|
Name |
Accession |
Description |
Interval |
E-value |
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-321 |
0e+00 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 535.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV-SGHDVRDRNVGFV 79
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDNVAFGLRMKPkhqrPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLL 159
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRP----PSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 160 LDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGD 239
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 240 SNRLH---------------------LGEDRHVLFRPHEVSLSR-SELEDHHAAEVRDIRPLGATTRVTLKVEGQS-ELI 296
Cdd:COG1118 237 VNVLRgrviggqleadgltlpvaeplPDGPAVAGVRPHDIEVSRePEGENTFPATVARVSELGPEVRVELKLEDGEgQPL 316
|
330 340
....*....|....*....|....*
gi 517442396 297 EAEVVKDHDSLVGLAKGETLFFKPK 321
Cdd:COG1118 317 EAEVTKEAWAELGLAPGDPVYLRPR 341
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-239 |
9.42e-173 |
|
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: 478.76 E-value: 9.42e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVF 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHMTVFDNVAFGLRMKPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 161 DEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGD 239
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-318 |
1.24e-158 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 447.24 E-value: 1.24e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQ 81
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 HYALFRHMTVFDNVAFGLRMKpkhqRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLD 161
Cdd:COG3842 85 DYALFPHLTVAENVAFGLRMR----GVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 162 EPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGDSN 241
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 242 RL---------------------------HLGEDRHVLFRPHEVSLSRSELEDHHAAEVRDIRPLGATTRVTLKVEGQSE 294
Cdd:COG3842 241 LLpgtvlgdegggvrtggrtlevpadaglAAGGPVTVAIRPEDIRLSPEGPENGLPGTVEDVVFLGSHVRYRVRLGDGQE 320
|
330 340
....*....|....*....|....
gi 517442396 295 LieaEVVKDHDSLVGLAKGETLFF 318
Cdd:COG3842 321 L---VVRVPNRAALPLEPGDRVGL 341
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-262 |
1.67e-155 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 439.52 E-value: 1.67e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVF 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHMTVFDNVAFGLRMKPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 161 DEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGDS 240
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 517442396 241 NR---------LHLGEDR-------------HVLFRPHEVSLSR 262
Cdd:PRK10851 241 NRlqgtirggqFHVGAHRwplgytpayqgpvDLFLRPWEVDISR 284
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-320 |
2.28e-137 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 393.28 E-value: 2.28e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQ 81
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 HYALFRHMTVFDNVAFGLRMkpkhQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLD 161
Cdd:COG3839 83 SYALYPHMTVYENIAFPLKL----RKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 162 EPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGD-- 239
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSpp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 240 ---------SNRLHLGEDRHVL---------------FRPHEVSLSRSElEDHHAAEVRDIRPLGATTRVTLKVEGQsel 295
Cdd:COG3839 239 mnllpgtveGGGVRLGGVRLPLpaalaaaaggevtlgIRPEHLRLADEG-DGGLEATVEVVEPLGSETLVHVRLGGQ--- 314
|
330 340
....*....|....*....|....*
gi 517442396 296 ieaEVVKDHDSLVGLAKGETLFFKP 320
Cdd:COG3839 315 ---ELVARVPGDTRLRPGDTVRLAF 336
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
3-243 |
4.08e-136 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 385.69 E-value: 4.08e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQH 82
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGLRMkpkhQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEI----RKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGDSNR 242
Cdd:TIGR00968 157 PFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
|
.
gi 517442396 243 L 243
Cdd:TIGR00968 237 L 237
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-238 |
5.04e-124 |
|
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: 355.01 E-value: 5.04e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQH 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGLRMKpkhqRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLK----KLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLG 238
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-318 |
3.77e-122 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 354.73 E-value: 3.77e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQH 82
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGLrmkpKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:TIGR03265 85 YALFPNLTVADNIAYGL----KNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGDSNR 242
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 243 LH--LGEDRHVLF----------------------RPHEVSLSRSELEDHH-AAEVRDIRPLGATTRVTLKVEGQSEL-I 296
Cdd:TIGR03265 241 LPgtRGGGSRARVggltlacapglaqpgasvrlavRPEDIRVSPAGNAANLlLARVEDMEFLGAFYRLRLRLEGLPGQaL 320
|
330 340
....*....|....*....|..
gi 517442396 297 EAEVVKDHDSLVGLAKGETLFF 318
Cdd:TIGR03265 321 VADVSASEVERLGIRAGQPIWI 342
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-241 |
1.54e-114 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 336.15 E-value: 1.54e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQH 82
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGLRMKpkhQRPNEsQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQ---KTPAA-EITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGDSN 241
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEIN 249
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-219 |
3.35e-114 |
|
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: 329.48 E-value: 3.35e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQH 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGLRMkpkhQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03259 81 YALFPHLTVAENIAFGLKL----RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIG 219
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-316 |
5.77e-102 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 301.62 E-value: 5.77e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFV 79
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDNVAFGLRMK--PKhqrpneSQIATKVHELLNMVQLD--WLADRYPEQLSGGQRQRIALARALAVEP 155
Cdd:COG1125 82 IQQIGLFPHMTVAENIATVPRLLgwDK------ERIRARVDELLELVGLDpeEYRDRYPHELSGGQQQRVGVARALAADP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 156 KVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYH 235
Cdd:COG1125 156 PILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 236 FLGDSNRLHLgedrhvlfrphevsLSRSELEDHHAAEVRDIRPlGATTRVTLKVEGQSELIEAEVVKDHDSLVGLAKGET 315
Cdd:COG1125 236 FVGADRGLRR--------------LSLLRVEDLMLPEPPTVSP-DASLREALSLMLERGVDWLLVVDEDGRPLGWLTLED 300
|
.
gi 517442396 316 L 316
Cdd:COG1125 301 L 301
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-218 |
7.29e-100 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 294.69 E-value: 7.29e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGhdvRDRNVGF 78
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG---PGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHMTVFDNVAFGLRMkpkhQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVL 158
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGLEL----RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 159 LLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKG---VIEQI 218
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARpgrIVEEI 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-219 |
1.16e-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: 289.93 E-value: 1.16e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQH 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGLRMKpkHQRPNEsqIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLR--KVPKDE--IDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIG 219
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-298 |
3.12e-98 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 293.93 E-value: 3.12e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQH 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGLRMkpkhQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKM----LGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGDSN- 241
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANi 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 242 -------------RLHLGEDRHVLF-----------RPHEVSLSrSELEDHHAAEVRDIRPLGATTRVTLKVEGQSELIE 297
Cdd:PRK11432 243 fpatlsgdyvdiyGYRLPRPAAFAFnlpdgectvgvRPEAITLS-EQGEESQRCTIKHVAYMGPQYEVTVDWHGQELLLQ 321
|
.
gi 517442396 298 A 298
Cdd:PRK11432 322 V 322
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-327 |
1.82e-97 |
|
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: 290.93 E-value: 1.82e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 33 LLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQHYALFRHMTVFDNVAFGLRMkpkhQRPNESQ 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKM----RKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 113 IATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVF 192
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 193 VTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGDSNRL------HLGEDR----------------- 249
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFeatvieRKSEQVvlagvegrrcdiytdvp 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 250 -------HVLFRPHEVSLsRSELEDHHA----AEVRDIRPLGATTRVTLKVE-GQSELIEAEVVKDHdslvglakgetLF 317
Cdd:TIGR01187 237 vekdqplHVVLRPEKIVI-EEEDEANSSnaiiGHVIDITYLGMTLEVHVRLEtGQKVLVSEFFNEDD-----------PH 304
|
330
....*....|
gi 517442396 318 FKPKVWQKVA 327
Cdd:TIGR01187 305 MSPSIGDRVG 314
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-212 |
2.96e-97 |
|
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: 286.68 E-value: 2.96e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDvrdRNVGF 78
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG---PDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHMTVFDNVAFGLRMkpkhQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVL 158
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLEL----QGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517442396 159 LLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNK 212
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-238 |
4.11e-93 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 280.96 E-value: 4.11e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVF 80
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHMTVFDNVAFGLRMK--PKHQrpnesqIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVL 158
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRgmPKAE------IEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 159 LLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLG 238
Cdd:PRK11650 157 LFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIG 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-238 |
1.62e-92 |
|
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: 275.33 E-value: 1.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFR-ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFV 79
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDNVAfglrMKPKHQRPNESQIATKVHELLNMVQLD--WLADRYPEQLSGGQRQRIALARALAVEPKV 157
Cdd:cd03295 81 IQQIGLFPHMTVEENIA----LVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 158 LLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFL 237
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
.
gi 517442396 238 G 238
Cdd:cd03295 237 G 237
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
3-289 |
1.14e-89 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 271.95 E-value: 1.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRaLDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQH 82
Cdd:NF040840 2 IRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGLRMKpkhqRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:NF040840 81 YMLFPHKTVFENIAFGLKLR----KVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGDSN- 241
Cdd:NF040840 157 PLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENi 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 242 -------------------RLHLGEDR----HVLFRPHEVSLSRSELE----DHHAAEVRDIRPLGATTRVTLKV 289
Cdd:NF040840 237 iegvaekggegtildtgniKIELPEEKkgkvRIGIRPEDITISTEKVKtsarNEFKGKVEEIEDLGPLVKLTLDV 311
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-241 |
9.76e-88 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 267.86 E-value: 9.76e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQH 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGLrmkpKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK11607 100 YALFPHMTVEQNIAFGL----KQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGDSN 241
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-237 |
1.02e-86 |
|
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: 260.30 E-value: 1.02e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD-----RNVG 77
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQHYALFRHMTVFDNVAFGLRMkpkHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKV 157
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLRE---HTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 158 LLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPaSDFVYHFL 237
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-241 |
3.04e-86 |
|
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: 259.19 E-value: 3.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRaLDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQH 82
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGLRMKpkhqRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKR----KVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGDSN 241
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNN 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-231 |
1.82e-85 |
|
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: 266.38 E-value: 1.82e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD---- 73
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 -RNVGFVFQH--YALFRHMTVFDNVAFGLRMkpkHQRPNESQIATKVHELLNMVQLD-WLADRYPEQLSGGQRQRIALAR 149
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRL---HGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPA 229
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
..
gi 517442396 230 SD 231
Cdd:COG1123 498 HP 499
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-231 |
4.97e-85 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 256.07 E-value: 4.97e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV--SGHDVRD--RNVGF 78
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKlrRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHMTVFDNVAFGLRmkpKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVL 158
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPI---KVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 159 LLDEPFGALD-------AKVRKELRRwlarlhEDInlTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASD 231
Cdd:COG1126 159 LFDEPTSALDpelvgevLDVMRDLAK------EGM--TMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-216 |
1.04e-80 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 244.57 E-value: 1.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHD------VR 72
Cdd:COG1136 5 LELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelarLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 73 DRNVGFVFQHYALFRHMTVFDNVAFGLRMKPKHQRpnesQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALA 152
Cdd:COG1136 85 RRHIGFVFQFFNLLPELTALENVALPLLLAGVSRK----ERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517442396 153 VEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDqEEAMEVADRIVVMNKGVIE 216
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-215 |
1.33e-80 |
|
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: 243.94 E-value: 1.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG------HDVR 72
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 73 DRNVGFVFQHYALFRHMTVFDNVAFGLRMKPKHQRpnesQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALA 152
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKK----ERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 153 VEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAmEVADRIVVMNKGVI 215
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-224 |
6.36e-80 |
|
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: 243.18 E-value: 6.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD-----RNVG 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQHYALFRHMTVFDNVAFGLRMkpkHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKV 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLRE---HTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 158 LLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDV 224
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-213 |
6.23e-79 |
|
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: 238.24 E-value: 6.23e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHD----VRDRNVGF 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHMTVFDNVAFGlrmkpkhqrpnesqiatkvhellnmvqldwladrypeqLSGGQRQRIALARALAVEPKVL 158
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 159 LLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-238 |
2.21e-78 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 243.78 E-value: 2.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQ 81
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 HYALFRHMTVFDNVAFGLrmkpKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLD 161
Cdd:PRK11000 83 SYALYPHLSVAENMSFGL----KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 162 EPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLG 238
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-228 |
4.12e-78 |
|
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: 238.00 E-value: 4.12e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFV 79
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQH--YALFrHMTVFDNVAFGlrmkPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKV 157
Cdd:COG1122 81 FQNpdDQLF-APTVEEDVAFG----PENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517442396 158 LLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-248 |
7.70e-75 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 233.43 E-value: 7.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV---SGHDVRD-- 73
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 RNVGFVFQHYALFRHMTVFDNVAFGLRM--KPKhqrpneSQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARAL 151
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIagVPK------AEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 152 AVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDqeeaMEV----ADRIVVMNKG-VIEQiGSPGDVYE 226
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE----MDVvrriCDRVAVLENGrIVEQ-GPVLDVFA 230
|
250 260
....*....|....*....|..
gi 517442396 227 NPASDFVYHFLGDSNRLHLGED 248
Cdd:COG1135 231 NPQSELTRRFLPTVLNDELPEE 252
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-243 |
1.30e-74 |
|
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: 230.61 E-value: 1.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 8 VSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG------HDVRDRNVGFVFQ 81
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkelRELRRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 HYALFRHMTVFDNVAFGLRMK--PKHQRpnesqiATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLL 159
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQgvPRAER------EERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 160 LDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGD 239
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
....
gi 517442396 240 SNRL 243
Cdd:cd03294 264 VDRA 267
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-219 |
1.90e-73 |
|
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: 225.64 E-value: 1.90e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQ---SGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGE---------DVSghdVRDRNVGFVFQHYAL 85
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkiNLP---PQQRKIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 86 FRHMTVFDNVAFGLRMKpkhqRPNESQIatKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFG 165
Cdd:cd03297 87 FPHLNVRENLAFGLKRK----RNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517442396 166 ALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIG 219
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-242 |
3.78e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 225.71 E-value: 3.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGH--DVRdRNVGFVF 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDpaEVR-RRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHMTVFDNVAFGLRMKPKhqrpNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGL----PRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 161 DEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGDS 240
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFLELTGEE 234
|
..
gi 517442396 241 NR 242
Cdd:COG1131 235 AR 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-215 |
4.62e-73 |
|
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: 224.72 E-value: 4.62e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVR----DRNVGF 78
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHMTVFDNVAFGLrMKPKHQRPNESQiaTKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVL 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAP-IKVKGMSKAEAE--ERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 159 LLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-317 |
8.16e-73 |
|
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: 228.83 E-value: 8.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRnVSKNFNAFrALDeISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGE----DVSGHDV--RDR 74
Cdd:COG4148 1 MMLEVD-FRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLppHRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 75 NVGFVFQHYALFRHMTVFDNVAFGLRMKPKHQRPnesqiaTKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVE 154
Cdd:COG4148 78 RIGYVFQEARLFPHLSVRGNLLYGRKRAPRAERR------ISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 155 PKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPAS---- 230
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLlpla 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 231 ----------------DFVYH-----FLGDS---NRLHLGEDRHVLFR--PHEVSLSRSELED-----HHAAEVRDIRPL 279
Cdd:COG4148 232 ggeeagsvleatvaahDPDYGltrlaLGGGRlwvPRLDLPPGTRVRVRirARDVSLALEPPEGssilnILPGRVVEIEPA 311
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 517442396 280 -GATTRVTLKVEGQSelIEAEVV-KDHDSLvGLAKGETLF 317
Cdd:COG4148 312 dGGQVLVRLDLGGQT--LLARITrRSADEL-GLAPGQTVY 348
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-240 |
2.71e-72 |
|
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: 223.91 E-value: 2.71e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNV 76
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHY--ALFRHMTVFDNVAFGLRMkpkHQRPNesqIATKVHELLNMVQLDW-LADRYPEQLSGGQRQRIALARALAV 153
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRI---HGLPD---REERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 154 EPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFV 233
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYT 235
|
....*..
