174 QFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIE 214
Cdd:cd03220 182 QRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-222 |
4.14e-27 |
|
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: 112.14 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYG-DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVNTV 81
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 FQDYALFPHmSILDNVAYG----LMVKGIDKKKRHAQARDALEKV--GLSFAVARKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGakenVSQDEIWAACEIAEIKDDIENMplGYQTELSEEGSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 156 LLLDEPLGALDLKLREQMQFELKKLQQElgiTFIFVTHdQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAH-RLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-223 |
4.20e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.79 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 7 FNNVSRLYG-----DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTiSIFG--------KEASELPP 73
Cdd:PRK13645 9 LDNVSYTYAkktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGdyaipanlKKIKEVKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 74 WERDVNTVFQ--DYALFPHmSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFA-VARKPSQLSGGQRQRVAIARALV 150
Cdd:PRK13645 88 LRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 151 NEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-226 |
5.40e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 107.16 E-value: 5.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEA-----SELPPWERDVN 79
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPHMSILDNVAYGLmvkgidkkKRHAQARDA---------LEKVGLSFAVARKPSQLSGGQRQRVAIARALV 150
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPL--------REHTQLPAPllhstvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 151 NEPRVLLLDEP--------LGALdLKLreqmqfeLKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:PRK11831 160 LEPDLIMFDEPfvgqdpitMGVL-VKL-------ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
....
gi 2673334298 223 YMRP 226
Cdd:PRK11831 232 QANP 235
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
8-223 |
8.14e-27 |
|
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: 106.45 E-value: 8.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 8 NNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAG----------FEQLSGGTISIFgkeasELPPWER- 76
Cdd:TIGR02323 7 SGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrlapdhgtatYIMRSGAELELY-----QLSEAERr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 77 -----DVNTVFQDYA--LFPHMSILDNVAYGLMVKGIdkkkRH-----AQARDALEKVGLSFA-VARKPSQLSGGQRQRV 143
Cdd:TIGR02323 82 rlmrtEWGFVHQNPRdgLRMRVSAGANIGERLMAIGA----RHygnirATAQDWLEEVEIDPTrIDDLPRAFSGGMQQRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 144 AIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI------EQV- 216
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVvesgltDQVl 237
|
....*..
gi 2673334298 217 DTPRDLY 223
Cdd:TIGR02323 238 DDPQHPY 244
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-212 |
1.65e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.22 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 2 TYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFG-KEASELPPWERDVNT 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvPVPARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFPHMSILDN-VAYGLMVkGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK13536 119 VPQFDNLDLEFTVRENlLVFGRYF-GMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 160 EPLGALDLKLREQMQFELKKLQQeLGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-218 |
2.68e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 104.58 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP---WERD 77
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakiMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 VNTVFQDYALFPHMSILDNVAYGlmvkGIDKKKRHAQARdaLEKVGLSFA-----VARKPSQLSGGQRQRVAIARALVNE 152
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMG----GFFAERDQFQER--IKWVYELFPrlherRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 153 PRVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDT 218
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-212 |
3.80e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 108.48 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLiagfeqLSG--------GTISIFGKE--ASE 70
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKV------LSGvyphgtyeGEIIFEGEElqASN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 71 LPPWERD-VNTVFQDYALFPHMSILDNVAYG--LMVKG-IDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIA 146
Cdd:PRK13549 76 IRDTERAgIAIIHQELALVKELSVLENIFLGneITPGGiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 147 RALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-211 |
6.28e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 107.95 E-value: 6.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP---WERD 77
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 VNTVFQDYALFPHMSILDNVAYG-------LMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALV 150
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGrhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 151 NEPRVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNG 211
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-213 |
7.41e-26 |
|
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: 103.33 E-value: 7.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVS-RLYGDVRAV-DGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKE-ASELPPW-ERDVNT 80
Cdd:cd03252 1 ITFEHVRfRYKPDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFpHMSILDNVAY---GLMVKGIDKKKRHAQARDALEKV--GLSFAVARKPSQLSGGQRQRVAIARALVNEPRV 155
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALadpGMSMERVIEAAKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 156 LLLDEPLGALDLKLREQMQFELKKLQQelGITFIFVTHdQGEALSMSDRVAVFNNGRI 213
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAH-RLSTVKNADRIIVMEKGRI 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-226 |
7.51e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.11 E-value: 7.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY-GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASE--LPPWERDVNTV 81
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 FQ--DYALFPhMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK13652 84 FQnpDDQIFS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 160 EPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRP 226
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-205 |
9.22e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.87 E-value: 9.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP--WERDVNTVFQ 83
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiYRQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 DYALFPHmSILDNVAYGLMVKGidKKKRHAQARDALEKVGLSFAVARKP-SQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:PRK10247 89 TPTLFGD-TVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2673334298 163 GALDLKLREQMQFELKKLQQELGITFIFVTHDQGEaLSMSDRV 205
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKV 207
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-213 |
1.05e-25 |
|
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: 101.35 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 18 RAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVF------QDYALFPHM 91
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedrKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 92 SILDNVAYglmvkgidkkkrhaqardalekvglsfavarkPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLRE 171
Cdd:cd03215 94 SVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2673334298 172 QMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03215 142 EIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-213 |
1.60e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.64 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 18 RAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE------------RdvntvfQDY 85
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiayvpedR------KGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 86 ALFPHMSILDNVAYGLMVKG-----IDKKKRHAQARDALEKVGLSFAVARKP-SQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:COG1129 340 GLVLDLSIRENITLASLDRLsrgglLDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 160 EP-----LGAldlKlreqmqFELKKLQQEL---GITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG1129 420 EPtrgidVGA---K------AEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-213 |
1.95e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.97 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVR-AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASE--LPPWERDVNT 80
Cdd:PRK13657 334 AVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvtRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFpHMSILDNVAYGL-------MVKGIDKkkrhAQARDALEK--VGLSFAVARKPSQLSGGQRQRVAIARALVN 151
Cdd:PRK13657 414 VFQDAGLF-NRSIEDNIRVGRpdatdeeMRAAAER----AQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 152 EPRVLLLDEPLGALDLKLREQMQFELKKLQQELgITFIfVTHdqgeALSM---SDRVAVFNNGRI 213
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGR-TTFI-IAH----RLSTvrnADRILVFDNGRV 547
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-194 |
2.13e-25 |
|
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: 106.29 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVNTVFQDYALFpHMS 92
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 93 ILDNVAYGlmvkgiDKKKRHAQARDALEKVGLSFAVARKP-----------SQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:TIGR02868 425 VRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|...
gi 2673334298 162 LGALDLKLREQMQFELkkLQQELGITFIFVTHD 194
Cdd:TIGR02868 499 TEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-213 |
5.51e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 102.86 E-value: 5.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 10 VSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEaselpPWE------RDVNTVF- 82
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKrrkefaRRIGVVFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 83 QDYALFPHMSILDNvaYGLM--VKGIDKKkRHAQARDALEKV-GLSfAVARKP-SQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:COG4586 103 QRSQLWWDLPAIDS--FRLLkaIYRIPDA-EYKKRLDELVELlDLG-ELLDTPvRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 159 DEP-LGaLDL----KLREqmqFeLKKLQQELGITFIFVTHDQG--EALsmSDRVAVFNNGRI 213
Cdd:COG4586 179 DEPtIG-LDVvskeAIRE---F-LKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHGRI 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-222 |
6.93e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 100.74 E-value: 6.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 9 NVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER---DVNTVFQDY 85
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 86 ALFPHMSILDNVAYGLMV-KGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 165 LDlklrEQMQFELKKLQQEL---GITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:PRK10895 168 VD----PISVIDIKRIIEHLrdsGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-226 |
1.16e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.85 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 16 DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISI--------FGKEASELPPWERD---------- 77
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkKNNHELITNPYSKKiknfkelrrr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 VNTVFQ--DYALFPHmSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFA-VARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK13631 118 VSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 155 VLLLDEPLGALDLKlREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRP 226
Cdd:PRK13631 197 ILIFDEPTAGLDPK-GEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-230 |
1.42e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 104.55 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 17 VRAVDGVTIAIRDGEFFSMLGPSGSGKT-TCLRLIAGFEQlSGGTISIFG-------KEASELPPWER---------DVN 79
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKmllrrrsRQVIELSEQSAaqmrhvrgaDMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQD--YALFPHMSILDNVAYGLMV-KGIDKKKRHAQARDALEKVGLSFA---VARKPSQLSGGQRQRVAIARALVNEP 153
Cdd:PRK10261 108 MIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 154 RVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPF 230
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPY 264
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-222 |
1.56e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.09 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 8 NNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPwerdvNTVFQDYAL 87
Cdd:PRK11231 6 ENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-----RQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 88 FP--HM-----SILDNVAYG----LMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:PRK11231 81 LPqhHLtpegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 157 LLDEPLGALDLklreQMQFELKKLQQEL---GITFIFVTHDQGEALSMSDRVAVFNNGRI------EQVDTPRDL 222
Cdd:PRK11231 161 LLDEPTTYLDI----NHQVELMRLMRELntqGKTVVTVLHDLNQASRYCDHLVVLANGHVmaqgtpEEVMTPGLL 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-230 |
1.83e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 103.63 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 18 RAVDGVTIAIRDGEFFSMLGPSGSGKT----TCLRLIAGFEQL-SGGTISIFGKE---ASElpPWERDVN-----TVFQD 84
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESllhASE--QTLRGVRgnkiaMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 --YALFPHMSILDNVAYGLMV-KGIDKKKRHAQARDALEKVGLSFAVARK---PSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:PRK15134 101 pmVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 159 DEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPF 230
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPY 252
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
12-253 |
1.88e-24 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 99.77 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 12 RLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKT-TCLRLI----AGFEQLSGgTISIFGK--EASELPpwERDVNTVFQD 84
Cdd:PRK10418 11 ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQTAG-RVLLDGKpvAPCALR--GRKIATIMQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 --YALFPHMSILDNVAYGLMVKGidKKKRHAQARDALEKVGLSFA---VARKPSQLSGGQRQRVAIARALVNEPRVLLLD 159
Cdd:PRK10418 88 prSAFNPLHTMHTHARETCLALG--KPADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 160 EPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFvagfvgTSN 239
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAV------TRS 239
|
250
....*....|....