gi 517442396 234 YHFLGDS 240
Cdd:COG1124 236 RELLAAS 242
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
17-239 |
6.11e-72 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 227.04 E-value: 6.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 17 ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHD------VRDRNVGFVFQHYALFRHMT 90
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSpvelreVRRKKIGMVFQQFALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 91 VFDNVAFGlrmkPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAK 170
Cdd:TIGR01186 88 ILQNTSLG----PELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 171 VRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGD 239
Cdd:TIGR01186 164 IRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-228 |
6.61e-72 |
|
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: 222.46 E-value: 6.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV---SGHDVRD-- 73
Cdd:cd03258 2 IELKNVSKVFgdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 RNVGFVFQHYALFRHMTVFDNVAFGLRM--KPKhqrpneSQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARAL 151
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIagVPK------AEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 152 AVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-217 |
7.11e-71 |
|
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: 219.68 E-value: 7.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHD-----VRD 73
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 RNVGFVFQHY--ALFRHMTVFDNVAFGLRmkpKHQRP-NESQIATKVHELLNMVQLD-WLADRYPEQLSGGQRQRIALAR 149
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLR---IHGKLsKKEARKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKG-VIEQ 217
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGkIVEE 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-237 |
1.73e-70 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 219.73 E-value: 1.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MS-IEVRNVSKNFNAFR----ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVrDRN 75
Cdd:COG4525 1 MSmLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 76 VgfVFQHYALFRHMTVFDNVAFGLRMK--PKHQRpneSQIAtkvHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAV 153
Cdd:COG4525 80 V--VFQKDALLPWLNVLDNVAFGLRLRgvPKAER---RARA---EELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 154 EPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNkgvieqiGSPGDVYENPASDFV 233
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMS-------PGPGRIVERLELDFS 224
|
....
gi 517442396 234 YHFL 237
Cdd:COG4525 225 RRFL 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-238 |
4.72e-70 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 217.70 E-value: 4.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRAldEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQH 82
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGLRmkPKhQRPNESQIAtKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLR--PG-LKLTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLG 238
Cdd:COG3840 156 PFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-213 |
6.29e-70 |
|
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: 216.56 E-value: 6.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVSKNFN--AFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFV 79
Cdd:cd03225 1 ELKNLSFSYPdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQH--YALFRHmTVFDNVAFGLRmkpkHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKV 157
Cdd:cd03225 81 FQNpdDQFFGP-TVEEEVAFGLE----NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 158 LLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-237 |
9.18e-69 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 214.57 E-value: 9.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNV----GF 78
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHMTVFDNVAFGlrmkPKHQRPNESQIATKV-HELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKV 157
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFG----PLRVRGASKEEAEKQaRELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 158 LLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFL 237
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-229 |
4.83e-68 |
|
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: 213.36 E-value: 4.83e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG---HDVRDRNVGFVF 80
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlppHRIARLGIARTF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHMTVFDNVAFGLRMKPKH-----------QRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALAR 149
Cdd:COG0411 86 QNPRLFPELTVLENVLVAAHARLGRgllaallrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKG-VIEQiGSPGDVYENP 228
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGrVIAE-GTPAEVRADP 244
|
.
gi 517442396 229 A 229
Cdd:COG0411 245 R 245
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-224 |
8.14e-67 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 210.29 E-value: 8.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFVF 80
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHMTVFDNVAFGlRM--KPKHQRPNESQIAtKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVL 158
Cdd:COG1120 82 QEPPAPFGLTVRELVALG-RYphLGLFGRPSAEDRE-AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 159 LLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDV 224
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-221 |
2.04e-66 |
|
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: 208.19 E-value: 2.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGL-----ETPDQGSIVFHGEDVSGHDVRD---- 73
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 RNVGFVFQHYALFRhMTVFDNVAFGLRMkpkHQRPNESQIATKVHELLNMVQL-DWLADR-YPEQLSGGQRQRIALARAL 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRL---HGIKLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 152 AVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDInlTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSP 221
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-229 |
4.53e-66 |
|
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: 207.67 E-value: 4.53e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRN---VGFV 79
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDNVAFGLRMKPKH------QRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAV 153
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSglllarARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 154 EPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKG-VIEQiGSPGDVYENPA 229
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGrVIAE-GTPDEVRNNPR 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-222 |
1.34e-64 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 203.36 E-value: 1.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD-----RNV 76
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHYALFRHMTVFDNVAFGLRMKPKhqrpNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGK----SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 157 VLLLDEPFGALDAkvrkELRRWLARLHEDINL--TSVFV-THDQEEAMEVADRIVVMNKGVIEQIGSPG 222
Cdd:COG2884 158 LLLADEPTGNLDP----ETSWEIMELLEEINRrgTTVLIaTHDLELVDRMPKRVLELEDGRLVRDEARG 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-248 |
2.65e-64 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 206.58 E-value: 2.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD----- 73
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 RNVGFVFQHYALFRHMTVFDNVAFGLRM--KPKhqrpneSQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARAL 151
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELagTPK------AEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 152 AVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKG-VIEQiGSPGDVYENPAS 230
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGrLVEQ-GTVSEVFSHPKH 234
|
250
....*....|....*...
gi 517442396 231 DFVYHFLGDSNRLHLGED 248
Cdd:PRK11153 235 PLTREFIQSTLHLDLPED 252
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-228 |
2.32e-63 |
|
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: 201.91 E-value: 2.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVS----KNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG------HDV 71
Cdd:TIGR04521 1 IKLKNVSyiyqPGTpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkkklKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 72 RdRNVGFVFQH--YALFRhMTVFDNVAFGlrmkPKHQRPNESQIATKVHELLNMVQLDW-LADRYPEQLSGGQRQRIALA 148
Cdd:TIGR04521 81 R-KKVGLVFQFpeHQLFE-ETVYKDIAFG----PKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-232 |
2.37e-63 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 201.05 E-value: 2.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV---SGHDVRD--RNV 76
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalRGRALRRlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHYALFRHMTVFDNVAFG-----------LRMKPKHQRPnesqiatKVHELLNMVQLDWLADRYPEQLSGGQRQRI 145
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLFPPEDRE-------RALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIeqigspgdVY 225
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV--------VF 227
|
....*..
gi 517442396 226 ENPASDF 232
Cdd:COG3638 228 DGPPAEL 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-215 |
4.46e-62 |
|
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: 195.31 E-value: 4.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVS--GHDVRdRNVGFVF 80
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKkePEEVK-RRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHMTVFDNVafglrmkpkhqrpnesqiatkvhellnmvqldwladrypeQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:cd03230 80 EEPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 161 DEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-230 |
2.02e-61 |
|
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: 203.98 E-value: 2.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF--NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPD---QGSIVFHGEDVSGHD--VRDRN 75
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSeaLRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 76 VGFVFQHY-ALFRHMTVFDNVAFGLRmkpkHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVE 154
Cdd:COG1123 85 IGMVFQDPmTQLNPVTVGDQIAEALE----NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 155 PKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPAS 230
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-224 |
2.65e-61 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 195.69 E-value: 2.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGhdvRDRNVGFVFQH 82
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRH--MTVFDNVAFGL-RMKPKHQRPNESQIAtKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLL 159
Cdd:COG1121 84 AEVDWDfpITVRDVVLMGRyGRRGLFRRPSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 160 LDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQiGSPGDV 224
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEV 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-229 |
7.44e-61 |
|
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: 197.20 E-value: 7.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFN----AFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETP---DQGSIVFHGEDVSG------H 69
Cdd:COG0444 2 LEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekelR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 70 DVRDRNVGFVFQH-Y-ALFRHMTVFDNVAFGLRmkpKHQRPNESQIATKVHELLNMVQLDW---LADRYPEQLSGGQRQR 144
Cdd:COG0444 82 KIRGREIQMIFQDpMtSLNPVMTVGDQIAEPLR---IHGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 145 IALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDV 224
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*
gi 517442396 225 YENPA 229
Cdd:COG0444 239 FENPR 243
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-227 |
9.22e-61 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 194.31 E-value: 9.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDR-NVGFVFQ 81
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 HYALFRHMTVFDNVAFGLRMKPKhqrpNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLD 161
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGL----FDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 162 EPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYEN 227
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-215 |
1.22e-60 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 192.72 E-value: 1.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFVF 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFrHMTVFDNVAFGLRMKpkHQRPNESqiatKVHELLNMVQLDW-LADRYPEQLSGGQRQRIALARALAVEPKVLL 159
Cdd:COG4619 81 QEPALW-GGTVRDNLPFPFQLR--ERKFDRE----RALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 160 LDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-229 |
1.25e-60 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 196.88 E-value: 1.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-----------NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV---SG 68
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 69 HDVRD--RNVGFVFQH-YA-LFRHMTVFDNVAFGLR---MKPKHQRpnesqiATKVHELLNMVQLD-WLADRYPEQLSGG 140
Cdd:COG4608 88 RELRPlrRRMQMVFQDpYAsLNPRMTVGDIIAEPLRihgLASKAER------RERVAELLELVGLRpEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 141 QRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGS 220
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAP 241
|
....*....
gi 517442396 221 PGDVYENPA 229
Cdd:COG4608 242 RDELYARPL 250
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-227 |
6.31e-59 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 191.03 E-value: 6.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFN-----AFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG-----HD 70
Cdd:PRK13637 1 MSIKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvklSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 71 VRDRnVGFVFQH--YALFRHmTVFDNVAFGlrmkPKHQRPNESQIATKVHELLNMVQLDW--LADRYPEQLSGGQRQRIA 146
Cdd:PRK13637 81 IRKK-VGLVFQYpeYQLFEE-TIEKDIAFG----PINLGLSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYE 226
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
.
gi 517442396 227 N 227
Cdd:PRK13637 235 E 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-219 |
1.13e-58 |
|
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: 188.44 E-value: 1.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSgHDVRDRNVgfVFQHYALFRHMTVFDNVAF 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-EPGPDRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 98 GL-RMKPKHQRPNESQIatkVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELR 176
Cdd:TIGR01184 78 AVdRVLPDLSKSERRAI---VEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517442396 177 RWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIG 219
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-232 |
1.95e-58 |
|
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: 188.16 E-value: 1.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV---SGHDVRD--RNV 76
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHYALFRHMTVFDNVAFG-----------LRMKPKHQRpnesQIATkvhELLNMVQLDWLADRYPEQLSGGQRQRI 145
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstwrslFGLFPKEEK----QRAL---AALERVGLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIeqigspgdVY 225
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI--------VF 225
|
....*..
gi 517442396 226 ENPASDF 232
Cdd:cd03256 226 DGPPAEL 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-242 |
1.54e-57 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 186.44 E-value: 1.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVrDRnvGFVFQH 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-ER--GVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGLRMK--PKHQRpnesqiATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAgvEKMQR------LEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 161 DEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGvieqigsPGDVYENPASDFVYHFL-GD 239
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG-------PGRVVERLPLNFARRFVaGE 225
|
...
gi 517442396 240 SNR 242
Cdd:PRK11248 226 SSR 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-237 |
1.91e-57 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 185.60 E-value: 1.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQG--SIVFHGEDVSGH----DVRD- 73
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlNIAGNHFDFSKTpsdkAIREl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 -RNVGFVFQHYALFRHMTVFDNV------AFGLrmkpkhqrpNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIA 146
Cdd:PRK11124 81 rRNVGMVFQQYNLWPHLTVQQNLieapcrVLGL---------SKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEdINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSpGDVYE 226
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFT 229
|
250
....*....|.
gi 517442396 227 NPASDFVYHFL 237
Cdd:PRK11124 230 QPQTEAFKNYL 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-237 |
4.74e-57 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 184.83 E-value: 4.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGE------DVSGHDVRD- 73
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRLl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 -RNVGFVFQHYALFRHMTVFDNvafgLRMKP-KHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARAL 151
Cdd:COG4161 81 rQKVGMVFQQYNLWPHLTVMEN----LIEAPcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 152 AVEPKVLLLDEPFGALDAKVRKELRRWLARLHEdINLTSVFVTHDQEEAMEVADRIVVMNKG-VIEQigspGD--VYENP 228
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGrIIEQ----GDasHFTQP 231
|
....*....
gi 517442396 229 ASDFVYHFL 237
Cdd:COG4161 232 QTEAFAHYL 240
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-237 |
7.18e-57 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 184.62 E-value: 7.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--------- 73
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvpadrr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 ------RNVGFVFQHYALFRHMTVFDNVAFGlrmkPKH-QRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIA 146
Cdd:COG4598 89 qlqrirTRLGMVFQSFNLWSHMTVLENVIEA----PVHvLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 147 LARALAVEPKVLLLDEPFGALDAK-VRKELR--RWLARLHEdinlTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGD 223
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPElVGEVLKvmRDLAEEGR----TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAE 240
|
250
....*....|....
gi 517442396 224 VYENPASDFVYHFL 237
Cdd:COG4598 241 VFGNPKSERLRQFL 254
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-217 |
1.34e-56 |
|
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: 183.40 E-value: 1.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRA----LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHD------VR 72
Cdd:COG4181 9 IELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedararLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 73 DRNVGFVFQHYALFRHMTVFDNVAFGLRMKpkhQRPNESQIATkvhELLNMVQLDWLADRYPEQLSGGQRQRIALARALA 152
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTALENVMLPLELA---GRRDARARAR---ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 153 VEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAmEVADRIVVMNKGVIEQ 217
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2-210 |
1.40e-55 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 179.99 E-value: 1.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPD---QGSIVFHGEDVSGHDVRDRNVGF 78
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHMTVFDNVAFGLRMK-PKHQRpnesqiATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKV 157
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALPPTiGRAQR------RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517442396 158 LLLDEPFGALDAKVRKELRRW-LARLHEDiNLTSVFVTHDQEEAmEVADRIVVM 210
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREFvFEQIRQR-GIPALLVTHDEEDA-PAAGRVLDL 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-226 |
1.20e-54 |
|
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: 189.66 E-value: 1.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSknfnaFR-------ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD- 73
Cdd:COG2274 473 DIELENVS-----FRypgdsppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASl 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 -RNVGFVFQHYALFrHMTVFDNVAFGlrmkpkHQRPNESQIatkvHELLNMVQLDWLADRYPE-----------QLSGGQ 141
Cdd:COG2274 548 rRQIGVVLQDVFLF-SGTIRENITLG------DPDATDEEI----IEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 142 RQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDInlTSVFVTHDqEEAMEVADRIVVMNKGVIEQIGSP 221
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTH 693
|
....*
gi 517442396 222 GDVYE 226
Cdd:COG2274 694 EELLA 698
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
17-317 |
1.40e-54 |
|
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: 181.85 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 17 ALDeISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGE---------DVSGHDvrdRNVGFVFQHYALFR 87
Cdd:TIGR02142 13 SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiFLPPEK---RRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 88 HMTVFDNVAFGLrmkpKHQRPNESQIA-TKVHELLNmvqLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGA 166
Cdd:TIGR02142 89 HLSVRGNLRYGM----KRARPSERRISfERVIELLG---IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 167 LDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYH------FLGDS 240
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLARedqgslIEGVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 241 NRLH-----------------------LGEDRHVLFRPHEVSLSRSELEDHHAAEVRDIRPLGA----TTRVTLKVEGQS 293
Cdd:TIGR02142 242 AEHDqhygltalrlggghlwvpenlgpTGARLRLRVPARDVSLALQKPEATSIRNILPARVVEIedsdIGRVGVVLESGG 321
|
330 340
....*....|....*....|....
gi 517442396 294 ELIEAEVVKDHDSLVGLAKGETLF 317
Cdd:TIGR02142 322 KTLWARITRWARDELGIAPGTPVF 345
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-232 |
1.41e-54 |
|
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: 178.26 E-value: 1.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV---SGHDVRD--RNV 76
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklRGKKLRKlrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHYALFRHMTVFDNVAFG-----------LRMKPKHQRpnesQIATkvhELLNMVQLDWLADRYPEQLSGGQRQRI 145
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGrlgykptwrslLGRFSEEDK----ERAL---SALERVGLADKAYQRADQLSGGQQQRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIeqigspgdVY 225
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI--------VF 226
|
....*..
gi 517442396 226 ENPASDF 232
Cdd:TIGR02315 227 DGAPSEL 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-228 |
1.47e-54 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 178.69 E-value: 1.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGL--ETPDQ---GSIVFHGEDVSGHDV-----R 72
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDIYDPDVdvvelR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 73 dRNVGFVFQHYALFRhMTVFDNVAFGLRMkpkHQRPNESQIATKVHELLNMVQLdW--LADRYPEQ---LSGGQRQRIAL 147
Cdd:COG1117 92 -RRVGMVFQKPNPFP-KSIYDNVAYGLRL---HGIKSKSELDEIVEESLRKAAL-WdeVKDRLKKSalgLSGGQQQRLCI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 148 ARALAVEPKVLLLDEPFGALD----AKVrKELrrwLARLHEDinLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGD 223
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDpistAKI-EEL---ILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQ 239
|
....*
gi 517442396 224 VYENP 228
Cdd:COG1117 240 IFTNP 244
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-215 |
2.61e-54 |
|
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: 176.53 E-value: 2.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 22 SLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQHYALFRHMTVFDNVAFG--- 98
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGlsp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 99 -LRMKPKHQRpnesqiatKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRR 177
Cdd:cd03298 98 gLKLTAEDRQ--------AIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 517442396 178 WLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-237 |
9.66e-54 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 176.48 E-value: 9.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MS-IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSI------VFHGEDVSGHDVRD 73
Cdd:PRK11264 1 MSaIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 RN----VGFVFQHYALFRHMTVFDNVAFGLRMKPKhqRPNESQIAtKVHELLNMVQLDWLADRYPEQLSGGQRQRIALAR 149
Cdd:PRK11264 81 RQlrqhVGFVFQNFNLFPHRTVLENIIEGPVIVKG--EPKEEATA-RARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPA 229
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
....*...
gi 517442396 230 SDFVYHFL 237
Cdd:PRK11264 237 QPRTRQFL 244
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-215 |
1.83e-53 |
|
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: 174.64 E-value: 1.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSghDVRDRnVGFVFQHY 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--KERKR-IGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 84 ALFRHM--TVFDNVAFGL-RMKPKHQRPNESQIAtKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:cd03235 78 SIDRDFpiSVRDVVLMGLyGHKGLFRRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 161 DEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-164 |
2.16e-53 |
|
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: 172.06 E-value: 2.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFVFQHYALFRHMTVFDNV 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 96 AFGLRMKpKHQRPNESQIATKVHELLNMV-QLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:pfam00005 81 RLGLLLK-GLSKREKDARAEEALEKLGLGdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-213 |
1.77e-52 |
|
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: 170.12 E-value: 1.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFVFQ 81
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 hyalfrhmtvfdnvafglrmkpkhqrpnesqiatkvhellnmvqldwladrypeqLSGGQRQRIALARALAVEPKVLLLD 161
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517442396 162 EPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-213 |
6.22e-52 |
|
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: 169.10 E-value: 6.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAF--RALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGF 78
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFrHMTVFDNVafglrmkpkhqrpnesqiatkvhellnmvqldwladrypeqLSGGQRQRIALARALAVEPKVL 158
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 159 LLDEPFGALDAKVRKELRRWLARLHEDinLTSVFVTHDqEEAMEVADRIVVMNKG 213
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKG--KTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-219 |
2.05e-51 |
|
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: 168.00 E-value: 2.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFVFQ 81
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 hyalfrhmtvfdnvafglrmkpkhqrpnesqiatkvheLLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLD 161
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517442396 162 EPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIG 219
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
20-219 |
5.02e-51 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 168.50 E-value: 5.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 20 EISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQHYALFRHMTVFDNVAFGL 99
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 100 rmKPKHQRPNESQiaTKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWL 179
Cdd:TIGR01277 96 --HPGLKLNAEQQ--EKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517442396 180 ARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIG 219
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-215 |
6.04e-51 |
|
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: 168.27 E-value: 6.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD----- 73
Cdd:TIGR02982 2 ISIRNLNHYYghgsLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQlvqlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 RNVGFVFQHYALFRHMTVFDNVAFGLRMkpkHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAV 153
Cdd:TIGR02982 82 RRIGYIFQAHNLLGFLTARQNVQMALEL---QPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVH 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517442396 154 EPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQeEAMEVADRIVVMNKGVI 215
Cdd:TIGR02982 159 HPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDN-RILDVADRILQMEDGKL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-231 |
1.12e-50 |
|
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: 176.03 E-value: 1.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-----------NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLEtPDQGSIVFHGEDVSGHDV 71
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 72 RD-----RNVGFVFQH-YALF--RhMTVFDNVAFGLRMkpkHQR-PNESQIATKVHELLNMVQLD-WLADRYPEQLSGGQ 141
Cdd:COG4172 355 RAlrplrRRMQVVFQDpFGSLspR-MTVGQIIAEGLRV---HGPgLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 142 RQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQE--EAMevADRIVVMNKG-VIEQi 218
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAvvRAL--AHRVMVMKDGkVVEQ- 507
|
250
....*....|...
gi 517442396 219 GSPGDVYENPASD 231
Cdd:COG4172 508 GPTEQVFDAPQHP 520
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-243 |
1.38e-50 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 167.90 E-value: 1.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDV--RDRN-VG 77
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhkRARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQHYALFRHMTVFDNVAFGLRMkpkhQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKV 157
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLEL----RKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 158 LLLDEPFGALDAKVRKELRRWLARLHE-DInltSVFVT-HDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYh 235
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHLKErGI---GVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVY- 233
|
....*...
gi 517442396 236 fLGDSNRL 243
Cdd:COG1137 234 -LGEDFRL 240
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-221 |
1.48e-50 |
|
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: 167.30 E-value: 1.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSK--NFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDR-NVGFV 79
Cdd:cd03263 1 LQIRNLTKtyKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARqSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDNVAFGLRMKPKHQRPNESQiatkVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLL 159
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEE----VELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517442396 160 LDEPFGALDAKVRKELRRWLARLHEdiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSP 221
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
2.14e-50 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 166.50 E-value: 2.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVR-DRNVGFV 79
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDNVAFGLRMKPKHQRpnesqiATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLL 159
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRAD------REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517442396 160 LDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEA 200
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLEL 194
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-215 |
2.30e-50 |
|
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: 164.91 E-value: 2.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNvgfvfqh 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 yalfrhmtvfdnvAFGLRMkpkhqrpnesqiatkVHellnmvqldwladrypeQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03216 74 -------------RAGIAM---------------VY-----------------QLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-237 |
1.53e-49 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 170.21 E-value: 1.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 17 ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG------HDVRDRNVGFVFQHYALFRHMT 90
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 91 VFDNVAFGLRMK--PKHQRPNesqiatKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:PRK10070 123 VLDNTAFGMELAgiNAEERRE------KALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 169 AKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFL 237
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-223 |
2.01e-49 |
|
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: 164.47 E-value: 2.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVS--GHDVRdRNVGFVF 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVrePREVR-RRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHMTVFDNVAFGLRMkpkHQRPNEsQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARL---YGVPGA-ERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 161 DEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGD 223
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-219 |
2.35e-49 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 165.24 E-value: 2.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 5 VRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDqgsivfHGEDVSG----HDVRDrNVGFVF 80
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPS------AGELLAGtaplAEARE-DTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHMTVFDNVAFGLRmkpKHQRPnesqiatKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLGLK---GQWRD-------AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 161 DEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGvieQIG 219
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIG 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-221 |
2.62e-49 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 173.04 E-value: 2.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSknfnaFR------ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD-- 73
Cdd:COG1132 339 EIEFENVS-----FSypgdrpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlr 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 RNVGFVFQHYALFrHMTVFDNVAFGlrmkpkhqRPNESQiaTKVHELLNMVQLDWLADRYPE-----------QLSGGQR 142
Cdd:COG1132 414 RQIGVVPQDTFLF-SGTIRENIRYG--------RPDATD--EEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 143 QRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDInlTSVFVTH------DqeeamevADRIVVMNKGVIE 216
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHrlstirN-------ADRILVLDDGRIV 553
|
....*
gi 517442396 217 QIGSP 221
Cdd:COG1132 554 EQGTH 558
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-210 |
2.80e-49 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 171.35 E-value: 2.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD---RNVGFV 79
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDNVAFGlRMKPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLL 159
Cdd:COG1129 85 HQELNLVPNLSVAENIFLG-REPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517442396 160 LDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVM 210
Cdd:COG1129 164 LDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-227 |
4.13e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 162.47 E-value: 4.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVS-KNFNAFR-ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGF 78
Cdd:PRK13632 8 IKVENVSfSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHY-ALFRHMTVFDNVAFGLRMKpkhqRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKV 157
Cdd:PRK13632 88 IFQNPdNQFIGATVEDDIAFGLENK----KVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 158 LLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMeVADRIVVMNKGVIEQIGSPGDVYEN 227
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-238 |
4.38e-48 |
|
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: 161.17 E-value: 4.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDR---NVGFV 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDNVAFGLRMKPKhqrpNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLL 159
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGL----SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 160 LDEPFGALDAKVRKELRRWLARLHE-DInltSVFVT-HDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYhfL 237
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDrGI---GVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY--L 231
|
.
gi 517442396 238 G 238
Cdd:cd03218 232 G 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-215 |
7.68e-48 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 160.52 E-value: 7.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 22 SLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQHYALFRHMTVFDNVAFGLrm 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGL-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 102 kpkHQ--RPNESQIAtKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWL 179
Cdd:PRK10771 97 ---NPglKLNAAQRE-KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 517442396 180 ARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-213 |
1.15e-47 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 167.13 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV---SGHDVRDRNVGFV 79
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirSPRDAIALGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDNVAFGLRmKPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLL 159
Cdd:COG3845 86 HQHFMLVPNLTVAENIVLGLE-PTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517442396 160 LDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:COG3845 165 LDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-227 |
2.18e-47 |
|
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: 167.63 E-value: 2.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGF 78
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFrHMTVFDNVAFGlrmkpkhqRPNESQiaTKVHELLNMVQLDWLADRYPE-----------QLSGGQRQRIAL 147
Cdd:COG4988 416 VPQNPYLF-AGTIRENLRLG--------RPDASD--EELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDinLTSVFVTHDqEEAMEVADRIVVMNKGVIEQIGSPGDVYEN 227
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHR-LALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-229 |
2.23e-46 |
|
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: 157.07 E-value: 2.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG---HDVRDRNVGFVF 80
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlppHRIARLGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHMTVFDNVAFGLRMKPKHQRPNESqiatkvhellnmvqLDWLADRYPE----------QLSGGQRQRIALARA 150
Cdd:COG0410 85 EGRRIFPSLTVEENLLLGAYARRDRAEVRAD--------------LERVYELFPRlkerrrqragTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPA 229
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-215 |
2.43e-46 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 156.03 E-value: 2.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD-----RNV 76
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHYALFRHMTVFDNVAFGLRMKPKHQRpnesQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPR----EIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517442396 157 VLLLDEPFGALDAKVRKElrrwLARLHEDINL---TSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:cd03292 157 ILIADEPTGNLDPDTTWE----IMNLLKKINKagtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
3.83e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 157.87 E-value: 3.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNA---F--RALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFhGEDVSGHDVRDRN 75
Cdd:PRK13634 1 MDITFQKVEHRYQYktpFerRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 76 -------VGFVFQ--HYALFRHmTVFDNVAFGlrmkPKHQRPNESQIATKVHELLNMVQLDW-LADRYPEQLSGGQRQRI 145
Cdd:PRK13634 80 lkplrkkVGIVFQfpEHQLFEE-TVEKDICFG----PMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVY 225
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIF 234
|
....
gi 517442396 226 ENPA 229
Cdd:PRK13634 235 ADPD 238
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-229 |
4.26e-46 |
|
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: 164.17 E-value: 4.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSknfnaFR-------ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV---SGHDV 71
Cdd:COG4987 333 SLELEDVS-----FRypgagrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLrdlDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 72 RdRNVGFVFQHYALFrHMTVFDNVAFGlrmkpkhqRPNesqiAT--KVHELLNMVQLDWLADRYPE-----------QLS 138
Cdd:COG4987 408 R-RRIAVVPQRPHLF-DTTLRENLRLA--------RPD----ATdeELWAALERVGLGDWLAALPDgldtwlgeggrRLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 139 GGQRQRIALARALAVEPKVLLLDEPFGALDA----KVRKELRRWLArlhediNLTSVFVTHDqEEAMEVADRIVVMNKGV 214
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAateqALLADLLEALA------GRTVLLITHR-LAGLERMDRILVLEDGR 546
|
250
....*....|....*
gi 517442396 215 IEQIGSPGDVYENPA 229
Cdd:COG4987 547 IVEQGTHEELLAQNG 561
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-226 |
8.16e-46 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 156.71 E-value: 8.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF--NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGF 78
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHY-ALFRHMTVFDNVAFGLRmkpKHQRPNESQIaTKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKV 157
Cdd:PRK13635 86 VFQNPdNQFVGATVQDDVAFGLE---NIGVPREEMV-ERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 158 LLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEvADRIVVMNKGVIEQIGSPGDVYE 226
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-224 |
1.13e-45 |
|
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: 154.51 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRN---VGFV 79
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDNVAFGLRMKPKHQRPNesqiatkvhellnmvQLDWLADRYPE----------QLSGGQRQRIALAR 149
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKA---------------RLERVYELFPRlkerrkqlagTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDV 224
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-215 |
1.33e-45 |
|
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: 153.91 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFQH 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGLRMkpkHQRPNEsqiatKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03268 81 PGFYPNLTARENLRLLARL---LGIRKK-----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517442396 163 PFGALDAKVRKELRRwLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:cd03268 153 PTNGLDPDGIKELRE-LILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-213 |
1.55e-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: 153.89 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGeLVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRN-VGFVFQ 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 HYALFRHMTVFDNVAFGLRMKPKHQRPNESQIAtkvhELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLD 161
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVD----EVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517442396 162 EPFGALDAKVRKELRRWLARLHEDInlTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-230 |
3.98e-45 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 154.84 E-value: 3.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFN---------AFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD 73
Cdd:PRK10419 4 LNVSGLSHHYAhgglsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 -----RNVGFVFQHY--ALFRHMTVFDNVAFGLRmkpkH-QRPNESQIATKVHELLNMVQLD-WLADRYPEQLSGGQRQR 144
Cdd:PRK10419 84 rkafrRDIQMVFQDSisAVNPRKTVREIIREPLR----HlLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 145 IALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVI--EQIGSPG 222
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDK 239
|
....*...