gi 2673334298 240 VFDAGLAqkICGME 253
Cdd:PRK10418 240 LVSAHLA--LYGME 251
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-193 |
2.21e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 103.73 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 20 VDGVTIAIRDGEffSML--GPSGSGKTTCLRLIAGFEQLSGGTIsifgkeasELPPWERdvntvfqdyALF----PHM-- 91
Cdd:COG4178 379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR---------VLFlpqrPYLpl 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 92 -SILDNVAYGLMVKGIDkkkrHAQARDALEKVGLS------FAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:COG4178 440 gTLREALLYPATAEAFS----DAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180 190
....*....|....*....|....*....|
gi 2673334298 165 LDLKLREQMqfeLKKLQQEL-GITFIFVTH 193
Cdd:COG4178 516 LDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-221 |
6.08e-24 |
|
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: 102.13 E-value: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 20 VDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGkeaSELPPWERDVNTVF-----QDYALFPHmSIL 94
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG---ADLSQWDREELGRHigylpQDVELFDG-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 95 DNVAyglmvkgidkkkRHAQARD-----ALEKVGLSFAVARKP-----------SQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:COG4618 424 ENIA------------RFGDADPekvvaAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 159 DEPLGALD----LKLREQMQfELKklqqELGITFIFVTHDQGeALSMSDRVAVFNNGRIEQVDtPRD 221
Cdd:COG4618 492 DEPNSNLDdegeAALAAAIR-ALK----ARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFG-PRD 551
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-215 |
8.35e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.85 E-value: 8.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 27 IRDGEFFSMLGPSGSGKTTCLRLIAGFeqLS-GGTISIFGKEASELPP--WERDVNTVFQDYALFpHMSILDNVAYGlmv 103
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGF--LPyQGSLKINGIELRELDPesWRKHLSWVGQNPQLP-HGTLRDNVLLG--- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 104 kgiDKKKRHAQARDALEKV-----------GLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQ 172
Cdd:PRK11174 447 ---NPDASDEQLQQALENAwvseflpllpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2673334298 173 MQFELKKLQQelGITFIFVTHdQGEALSMSDRVAVFNNGRIEQ 215
Cdd:PRK11174 524 VMQALNAASR--RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQ 563
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-226 |
8.85e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.52 E-value: 8.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGD-VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEA---SELPPWERDVNT 80
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQD-YALFPHMSILDNVAYG---LMVKGIDKKKRhaqARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVL 156
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGpenLCLPPIEIRKR---VDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 157 LLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQgEALSMSDRVAVFNNGRIEQVDTPRDLYMRP 226
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNL-EELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-194 |
1.59e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 7 FNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIfgkeaselPPWERdVNTVFQDYA 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGLR-IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 87 LFPHMSILDNV----------------AYGLMVKGIDKKKRHA----------------QARDALEKVGLSFAVARKP-S 133
Cdd:COG0488 72 LDDDLTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAelqeefealggweaeaRAEEILSGLGFPEEDLDRPvS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 134 QLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK----LREqmqfELKKLQqelgITFIFVTHD 194
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLEsiewLEE----FLKNYP----GTVLVVSHD 208
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-213 |
2.09e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 97.17 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 17 VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISI------FGKEASElppwERDVNTVFQD--YALF 88
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddhplhFGDYSYR----SQRIRMIFQDpsTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 89 PHMSILDNVAYGLMVK-GIDKKKRHAQARDALEKVGL-SFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:PRK15112 102 PRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2673334298 167 LKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
4-213 |
2.15e-23 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 100.97 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAV--DGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASEL-PPW-ERDVN 79
Cdd:TIGR01846 455 AITFENIRFRYAPDSPEvlSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIAdPAWlRRQMG 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPHmSILDNVAY---GLMVKGIDKKKRHAQARDALEKV--GLSFAVARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:TIGR01846 535 VVLQENVLFSR-SIRDNIALcnpGAPFEHVIHAAKLAGAHDFISELpqGYNTEVGEKGANLSGGQRQRIAIARALVGNPR 613
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQelGITFIFVTHdQGEALSMSDRVAVFNNGRI 213
Cdd:TIGR01846 614 ILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQI 669
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
8-230 |
6.14e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 97.12 E-value: 6.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 8 NNVSRLYGDV----RAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGF----EQLSGGTISIFGKEASELPPWER--- 76
Cdd:PRK11022 7 DKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERrnl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 77 ---DVNTVFQDyalfpHMSILD---NVAYGLMV-----KGIDKKKRHAQARDALEKVGLSFAVAR---KPSQLSGGQRQR 142
Cdd:PRK11022 87 vgaEVAMIFQD-----PMTSLNpcyTVGFQIMEaikvhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 143 VAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
....*...
gi 2673334298 223 YMRPRTPF 230
Cdd:PRK11022 242 FRAPRHPY 249
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-221 |
8.10e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.15 E-value: 8.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVS---RLY-------------------GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSG 58
Cdd:COG1134 1 MSSMIEVENVSksyRLYhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 59 GTISIFGKEASELppwerDVNTVFQdyalfPHMSILDNVAYGLMVKGIDKKkrhaQARDALEKVgLSFA---------VA 129
Cdd:COG1134 81 GRVEVNGRVSALL-----ELGAGFH-----PELTGRENIYLNGRLLGLSRK----EIDEKFDEI-VEFAelgdfidqpVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 130 RkpsqLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFN 209
Cdd:COG1134 146 T----YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLE 220
|
250
....*....|..
gi 2673334298 210 NGRIEQVDTPRD 221
Cdd:COG1134 221 KGRLVMDGDPEE 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-213 |
1.06e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.58 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP---WERD 77
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 VNTVFQDYALFPHMSILDNVAYGLmVKGIDKKKRHAQardALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGL-PKRQASMQKMKQ---LLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 158 LDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-213 |
1.69e-22 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 98.19 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 20 VDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGkeaSELPPWERD-----VNTVFQDYALFPHmSIL 94
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG---ADLKQWDREtfgkhIGYLPQDVELFPG-TVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 95 DNVAYglMVKGIDKKKRHAQARDA-LEKVGLSF------AVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD- 166
Cdd:TIGR01842 410 ENIAR--FGENADPEKIIEAAKLAgVHELILRLpdgydtVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDe 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2673334298 167 ---LKLREQMQfELKKlqqeLGITFIFVTHDQGeALSMSDRVAVFNNGRI 213
Cdd:TIGR01842 488 egeQALANAIK-ALKA----RGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-214 |
1.88e-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: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIfGKeaselppwerdvnTVFQD 84
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-------------TVKIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 Y------ALFPHMSILDNVAYGlmvkgiDKKKRHAQARDALEKVGLSFAVARKP-SQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:COG0488 382 YfdqhqeELDPDKTVLDELRDG------APGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 158 LDEPLGALDLKLREQM-----QFElkklqqelGiTFIFVTHDQgEAL-SMSDRVAVFNNGRIE 214
Cdd:COG0488 456 LDEPTNHLDIETLEALeealdDFP--------G-TVLLVSHDR-YFLdRVATRILEFEDGGVR 508
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-213 |
2.14e-22 |
|
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: 92.61 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 20 VDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGfeQLSG----GTISIFGKEaSELPPWERDVNTVFQDYALFPHMSILD 95
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG--RRTGlgvsGEVLINGRP-LDKRSFRKIIGYVPQDDILHPTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 96 NVAYGLMVKGIdkkkrhaqardalekvglsfavarkpsqlSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQF 175
Cdd:cd03213 102 TLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 2673334298 176 ELKKLQQElGITFIFVTHD-QGEALSMSDRVAVFNNGRI 213
Cdd:cd03213 153 LLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-205 |
2.31e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.68 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 14 YGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKeaselppweRDVNTVFQDYAL---FPh 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------ARVAYVPQRSEVpdsLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 91 MSILDNVAYGLMVK--GIDKKKRHAQAR--DALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:NF040873 72 LTVRDLVAMGRWARrgLWRRLTRDDRAAvdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 2673334298 167 LKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRV 205
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCV 189
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-214 |
6.74e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 90.84 E-value: 6.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYG--DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVF 82
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 83 QDYALFPHMSILDNVAyglmvkgidkkkrhaqardalekvglsfavarkpSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:cd03247 81 NQRPYLFDTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 163 GALDLKLREQMqfeLKKLQQEL-GITFIFVTHdQGEALSMSDRVAVFNNGRIE 214
Cdd:cd03247 127 VGLDPITERQL---LSLIFEVLkDKTLIWITH-HLTGIEHMDKILFLENGKII 175
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-212 |
6.84e-22 |
|
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: 96.05 E-value: 6.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSG--GTISIFGKE--ASELPPWERD-VN 79
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPlkASNIRDTERAgIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPHMSILDNVAYG--LMVKG--IDKKKRHAQARDALEKVGLS-FAVARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGneITLPGgrMAYNAMYLRAKNLLRELQLDaDNVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-219 |
9.27e-22 |
|
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: 95.64 E-value: 9.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAG---FEQLSGGTI---------------SIFGK 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqYEPTSGRIIyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 67 E----ASELPPWERDV----NTVFQD------------YALFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSF 126
Cdd:TIGR03269 81 PcpvcGGTLEPEEVDFwnlsDKLRRRirkriaimlqrtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 127 AVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVA 206
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|...