gi 517442396 223 DVYENPAS 230
Cdd:PRK10419 240 LTFSSPAG 247
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-218 |
9.71e-45 |
|
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: 153.81 E-value: 9.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNA---FRA------LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHD--- 70
Cdd:TIGR02769 3 LEVRDVTHTYRTgglFGAkqrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 71 ---VRdRNVGFVFQ--HYALFRHMTVFDNVAFGLRmkpKHQRPNESQIATKVHELLNMVQL-DWLADRYPEQLSGGQRQR 144
Cdd:TIGR02769 83 rraFR-RDVQLVFQdsPSAVNPRMTVRQIIGEPLR---HLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 145 IALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKG-VIEQI 218
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGqIVEEC 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-224 |
1.09e-44 |
|
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: 152.93 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQG-SIVFHGEDVSGHDVRD--RNVGFV 79
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWElrKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 --FQHYALFRHMTVFDNVA------FGLrmkpkHQRPNESQIAtKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARAL 151
Cdd:COG1119 84 spALQLRFPRDETVLDVVLsgffdsIGL-----YREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 152 AVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDV 224
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-228 |
3.12e-44 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 152.61 E-value: 3.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG------HDVRDRnV 76
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsrlYTVRKR-M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHYALFRHMTVFDNVAFGLRmkpKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLR---EHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 157 VLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRI-VVMNKGVIEQiGSPGDVYENP 228
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAyIVADKKIVAH-GSAQALQANP 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-240 |
4.01e-44 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 152.05 E-value: 4.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVsgHDVRDRN------- 75
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTI--NLVRDKDgqlkvad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 76 ----------VGFVFQHYALFRHMTVFDNV------AFGLrmkpkhqrpNESQIATKVHELLNMVQLDWLA-DRYPEQLS 138
Cdd:PRK10619 84 knqlrllrtrLTMVFQHFNLWSHMTVLENVmeapiqVLGL---------SKQEARERAVKYLAKVGIDERAqGKYPVHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 139 GGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQI 218
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
250 260
....*....|....*....|..
gi 517442396 219 GSPGDVYENPASDFVYHFLGDS 240
Cdd:PRK10619 234 GAPEQLFGNPQSPRLQQFLKGS 255
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-213 |
1.46e-43 |
|
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: 149.04 E-value: 1.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG------HDVR 72
Cdd:TIGR02211 2 LKCENLGKRYqegkLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKlssnerAKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 73 DRNVGFVFQHYALFRHMTVFDNVAFGL---RMKPKHqrpnesqIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALAR 149
Cdd:TIGR02211 82 NKKLGFIYQFHHLLPDFTALENVAMPLligKKSVKE-------AKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517442396 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAmEVADRIVVMNKG 213
Cdd:TIGR02211 155 ALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELA-KKLDRVLEMKDG 217
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-224 |
2.02e-43 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 149.85 E-value: 2.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFVF 80
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHMTVFDNVAFGlRMkPKHQ-RPNESQIAtKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLL 159
Cdd:COG4604 82 QENHINSRLTVRELVAFG-RF-PYSKgRLTAEDRE-IIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 160 LDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDV 224
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-215 |
2.25e-43 |
|
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: 148.17 E-value: 2.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 16 RALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDvRDRNVGFVFQH--YALFRHmTVFD 93
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-RRKSIGYVMQDvdYQLFTD-SVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 94 NVAFGLRMKPKHQrpnesqiaTKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRK 173
Cdd:cd03226 92 ELLLGLKELDAGN--------EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517442396 174 ELRRWLARLHEDINlTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:cd03226 164 RVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-243 |
3.49e-43 |
|
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: 148.96 E-value: 3.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG---HDVRDRNVGF 78
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlpmHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHMTVFDNVAFGLRMKPKHQRpneSQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVL 158
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKDLDR---AEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 159 LLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYhfLG 238
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVY--LG 234
|
....*
gi 517442396 239 DSNRL 243
Cdd:TIGR04406 235 EQFRL 239
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-215 |
1.22e-42 |
|
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: 146.58 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNFNAFR--ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVG 77
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQHYALFrHMTVFDNVAFGlrmkpkhqrpneSQIAT--KVHELLNMVQLDWLADRYP-----------EQLSGGQRQR 144
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLG------------APLADdeRILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 145 IALARALAVEPKVLLLDEPFGALD----AKVRKELRRWLArlhediNLTSVFVTHDQeEAMEVADRIVVMNKGVI 215
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDmnseERLKERLRQLLG------DKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-215 |
2.11e-42 |
|
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: 145.97 E-value: 2.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNA----FRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSgHDVRD--RNV 76
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEPAEarRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHYALFRHMTVFDNVAF-----GLRMKPKHQRpnesqiatkVHELLNMVQLDWLADRYPEQLSGGQRQRIALARAL 151
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYfaglyGLKGDELTAR---------LEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517442396 152 AVEPKVLLLDEPFGALDAKVRKELRRWLARLhEDINLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-226 |
3.57e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 147.21 E-value: 3.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFN---AFrALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVG 77
Cdd:PRK13648 8 IVFKNVSFQYQsdaSF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQH-YALFRHMTVFDNVAFGLRmkpKHQRPNEsQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:PRK13648 87 IVFQNpDNQFVGSIVKYDVAFGLE---NHAVPYD-EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 157 VLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEvADRIVVMNKGVIEQIGSPGDVYE 226
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-229 |
1.59e-41 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 147.71 E-value: 1.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 20 EISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHD------VRDRNVGFVFQHYALFRHMTVFD 93
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclpPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 94 NVAFGlrMKPKhqrpNESQIAtKVHELLNmvqLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRK 173
Cdd:PRK11144 96 NLRYG--MAKS----MVAQFD-KIVALLG---IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 174 ELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPA 229
Cdd:PRK11144 166 ELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-221 |
2.27e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 145.26 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFR---ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVG 77
Cdd:PRK13650 5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDirHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQHY-ALFRHMTVFDNVAFGLrmkpKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:PRK13650 85 MVFQNPdNQFVGATVEDDVAFGL----ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 157 VLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEaMEVADRIVVMNKGVIEQIGSP 221
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTP 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-224 |
4.07e-41 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 144.10 E-value: 4.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFVF 80
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYAL---FrhmTVFDNVAFGLRMKPKHQRPNEsQIatkVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALA----- 152
Cdd:COG4559 82 QHSSLafpF---TVEEVVALGRAPHGSSAAQDR-QI---VREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwep 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 153 --VEPKVLLLDEPFGALDAK----VRKELRRWLAR-------LHeDINLTSVFvthdqeeamevADRIVVMNKGVIEQIG 219
Cdd:COG4559 155 vdGGPRWLFLDEPTSALDLAhqhaVLRLARQLARRgggvvavLH-DLNLAAQY-----------ADRILLLHQGRLVAQG 222
|
....*
gi 517442396 220 SPGDV 224
Cdd:COG4559 223 TPEEV 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-231 |
4.18e-41 |
|
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: 150.22 E-value: 4.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAFRALDEISLDIQSGELVALLGPSGCGKT----TLLRIIAGLETPDQGSIVFHGEDVSGHD---- 70
Cdd:COG4172 7 LSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSerel 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 71 --VRDRNVGFVFQH--YALFRHMTVFDNVAFGLRMkpkHQRPNESQIATKVHELLNMVQLD---WLADRYPEQLSGGQRQ 143
Cdd:COG4172 87 rrIRGNRIAMIFQEpmTSLNPLHTIGKQIAEVLRL---HRGLSGAAARARALELLERVGIPdpeRRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 144 RIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGD 223
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
....*...
gi 517442396 224 VYENPASD 231
Cdd:COG4172 244 LFAAPQHP 251
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-226 |
7.24e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 144.12 E-value: 7.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNA---F--RALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD-- 73
Cdd:PRK13649 1 MGINLQNVSYTYQAgtpFegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 ----RNVGFVFQ--HYALFRHmTVFDNVAFGlrmkPKHQRPNESQIATKVHELLNMVQLDW-LADRYPEQLSGGQRQRIA 146
Cdd:PRK13649 81 kqirKKVGLVFQfpESQLFEE-TVLKDVAFG----PQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYE 226
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-240 |
9.89e-41 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 142.82 E-value: 9.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV---SGHDVRDRNVGFV 79
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDN--VA----------FGLRMKPKHQRpNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIAL 147
Cdd:PRK11300 86 FQHVRLFREMTVIENllVAqhqqlktglfSGLLKTPAFRR-AESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYEN 227
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 244
|
250
....*....|...
gi 517442396 228 PasDFVYHFLGDS 240
Cdd:PRK11300 245 P--DVIKAYLGEA 255
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-215 |
1.07e-40 |
|
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: 141.26 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSgHDVRDRnVGFVFQH 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-IAARNR-IGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGLRMKPKhqrpNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGL----KKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 163 PFGALD---AKVRKELRRWLARLhediNLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:cd03269 155 PFSGLDpvnVELLKDVIRELARA----GKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
3-231 |
1.23e-40 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 143.05 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF---------NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHD--V 71
Cdd:COG4167 5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDykY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 72 RDRNVGFVFQH--YALFRHMTVFDNVAFGLRMkpkHQRPNESQIATKVHELLNMVQLdwLADR---YPEQLSGGQRQRIA 146
Cdd:COG4167 85 RCKHIRMIFQDpnTSLNPRLNIGQILEEPLRL---NTDLTAEEREERIFATLRLVGL--LPEHanfYPHMLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKG-VIEQiGSPGDVY 225
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGeVVEY-GKTAEVF 238
|
....*.
gi 517442396 226 ENPASD 231
Cdd:COG4167 239 ANPQHE 244
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-249 |
1.43e-40 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 144.34 E-value: 1.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 16 RALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHD-----VRDRNVGFVFQH-YA-LFRH 88
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaqkLLRQKIQIVFQNpYGsLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 89 MTVFDNVAFGLRMK---PKHQRpnesqiATKVHELLNMVQLD-WLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:PRK11308 109 KKVGQILEEPLLINtslSAAER------REKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 165 GALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLGDSNRLH 244
Cdd:PRK11308 183 SALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATPRLN 262
|
....*
gi 517442396 245 LGEDR 249
Cdd:PRK11308 263 PDDRR 267
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-228 |
1.60e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 143.02 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFR--ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPD---QGSIVFHGEDVSGH---DVRDR 74
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKtvwDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 75 nVGFVFQHY-ALFRHMTVFDNVAFGL--RMKPKhqrpneSQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARAL 151
Cdd:PRK13640 86 -VGIVFQNPdNQFVGATVGDDVAFGLenRAVPR------PEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 152 AVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAmEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-228 |
2.00e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 141.90 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGL-----ETPDQGSIVFHGEDVSGHDVRD--- 73
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPiev 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 -RNVGFVFQHYALFRHMTVFDNVAFGLRM----KPKHQRPNESQIATKVHELLNMVQlDWLADrYPEQLSGGQRQRIALA 148
Cdd:PRK14267 84 rREVGMVFQYPNPFPHLTIYDNVAIGVKLnglvKSKKELDERVEWALKKAALWDEVK-DRLND-YPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDinLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
8.37e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 141.03 E-value: 8.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHD---VRDRnVGF 78
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwVRSK-VGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHY--ALFRhMTVFDNVAFGlrmkPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:PRK13647 84 VFQDPddQVFS-STVWDDVAFG----PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 157 VLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSP 221
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-215 |
1.38e-39 |
|
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: 147.71 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNF-NAFR-ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVG 77
Cdd:TIGR03375 463 EIEFRNVSFAYpGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQHYALFrHMTVFDNVAFGlrmkpkhqRPNESQiatkvHELLNMVQ---LDWLADRYP-----------EQLSGGQRQ 143
Cdd:TIGR03375 543 YVPQDPRLF-YGTLRDNIALG--------APYADD-----EEILRAAElagVTEFVRRHPdgldmqigergRSLSGGQRQ 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 144 RIALARALAVEPKVLLLDEPFGALD----AKVRKELRRWLArlhediNLTSVFVTHDQeEAMEVADRIVVMNKGVI 215
Cdd:TIGR03375 609 AVALARALLRDPPILLLDEPTSAMDnrseERFKDRLKRWLA------GKTLVLVTHRT-SLLDLVDRIIVMDNGRI 677
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-213 |
1.48e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 141.01 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVrdRNVGFVFQ 81
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR--RRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 HYALFRHMTVFDNVAF--GLR-MKPKhqrpnesQIATKVHELLNMVQL-DWLADRYpEQLSGGQRQRIALARALAVEPKV 157
Cdd:COG4152 79 ERGLYPKMKVGEQLVYlaRLKgLSKA-------EAKRRADEWLERLGLgDRANKKV-EELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517442396 158 LLLDEPFGALDA----KVRKELRRwLARlhediNLTSV-FVTHDQEEAMEVADRIVVMNKG 213
Cdd:COG4152 151 LILDEPFSGLDPvnveLLKDVIRE-LAA-----KGTTViFSSHQMELVEELCDRIVIINKG 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-226 |
3.33e-39 |
|
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: 144.95 E-value: 3.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFH-GED-----VSGHDV 71
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvdmtKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 72 RDRN---VGFVFQHYALFRHMTVFDNV--AFGLRMkpkhqrPNESQIATKVHeLLNMVQLD-----WLADRYPEQLSGGQ 141
Cdd:TIGR03269 360 RGRAkryIGILHQEYDLYPHRTVLDNLteAIGLEL------PDELARMKAVI-TLKMVGFDeekaeEILDKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 142 RQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSP 221
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
....*
gi 517442396 222 GDVYE 226
Cdd:TIGR03269 513 EEIVE 517
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-220 |
8.87e-39 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 136.98 E-value: 8.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSknfnaFR-------ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD-- 73
Cdd:cd03251 1 VEFKNVT-----FRypgdgppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 RNVGFVFQHYALFrHMTVFDNVAFGlrmkpkhqRPNESQiaTKVHELLNMVQLDWLADRYPE-----------QLSGGQR 142
Cdd:cd03251 76 RQIGLVSQDVFLF-NDTVAENIAYG--------RPGATR--EEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517442396 143 QRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEdiNLTSVFVTHdQEEAMEVADRIVVMNKGVIEQIGS 220
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLEDGKIVERGT 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-228 |
1.17e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 138.01 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFR-ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFV 79
Cdd:PRK13652 4 IETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHY--ALFRhMTVFDNVAFGlrmkPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKV 157
Cdd:PRK13652 84 FQNPddQIFS-PTVEQDIAFG----PINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517442396 158 LLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-221 |
1.21e-38 |
|
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: 145.10 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSknfnaFR-------ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD- 73
Cdd:TIGR03797 451 AIEVDRVT-----FRyrpdgplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAv 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 -RNVGFVFQHYALFRHmTVFDNVAFGLRMKPKhqrpnESQIATKvhellnMVQLDWLADRYP-----------EQLSGGQ 141
Cdd:TIGR03797 526 rRQLGVVLQNGRLMSG-SIFENIAGGAPLTLD-----EAWEAAR------MAGLAEDIRAMPmgmhtviseggGTLSGGQ 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 142 RQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLhediNLTSVFVTHDQEEAMEvADRIVVMNKGVIEQIGSP 221
Cdd:TIGR03797 594 RQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL----KVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTY 668
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
7-243 |
2.01e-38 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 136.56 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 7 NVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVS---GHDVRDRNVGFVFQHY 83
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllpLHARARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 84 ALFRHMTVFDNVAFGLRMKpkhQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIR---DDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 164 FGALDAKVRKELRRWLARLhEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYhfLGDSNRL 243
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY--LGEDFRL 241
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-227 |
4.42e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 137.06 E-value: 4.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 15 FRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGH-----DVRD--RNVGFVFQ--HYAL 85
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkkikEVKRlrKEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 86 FRHmTVFDNVAFGlrmkPKHQRPNESQIATKVHELLNMVQL-DWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:PRK13645 104 FQE-TIEKDIAFG----PVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 165 GALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYEN 227
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-210 |
5.27e-38 |
|
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: 141.66 E-value: 5.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGF 78
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHmTVFDNVAFGLRmkpkHQRPNESQIATKVHELLNMVQ-----LDWLADRYPEQLSGGQRQRIALARALAV 153
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARP----DASDAEIREALERAGLDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 154 EPKVLLLDEPFGALDAKVRKELRRWLARLHEdiNLTSVFVTHDqEEAMEVADRIVVM 210
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-224 |
1.51e-37 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 134.76 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGF 78
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHMTVFDNVAFGL--------RMKPKHQRpnesqiatKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARA 150
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRspwlslwgRLSAEDNA--------RVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKG-VIEQiGSPGDV 224
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGhVMAQ-GTPEEV 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-224 |
1.58e-37 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 138.05 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGF 78
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHMTVFDNVAFGlrMKPKHQR--PNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMG--RTPHRSRfdTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517442396 157 VLLLDEPFGALDA--KVRK-ELRRWLArlheDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDV 224
Cdd:PRK09536 160 VLLLDEPTASLDInhQVRTlELVRRLV----DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-228 |
1.93e-37 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 136.37 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFN-------------AFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG- 68
Cdd:PRK15079 9 LEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGm 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 69 -----HDVRdRNVGFVFQH--YALFRHMTVFDNVAFGLRM-KPKHQRpneSQIATKVHELLNMVQL-DWLADRYPEQLSG 139
Cdd:PRK15079 89 kddewRAVR-SDIQMIFQDplASLNPRMTIGEIIAEPLRTyHPKLSR---QEVKDRVKAMMLKVGLlPNLINRYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 140 GQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIG 219
Cdd:PRK15079 165 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 244
|
....*....
gi 517442396 220 SPGDVYENP 228
Cdd:PRK15079 245 TYDEVYHNP 253
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-215 |
2.30e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 134.44 E-value: 2.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNA-----FRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGH--DVRDRN 75
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 76 VGFVFQHYAL--FRHMTVFDNVA--------FGLRMKPKHQRPNEsqiatkVHELLNMVQLDwLADRYP---EQLSGGQR 142
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLTKKRREL------FRELLATLGLG-LENRLDtkvGLLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 143 QRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-224 |
2.33e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 134.13 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDR------ 74
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 75 -----NVGFVFqhyalfrhmTVFDNVAFGLrmKPKHQRPNESQIAtkVHELLNMVQLDWLADRYPEQLSGGQRQRIALAR 149
Cdd:PRK13548 81 lpqhsSLSFPF---------TVEEVVAMGR--APHGLSRAEDDAL--VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 150 ALA------VEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGD 223
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
.
gi 517442396 224 V 224
Cdd:PRK13548 228 V 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-215 |
6.13e-37 |
|
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: 130.41 E-value: 6.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSknfnaFRA-------LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD-- 73
Cdd:cd03246 1 LEVENVS-----FRYpgaeppvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 RNVGFVFQHYALFRHmTVFDNVafglrmkpkhqrpnesqiatkvhellnmvqldwladrypeqLSGGQRQRIALARALAV 153
Cdd:cd03246 76 DHVGYLPQDDELFSG-SIAENI-----------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517442396 154 EPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHdQEEAMEVADRIVVMNKGVI 215
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-237 |
1.07e-36 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 131.89 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSknfnaFR--------ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD- 73
Cdd:cd03249 1 IEFKNVS-----FRypsrpdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 -RNVGFVFQHYALFrHMTVFDNVAFGlrmkpKHQRPNESQI-ATKV---HELLNMvqldwLADRYPE-------QLSGGQ 141
Cdd:cd03249 76 rSQIGLVSQEPVLF-DGTIAENIRYG-----KPDATDEEVEeAAKKaniHDFIMS-----LPDGYDTlvgergsQLSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 142 RQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDInlTSVFVTHdQEEAMEVADRIVVMNKGVIEQIGSP 221
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTH 221
|
250
....*....|....*.
gi 517442396 222 GDVYENPAsdfVYHFL 237
Cdd:cd03249 222 DELMAQKG---VYAKL 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.13e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 133.67 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNA-----FRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGH------ 69
Cdd:PRK13651 1 MQIKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 70 ---------------------DVRdRNVGFVFQ--HYALFRHmTVFDNVAFG-LRMKPKHQRPNEsqiatKVHELLNMVQ 125
Cdd:PRK13651 81 ekvleklviqktrfkkikkikEIR-RRVGVVFQfaEYQLFEQ-TIEKDIIFGpVSMGVSKEEAKK-----RAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 126 LD--WLaDRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEV 203
Cdd:PRK13651 154 LDesYL-QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEW 231
|
250 260
....*....|....*....|...
gi 517442396 204 ADRIVVMNKGvieQIGSPGDVYE 226
Cdd:PRK13651 232 TKRTIFFKDG---KIIKDGDTYD 251
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-229 |
1.75e-36 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 131.82 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGL-----ETPDQGSIVFHGEDVSGH-----DVR 72
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPrtdtvDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 73 dRNVGFVFQHYALFRhMTVFDNVAFGLRMKPKHqrpnESQIATKVHE--LLNMVQLDWLADRYPEQ---LSGGQRQRIAL 147
Cdd:PRK14239 86 -KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIK----DKQVLDEAVEksLKGASIWDEVKDRLHDSalgLSGGQQQRVCI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDinLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYEN 227
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMN 237
|
..
gi 517442396 228 PA 229
Cdd:PRK14239 238 PK 239
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-227 |
2.97e-36 |
|
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: 130.34 E-value: 2.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG---HDVRDRNVGFVF 80
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKlppHERARAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHMTVFDNVAFGL--RMKPKHQRPNEsqiatkVHELLNMvqLDWLADRYPEQLSGGQRQRIALARALAVEPKVL 158
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLaaLPRRSRKIPDE------IYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 159 LLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYEN 227
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDED 222
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-229 |
7.29e-36 |
|
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: 129.20 E-value: 7.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 23 LDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGhdvRDRNVGFVFQhyalfRH-------MTVFDNV 95
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGK---GWRHIGYVPQ-----RHefawdfpISVAHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 96 AFG-LRMKPKHQRPNESQIATkVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKE 174
Cdd:TIGR03771 73 MSGrTGHIGWLRRPCVADFAA-VRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 175 LRRWLARLHEDINlTSVFVTHDQEEAMEVADRIVVMNKGVIEQiGSPGDVyENPA 229
Cdd:TIGR03771 152 LTELFIELAGAGT-AILMTTHDLAQAMATCDRVVLLNGRVIAD-GTPQQL-QDPA 203
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-210 |
4.32e-35 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 126.19 E-value: 4.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 17 ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGedvsghdvrDRNVGFVFQHYALFRHM--TVFDN 94
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVPDSLplTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 95 VAFGLRMKPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKE 174
Cdd:NF040873 78 VAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 517442396 175 LRRWLARLHEDiNLTSVFVTHDQEEAMEvADRIVVM 210
Cdd:NF040873 158 IIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-217 |
5.53e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 127.24 E-value: 5.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG------HDVRDRNVGFVFQHYALFRHMTV 91
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakAELRNQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 92 FDNVAFGLRMKPKhqrpNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKV 171
Cdd:PRK11629 105 LENVAMPLLIGKK----KPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517442396 172 RKELRRWLARLHEDINLTSVFVTHDQEEAMEVaDRIVVMNKGVIEQ 217
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-210 |
9.99e-35 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 126.37 E-value: 9.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGH--DVRDRNVGFVF 80
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLkpEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHmTVFDNVAFGLRMkpKHQRPNESQIATkvhELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK10247 88 QTPTLFGD-TVYDNLIFPWQI--RNQQPDPAIFLD---DLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517442396 161 DEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEaMEVADRIVVM 210
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITL 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-228 |
1.41e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.50 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFN-AFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV-----SGHDVRdRNV 76
Cdd:PRK13639 2 LETRDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkkSLLEVR-KTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHY--ALFRHmTVFDNVAFGlrmkPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVE 154
Cdd:PRK13639 81 GIVFQNPddQLFAP-TVEEDVAFG----PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517442396 155 PKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-228 |
2.40e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 126.18 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGL-----ETPDQGSIVFHGEDVSGHDVRD--RN 75
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIElrRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 76 VGFVFQHYALFRHMTVFDNVAFGLRMKpkHQRPNESQIATKVHELLNMVQL-DWLADRY---PEQLSGGQRQRIALARAL 151
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLN--RLVKSKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 152 AVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDinLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-220 |
2.77e-34 |
|
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: 131.76 E-value: 2.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF--NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGF 78
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHmTVFDNVAFGlrmkpkhqRPNESQIAtKVHELLNMVQLDWLADRYPE-----------QLSGGQRQRIAL 147
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG--------RTEQADRA-EIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEdiNLTSVFVTHdQEEAMEVADRIVVMNKGVIEQIGS 220
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGT 550
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-221 |
5.14e-34 |
|
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: 124.65 E-value: 5.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFR-ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG---HDVRdRNVGF 78
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtlDSLR-RAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFrHMTVFDNVAFGlrmkpkhqRPN-------ESQIATKVHELLNmvqldwladRYPEQ-----------LSGG 140
Cdd:cd03253 80 VPQDTVLF-NDTIGYNIRYG--------RPDatdeeviEAAKAAQIHDKIM---------RFPDGydtivgerglkLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 141 QRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEdiNLTSVFVTHDQEEAMEvADRIVVMNKGVIEQIGS 220
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
.
gi 517442396 221 P 221
Cdd:cd03253 219 H 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-227 |
1.02e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 125.20 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 17 ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGH----DVRDRnVGFVFQH-----YALFr 87
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEenlwDIRNK-AGMVFQNpdnqiVATI- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 88 hmtVFDNVAFG---LRMKPKhqrpnesQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:PRK13633 103 ---VEEDVAFGpenLGIPPE-------EIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 165 GALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEvADRIVVMNKGVIEQIGSPGDVYEN 227
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-224 |
1.17e-33 |
|
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: 129.87 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFVFQHYALFRHmTVFDNV 95
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-TIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 96 AfglRMKPkhqrPNESQI---ATK--VHEllnMVQLdwLADRY-------PEQLSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:COG4618 427 A---RFGD----ADPEKVvaaAKLagVHE---MILR--LPDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517442396 164 FGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQeEAMEVADRIVVMNKGVIEQIGSPGDV 224
Cdd:COG4618 495 NSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-234 |
4.55e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 122.97 E-value: 4.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLR-------IIAGLETpdQGSIVFHGEDVSGHDVRD-- 73
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLYAPDVDPve 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 --RNVGFVFQHYALFRHmTVFDNVAFGLRMKPKHQRPNESqiatkVHELLNMVQL-DWLADRYPEQ---LSGGQRQRIAL 147
Cdd:PRK14243 89 vrRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDEL-----VERSLRQAALwDEVKDKLKQSglsLSGGQQQRLCI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDinLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYEN 227
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVEF 240
|
....*..
gi 517442396 228 PASDFVY 234
Cdd:PRK14243 241 DRTEKIF 247
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-265 |
5.89e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 123.31 E-value: 5.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 14 AFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD------RNVGFVFQ--HYAL 85
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrKKVGVVFQfpESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 86 FRHmTVFDNVAFGlrmkPKH---QRPNESQIATKVHELLNMVQLDWlaDRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK13643 98 FEE-TVLKDVAFG----PQNfgiPKEKAEKIAAEKLEMVGLADEFW--EKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 163 PFGALDAKVRKELRRWLARLHEdINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENpaSDFV-YHFLGDSN 241
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE--VDFLkAHELGVPK 247
|
250 260
....*....|....*....|....*.
gi 517442396 242 RLHLGE--DRHVLFRPHEVSLSRSEL 265
Cdd:PRK13643 248 ATHFADqlQKTGAVTFEKLPITRAEL 273
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-234 |
5.92e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 122.81 E-value: 5.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGS---IVFHGEDVS-----GHDVRDR 74
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQregrlARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 75 --NVGFVFQHYALFRHMTVFDNVAFG-----------LRMKPKHQRPNESQIATKVhellNMVQldwLADRYPEQLSGGQ 141
Cdd:PRK09984 85 raNTGYIFQQFNLVNRLSVLENVLIGalgstpfwrtcFSWFTREQKQRALQALTRV----GMVH---FAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 142 RQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSp 221
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS- 236
|
250
....*....|...
gi 517442396 222 GDVYENPASDFVY 234
Cdd:PRK09984 237 SQQFDNERFDHLY 249
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-221 |
9.60e-33 |
|
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: 121.18 E-value: 9.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFR-ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG---HDVRdRNVGF 78
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDisrKSLR-SMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHmTVFDNVAFGlrmkpkhqRPNESQiaTKVHELLNMVQLDWLADRYPE-----------QLSGGQRQRIAL 147
Cdd:cd03254 82 VLQDTFLFSG-TIMENIRLG--------RPNATD--EEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517442396 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEdiNLTSVFVTHdQEEAMEVADRIVVMNKGVIEQIGSP 221
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTH 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-229 |
1.01e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 123.42 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVS-----KNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFhGEDVSGHDVRD--- 73
Cdd:PRK13631 21 ILRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV-GDIYIGDKKNNhel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 ----------------RNVGFVFQ--HYALFRHmTVFDNVAFG-LRMKpkhQRPNESQIATKVHelLNMVQLDW-LADRY 133
Cdd:PRK13631 100 itnpyskkiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGpVALG---VKKSEAKKLAKFY--LNKMGLDDsYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 134 PEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRwLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-LILDAKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
250
....*....|....*.