gi 2673334298 207 VFNNGRIEQVDTP 219
Cdd:TIGR03269 241 WLENGEIKEEGTP 253
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-219 |
2.30e-21 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 90.63 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGD--VRAVDGVTIAIRDGEFFSMLGPSGSGKTTC----LRLIagfeQLSGGTISIFGKEASELPP--WER 76
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLhdLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 77 DVNTVFQDYALFPhmsildnvayGLMVKGIDKKKRHAQAR--DALEKVGLSFAVARKP-----------SQLSGGQRQRV 143
Cdd:cd03244 79 RISIIPQDPVLFS----------GTIRSNLDPFGEYSDEElwQALERVGLKEFVESLPggldtvveeggENLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 144 AIARALVNEPRVLLLDEPLGALDLKLREQMQfelKKLQQEL-GITFIFVTHdQGEALSMSDRVAVFNNGRIEQVDTP 219
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQ---KTIREAFkDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-221 |
3.53e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.08 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLygDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER------DVN 79
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAvkkgmaYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPHMSILDNVA---------YGLMVKGIDKKKRHAQARDALEKVGLSFA-VARKPSQLSGGQRQRVAIARAL 149
Cdd:PRK09700 345 ESRRDNGFFPNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQRELLALKCHsVNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 150 VNEPRVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRD 221
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-213 |
6.72e-21 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 89.64 E-value: 6.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 16 DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQ---LSGGTISIFGKEaSELPPWERDVNTVFQDYALFPHMS 92
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQP-RKPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 93 ILDNVAYGLMVKGIDKK-KRHAQARDA---LEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:cd03234 98 VRETLTYTAILRLPRKSsDAIRKKRVEdvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2673334298 169 LREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-213 |
9.71e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.77 E-value: 9.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLY--GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASE--LPPWERDVNT 80
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFpHMSILDNVAYGLMVK----GIDKKKRHAQARDALEKV--GLSFAVARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:PRK11176 422 VSQNVHLF-NDTIANNIAYARTEQysreQIEEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQELgiTFIFVTHdqgeALSM---SDRVAVFNNGRI 213
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNR--TSLVIAH----RLSTiekADEILVVEDGEI 556
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-219 |
1.84e-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: 92.77 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 19 AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKE-ASELPPWERDVNTVFQDYALFPHMSILDNV 97
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDiETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 98 AYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFEL 177
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2673334298 178 KKLQQelGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTP 219
Cdd:TIGR01257 1105 LKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-213 |
2.88e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.24 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 17 VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER---DVNTVFQD---YALFPH 90
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYIPEDrlgRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 91 MSILDNVAYGL-----MVKG--IDKKKRHAQARDALEKvglsFAVaRKPS------QLSGGQRQRVAIARALVNEPRVLL 157
Cdd:COG3845 351 MSVAENLILGRyrrppFSRGgfLDRKAIRAFAEELIEE----FDV-RTPGpdtparSLSGGNQQKVILARELSRDPKLLI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 158 LDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:COG3845 426 AAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-212 |
3.78e-20 |
|
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: 87.49 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSR-----LYGDVR--AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEA----S 69
Cdd:COG4778 1 MTTLLEVENLSKtftlhLQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGwvdlA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 70 ELPPWE------RDVNTVFQdyalF----PHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLS---FAVArkPSQLS 136
Cdd:COG4778 81 QASPREilalrrRTIGYVSQ----FlrviPRVSALDVVAEPLLERGVDREEARARARELLARLNLPerlWDLP--PATFS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 137 GGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQmqfeLKKLQQEL---GITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAV----VVELIEEAkarGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
5-226 |
9.11e-20 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 90.39 E-value: 9.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRA--VDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPwERDVN--- 79
Cdd:TIGR03796 478 VELRNITFGYSPLEPplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPR-EVLANsva 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFpHMSILDNVAygLMVKGIDKKKRHAQARDA--LEKV-----GLSFAVARKPSQLSGGQRQRVAIARALVNE 152
Cdd:TIGR03796 557 MVDQDIFLF-EGTVRDNLT--LWDPTIPDADLVRACKDAaiHDVItsrpgGYDAELAEGGANLSGGQRQRLEIARALVRN 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 153 PRVLLLDEPLGALDLKLREQMQFELKKlqqeLGITFIFVTHdqgeALSM---SDRVAVFNNGRIEQVDTPRDLYMRP 226
Cdd:TIGR03796 634 PSILILDEATSALDPETEKIIDDNLRR----RGCTCIIVAH----RLSTirdCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-166 |
1.53e-19 |
|
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: 85.10 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP-WERDVNTVFQDYALFPHMSI 93
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 94 LDNVAYGLMVKGIDKKKRHaqarDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIE----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-234 |
5.58e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.78 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTIsifgkeasELPPWERdVNT 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR-IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFPHMSIldNVAYGLMVKGIDKKkrhAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:PRK09544 72 VPQKLYLDTTLPL--TVNRFLRLRPGTKK---EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 161 PLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFnNGRIEQVDTPRDLYMRPRtpFVAGF 234
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE--FISMF 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-213 |
6.45e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.57 E-value: 6.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 3 YAVEFNNVSRLYGD--VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPpwERD--- 77
Cdd:PRK11160 337 VSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS--EAAlrq 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 -VNTVFQDYALFPHmSILDNVAYGlmvkgiDKKKRHAQARDALEKVGLSFAVARKPS----------QLSGGQRQRVAIA 146
Cdd:PRK11160 415 aISVVSQRVHLFSA-TLRDNLLLA------APNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 147 RALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQelGITFIFVTHdQGEALSMSDRVAVFNNGRI 213
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH-RLTGLEQFDRICVMDNGQI 551
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-248 |
1.31e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 84.96 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFE----QLSGGTISIFGKEASELPPWER------DVNTVFQD 84
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 yalfPhMSILD---NVAYGLM-------VKGI---DKKKRHAQARDALEKVGL--------SFavarkPSQLSGGQRQRV 143
Cdd:COG4170 98 ----P-SSCLDpsaKIGDQLIeaipswtFKGKwwqRFKWRKKRAIELLHRVGIkdhkdimnSY-----PHELTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 144 AIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:COG4170 168 MIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQIL 247
|
250 260
....*....|....*....|....*
gi 2673334298 224 MRPRTPFVAGFVGTSNVFDAGLAQK 248
Cdd:COG4170 248 KSPHHPYTKALLRSMPDFRQPLPHK 272
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-215 |
1.58e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 86.41 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAV-DGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP--WERDVNT 80
Cdd:COG5265 357 EVRFENVSFGYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQasLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFpHMSILDNVAYGlmvkgidkkkR----HAQARDALEKVGLSFAVARKPSQ-----------LSGGQRQRVAI 145
Cdd:COG5265 437 VPQDTVLF-NDTIAYNIAYG----------RpdasEEEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAI 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 146 ARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQelGITFIFVTHdqgeALSM---SDRVAVFNNGRI-EQ 215
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH----RLSTivdADEILVLEAGRIvER 573
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-211 |
2.09e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 17 VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP---WERDVNTVFQDYALFPHMSI 93
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkssQEAGIGIIHQELNLIPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 94 LDNVAYGLMVK----GIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKL 169
Cdd:PRK10762 97 AENIFLGREFVnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2673334298 170 REQMqF----ELKklQQELGITFIfvTHDQGEALSMSDRVAVFNNG 211
Cdd:PRK10762 177 TESL-FrvirELK--SQGRGIVYI--SHRLKEIFEICDDVTVFRDG 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-221 |
2.22e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 85.61 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLiagfeqLSG--------GTISIFGKE-------ASE 70
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKV------LSGvyphgsyeGEILFDGEVcrfkdirDSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 71 lppwERDVNTVFQDYALFPHMSILDNV-------AYGLmvkgIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRV 143
Cdd:NF040905 77 ----ALGIVIIHQELALIPYLSIAENIflgneraKRGV----IDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 144 AIARALVNEPRVLLLDEPLGALD-----------LKLREQmqfelkklqqelGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNeedsaalldllLELKAQ------------GITSIIISHKLNEIRRVADSITVLRDGR 216
|
250
....*....|
gi 2673334298 213 -IEQVDTPRD 221
Cdd:NF040905 217 tIETLDCRAD 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-193 |
2.33e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 81.05 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSrLY---GDVRaVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIfgkeaselpPWERDVntv 81
Cdd:cd03223 1 IELENLS-LAtpdGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDL--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 fqdyaLF----PHM---SILDNVAYglmvkgidkkkrhaqardALEKVglsfavarkpsqLSGGQRQRVAIARALVNEPR 154
Cdd:cd03223 67 -----LFlpqrPYLplgTLREQLIY------------------PWDDV------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*....
gi 2673334298 155 VLLLDEPLGALDlklrEQMQFELKKLQQELGITFIFVTH 193
Cdd:cd03223 112 FVFLDEATSALD----EESEDRLYQLLKELGITVISVGH 146
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-166 |
3.85e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEfnNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNT 80
Cdd:PRK13539 1 MMLEGE--DLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDyALFPHMSILDNVAYGLMVKGidkkKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDE 160
Cdd:PRK13539 79 GHRN-AMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
....*.
gi 2673334298 161 PLGALD 166
Cdd:PRK13539 154 PTAALD 159
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-195 |
4.63e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.54 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 18 RAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGfeQLSGGTISIFGkeasELP--PWERDVntvfqdyalfphmSILD 95
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--ALKGTPVAGCV----DVPdnQFGREA-------------SLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 96 NvayglmvkgIDKKKRHAQARDALEKVGLSFAVA--RKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQM 173
Cdd:COG2401 105 A---------IGRKGDFKDAVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180
....*....|....*....|..
gi 2673334298 174 QFELKKLQQELGITFIFVTHDQ 195
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHHY 197
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-222 |
1.01e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 14 YGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVNTVFQDYALFPHM 91
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 92 SILDNVAYG------LMVKGidKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:PRK10253 97 TVQELVARGryphqpLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 166 DLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-195 |
3.39e-17 |
|
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: 77.10 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEaselppwerdvntvfqd 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 yalfphmsildNVAYglmvkgidkkkrhaqardalekvglsFAvarkpsQLSGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:cd03221 64 -----------KIGY--------------------------FE------QLSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190
....*....|....*....|....*....|.
gi 2673334298 165 LDLKLREQMQFELKKLQQelgiTFIFVTHDQ 195
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDR 127
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-208 |
4.98e-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: 79.37 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 27 IRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPpwerdvNTVFQDYalfphmsilDNVAYGLMVKGI 106
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP------QYIKADY---------EGTVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 107 DKKKRHAQAR-DALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELG 185
Cdd:cd03237 87 KDFYTHPYFKtEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180
....*....|....*....|...
gi 2673334298 186 ITFIFVTHDQGEALSMSDRVAVF 208
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIVF 189
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-212 |
5.43e-17 |
|
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: 78.28 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVR-----AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEA--SELPpWerd 77
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAyvSQEP-W--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 vntvfqdyaLFPhMSILDNVAYGlmvKGIDKKkRHAQARDA--LEK------VGLSFAVARKPSQLSGGQRQRVAIARAL 149
Cdd:cd03250 77 ---------IQN-GTIRENILFG---KPFDEE-RYEKVIKAcaLEPdleilpDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 150 VNEPRVLLLDEPLGALDLKLREQMqFE---LKKLQqeLGITFIFVTHdQGEALSMSDRVAVFNNGR 212
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHI-FEnciLGLLL--NNKTRILVTH-QLQLLPHADQIVVLDNGR 204
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-226 |
6.72e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 80.55 E-value: 6.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTclrliagfeqlSGGTISIFGKEASElPPWeRDVNTVFQ 83
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-----------GALPAHV*GPDAGR-RPW-RF*TWCAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 DYALFPHMSILDNVAYG------------LMVKGIDKKKRHAQAR--DALEKVGLSFAVARKPSQLSGGQRQRVAIARAL 149
Cdd:NF000106 80 RRALRRTIG*HRPVR*GrresfsgrenlyMIGR*LDLSRKDARARadELLERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 150 VNEPRVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEA------LSMSDRVAVFNNGRIEQVDTP---R 220
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDELKTKvggR 238
|
....*.