gi 517442396 214 VIEQIGSPGDVYENPA 229
Cdd:PRK13631 253 KILKTGTPYEIFTDQH 268
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-215 |
1.34e-32 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 127.53 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNA----FRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHD------VR 72
Cdd:PRK10535 5 LELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalaqLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 73 DRNVGFVFQHYALFRHMTVFDNVAF-----GLRMKPKHQRpnesqiatkVHELLNMVQLDWLADRYPEQLSGGQRQRIAL 147
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVpavyaGLERKQRLLR---------AQELLQRLGLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517442396 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINlTSVFVTHDQEEAMEvADRIVVMNKGVI 215
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-226 |
1.44e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 122.61 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDR-NVGFVFQ 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARqRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 HYALFRHMTVFDNVA-----FGLrmkpkhqrpNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:PRK13537 88 FDNLDPDFTVRENLLvfgryFGL---------SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517442396 157 VLLLDEPFGALDAKVR----KELRRWLARlhediNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYE 226
Cdd:PRK13537 159 VLVLDEPTTGLDPQARhlmwERLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
2.18e-32 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 118.69 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVSknfnAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRN---VGFV- 79
Cdd:cd03215 6 EVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 --FQHYALFRHMTVFDNVAFglrmkpkhqrpnesqiatkvhellnmvqldwladryPEQLSGGQRQRIALARALAVEPKV 157
Cdd:cd03215 82 edRKREGLVLDLSVAENIAL------------------------------------SSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 158 LLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-226 |
2.72e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 123.02 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDR-NVGFV 79
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDN-VAFGlrmkpKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVL 158
Cdd:PRK13536 120 PQFDNLDLEFTVRENlLVFG-----RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517442396 159 LLDEPFGALDAKVR----KELRRWLARlhediNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYE 226
Cdd:PRK13536 195 ILDEPTTGLDPHARhliwERLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-208 |
3.19e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 125.56 E-value: 3.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 5 VRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGedvsghDVRdrnVGFVFQHYA 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR---IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 85 LFRHMTVFDNVAFGLR-------------MKPKHQRPNESQIA---------------TKVHELLNMVQL-DWLADRYPE 135
Cdd:COG0488 72 LDDDLTVLDTVLDGDAelraleaeleeleAKLAEPDEDLERLAelqeefealggweaeARAEEILSGLGFpEEDLDRPVS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 136 QLSGGQRQRIALARALAVEPKVLLLDEPFGALDAkvrkELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIV 208
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRIL 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-228 |
4.22e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 126.12 E-value: 4.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 17 ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV---SGHDVRD--RNVGFVFQH-YA-LFRHM 89
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQAlrRDIQFIFQDpYAsLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 90 TVFDNVAFGLRMkpkHQRPNESQIATKVHELLNMVQLD----WladRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFG 165
Cdd:PRK10261 419 TVGDSIMEPLRV---HGLLPGKAAAARVAWLLERVGLLpehaW---RYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 166 ALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-213 |
4.76e-32 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 119.21 E-value: 4.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFR-ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD-----RNV 76
Cdd:PRK10908 2 IRFEHVSKAYLGGRqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHYALFRHMTVFDNVAFGLRMKPKhqrpNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGA----SGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 157 VLLLDEPFGALDakvrKELRRWLARLHEDIN---LTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:PRK10908 158 VLLADEPTGNLD----DALSEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-229 |
5.04e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 120.48 E-value: 5.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG----HDVRdRNVG 77
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsklQGIR-KLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQH-YALFRHMTVFDNVAFGlrmkPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFG----PENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 157 VLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEaMEVADRIVVMNKGVIEQIGSPGDVYENPA 229
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-217 |
5.57e-32 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 120.03 E-value: 5.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 5 VRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNV-------- 76
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEaerrrllr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 ---GFVFQHYALFRHMTVFDNVAFGLRMKPKHQRpNESQIATKVHELLNMVQLDwlADR---YPEQLSGGQRQRIALARA 150
Cdd:PRK11701 89 tewGFVHQHPRDGLRMQVSAGGNIGERLMAVGAR-HYGDIRATAGDWLERVEID--AARiddLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517442396 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKG-VIEQ 217
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGrVVES 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-196 |
5.98e-32 |
|
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: 124.78 E-value: 5.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGF 78
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFrHMTVFDNVAFGlrmkpkhqRPNESQiaTKVHELLNMVQL-DWLADRyPE-----------QLSGGQRQRIA 146
Cdd:TIGR02868 414 CAQDAHLF-DTTVRENLRLA--------RPDATD--EELWAALERVGLaDWLRAL-PDgldtvlgeggaRLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517442396 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLarLHEDINLTSVFVTHD 196
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-225 |
9.84e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 119.88 E-value: 9.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNA-----FRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSgHDVRDR- 74
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIT-HKTKDKy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 75 ------NVGFVFQhyalFRHMTVF-DNVAFGLRMKPKHQRPNESQIATKVHELLnmVQLDWLAD---RYPEQLSGGQRQR 144
Cdd:PRK13646 80 irpvrkRIGMVFQ----FPESQLFeDTVEREIIFGPKNFKMNLDEVKNYAHRLL--MDLGFSRDvmsQSPFQMSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 145 IALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDV 224
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
.
gi 517442396 225 Y 225
Cdd:PRK13646 234 F 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-228 |
1.34e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 119.93 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNA-----FRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGH------ 69
Cdd:PRK13641 1 MSIKFENVDYIYSPgtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 70 -DVRdRNVGFVFQ--HYALFRHmTVFDNVAFGlrmkPKHQRPNESQIATKVHELLNMVQL-DWLADRYPEQLSGGQRQRI 145
Cdd:PRK13641 81 kKLR-KKVSLVFQfpEAQLFEN-TVLKDVEFG----PKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRwLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVY 225
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
...
gi 517442396 226 ENP 228
Cdd:PRK13641 234 SDK 236
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-215 |
1.36e-31 |
|
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: 118.20 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFR---------------------ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVF 61
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 62 HGEDVSGHDVRD-RNVGFVF-QHYALFRHMTVFDnvafGLRMKPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSG 139
Cdd:cd03267 81 AGLVPWKRRKKFlRRIGVVFgQKTQLWWDLPVID----SFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 140 GQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-237 |
1.47e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 119.00 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGL-ETPDQ-----GSIVFHGEDVSGHDVRD--RNVGFVFQHYALFRHM 89
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSkikvdGKVLYFGKDIFQIDAIKlrKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 90 TVFDNVAFGLRmkpKHQRPNESQIATKVHELLNMVQLdW--LADRY---PEQLSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:PRK14246 106 SIYDNIAYPLK---SHGIKEKREIKKIVEECLRKVGL-WkeVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 165 GALDAKVRKELRRWLARLHEDInlTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFL 237
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-238 |
2.74e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 118.22 E-value: 2.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGL-----ETPDQGSIVFHGEDVSGHDVR---- 72
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 73 DRNVGFVFQHYALFRhMTVFDNVAFGLRM---KPKHQRPNESQIATKVHELLNMVQLDwlADRYPEQLSGGQRQRIALAR 149
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwRPKLEIDDIVESALKDADLWDEIKHK--IHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVM--NKGVIEQI---GSPGDV 224
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQLvefGLTKKI 243
|
250
....*....|....*...
gi 517442396 225 YENP----ASDFVYHFLG 238
Cdd:PRK14258 244 FNSPhdsrTREYVLSRLG 261
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-228 |
3.01e-31 |
|
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: 118.01 E-value: 3.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDV-------RDR- 74
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELyqlseaeRRRl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 75 ---NVGFVFQHYALFRHMTVFDNVAFGLRMKPKHQRpNESQIATKVHELLNMVQLDW-LADRYPEQLSGGQRQRIALARA 150
Cdd:TIGR02323 84 mrtEWGFVHQNPRDGLRMRVSAGANIGERLMAIGAR-HYGNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517442396 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-226 |
3.41e-31 |
|
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: 122.60 E-value: 3.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLET--PDQGSIVFH----------------GE 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 65 --------------------DVSGHDVRDRNVGFVFQHYALFRHMTVFDNVafglrMKPKHQRPNESQIAT-KVHELLNM 123
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsDKLRRRIRKRIAIMLQRTFALYGDDTVLDNV-----LEALEEIGYEGKEAVgRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 124 VQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEV 203
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|...
gi 517442396 204 ADRIVVMNKGVIEQIGSPGDVYE 226
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVA 258
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
17-220 |
4.09e-31 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 122.89 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 17 ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFVFQHYALFRHmTVFDN 94
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAElrARMALVPQDPVLFAA-SVMEN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 95 VAFGlRMKPKHQRPNESQIATKVHELLNmvqldwladRYPE-----------QLSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:TIGR02204 434 IRYG-RPDATDEEVEAAARAAHAHEFIS---------ALPEgydtylgergvTLSGGQRQRIAIARAILKDAPILLLDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 164 FGALDAKVRKELRRWLARLHEDinLTSVFVTHDQEEAMEvADRIVVMNKGVIEQIGS 220
Cdd:TIGR02204 504 TSALDAESEQLVQQALETLMKG--RTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGT 557
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-219 |
4.25e-31 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 116.48 E-value: 4.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----------------------NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIV 60
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 61 FHGEDVSGHDVrdrNVGFvfqHYALfrhmTVFDNVAFGLR---MKPKhqrpnesQIATKVHELLNMVQLDWLADRYPEQL 137
Cdd:cd03220 81 VRGRVSSLLGL---GGGF---NPEL----TGRENIYLNGRllgLSRK-------EIDEKIDEIIEFSELGDFIDLPVKTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 138 SGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINlTSVFVTHDQEEAMEVADRIVVMNKGVIEQ 217
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
..
gi 517442396 218 IG 219
Cdd:cd03220 223 DG 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-215 |
4.32e-31 |
|
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: 116.60 E-value: 4.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 16 RALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPD---QGSIVFHGEDVSGHDVRDRnVGFVFQHYALFRHMTVF 92
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 93 DNVAFGLRMK-PKHQRPNESQIATKVhELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKV 171
Cdd:cd03234 100 ETLTYTAILRlPRKSSDAIRKKRVED-VLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517442396 172 RKELRRWLARLHEDINLtsVFVTHDQ--EEAMEVADRIVVMNKGVI 215
Cdd:cd03234 179 ALNLVSTLSQLARRNRI--VILTIHQprSDLFRLFDRILLLSSGEI 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-200 |
4.87e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 116.80 E-value: 4.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHD------VR 72
Cdd:PRK10584 7 VEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearakLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 73 DRNVGFVFQHYALFRHMTVFDNVAFGLRMKPKHQRPNESQIAtkvhELLNMVQLDWLADRYPEQLSGGQRQRIALARALA 152
Cdd:PRK10584 87 AKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAK----ALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517442396 153 VEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEA 200
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-213 |
5.36e-31 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 116.38 E-value: 5.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFN-------AFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGE----DVSG--- 68
Cdd:COG4778 5 LEVENLSKTFTlhlqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQasp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 69 ---HDVRDRNVGFVFQH-YALFRhMTVFDNVAFGLRmkpkHQRPNESQIATKVHELLNMVQLD-WLADRYPEQLSGGQRQ 143
Cdd:COG4778 85 reiLALRRRTIGYVSQFlRVIPR-VSALDVVAEPLL----ERGVDREEARARARELLARLNLPeRLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517442396 144 RIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARL-HEDINLTSVFvtHDqEEAME-VADRIVVMNKG 213
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIF--HD-EEVREaVADRVVDVTPF 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-226 |
5.90e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 116.72 E-value: 5.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MS--IEVRNVSKNFNA----------------------FRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQ 56
Cdd:COG1134 1 MSsmIEVENVSKSYRLyhepsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 57 GSIVFHGEdVSGhdVRDRNVGFVfqhyalfRHMTVFDNVAFGLR---MKPKhqrpnesQIATKVHELLnmvqldWLAD-- 131
Cdd:COG1134 81 GRVEVNGR-VSA--LLELGAGFH-------PELTGRENIYLNGRllgLSRK-------EIDEKFDEIV------EFAElg 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 132 --------RYpeqlSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINlTSVFVTHDQEEAMEV 203
Cdd:COG1134 138 dfidqpvkTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRL 212
|
250 260
....*....|....*....|...
gi 517442396 204 ADRIVVMNKGVIEQIGSPGDVYE 226
Cdd:COG1134 213 CDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-224 |
5.91e-31 |
|
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: 122.07 E-value: 5.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFVFQHYALFRHmTVFDNV 95
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 96 A-FGLRMKPkhQRPNESQIATKVHEL-LNmvqldwLADRYP-------EQLSGGQRQRIALARALAVEPKVLLLDEPFGA 166
Cdd:TIGR01842 413 ArFGENADP--EKIIEAAKLAGVHELiLR------LPDGYDtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517442396 167 LDAKVRKELRRWLARLHEDiNLTSVFVTHdQEEAMEVADRIVVMNKGVIEQIGSPGDV 224
Cdd:TIGR01842 485 LDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-213 |
6.26e-30 |
|
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: 112.95 E-value: 6.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVS-----KNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGedvsghdvrdrNVG 77
Cdd:cd03250 1 ISVEDASftwdsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQhYALFRHMTVFDNVAFGLRMKPKhqrpnesqiatKVHELLNMVQLDWLADRYPEQ-----------LSGGQRQRIA 146
Cdd:cd03250 70 YVSQ-EPWIQNGTIRENILFGKPFDEE-----------RYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRIS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517442396 147 LARALAVEPKVLLLDEPFGALDAKVRKEL-----RRWLARlhediNLTSVFVTHdQEEAMEVADRIVVMNKG 213
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIfenciLGLLLN-----NKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-228 |
8.30e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 119.83 E-value: 8.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVR--DRNVGFVFQHYALFRHmTVFDNV 95
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 96 AFGLRMKPKHQRPNESQIATKVHELLNMVQ-LDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKE 174
Cdd:TIGR00958 576 AYGLTDTPDEEIMAAAKAANAHDFIMEFPNgYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517442396 175 LRRWLARLhediNLTSVFVTHdQEEAMEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:TIGR00958 656 LQESRSRA----SRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
17-238 |
1.29e-29 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 112.85 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 17 ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPD----QGSIVFHGEDVSGHDVRDRNVGFVFQHyalfrHMTVF 92
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSIRGRHIATIMQN-----PRTAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 93 DNVafgLRMKPK-------HQRPNESQIATKVHELL--NMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:TIGR02770 76 NPL---FTMGNHaietlrsLGKLSKQARALILEALEavGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 164 FGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHFLG 238
Cdd:TIGR02770 153 TTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-225 |
1.30e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 114.42 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFVFQHY-ALFRHMTVFDN 94
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlrRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 95 VAFGLrmkpKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKE 174
Cdd:PRK13642 103 VAFGM----ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517442396 175 LRRWLARLHEDINLTSVFVTHDQEEAMEvADRIVVMNKGVIEQIGSPGDVY 225
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-219 |
1.41e-29 |
|
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: 111.25 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF--NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG-HDVRDRNVGFV 79
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDlEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFrHMTVFDNVAfglrmkpkhqrpnesqiatkvhellnmvqldwladrypEQLSGGQRQRIALARALAVEPKVLL 159
Cdd:cd03247 81 NQRPYLF-DTTLRNNLG--------------------------------------RRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 160 LDEPFGALDAKVRKELRRWLARLHEDinLTSVFVTHdQEEAMEVADRIVVMNKGVIEQIG 219
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITH-HLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-220 |
2.34e-29 |
|
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: 112.58 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 17 ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVR--DRNVGFVFQHYALFRHmTVFDN 94
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLFNR-SIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 95 VAFGLRMKPKHQRPNESQIAtKVHELLNMVQL--DWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAkvr 172
Cdd:cd03252 96 IALADPGMSMERVIEAAKLA-GAHDFISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY--- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517442396 173 kELRRWLARLHEDI--NLTSVFVTHdQEEAMEVADRIVVMNKGVIEQIGS 220
Cdd:cd03252 172 -ESEHAIMRNMHDIcaGRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGS 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-213 |
2.77e-29 |
|
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: 111.10 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNV-----SKNFNAFRA-LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGL--ETPDQGSIVFHGEDVSGHDVR 72
Cdd:cd03213 2 VTLSFRNLtvtvkSSPSKSGKQlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 73 DRnVGFVFQHYALFRHMTVFDNVAFGLRMKpkhqrpnesqiatkvhellnmvqldwladrypeQLSGGQRQRIALARALA 152
Cdd:cd03213 82 KI-IGYVPQDDILHPTLTVRETLMFAAKLR---------------------------------GLSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 153 VEPKVLLLDEPFGALDA----KVRKELRRwLArlheDINLTSVFVTHD-QEEAMEVADRIVVMNKG 213
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSssalQVMSLLRR-LA----DTGRTIICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-215 |
4.24e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.66 E-value: 4.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVSKNfnafRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNvGFVF- 80
Cdd:COG1129 258 EVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaiRA-GIAYv 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 ----QHYALFRHMTVFDNVAFG-LRMKPKH---QRPNESQIATKVHELLNMVQLDwladryPEQ----LSGGQRQRIALA 148
Cdd:COG1129 333 pedrKGEGLVLDLSIRENITLAsLDRLSRGgllDRRRERALAEEYIKRLRIKTPS------PEQpvgnLSGGNQQKVVLA 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:COG1129 407 KWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-225 |
6.53e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 112.63 E-value: 6.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGE--DVSGHDVRD--RNVG 77
Cdd:PRK13636 6 LKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKlrESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQH--YALFRhMTVFDNVAFGlrmkPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEP 155
Cdd:PRK13636 86 MVFQDpdNQLFS-ASVYQDVSFG----AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 156 KVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVY 225
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-237 |
2.15e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 114.80 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 17 ALDEISLDIQSGELVALLGPSGCGKTT----LLRIIAGletpdQGSIVFHGEDVSGHDVRD-----RNVGFVFQ--HYAL 85
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 86 FRHMTVFDNVAFGLRMkpkHQRP-NESQIATKVHELLNMVQLD-WLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:PRK15134 376 NPRLNVLQIIEEGLRV---HQPTlSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 164 FGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKG-VIEQiGSPGDVYENPASDFVYHFL 237
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGeVVEQ-GDCERVFAAPQQEYTRQLL 526
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-226 |
3.48e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.01 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFhgedvsGHDVRdrnVGFVFQH 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL------GETVK---IGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFR-HMTVFDNVAfglrmkpkHQRPNESQIatkvhELLNMVQlDWL-----ADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:COG0488 387 QEELDpDKTVLDELR--------DGAPGGTEQ-----EVRGYLG-RFLfsgddAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 157 VLLLDEPFGALDAkvrkELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIgsPGDVYE 226
Cdd:COG0488 453 VLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY--PGGYDD 516
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-215 |
6.47e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.20 E-value: 6.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVS-KNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDR---NVGFV 79
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 ---FQHYALFRHMTVFDNVAFGLRMKPKHQRP---NESQIATKVHELLnmvqldwlaDRY------PEQ----LSGGQRQ 143
Cdd:COG3845 339 pedRLGRGLVPDMSVAENLILGRYRRPPFSRGgflDRKAIRAFAEELI---------EEFdvrtpgPDTparsLSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 144 RIALARALAVEPKVLLLDEPFGALD----AKVRKELRRwlARlheDINLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLE--LR---DAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-215 |
8.34e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 110.18 E-value: 8.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----------NAFR-----------ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVf 61
Cdd:COG4586 2 IEVENLSKTYrvyekepglkGALKglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 62 hgedVSGHD-VRDR-----NVGFVF-QHYALFRHMTVFDNvafgLRMKPKHQRPNESQIATKVHELLNMVQLDWLADRYP 134
Cdd:COG4586 81 ----VLGYVpFKRRkefarRIGVVFgQRSQLWWDLPAIDS----FRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 135 EQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGV 214
Cdd:COG4586 153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGR 232
|
.
gi 517442396 215 I 215
Cdd:COG4586 233 I 233
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-220 |
9.69e-28 |
|
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: 113.68 E-value: 9.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHD---VRdRNVGFVFQHYALFRHmTVFDN 94
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADpawLR-RQMGVVLQENVLFSR-SIRDN 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 95 VAFGlrmKPkhQRPNESQIATK----VHELLNMVQ--LDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:TIGR01846 551 IALC---NP--GAPFEHVIHAAklagAHDFISELPqgYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALD 625
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517442396 169 AKVRKELRRWLARLHEdiNLTSVFVTHdQEEAMEVADRIVVMNKGVIEQIGS 220
Cdd:TIGR01846 626 YESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGR 674
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-215 |
9.97e-28 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 112.84 E-value: 9.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG-HDVRDRNVG--FV 79
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAKAHQLGiyLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDNVAFGLrmkPKHQRPnESQIATKVHELLNMVQLDWLADrypeQLSGGQRQRIALARALAVEPKVLL 159
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGL---PKRQAS-MQKMKQLLAALGCQLDLDSSAG----SLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 160 LDEPFGALD-AKVRKELRRWLARLHEDINLtsVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:PRK15439 164 LDEPTASLTpAETERLFSRIRELLAQGVGI--VFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-181 |
1.39e-27 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 106.81 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 19 DEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVsgHDVRD---RNVGFVFQHYALFRHMTVFDNV 95
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--RRQRDeyhQDLLYLGHQPGIKTELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 96 AFGLRMkpkHQRPNESQIatkvHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKEL 175
Cdd:PRK13538 96 RFYQRL---HGPGDDEAL----WEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
....*.
gi 517442396 176 RRWLAR 181
Cdd:PRK13538 169 EALLAQ 174
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-213 |
1.75e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 111.94 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLeTPD---QGSIVFHGEDVSGHDVRD---RNV 76
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIRDterAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHYALFRHMTVFDNVAFGLRMKPkHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNEITP-GGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 157 VLLLDEPFGALDAkvrKELRRWLARLHE--DINLTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:PRK13549 164 LLILDEPTASLTE---SETAVLLDIIRDlkAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-215 |
7.86e-27 |
|
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: 105.25 E-value: 7.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVR--DRNVGFVFQHYALFRHmTVFDNV 95
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 96 AFGLRMKPkHQRPNESQIATKVHELLNMVQL--DWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRK 173
Cdd:cd03248 109 AYGLQSCS-FECVKEAAQKAHAHSFISELASgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517442396 174 ELRRWLARLHEDinlTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:cd03248 188 QVQQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-170 |
9.55e-27 |
|
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: 104.36 E-value: 9.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVS-GHDVRDRNVGFVFQ 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAeQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 HYALFRHMTVFDNVAFGLRMKPKHQRpnesqiatKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLD 161
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQR--------TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
....*....
gi 517442396 162 EPFGALDAK 170
Cdd:TIGR01189 153 EPTTALDKA 161
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-217 |
9.72e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 110.30 E-value: 9.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNF--NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVG 77
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQHYALFRHmTVFDNVAFGlrmKPKHQRPNESQIATKVhELLNMVQ----LD-WLAD--RypeQLSGGQRQRIALARA 150
Cdd:PRK11160 418 VVSQRVHLFSA-TLRDNLLLA---APNASDEALIEVLQQV-GLEKLLEddkgLNaWLGEggR---QLSGGEQRRLGIARA 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 151 LAVEPKVLLLDEPFGALDAkvRKElRRWLARLHEDI-NLTSVFVTHdQEEAMEVADRIVVMNKG-VIEQ 217
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDA--ETE-RQILELLAEHAqNKTVLMITH-RLTGLEQFDRICVMDNGqIIEQ 554
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-213 |
1.12e-26 |
|
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: 102.53 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHgedvsghdvrdrnvgfvfqh 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 yalfrhmtvfDNVAFGlrmkpkhqrpnesqiatkvhellnmvqldwladrYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:cd03221 61 ----------STVKIG----------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517442396 163 PFGALDAKVRKELRRWLarlhEDINLTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:cd03221 97 PTNHLDLESIEALEEAL----KEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
3-220 |
2.60e-26 |
|
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: 109.26 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRA--LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVS--GHDVRDRNVGF 78
Cdd:TIGR03796 478 VELRNITFGYSPLEPplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREeiPREVLANSVAM 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHmTVFDNVAFGLRMKPkhqrpnESQI--ATK---VHELLNMvqldwLADRYPEQL-------SGGQRQRIA 146
Cdd:TIGR03796 558 VDQDIFLFEG-TVRDNLTLWDPTIP------DADLvrACKdaaIHDVITS-----RPGGYDAELaegganlSGGQRQRLE 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517442396 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLhediNLTSVFVTHdQEEAMEVADRIVVMNKGVIEQIGS 220
Cdd:TIGR03796 626 IARALVRNPSILILDEATSALDPETEKIIDDNLRRR----GCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-220 |
3.39e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 104.19 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG---HDVRDRNVGFV 79
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDNVAFGLRMKPKHQRpneSQIATKVHELLNMvqldwLADRYPEQ---LSGGQRQRIALARALAVEPK 156
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGGFFAERDQF---QERIKWVYELFPR-----LHERRIQRagtMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 157 VLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKG--VIEQIGS 220
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGhvVLEDTGD 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-169 |
5.29e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 102.64 E-value: 5.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRnvgfvf 80
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHY-----ALFRHMTVFDNVAFGLRMKPKHQrpnesqiaTKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEP 155
Cdd:PRK13539 75 CHYlghrnAMKPALTVAENLEFWAAFLGGEE--------LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNR 146
|
170
....*....|....
gi 517442396 156 KVLLLDEPFGALDA 169
Cdd:PRK13539 147 PIWILDEPTAALDA 160
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-220 |
6.27e-26 |
|
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: 107.60 E-value: 6.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPD--QGSIVFHGEDVSGHDVRD---RNVG 77
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDterAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQHYALFRHMTVFDNVAFGLRMKPKHQRPNESQIATKVHELLNMVQLDWLADRYP-EQLSGGQRQRIALARALAVEPK 156
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517442396 157 VLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGviEQIGS 220
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG--QHVAT 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-213 |
9.60e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 106.92 E-value: 9.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD---RNVGFVF 80
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHMTVFDNVAFGlRMKPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK11288 86 QELHLVPEMTVAENLYLG-QLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517442396 161 DEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-220 |
1.33e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 107.24 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 16 RALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLeTPDQGSIVFHGEDVSGHDVRD--RNVGFVFQHYALFrHMTVFD 93
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESwrKHLSWVGQNPQLP-HGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 94 NVAFGlrmkpkHQRPNESQI-----ATKVHELLNMvQLDWLADRYPEQ---LSGGQRQRIALARALAVEPKVLLLDEPFG 165
Cdd:PRK11174 442 NVLLG------NPDASDEQLqqaleNAWVSEFLPL-LPQGLDTPIGDQaagLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 166 ALDAKVRKELRRWLARLHEDinLTSVFVTHdQEEAMEVADRIVVMNKGVIEQIGS 220
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASRR--QTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-228 |
2.43e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 102.87 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 7 NVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETP-----DQGSIVFHGEDVSGH-DVRD--RNVGF 78
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEfrRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRhMTVFDNVAFGLR---MKPKHQRPNESQIATKVHELLNMVQlDWLADRyPEQLSGGQRQRIALARALAVEP 155
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRahkLVPRKEFRGVAQARLTEVGLWDAVK-DRLSDS-PFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 156 KVLLLDEPFGALDAKVRKELRRWLARLHEdiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-225 |
9.22e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 100.85 E-value: 9.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 15 FRALDE-----ISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVS----GHDVRDRNVGFVFQ--HY 83
Cdd:PRK13638 9 FRYQDEpvlkgLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQdpEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 84 ALFrHMTVFDNVAFGLRmkpkHQRPNESQIATKVHELLNMVQldwlADRYPEQ----LSGGQRQRIALARALAVEPKVLL 159
Cdd:PRK13638 89 QIF-YTDIDSDIAFSLR----NLGVPEAEITRRVDEALTLVD----AQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 160 LDEPFGALDAKVRKELRRWLARLHEDINLTsVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVY 225
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
15-228 |
1.11e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 101.74 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 15 FRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGL-ETPDQ---GSIVFHGEDVSGHDVRDR------NVGFVFQHya 84
Cdd:PRK11022 20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPGRvmaEKLEFNGQDLQRISEKERrnlvgaEVAMIFQD-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 85 lfrHMTVFD---NVAFGLRMKPK-HQRPNESQIATKVHELLNMVQLDWLADR---YPEQLSGGQRQRIALARALAVEPKV 157
Cdd:PRK11022 98 ---PMTSLNpcyTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517442396 158 LLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-224 |
1.60e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.06 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 19 DEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFVFQHYALFRHMTVFDNVA 96
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 97 fglRMKPKHQ------RPNESQIATKVHELLNMVQLdwlADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAK 170
Cdd:PRK10253 104 ---RGRYPHQplftrwRKEDEEAVTKAMQATGITHL---ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517442396 171 VRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDV 224
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-247 |
2.03e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 99.86 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNA----FR-----ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDV-- 71
Cdd:PRK15112 5 LEVRNLSKTFRYrtgwFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYsy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 72 RDRNVGFVFQ--HYALFRHMTVFDNVAFGLRMKPKHQRPNESQiatKVHELLNMVQLdwLADR---YPEQLSGGQRQRIA 146
Cdd:PRK15112 85 RSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREK---QIIETLRQVGL--LPDHasyYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYE 226
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
250 260
....*....|....*....|.