gi 2673334298 221 DLYMRP 226
Cdd:NF000106 239 TLQIRP 244
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-240 |
8.85e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.60 E-value: 8.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 2 TYAVEFNNVSRLYGDVR--AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASElppwerDVN 79
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NIS 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPHMSILDNVAYG-------LMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNE 152
Cdd:TIGR01257 2009 DVHQNMGYCPQFDAIDDLLTGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 153 PRVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLymrpRTPFVA 232
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL----KSKFGD 2163
|
....*...
gi 2673334298 233 GFVGTSNV 240
Cdd:TIGR01257 2164 GYIVTMKI 2171
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-166 |
9.49e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.54 E-value: 9.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 21 DGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPwerdvntVFQDYALF--------PHMS 92
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-------EYHQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 93 ILDNVAYGLMVKGidkKKRHAQARDALEKVGLSfAVARKP-SQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:PRK13538 91 ALENLRFYQRLHG---PGDDEALWEALAQVGLA-GFEDVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-267 |
1.07e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.90 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 14 YGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGK----EASELPPWERDVNTVFQD--YAL 87
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldySKRGLLALRQQVATVFQDpeQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 88 FpHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSfAVARKPSQ-LSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:PRK13638 91 F-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQ-HFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 167 LKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPFVAGFVGTSNV-FDAGL 245
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGLTQPWLVkLHTQL 247
|
250 260
....*....|....*....|..
gi 2673334298 246 AQKICGMEGSYSLRPEHIRLDE 267
Cdd:PRK13638 248 GLPLCKTETEFFHRMQKCAFRE 269
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-212 |
1.53e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 80.31 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 20 VDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVFQDYALFPHMSILDNVAY 99
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 100 GLMV---KGIDKKKRHAQARDALEKVGL----------SFAVArkpsqLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:PLN03211 164 CSLLrlpKSLTKQEKILVAESVISELGLtkcentiignSFIRG-----ISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2673334298 167 LKLREQMQFELKKLQQElGITFIFVTHD-QGEALSMSDRVAVFNNGR 212
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-166 |
2.90e-16 |
|
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: 75.99 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 16 DVRAV-DGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP-WERDVNTVFQDYALFPHMSI 93
Cdd:cd03231 11 DGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDsIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 94 LDNVAYGLMVKGIDkkkrhaQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:cd03231 91 LENLRFWHADHSDE------QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-213 |
4.11e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.89 E-value: 4.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 20 VDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVF---QDY---ALFPHMSI 93
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVyisEDRkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 94 LDNVAYGLMVKGIDK--KKRHAQARDALEKVGLSFAVaRKPSQ------LSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:PRK10762 348 KENMSLTALRYFSRAggSLKHADEQQAVSDFIRLFNI-KTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2673334298 166 DLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK10762 427 DVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
15-230 |
4.99e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.54 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQ----LSGGTISIFGKEASELPPWER------DVNTVFQD 84
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 --YALFPHMSI---LDNVAYGLMVKGIDKKKRHAQARDALE---KVGLS---FAVARKPSQLSGGQRQRVAIARALVNEP 153
Cdd:PRK15093 98 pqSCLDPSERVgrqLMQNIPGWTYKGRWWQRFGWRKRRAIEllhRVGIKdhkDAMRSFPYELTEGECQKVMIAIALANQP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 154 RVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPF 230
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPY 254
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-222 |
8.02e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.63 E-value: 8.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 3 YAVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEaseLPPweRDVNT-- 80
Cdd:NF033858 265 PAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP---VDA--GDIATrr 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 ----VFQDYALFPHMSILDNVAygLMVK--GIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:NF033858 340 rvgyMSQAFSLYGELTVRQNLE--LHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQELGITfIFV-THDQGEALSmSDRVAVFNNGRIEQVDTPRDL 222
Cdd:NF033858 418 LLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-203 |
8.82e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.07 E-value: 8.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 20 VDGVTI-------AIRDGEF-------FSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASE--------LPPWERD 77
Cdd:PRK15056 9 VNDVTVtwrnghtALRDASFtvpggsiAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQalqknlvaYVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 78 VNTVF----QDYAL---FPHMSILDnvayglmvkgIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALV 150
Cdd:PRK15056 89 VDWSFpvlvEDVVMmgrYGHMGWLR----------RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 151 NEPRVLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSD 203
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD 210
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-226 |
1.39e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 75.63 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 18 RAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGfeQLSGGTIS----IFGKEASELPPWER-DVNTVFQDYALFPHMS 92
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGGGAPrgarVTGDVTLNGEPLAAiDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 93 ildNVAYGLMVKGIDKKKRHAQAR--------------DALEKVGLSFAVARKPSQLSGGQRQRVAIARALVN------- 151
Cdd:PRK13547 93 ---QPAFAFSAREIVLLGRYPHARragalthrdgeiawQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 152 --EPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLyMRP 226
Cdd:PRK13547 170 aqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV-LTP 245
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-212 |
1.97e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 76.69 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 9 NVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKE---ASELPPWERDVNTVFQDY 85
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfKSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 86 ALFPHMSILDNVAYGLM-VKG--IDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:PRK10982 83 NLVLQRSVMDNMWLGRYpTKGmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2673334298 163 GALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGR 212
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-213 |
2.67e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.51 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 17 VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGTISIFGKEASELPPWE---RDVNTVFQD---YALFP 89
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 90 HMSILDNV---AYGLMVKG--IDKKKRHAQARDALEKVGLSFAVARKP-SQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:PRK13549 355 VMGVGKNItlaALDRFTGGsrIDDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 164 ALDLKLReqmqFELKKLQQEL---GITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK13549 435 GIDVGAK----YEIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-213 |
4.48e-15 |
|
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: 72.56 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFE--QLSGGTISIFGKEASELPPWERDVNTV---FQDYALFP 89
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIflaFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 90 HMSILDNVAYglmvkgidkkkrhaqardalekVGLSFavarkpsqlSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKL 169
Cdd:cd03217 91 GVKNADFLRY----------------------VNEGF---------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2673334298 170 REQMQFELKKLQQElGITFIFVTHDQGEALSM-SDRVAVFNNGRI 213
Cdd:cd03217 140 LRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRI 183
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-161 |
4.60e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.32 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASElppwERDVNTVFQ 83
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD----ARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 84 DYA---------LFPHMSILDNVAYGLMVKGIDKKKRHAQARDALEKVGLS-FAvARKPSQLSGGQRQRVAIARALVNEP 153
Cdd:NF033858 77 RIAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLApFA-DRPAGKLSGGMKQKLGLCCALIHDP 155
|
....*...
gi 2673334298 154 RVLLLDEP 161
Cdd:NF033858 156 DLLILDEP 163
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-213 |
4.74e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.78 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVR-AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPP--WERDVNTV 81
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPedYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 FQDYALFPHMsiLDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAvarkPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:PRK10522 403 FTDFHLFDQL--LGPEGKPANPALVEKWLERLKMAHKLELEDGRIS----NLKLSKGQKKRLALLLALAEERDILLLDEW 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 162 LGALDLKLREQMQFELKKLQQELGITFIFVTHDQgEALSMSDRVAVFNNGRI 213
Cdd:PRK10522 477 AADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQL 527
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-205 |
4.87e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 75.76 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTIsIFGKE--ASEL---PPweRDVN 79
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDliVARLqqdPP--RNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 -TVFqDY----------ALFPHMSILDNVAYGLMVKGIDKKKR------HAQA-------RDALEKVGLSfavARKP-SQ 134
Cdd:PRK11147 81 gTVY-DFvaegieeqaeYLKRYHDISHLVETDPSEKNLNELAKlqeqldHHNLwqlenriNEVLAQLGLD---PDAAlSS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 135 LSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQelgiTFIFVTHDQGEALSMSDRV 205
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRI 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-213 |
8.20e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.08 E-value: 8.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 22 GVTIAIRDGEFFSMLGPSGSGKTTCLRLIAgFEQLSG----GTISIFGKEAsELPPWERDVNTVFQDYALFPHMSILDNV 97
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGvkgsGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 98 AYGLMVK---GIDKKKRHAQARDALEKVGLSFA------VARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:TIGR00955 121 MFQAHLRmprRVTKKEKRERVDEVLQALGLRKCantrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2673334298 169 LREQMQFELKKLQQElGITFIFVTHD-QGEALSMSDRVAVFNNGRI 213
Cdd:TIGR00955 201 MAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRV 245
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
30-228 |
1.21e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.90 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 30 GEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASEL--PPWERDVNTVFQDYALFPHMSILDNVAYGLM----V 103
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWssKAFARKVAYLPQQLPAAEGMTVRELVAIGRYpwhgA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 104 KGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQE 183
Cdd:PRK10575 117 LGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQE 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2673334298 184 LGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLyMRPRT 228
Cdd:PRK10575 197 RGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL-MRGET 240
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-166 |
1.16e-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: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIfGkeaselppwerdvNTVFQD 84
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-G-------------ETVKLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 Y------ALFPHMSILDNVAYGLMVkgIDKKKRHAQARDALEKVGLSFAVARKP-SQLSGGQRQRVAIARALVNEPRVLL 157
Cdd:TIGR03719 389 YvdqsrdALDPNKTVWEEISGGLDI--IKLGKREIPSRAYVGRFNFKGSDQQKKvGQLSGGERNRVHLAKTLKSGGNVLL 466
|
....*....
gi 2673334298 158 LDEPLGALD 166
Cdd:TIGR03719 467 LDEPTNDLD 475
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-213 |
1.81e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.94 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 21 DGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFE--QLSGGTISIFGKEASELPPWER---DVNTVFQDYALFPHMSILD 95
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSVSN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 96 --NVAYG-LMVKGIDKKKRHAQARDALEKVGLSFAVARKP--SQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL--- 167
Cdd:COG0396 97 flRTALNaRRGEELSAREFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdal 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2673334298 168 -KLREqmqfELKKLQQElGITFIFVTHdQGEALSM--SDRVAVFNNGRI 213
Cdd:COG0396 177 rIVAE----GVNKLRSP-DRGILIITH-YQRILDYikPDFVHVLVDGRI 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-222 |
3.03e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 68.33 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 20 VDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQlSGGTISIFGKEASELPPWE--------------RDVNTVFQDY 85
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElarhraylsqqqspPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 86 ALFPHMSILDNVAYGLMVkgidkkkrhaqarDALEKVGLSFAVARKPSQLSGGQRQRVAIARAL------VN-EPRVLLL 158
Cdd:COG4138 91 ALHQPAGASSEAVEQLLA-------------QLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 159 DEPLGALDLklreQMQFELKKLQQEL---GITFIFVTHDQGEALSMSDRVAVFNNGRI------EQVDTPRDL 222
Cdd:COG4138 158 DEPMNSLDV----AQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLvasgetAEVMTPENL 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-219 |
3.10e-13 |
|
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: 67.82 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGD--VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELP--PWERDVNT 80
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFPhmsildnvayGLMVKGIDKKKRH--AQARDALEkvglsfaVARKPSQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:cd03369 87 IPQDPTLFS----------GTIRSNLDPFDEYsdEEIYGALR-------VSEGGLNLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 159 DEPLGALDLKLREQMQfelKKLQQEL-GITFIFVTHDQGEALSMsDRVAVFNNGRIEQVDTP 219
Cdd:cd03369 150 DEATASIDYATDALIQ---KTIREEFtNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
76-210 |
3.54e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 76 RDVNTVF----QDYALFpHMSILDNVAYG---LMVKGIDKKKRHAQARDALEKVGLSFAVARKP--SQLSGGQRQRVAIA 146
Cdd:PTZ00265 1292 KDLRNLFsivsQEPMLF-NMSIYENIKFGkedATREDVKRACKFAAIDEFIESLPNKYDTNVGPygKSLSGGQKQRIAIA 1370
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 147 RALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQELGITFIFVTHdQGEALSMSDRVAVFNN 210
Cdd:PTZ00265 1371 RALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFNN 1433
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-213 |
5.29e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 23 VTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWER-DVNTVF-----QDYALFPHMSILDN 96
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 97 V---AYGLMVKGIDKKKRHA---QARDALekvGLSFAVARKPSQ-LSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKL 169
Cdd:PRK15439 362 VcalTHNRRGFWIKPARENAvleRYRRAL---NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2673334298 170 REQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK15439 439 RNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-215 |
7.18e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.36 E-value: 7.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 19 AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASE--LPPWERDVNTVFQDYALFPHmSILDN 96
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqLDSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 97 VAYG---LMVKGIDKKKRHAQARDALEKV--GLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLRE 171
Cdd:PRK10789 409 IALGrpdATQQEIEHVARLASVHDDILRLpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2673334298 172 QMQFELKKLQQelGITFIFVTHdQGEALSMSDRVAVFNNGRIEQ 215
Cdd:PRK10789 489 QILHNLRQWGE--GRTVIISAH-RLSALTEASEILVMQHGHIAQ 529
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-193 |
9.19e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.98 E-value: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAV-DGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELP--PWERDVNT 80
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 81 VFQDYALFPHmSILDNVAYGlmvKGIDKkkrhAQARDALEKVGLSFAVARKP-----------SQLSGGQRQRVAIARAL 149
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLG---RDISE----EQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2673334298 150 VNEPRVLLLDEPLGALDLKLREQMQFELKKLQQElgITFIFVTH 193
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH 533
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-194 |
1.80e-12 |
|
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: 66.24 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 28 RDGEFFSMLGPSGSGKTTCLRLiagfeqLSGGTISIFGKEASElPPWERDVN----TVFQDY-----------ALFP-HM 91
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKI------LAGKLKPNLGKFDDP-PDWDEILDefrgSELQNYftkllegdvkvIVKPqYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 92 SILDNVAYGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLRE 171
Cdd:cd03236 97 DLIPKAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|...
gi 2673334298 172 QMQFELKKLQQElGITFIFVTHD 194
Cdd:cd03236 177 NAARLIRELAED-DNYVLVVEHD 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
12-194 |
1.82e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.91 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 12 RLYGdvravdgvTIAIRDGEFFSMLGPSGSGKTTCLRLiagfeqLSGGTISIFGKEASElPPWERDVN----TVFQDY-- 85
Cdd:PRK13409 89 KLYG--------LPIPKEGKVTGILGPNGIGKTTAVKI------LSGELIPNLGDYEEE-PSWDEVLKrfrgTELQNYfk 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 86 ---------ALFPHM------SILDNVayGLMVKGIDKKKRhaqARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALV 150
Cdd:PRK13409 154 klyngeikvVHKPQYvdlipkVFKGKV--RELLKKVDERGK---LDEVVERLGLENILDRDISELSGGELQRVAIAAALL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2673334298 151 NEPRVLLLDEPLGALDLKLReqmqFELKKLQQEL--GITFIFVTHD 194
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIRQR----LNVARLIRELaeGKYVLVVEHD 270
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-214 |
1.89e-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: 67.93 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 17 VRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGTISIFGKEASELPPW---ERDVNTVFQD---YALFP 89
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNPAqaiRAGIAMVPEDrkrHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 90 HMSILDNVAYGLMVK-----GIDKKKRHAQARDALEKVGLSFAVARKP-SQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:TIGR02633 353 ILGVGKNITLSVLKSfcfkmRIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 164 ALDLKLREQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNNGRIE 214
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-193 |
3.79e-12 |
|
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: 64.66 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 16 DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGTISIFGKEASELPPWERDVNTVFQDYA----LFPH 90
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAaqkpWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 91 MSILDNVAYGLMVKgidkKKRHAQARDA--------LEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:cd03290 93 ATVEENITFGSPFN----KQRYKAVTDAcslqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190
....*....|....*....|....*....|..
gi 2673334298 163 GALDLKLREQ-MQFELKKLQQELGITFIFVTH 193
Cdd:cd03290 169 SALDIHLSDHlMQEGILKFLQDDKRTLVLVTH 200
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-167 |
3.96e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 27 IRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASelppweRDVNTVFQDY-----ALFPHMSILDNVAYGL 101
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT------RGDRSRFMAYlghlpGLKADLSTLENLHFLC 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 102 MVKGidkkkRHAQAR--DALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:PRK13543 108 GLHG-----RRAKQMpgSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
12-194 |
4.54e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 66.73 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 12 RLYGdvravdgvTIAIRDGEFFSMLGPSGSGKTTCLRLiagfeqLSGGTISIFGKEASElPPWErDVNTVFQDYALFPHM 91
Cdd:COG1245 89 RLYG--------LPVPKKGKVTGILGPNGIGKSTALKI------LSGELKPNLGDYDEE-PSWD-EVLKRFRGTELQDYF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 92 SILDN----VAY--------GLMVKG-----IDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPR 154
Cdd:COG1245 153 KKLANgeikVAHkpqyvdliPKVFKGtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2673334298 155 VLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHD 194
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHD 271
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-213 |
9.34e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 11 SRLYGDVR-AVDG---------VTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEAS----------- 69
Cdd:PRK11288 250 PRPLGEVRlRLDGlkgpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdairag 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 70 -ELPPWERDvntvfQDyALFPHMSILDNVA---------YGLMvkgIDKKKRHAQARDALEKVGLSFAVARKP-SQLSGG 138
Cdd:PRK11288 330 iMLCPEDRK-----AE-GIIPVHSVADNINisarrhhlrAGCL---INNRWEAENADRFIRSLNIKTPSREQLiMNLSGG 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2673334298 139 QRQRVAIARALVNEPRVLLLDEPLGALDLKLRE---QMQFELKklqqELGITFIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHeiyNVIYELA----AQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-189 |
2.54e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.05 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYG---DVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISI---FGKEASELPPWERDV 78
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndsHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 79 NTVFQDYALFPHmSILDNVAYGL----------------------------------------MVKGIDKK-----KRHA 113
Cdd:PTZ00265 463 GVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndMSNTTDSNeliemRKNY 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 114 QARDALEKVGLS-------FA----------VARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFE 176
Cdd:PTZ00265 542 QTIKDSEVVDVSkkvlihdFVsalpdkyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250
....*....|....
gi 2673334298 177 LKKLQ-QELGITFI 189
Cdd:PTZ00265 622 INNLKgNENRITII 635
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-166 |
3.91e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGTISIFGKE-ASELPPWE--RDV-- 78
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdHPQGYSNDLTLFGRRrGSGETIWDikKHIgy 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 79 --NTVFQDYALfpHMSILDNVAYGLMVK-GIDKKKRHAQ---ARDALEKVGLSFAVARKPSQ-LSGGQRQRVAIARALVN 151
Cdd:PRK10938 341 vsSSLHLDYRV--STSVRNVILSGFFDSiGIYQAVSDRQqklAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVK 418
|
170
....*....|....*
gi 2673334298 152 EPRVLLLDEPLGALD 166
Cdd:PRK10938 419 HPTLLILDEPLQGLD 433
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-222 |
5.12e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 23 VTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFeqLSG-GTISIFGK-----EASEL------------PPWERDVntvFQD 84
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL--LPGsGSIQFAGQpleawSAAELarhraylsqqqtPPFAMPV---FQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 YALFPHmsildnvayglmvkgidKKKRHAQARDAL----EKVGLSFAVARKPSQLSGGQRQRVAIA-------RALVNEP 153
Cdd:PRK03695 90 LTLHQP-----------------DKTRTEAVASALnevaEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 154 RVLLLDEPLGALDLKLREQMQFELKKLQQeLGITFIFVTHDQGEALSMSDRVAVFNNGRI------EQVDTPRDL 222
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLlasgrrDEVLTPENL 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-166 |
6.90e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIfGKeaselppwerdvnTVFQD 84
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE-------------TVKLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 Y------ALFPHMSILDNVAYGLMV-------------------KGIDKKKrhaqardaleKVGlsfavarkpsQLSGGQ 139
Cdd:PRK11819 391 YvdqsrdALDPNKTVWEEISGGLDIikvgnreipsrayvgrfnfKGGDQQK----------KVG----------VLSGGE 450
|
170 180
....*....|....*....|....*..
gi 2673334298 140 RQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-230 |
8.13e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 8.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 22 GVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASE--LPPWERDVNTVFQDYALFPhmsildnvay 99
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFS---------- 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 100 GLMVKGIDKKKRHAQAR--DALEKVGLSFAVARKPSQL-----------SGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:PLN03232 1324 GTVRFNIDPFSEHNDADlwEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 167 LKLREQMQfelKKLQQEL-GITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDTPRDLYMRPRTPF 230
Cdd:PLN03232 1404 VRTDSLIQ---RTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-204 |
8.46e-11 |
|
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: 59.31 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 30 GEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERDVNTVfqdyalfphmsildnvayglmvkgidkk 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 110 krhaqardalekvglsfaVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFE-----LKKLQQEL 184
Cdd:smart00382 54 ------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEK 115
|
170 180
....*....|....*....|
gi 2673334298 185 GITFIFVTHDQGEALSMSDR 204
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLR 135
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-208 |
1.10e-10 |
|
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: 59.89 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 27 IRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISifgkeaselppWERdvntvfqdyalfphmsildnvayglmvkgi 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE-----------WDG------------------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 107 dkkkrhaqardalekvglsFAVARKPS--QLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQEL 184
Cdd:cd03222 61 -------------------ITPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
170 180
....*....|....*....|....
gi 2673334298 185 GITFIFVTHDQGEALSMSDRVAVF 208
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-193 |
1.60e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 62.07 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVrAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPwERDVNTV--FQDYALFPhMS 92
Cdd:TIGR00954 464 GDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVP-QRPYMTLgtLRDQIIYP-DS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 93 ILDNVAYGLMVKGIDKKKRHAQARDALEK-VGLSfAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLrE 171
Cdd:TIGR00954 541 SEDMKRRGLSDKDLEQILDNVQLTHILEReGGWS-AVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV-E 618
|
170 180
....*....|....*....|..
gi 2673334298 172 QMQFELKKlqqELGITFIFVTH 193
Cdd:TIGR00954 619 GYMYRLCR---EFGITLFSVSH 637
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-194 |
1.67e-10 |
|
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: 61.87 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 3 YAVEFNNVSRLYGDVRAV-DGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGtisifgkEASELPpwERDVNTV 81
Cdd:TIGR03719 3 YIYTMNRVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------EARPQP--GIKVGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 FQDYALFPHMSILDNVAYGLmvkgidKKKRHAQARdaLEKVGLSFA---------------------------------V 128
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVEEGV------AEIKDALDR--FNEISAKYAepdadfdklaaeqaelqeiidaadawdldsqleI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 129 A----RKP------SQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDlklREQMQFELKKLQQELGiTFIFVTHD 194
Cdd:TIGR03719 146 AmdalRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPG-TVVAVTHD 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-213 |
2.64e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 23 VTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWERdVNTVF-------QDYALFPHMSIld 95
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA-INHGFalvteerRSTGIYAYLDI-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 96 nvAYGLMVKGIDKKKRH------AQARDALEKVGLSFAVaRKPSQ------LSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:PRK10982 344 --GFNSLISNIRNYKNKvglldnSRMKSDTQWVIDSMRV-KTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 164 ALDLKLReqmqFELKKLQQEL-----GItfIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PRK10982 421 GIDVGAK----FEIYQLIAELakkdkGI--IIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-194 |
3.78e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 6 EFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGK-EASelppwerdvntVFQD 84
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVA-----------YFDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 Y--ALFPHMSILDNVAYG---LMVKGidkKKRHAQA--RDALekvgLSFAVARKPSQ-LSGGQRQRVAIARALVNEPRVL 156
Cdd:PRK11147 390 HraELDPEKTVMDNLAEGkqeVMVNG---RPRHVLGylQDFL----FHPKRAMTPVKaLSGGERNRLLLARLFLKPSNLL 462
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2673334298 157 LLDEPLGALD---LKLREQMqfeLKKLQQelgiTFIFVTHD 194
Cdd:PRK11147 463 ILDEPTNDLDvetLELLEEL---LDSYQG----TVLLVSHD 496
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-213 |
3.88e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.03 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 34 SMLGPSGSGKTTCLRLIAGFEQLSGGTIsiFGKEASELppwerdvnTVFQDYalfpHMSILDNVAYGL--MVK---GIDK 108
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTV--FRSAKVRM--------AVFSQH----HVDGLDLSSNPLlyMMRcfpGVPE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 109 KKRHAQardaLEKVGLSFAVARKPS-QLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQelGIt 187
Cdd:PLN03073 605 QKLRAH----LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG--GV- 677
|
170 180
....*....|....*....|....*.
gi 2673334298 188 fIFVTHDQGEALSMSDRVAVFNNGRI 213
Cdd:PLN03073 678 -LMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
14-203 |
6.31e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 14 YGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKE-ASELPPWERDVNTVFQDYALFPHMS 92
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSiKKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 93 ILDNVAYGLMVK----GIDKKKRHAQARDALE-KVGLsfavarkpsqLSGGQRQRVAIARALVNEPRVLLLDEPLGALDL 167
Cdd:PRK13540 91 LRENCLYDIHFSpgavGITELCRLFSLEHLIDyPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 2673334298 168 KLREQMQFELKKLQQELGItfIFVTHDQGEALSMSD 203
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGA--VLLTSHQDLPLNKAD 194
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-225 |
6.93e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.34 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLR-LIAGFEQLSGgTISIFGKeaselppwerdVNTVFQDyALFPHMSI 93
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEG-HVHMKGS-----------VAYVPQQ-AWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 94 LDNVAYGLMVKgidkKKRHAQARDA------LEKV--GLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGAL 165
Cdd:TIGR00957 716 RENILFGKALN----EKYYQQVLEAcallpdLEILpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2673334298 166 DLKLREQMqFElkKLQQELGI----TFIFVTHDQgEALSMSDRVAVFNNGRIEQVDTPRDLYMR 225
Cdd:TIGR00957 792 DAHVGKHI-FE--HVIGPEGVlknkTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
40-222 |
7.63e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 59.81 E-value: 7.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 40 GSGKTTCLRLIAGFEQLSGGTISIFGKE-ASELPPWERD-VNTVFQDYALFPHmsildnvaygLMvkGIDKKKRHAQARD 117
Cdd:COG4615 368 GSGKSTLAKLLTGLYRPESGEILLDGQPvTADNREAYRQlFSAVFSDFHLFDR----------LL--GLDGEADPARARE 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 118 ALEKVGLsfavARKPS---------QLSGGQRQRVAIARALVnEPR-VLLLDE------PlgaldlklreqmQF------ 175
Cdd:COG4615 436 LLERLEL----DHKVSvedgrfsttDLSQGQRKRLALLVALL-EDRpILVFDEwaadqdP------------EFrrvfyt 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 176 ----ELKKlqqeLGITFIFVTHDqGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:COG4615 499 ellpELKA----RGKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPAAL 544
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-205 |
7.96e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.91 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTIsifgK--EASELPPWERDVNTV 81
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KwsENANIGYYAQDHAYD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 F-QDYALFPHMSILDNVAYG-LMVKGIdkkkrhaqardaLEKVGLSFAVARKPSQ-LSGGQRQRVAIARALVNEPRVLLL 158
Cdd:PRK15064 395 FeNDLTLFDWMSQWRQEGDDeQAVRGT------------LGRLLFSQDDIKKSVKvLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2673334298 159 DEPLGALDLKLREQMQFELKKLQQelgiTFIFVTHDQGEALSMSDRV 205
Cdd:PRK15064 463 DEPTNHMDMESIESLNMALEKYEG----TLIFVSHDREFVSSLATRI 505
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-213 |
1.79e-09 |
|
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: 56.89 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 20 VDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGfeqLSGGTISIFG---------KEASELPPweRDVNTVFQDYALFPH 90
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGdihyngipyKEFAEKYP--GEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 91 MSIldnvayglmvkgidkkkrhaqaRDALEkvglsFAVARKPSQ----LSGGQRQRVAIARALVNEPRVLLLDEPLGALD 166
Cdd:cd03233 98 LTV----------------------RETLD-----FALRCKGNEfvrgISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2673334298 167 LKLREQMQFELKKLQQELGITfIFVTHDQ--GEALSMSDRVAVFNNGRI 213
Cdd:cd03233 151 SSTALEILKCIRTMADVLKTT-TFVSLYQasDEIYDLFDKVLVLYEGRQ 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-166 |
2.22e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 17 VRAVDGVtiaIRDGEFFSMLGPSGSGKTTCLRLIA----GFEQLSGGTISIFGKEASELPPWER-DVNTVFQDYALFPHM 91
Cdd:TIGR00956 77 LKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 92 SI---LDNVAY----GLMVKGIDKKKRHAQARD-ALEKVGLSFAVARKPSQ-----LSGGQRQRVAIARALVNEPRVLLL 158
Cdd:TIGR00956 154 TVgetLDFAARcktpQNRPDGVSREEYAKHIADvYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCW 233
|
....*...
gi 2673334298 159 DEPLGALD 166
Cdd:TIGR00956 234 DNATRGLD 241
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
113-193 |
6.43e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.18 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 113 AQARDALEKVGLSFAV---ARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQelgiTFI 189
Cdd:PLN03073 320 AEARAASILAGLSFTPemqVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFI 395
|
....
gi 2673334298 190 FVTH 193
Cdd:PLN03073 396 VVSH 399
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
5-208 |
9.76e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVR-AVDGVTIaiRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISiFGKEASELPPW-ERDVNTVF 82
Cdd:PRK13409 341 VEYPDLTKKLGDFSlEVEGGEI--YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-PELKISYKPQYiKPDYDGTV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 83 QDYaLFPHMSILDNVAYGLmvkgidkkkrhaqarDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:PRK13409 418 EDL-LRSITDDLGSSYYKS---------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2673334298 163 GALDLKLREQMQFELKKLQQELGITFIFVTHDqgeaLSM----SDRVAVF 208
Cdd:PRK13409 482 AHLDVEQRLAVAKAIRRIAEEREATALVVDHD----IYMidyiSDRLMVF 527
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
5-208 |
1.24e-08 |
|
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: 56.33 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 5 VEFNNVSRLYGDVR-AVDGVTIaiRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISiFGKEASELPPW-ERDVN-TV 81
Cdd:COG1245 342 VEYPDLTKSYGGFSlEVEGGEI--REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKISYKPQYiSPDYDgTV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 82 fqdyalfphMSILDNVAYglmvKGIDKKKRHAQArdaLEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEP 161
Cdd:COG1245 419 ---------EEFLRSANT----DDFGSSYYKTEI---IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 162 LGALDLKLREQMQFELKKLQQELGITFIFVTHDqgeaLSM----SDRVAVF 208
Cdd:COG1245 483 SAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD----IYLidyiSDRLMVF 529
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-236 |
1.35e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 23 VTIAIRDGEFFSMLGPSGSGKTTCLR-LIAGFEQLSGGTisifgkeaselppW-ERDVNTVFQDyALFPHMSILDNVAYg 100
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFEISEGRV-------------WaERSIAYVPQQ-AWIMNATVRGNILF- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 101 lmvkgIDKKkRHAQARDA-----LEK------VGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKL 169
Cdd:PTZ00243 744 -----FDEE-DAARLADAvrvsqLEAdlaqlgGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 170 REQMQFELkKLQQELGITFIFVTHdQGEALSMSDRVAVFNNGRIEQVDTPRDlYMrpRTPFVAGFVG 236
Cdd:PTZ00243 818 GERVVEEC-FLGALAGKTRVLATH-QVHVVPRADYVVALGDGRVEFSGSSAD-FM--RTSLYATLAA 879
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-194 |
1.37e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 8 NNVSRLYGDVRAV-DGVTIAirdgeFF-----SMLGPSGSGKTTCLRLIAGFEQLSGG--------TISIFGKEAsELPP 73
Cdd:PRK11819 10 NRVSKVVPPKKQIlKDISLS-----FFpgakiGVLGLNGAGKSTLLRIMAGVDKEFEGearpapgiKVGYLPQEP-QLDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 74 wERDVNTVFQDyALFPHMSILD-----NVAYG--------LMVKG------IDKKKRH------AQARDALekvglsfav 128
Cdd:PRK11819 84 -EKTVRENVEE-GVAEVKAALDrfneiYAAYAepdadfdaLAAEQgelqeiIDAADAWdldsqlEIAMDAL--------- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 129 aRKP------SQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDlklREQMQFELKKLQQELGiTFIFVTHD 194
Cdd:PRK11819 153 -RCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLEQFLHDYPG-TVVAVTHD 219
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1-166 |
1.67e-08 |
|
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: 53.79 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRlygdvRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLS--GGTISIFGKEASElpPWERDV 78
Cdd:cd03232 9 LNYTVPVKGGKR-----QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK--NFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 79 NTVFQDYALFPHMSIldnvayglmvkgidkkkrhaqaRDALEkvgLSfAVARkpsQLSGGQRQRVAIARALVNEPRVLLL 158
Cdd:cd03232 82 GYVEQQDVHSPNLTV----------------------REALR---FS-ALLR---GLSVEQRKRLTIGVELAAKPSILFL 132
|
....*...
gi 2673334298 159 DEPLGALD 166
Cdd:cd03232 133 DEPTSGLD 140
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-213 |
2.11e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 15 GDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFE--QLSGGTISIFGKEASELPPWERdvntvfqdyalfPHMS 92
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEER------------AHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 93 ILDNVAYGLMVKGID---------KKKRHAQARDALEKvgLSF---------AVARKPSQL--------SGGQRQRVAIA 146
Cdd:CHL00131 86 IFLAFQYPIEIPGVSnadflrlayNSKRKFQGLPELDP--LEFleiineklkLVGMDPSFLsrnvnegfSGGEKKRNEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 147 RALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQ-QELGItfIFVTHDQgEALS--MSDRVAVFNNGRI 213
Cdd:CHL00131 164 QMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSI--ILITHYQ-RLLDyiKPDYVHVMQNGKI 230
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-222 |
2.35e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 30 GEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGTISIFGKEAselppWERDVNTVFqdyalfpHMSILDNVAYGLMV----- 103
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTVA-----YVPQVSWIF-------NATVRDNILFGSPFdpery 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 104 -KGIDKKkrhAQARD-ALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMqFElKKLQ 181
Cdd:PLN03130 711 eRAIDVT---ALQHDlDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV-FD-KCIK 785
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2673334298 182 QEL-GITFIFVThDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:PLN03130 786 DELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-211 |
2.38e-08 |
|
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: 55.69 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 7 FNNVSRLYGDVraVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEA-SELPPWerdvntvfqdy 85
Cdd:TIGR01271 431 FSNFSLYVTPV--LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISfSPQTSW----------- 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 86 aLFPHmSILDNVAYGLMVkgidKKKRHAQARDA--LEKVGLSFAVARKPS------QLSGGQRQRVAIARALVNEPRVLL 157
Cdd:TIGR01271 498 -IMPG-TIKDNIIFGLSY----DEYRYTSVIKAcqLEEDIALFPEKDKTVlgeggiTLSGGQRARISLARAVYKDADLYL 571
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 158 LDEPLGALDLkLREQMQFE--LKKLQQELgiTFIFVThDQGEALSMSDRVAVFNNG 211
Cdd:TIGR01271 572 LDSPFTHLDV-VTEKEIFEscLCKLMSNK--TRILVT-SKLEHLKKADKILLLHEG 623
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-211 |
2.98e-08 |
|
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: 54.09 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 23 VTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKeaselppwerdVNTVFQDYALFPHmSILDNVAYGLM 102
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIFGVS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 103 VKgidkKKRHAQARDA--LEKVGLSFA------VARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMq 174
Cdd:cd03291 124 YD----EYRYKSVVKAcqLEEDITKFPekdntvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI- 198
|
170 180 190
....*....|....*....|....*....|....*..
gi 2673334298 175 FELKKLQQELGITFIFVThDQGEALSMSDRVAVFNNG 211
Cdd:cd03291 199 FESCVCKLMANKTRILVT-SKMEHLKKADKILILHEG 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
123-222 |
5.16e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.57 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 123 GLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKklQQELGITFIFVTHDQGEALSMS 202
Cdd:TIGR00957 1410 KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT 1487
|
90 100
....*....|....*....|
gi 2673334298 203 dRVAVFNNGRIEQVDTPRDL 222
Cdd:TIGR00957 1488 -RVIVLDKGEVAEFGAPSNL 1506
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-213 |
9.86e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.10 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 22 GVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFE--QLSGGTISIFGKEASELPPWERDVNTVFQdyaLFPHMSILDNVAY 99
Cdd:PRK09580 19 GLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFM---AFQYPVEIPGVSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 100 GLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQL---------------SGGQRQRVAIARALVNEPRVLLLDEPLGA 164
Cdd:PRK09580 96 QFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 165 LDLKLREQMQFELKKLQQElGITFIFVTHDQgEALSM--SDRVAVFNNGRI 213
Cdd:PRK09580 176 LDIDALKIVADGVNSLRDG-KRSFIIVTHYQ-RILDYikPDYVHVLYQGRI 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-239 |
1.55e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 4 AVEFNNVSRLY-GDVRAV-DGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKEASELPPWE--RDVN 79
Cdd:PLN03130 1237 SIKFEDVVLRYrPELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 80 TVFQDYALFPhmsildnvayGLMVKGIDKKKRHAQAR--DALEKVGLSFAVARKPSQL-----------SGGQRQRVAIA 146
Cdd:PLN03130 1317 IIPQAPVLFS----------GTVRFNLDPFNEHNDADlwESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLA 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 147 RALVNEPRVLLLDEPLGALDLKLREQMQfelKKLQQEL-GITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDTPRDLYMR 225
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDVRTDALIQ---KTIREEFkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
250
....*....|....*..
gi 2673334298 226 PRTPFvAGFV---GTSN 239
Cdd:PLN03130 1463 EGSAF-SKMVqstGAAN 1478
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-210 |
1.61e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 25 IAIRDGEFFSMLGPSGSGKTTCLRLIAG-FEQLSGGTISIFG-----------KEASElpPWERDvNTvfqdyalfpHMS 92
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGeLPLLSGERQSQFShitrlsfeqlqKLVSD--EWQRN-NT---------DML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 93 ILDNVAYGLMVKGIDKKKRHAQARDAL--EKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLR 170
Cdd:PRK10938 92 SPGEDDTGRTTAEIIQDEVKDPARCEQlaQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2673334298 171 EQMQFELKKLQQElGITFIFVTHDQGEALSMSDRVAVFNN 210
Cdd:PRK10938 172 QQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-230 |
1.76e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 22 GVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGKE--ASELPPWERDVNTVFQDYALFPHmSILDNVAY 99
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREigAYGLRELRRQFSMIPQDPVLFDG-TVRQNVDP 1406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 100 GLmvkgidkKKRHAQARDALEKVGLSFAVARKP-----------SQLSGGQRQRVAIARALVNEPR-VLLLDEPLGALDL 167
Cdd:PTZ00243 1407 FL-------EASSAEVWAALELVGLRERVASESegidsrvleggSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDP 1479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2673334298 168 KLREQMQFELkkLQQELGITFIFVTHdQGEALSMSDRVAVFNNGRIEQVDTPRDLYMRPRTPF 230
Cdd:PTZ00243 1480 ALDRQIQATV--MSAFSAYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-223 |
2.06e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 23 VTIAIRDGEFFSMLGPSGSGKTTCLRLIAGfeqlsggtisifgkeasELPPWERDVNTVFQDYALFPHMS------ILDN 96
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVVIRGSVAYVPQVSwifnatVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 97 VAYGLMVKgidkKKRHAQARD--ALEKVGLSFA------VARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLK 168
Cdd:PLN03232 699 ILFGSDFE----SERYWRAIDvtALQHDLDLLPgrdlteIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 169 LREQ-----MQFELKklqqelGITFIFVThDQGEALSMSDRVAVFNNGRIEQVDTPRDLY 223
Cdd:PLN03232 775 VAHQvfdscMKDELK------GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-225 |
2.38e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.09 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 10 VSRLYGDVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISI-----FGKEASELPPWERDVNTVFQd 84
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLakgikLGYFAQHQLEFLRADESPLQ- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 85 yalfpHMSILDnvayglmvkgidKKKRHAQARDALEKVGLSF-AVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:PRK10636 397 -----HLARLA------------PQELEQKLRDYLGGFGFQGdKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2673334298 164 ALDLKLREQMQFELKKLQQELgitfIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDLYMR 225
Cdd:PRK10636 460 HLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-215 |
9.10e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 19 AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGTISIFGkeaselppwerDVNTVFQDYALFPHMSILDNVA 98
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIAISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 99 YGLMVKGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMqfeLK 178
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC---LD 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 2673334298 179 KLQQ--ELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQ 215
Cdd:PRK13546 185 KIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
23-237 |
1.22e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 49.14 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 23 VTIAIRDGEFFSMLGPSGSGKTTC----LRLIAGFEqlsgGTISIFGKEASELP--PWERDVNTVFQDYALFPhmsildn 96
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPlhTLRSRLSIILQDPILFS------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 97 vayGLMVKGIDKKKRHAQAR--DALEKVGLSFAVARKPSQL-----------SGGQRQRVAIARALVNEPRVLLLDEPLG 163
Cdd:cd03288 109 ---GSIRFNLDPECKCTDDRlwEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2673334298 164 ALDLKLREQMQfelKKLQQELG-ITFIFVTHDQGEALSmSDRVAVFNNGRIEQVDTPRDLYMRPRTPFvAGFVGT 237
Cdd:cd03288 186 SIDMATENILQ---KVVMTAFAdRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF-ASLVRT 255
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
257-333 |
1.25e-06 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 45.30 E-value: 1.25e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2673334298 257 SLRPEHIRLDEGGDVQVQGVVQAvQYQGAATRLELKLADGARLLVSQANLSEASPlsgiAPGQAVTASWSREAMIRL 333
Cdd:pfam08402 2 AIRPEKIRLAAAANGLSGTVTDV-EYLGDHTRYHVELAGGEELVVRVPNAHARPP----APGDRVGLGWDPEDAHVL 73
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-222 |
1.38e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.08 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 20 VDGVTIAIRDGEFFSMLGPSGSGKTTclrLIAGFEQL--SGGTISIFGKEASELP--PWERDVNTVFQDYALFPhmsild 95
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKST---LLSAFLRLlnTEGDIQIDGVSWNSVPlqKWRKAFGVIPQKVFIFS------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 96 nvayGLMVKGIDKKKRHAQAR--DALEKVGLSFAVARKPSQL-----------SGGQRQRVAIARALVNEPRVLLLDEPL 162
Cdd:cd03289 91 ----GTFRKNLDPYGKWSDEEiwKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 163 GALDlklREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:cd03289 167 AHLD---PITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-193 |
2.62e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 1 MTYAVEFNNVSRLY-------------------GDVR-AVDGVTIAIRDGEFFSMLGPSGSGKTTCLRLIAGFEQLSGGT 60
Cdd:PRK13545 1 MNYKVKFEHVTKKYkmynkpfdklkdlffrskdGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 61 ISIFGKEAselppwerdvnTVFQDYALFPHMSILDNVAY-GLMVkGIDKKKRHAQARDALEKVGLSFAVARKPSQLSGGQ 139
Cdd:PRK13545 81 VDIKGSAA-----------LIAISSGLNGQLTGIENIELkGLMM-GLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGM 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 140 RQRVAIARALVNEPRVLLLDEPLGALDLKLREQMqfeLKKLQQ--ELGITFIFVTH 193
Cdd:PRK13545 149 KSRLGFAISVHINPDILVIDEALSVGDQTFTKKC---LDKMNEfkEQGKTIFFISH 201
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
9-205 |
2.69e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.93 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 9 NVSRLYgdVRAVDGVTIAIRDGEFFSMLGPSGSGKTTCLrliagfeqLSGGTISIFGKEASELPPWERDvNTVFqdyalf 88
Cdd:cd03238 2 TVSGAN--VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV--------NEGLYASGKARLISFLPKFSRN-KLIF------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 89 phmsildnvayglmvkgIDKKKRhaqardaLEKVGLSF-AVARKPSQLSGGQRQRVAIARALVNEPR--VLLLDEPLGAL 165
Cdd:cd03238 65 -----------------IDQLQF-------LIDVGLGYlTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2673334298 166 DLKLREQMQFELKKLQQeLGITFIFVTHDQgEALSMSDRV 205
Cdd:cd03238 121 HQQDINQLLEVIKGLID-LGNTVILIEHNL-DVLSSADWI 158
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-222 |
6.65e-06 |
|
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: 47.98 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 18 RAV-DGVTIAIRDGEFFSMLGPSGSGKTTclrLIAGFEQL--SGGTISIFGK--EASELPPWERDVNTVFQDYALFPhms 92
Cdd:TIGR01271 1232 RAVlQDLSFSVEGGQRVGLLGRTGSGKST---LLSALLRLlsTEGEIQIDGVswNSVTLQTWRKAFGVIPQKVFIFS--- 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 93 ildnvayGLMVKGIDKkkrHAQARD-----ALEKVGLSFAVARKPSQL-----------SGGQRQRVAIARALVNEPRVL 156
Cdd:TIGR01271 1306 -------GTFRKNLDP---YEQWSDeeiwkVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2673334298 157 LLDEPLGALDlklREQMQFELKKLQQELGITFIFVTHDQGEALSMSDRVAVFNNGRIEQVDTPRDL 222
Cdd:TIGR01271 1376 LLDEPSAHLD---PVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKL 1438
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
128-213 |
8.38e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 128 VARKPSQLSGGQRQRVAIARALVNEPRVLLLDEP-----LGAldlklreqmQFELKKLQQEL---GITFIFVTHDQGEAL 199
Cdd:NF040905 398 VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPtrgidVGA---------KYEIYTIINELaaeGKGVIVISSELPELL 468
|
90
....*....|....
gi 2673334298 200 SMSDRVAVFNNGRI 213
Cdd:NF040905 469 GMCDRIYVMNEGRI 482
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
92-195 |
5.77e-05 |
|
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: 42.73 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 92 SILDNVAYGLMVKGIDKKKRHAQARD---ALEKVGLSFAVarkpSQLSGGQRQRVAIARALVNE---PRVL-LLDEPLGA 164
Cdd:cd03227 36 TILDAIGLALGGAQSATRRRSGVKAGcivAAVSAELIFTR----LQLSGGEKELSALALILALAslkPRPLyILDEIDRG 111
|
90 100 110
....*....|....*....|....*....|.
gi 2673334298 165 LDLKLREQMQFELKKLQQElGITFIFVTHDQ 195
Cdd:cd03227 112 LDPRDGQALAEAILEHLVK-GAQVIVITHLP 141
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
26-63 |
4.13e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 41.99 E-value: 4.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2673334298 26 AIRDGEFFSML--GPSGSGKTTCLRLIAG-----FEQLSGGTISI 63
Cdd:PRK13342 30 MIEAGRLSSMIlwGPPGTGKTTLARIIAGatdapFEALSAVTSGV 74
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
119-205 |
5.30e-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: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 119 LEKVGLSF-AVARKPSQLSGGQRQRVAIAR----ALVNeprVL-LLDEPLGALDLKLREQMQFELKKLqQELGITFIFVT 192
Cdd:TIGR00630 472 LIDVGLDYlSLSRAAGTLSGGEAQRIRLATqigsGLTG---VLyVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVE 547
|
90
....*....|...
gi 2673334298 193 HDQgEALSMSDRV 205
Cdd:TIGR00630 548 HDE-DTIRAADYV 559
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
114-195 |
1.00e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 114 QARDALEKVGLSFA---VARKPSQLSGGQRQRVAIARALVNEPRVLLLDEPLGALDLKLREQMQFELKKLQQelgiTFIF 190
Cdd:PRK10636 126 RSRAASLLHGLGFSneqLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLIL 201
|
....*
gi 2673334298 191 VTHDQ 195
Cdd:PRK10636 202 ISHDR 206
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
37-89 |
1.75e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 38.24 E-value: 1.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2673334298 37 GPSGSGKTTCLRLIA---GFEQLSGGTISI--FGKEASE---LPPWERDVNTVFQDYALFP 89
Cdd:cd02020 6 GPAGSGKSTVAKLLAkklGLPYLDTGGIRTeeVGKLASEvaaIPEVRKALDERQRELAKKP 66
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-205 |
2.28e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 119 LEKVGLSF-AVARKPSQLSGGQRQRVAIARALVNEPR--VLLLDEPLGALDLKLREQMQFELKKLQQElGITFIFVTHDQ 195
Cdd:PRK00635 460 LIDLGLPYlTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDE 538
|
90
....*....|
gi 2673334298 196 gEALSMSDRV 205
Cdd:PRK00635 539 -QMISLADRI 547
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
120-205 |
5.26e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.51 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 120 EKVGLSFavarkpsqLSGGQRQ------RVAIARALVNEPRVLLLDEPLGALD----LKLREQMQFELKKLQQelgitFI 189
Cdd:PRK03918 782 KERPLTF--------LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDeerrRKLVDIMERYLRKIPQ-----VI 848
|
90
....*....|....*.
gi 2673334298 190 FVTHDQgEALSMSDRV 205
Cdd:PRK03918 849 IVSHDE-ELKDAADYV 863
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-194 |
9.25e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 36.82 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 31 EFFSML----GPSGSGKTT---CLRLiagfeqlsggtiSIFGkeasELPPWERDVntvfqdyALFPHM-SILDNVAY-GL 101
Cdd:cd03240 19 EFFSPLtlivGQNGAGKTTiieALKY------------ALTG----ELPPNSKGG-------AHDPKLiREGEVRAQvKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 102 MVKGIDKKKRHAQAR-DALEKV-----GLSFA-VARKPSQLSGGQRQ------RVAIARALVNEPRVLLLDEPLGALD-- 166
Cdd:cd03240 76 AFENANGKKYTITRSlAILENVifchqGESNWpLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDee 155
|
170 180 190
....*....|....*....|....*....|.
gi 2673334298 167 ---LKLREQMQFELKKLQQELGItfifVTHD 194
Cdd:cd03240 156 nieESLAEIIEERKSQKNFQLIV----ITHD 182
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
119-205 |
9.79e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 36.85 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2673334298 119 LEKVGLSF-AVARKPSQLSGGQRQRVAIARALVNEPRVLL--LDEPLGALDLKLREQMQFELKKLQQeLGITFIFVTHDQ 195
Cdd:cd03270 121 LVDVGLGYlTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDE 199
|
90
....*....|
gi 2673334298 196 gEALSMSDRV 205
Cdd:cd03270 200 -DTIRAADHV 208
|
|
| |