gi 517442396 227 NPASDFVYHFLGDsnrlHLGE 247
Cdd:PRK15112 240 SPLHELTKRLIAG----HFGE 256
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-217 |
5.54e-24 |
|
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: 102.21 E-value: 5.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNFNAFRA-LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGED---VSGHDVRdRNVG 77
Cdd:COG5265 357 EVRFENVSFGYDPERPiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDirdVTQASLR-AAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQHYALFrHMTVFDNVAFGlrmkpkhqRPNESQiaTKVHELLNMVQLDWLADRYPEQ-----------LSGGQRQRIA 146
Cdd:COG5265 436 IVPQDTVLF-NDTIAYNIAYG--------RPDASE--EEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVA 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517442396 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEdiNLTSVFVTH------DqeeamevADRIVVMNKG-VIEQ 217
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGrIVER 573
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-221 |
7.65e-24 |
|
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: 102.40 E-value: 7.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 5 VRNVSKNFNAF--RALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGH-DVRDRNVGFVFQ 81
Cdd:TIGR01257 931 VKNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNlDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 HYALFRHMTVFDNVAFGLRMKPKHQrpNESQIatKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLD 161
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSW--EEAQL--EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 162 EPFGALDAKVRKELrrWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSP 221
Cdd:TIGR01257 1087 EPTSGVDPYSRRSI--WDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-220 |
1.79e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 100.86 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNA--FRALDEISLDIQSGELVALLGPSGCGKTTllriIAGLETP----DQGSIVfhgedVSGHDVRD--- 73
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRfydiDEGEIL-----LDGHDLRDytl 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 ----RNVGFVFQHYALFRHmTVFDNVAFGlrMKPKHQRPNESQIATKVH--ELLNMVQ--LDWLADRYPEQLSGGQRQRI 145
Cdd:PRK11176 413 aslrNQVALVSQNVHLFND-TIANNIAYA--RTEQYSREQIEEAARMAYamDFINKMDngLDTVIGENGVLLSGGQRQRI 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEdiNLTSVFVTHdQEEAMEVADRIVVMNKGVIEQIGS 220
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEKADEILVVEDGEIVERGT 561
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-243 |
4.27e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.93 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 15 FRALDEISLDIQSGELVALLGPSGCGKT----TLLRII--AGLETPDQG--------SIVFHGE--DVSGHDVRDRNVGF 78
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKmllrrrsrQVIELSEqsAAQMRHVRGADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQH--YALFRHMTVFDNVAFGLRMKPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 157 VLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVYHF 236
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRAL 268
|
....*..
gi 517442396 237 LGDSNRL 243
Cdd:PRK10261 269 LAAVPQL 275
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-217 |
4.50e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.39 E-value: 4.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 16 RALDEISLDIQSGELVALLGPSGCGKT-TLLRIIAGLETPD----QGSIVFHGEDVSGHD------VRDRNVGFVFQH-- 82
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASeqtlrgVRGNKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 ------YALFRHMTVFDNVAFGLRMKPKHqrpnesqiaTKVHELLNMVQLDWLADR---YPEQLSGGQRQRIALARALAV 153
Cdd:PRK15134 103 vslnplHTLEKQLYEVLSLHRGMRREAAR---------GEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 154 EPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKG-VIEQ 217
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGrCVEQ 238
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-217 |
4.76e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 99.65 E-value: 4.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF-NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFV 79
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHmTVFDNVAFGlrmkpkhqRPN----ESQIATKVHELLNMVQ-----LDWLADRYPEQLSGGQRQRIALARA 150
Cdd:PRK13657 415 FQDAGLFNR-SIEDNIRVG--------RPDatdeEMRAAAERAQAHDFIErkpdgYDTVVGERGRQLSGGERQRLAIARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517442396 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEdiNLTSVFVTHDQEEAMEvADRIVVMNKG-VIEQ 217
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGrVVES 550
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-217 |
5.54e-23 |
|
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: 99.43 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNFNAFR-ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHG---EDVSGHDVRdRNVG 77
Cdd:TIGR01193 473 DIVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfslKDIDRHTLR-QFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQHYALFRHmTVFDNVAFGlrmkpkhQRPNESQiaTKVHELLNMVQLDWLADRYPE-----------QLSGGQRQRIA 146
Cdd:TIGR01193 552 YLPQEPYIFSG-SILENLLLG-------AKENVSQ--DEIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517442396 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDinlTSVFVTHDQEEAmEVADRIVVMNKG-VIEQ 217
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGkIIEQ 689
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-213 |
9.02e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 99.04 E-value: 9.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHD--VRdRNVGFVF 80
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDiaTR-RRVGYMS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QHYALFRHMTVFDNVA-----FGLrmkpkhqrPnESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEP 155
Cdd:NF033858 346 QAFSLYGELTVRQNLElharlFHL--------P-AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 156 KVLLLDEPFGALDAKVRKELRRWLARLHEDINLTsVFV-THDQEEAmEVADRIVVMNKG 213
Cdd:NF033858 417 ELLILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFIsTHFMNEA-ERCDRISLMHAG 473
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-233 |
1.13e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 98.58 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPD---QGSIVFHGEDVSGHDVRDRNvGFVFQHYALFRHMTVFDN 94
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIS-AYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 95 VAFGLRMKPKHQRPNESQIAtKVHELLNMVQLDWLADR---YPEQ---LSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:TIGR00955 120 LMFQAHLRMPRRVTKKEKRE-RVDEVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 169 A----KVRKELRRwLARlhediNLTSVFVTHDQ--EEAMEVADRIVVMNKGVIEQIGSPGDV-------------YENPA 229
Cdd:TIGR00955 199 SfmaySVVQVLKG-LAQ-----KGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQAvpffsdlghpcpeNYNPA 272
|
....
gi 517442396 230 sDFV 233
Cdd:TIGR00955 273 -DFY 275
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-213 |
1.93e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.55 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDR---NVGFV 79
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDNVAFGLRMKPKHQRPN---ESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 157 VLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-234 |
7.24e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.93 E-value: 7.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 5 VRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFVFQH 82
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGlrMKPKHQRPNESQIA--TKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK10575 94 LPAAEGMTVRELVAIG--RYPWHGALGRFGAAdrEKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517442396 161 DEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDFVY 234
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-211 |
7.74e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 92.48 E-value: 7.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVfhgedvsgHDVRDRnVGFVFQH 82
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLR-IGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALfrHMTVFDNVAFGLRMKPKHQRPNesqiatkVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK09544 76 LYL--DTTLPLTVNRFLRLRPGTKKED-------ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMN 211
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-209 |
1.03e-21 |
|
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: 92.09 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSG-----ELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSghdvrdrnvgFVFQHYALFRHMTVF 92
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS----------YKPQYIKADYEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 93 DnvafgLRMKPKHQRPNESQIATkvhELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVR 172
Cdd:cd03237 80 D-----LLSSITKDFYTHPYFKT---EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 517442396 173 KELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVV 209
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-213 |
1.18e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.26 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHgedvsghdvRDRNVGFVFQH-YalfrhM---TVFD 93
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP---------AGARVLFLPQRpY-----LplgTLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 94 NVAFglrmkpkhqrPNESQIAT--KVHELLNMVQLDWLADRYPEQ------LSGGQRQRIALARALAVEPKVLLLDEPFG 165
Cdd:COG4178 445 ALLY----------PATAEAFSdaELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517442396 166 ALDAKVRKELrrwLARLHEDI-NLTSVFVTHdQEEAMEVADRIVVMNKG 213
Cdd:COG4178 515 ALDEENEAAL---YQLLREELpGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-215 |
1.53e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 94.73 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 20 EISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDR-NVGFVF-----QHYALFRHMTVFD 93
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 94 NV-AFGLRMKPKHQRP-NESQIATKVHELLNMVQLDwlADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKV 171
Cdd:PRK15439 361 NVcALTHNRRGFWIKPaRENAVLERYRRALNIKFNH--AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517442396 172 RKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:PRK15439 439 RNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-221 |
2.28e-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: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNF--NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG---HDVRDRnV 76
Cdd:cd03244 2 DIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiglHDLRSR-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHYALFRHmTVFDNVAfglrmkPKHQRPNEsqiatKVHELLNMVQLDWLADRYP-----------EQLSGGQRQRI 145
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSNLD------PFGEYSDE-----ELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 146 ALARALAVEPKVLLLDEPFGALD----AKVRKELRRWLArlhediNLTSVFVTHDQEEAMEvADRIVVMNKGVIEQIGSP 221
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDpetdALIQKTIREAFK------DCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-198 |
5.10e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 89.63 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNFNA------FRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLE--TPDQGSIvfhgedvsghDVRD 73
Cdd:COG2401 24 SERVAIVLEAFGVelrvveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV----------DVPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 RNVGfvfqhyalfRHMTVFDNVAfglRMKPKHQrpnesqiatkVHELLNMVQLD--WLADRYPEQLSGGQRQRIALARAL 151
Cdd:COG2401 94 NQFG---------REASLIDAIG---RKGDFKD----------AVELLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517442396 152 AVEPKVLLLDEpFGA-LDAKVRKELRRWLARLHEDINLTSVFVTHDQE 198
Cdd:COG2401 152 AERPKLLVIDE-FCShLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-231 |
5.90e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 93.65 E-value: 5.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIvfhgeDVSGHDVRDRnvgfvfqh 82
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV-----EVLGGDMADA-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 yalfRH----------M------------TVFDNVAF-----GLRMKPKHQRpnesqiatkVHELLNMVQLDWLADRYPE 135
Cdd:NF033858 69 ----RHrravcpriayMpqglgknlyptlSVFENLDFfgrlfGQDAAERRRR---------IDELLRATGLAPFADRPAG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 136 QLSGGQRQRIALARALAVEPKVLLLDEP-----------FGALDAKVRKElRRWLarlhedinltSVFV-THDQEEAmEV 203
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPttgvdplsrrqFWELIDRIRAE-RPGM----------SVLVaTAYMEEA-ER 203
|
250 260
....*....|....*....|....*...
gi 517442396 204 ADRIVVMNKGVIEQIGSPGDVYENPASD 231
Cdd:NF033858 204 FDWLVAMDAGRVLATGTPAELLARTGAD 231
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-221 |
7.94e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 89.36 E-value: 7.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLE--TPDQGSIVFHGEDVSGHDVRDR---NVGF 78
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHMTVFDnvaFgLRMKPKHQRPNESQIAT---KVHELLNMVQLDW-LADRY-PEQLSGGQRQRIALARALAV 153
Cdd:COG0396 82 AFQYPVEIPGVSVSN---F-LRTALNARRGEELSAREflkLLKEKMKELGLDEdFLDRYvNEGFSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 154 EPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHdQEEAME--VADRIVVMNKGVIEQIGSP 221
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITH-YQRILDyiKPDFVHVLVDGRIVKSGGK 225
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-217 |
9.34e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 92.86 E-value: 9.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSknFnAFRA----LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVS--GHDVRDRN 75
Cdd:PRK10790 340 RIDIDNVS--F-AYRDdnlvLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSslSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 76 VGFVFQHYALFRHmTVFDNVAFGlrmkpkhqRPNESQiatKVHELLNMVQLDWLADRYP--------EQ---LSGGQRQR 144
Cdd:PRK10790 417 VAMVQQDPVVLAD-TFLANVTLG--------RDISEE---QVWQALETVQLAELARSLPdglytplgEQgnnLSVGQKQL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517442396 145 IALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEdiNLTSVFVTHDQEEAMEvADRIVVMNKG-VIEQ 217
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGqAVEQ 555
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-196 |
5.19e-20 |
|
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: 90.38 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 7 NVSKNFNAFRA-LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPdqgsivFHGEDVSGHDVRdrnVGFVFQHYAL 85
Cdd:TIGR03719 9 RVSKVVPPKKEiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------FNGEARPQPGIK---VGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 86 FRHMTVFDNVAFGLR-MKPKHQRPNE------------SQIATKVHELLNMV----------QLDWLAD--RYP------ 134
Cdd:TIGR03719 80 DPTKTVRENVEEGVAeIKDALDRFNEisakyaepdadfDKLAAEQAELQEIIdaadawdldsQLEIAMDalRCPpwdadv 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517442396 135 EQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAkvrkELRRWLARLHEDINLTSVFVTHD 196
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHD 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-224 |
5.34e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 87.30 E-value: 5.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 21 ISLDIQSGELVALLGPSGCGKTTLLRIIAGLeTPDQGSIVFHGEDVSGHDVRD--RNVGFVFQHYALFRHMTVFDNVAFG 98
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAElaRHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 99 LrmkpkHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARA-LAVEP------KVLLLDEPFGALDAKV 171
Cdd:PRK03695 94 Q-----PDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPdinpagQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517442396 172 RKELRRWLARLHEdINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDV 224
Cdd:PRK03695 169 QAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-213 |
1.07e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.29 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRN---VGFV 79
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQHYALFRHMTVFDNVAFGLRMKPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLL 159
Cdd:PRK10762 85 HQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517442396 160 LDEPFGAL-DA------KVRKELRrwlarlheDINLTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:PRK10762 165 MDEPTDALtDTeteslfRVIRELK--------SQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-213 |
1.36e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 89.02 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 6 RNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV---SGHDVRDRNVGFVFQH 82
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVAFGlRMKPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK10982 82 LNLVLQRSVMDNMWLG-RYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-227 |
1.67e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 89.24 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGfvfqhyalfrhMTVFDNV 95
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDppRNVE-----------GTVYDFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 96 AFGLR-----MKPKHQ-------RPNES------------------QIATKVHELLNMVQLDwlADRYPEQLSGGQRQRI 145
Cdd:PRK11147 88 AEGIEeqaeyLKRYHDishlvetDPSEKnlnelaklqeqldhhnlwQLENRINEVLAQLGLD--PDAALSSLSGGWLRKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 146 ALARALAVEPKVLLLDEPFGALDAkvrkELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIeqIGSPGDvY 225
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL--VSYPGN-Y 238
|
..
gi 517442396 226 EN 227
Cdd:PRK11147 239 DQ 240
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-236 |
2.95e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 88.11 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF--NAFrALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGF-- 78
Cdd:PRK10522 323 LELRNVTFAYqdNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFsa 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 79 VFQHYALFRHMtvfdnvafglrMKPKHQRPNESQIATKVhELLNM---VQLD--WLADRypeQLSGGQRQRIALARALAV 153
Cdd:PRK10522 402 VFTDFHLFDQL-----------LGPEGKPANPALVEKWL-ERLKMahkLELEdgRISNL---KLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 154 EPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDqEEAMEVADRIVVMNKGVIEQIgsPGDVYENPASDFV 233
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSEL--TGEERDAASRDAV 543
|
...
gi 517442396 234 YHF 236
Cdd:PRK10522 544 ART 546
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-219 |
3.47e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 88.23 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 17 ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHG---EDVSGHDVRDRnVGFVFQHYALFRHmTVFD 93
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDiplTKLQLDSWRSR-LAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 94 NVAFGlrmkpkhqRPNESQIATKVHELLNMVQLDWLadRYPE-----------QLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK10789 408 NIALG--------RPDATQQEIEHVARLASVHDDIL--RLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517442396 163 PFGALDAK----VRKELRRWLARlhedinlTSVFVTHDQEEAMEVADRIVVMNKGVIEQIG 219
Cdd:PRK10789 478 ALSAVDGRtehqILHNLRQWGEG-------RTVIISAHRLSALTEASEILVMQHGHIAQRG 531
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-169 |
6.46e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 83.31 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVsgHDVRD---RNVGFVFQHYALFRHMTVFDN 94
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL--DFQRDsiaRGLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 95 VAFglrMKPKHQRpnesqiaTKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDA 169
Cdd:cd03231 94 LRF---WHADHSD-------EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-221 |
6.93e-19 |
|
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: 83.35 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLE--TPDQGSIVFHGEDVSghdvrdrnvgfvf 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDIT------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 qhyalfrHMTVFDNVAFGLRMKPkhQRPNESQiATKVHELLNMVQldwladrypEQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:cd03217 68 -------DLPPEERARLGIFLAF--QYPPEIP-GVKNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517442396 161 DEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEV-ADRIVVMNKGVIEQIGSP 221
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-224 |
1.04e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 84.49 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 16 RALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPD--------QGSIVFHGEDVSGHD----VRDRNV------- 76
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDaprlARLRAVlpqaaqp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFqhyalfrhmTVFDNVAFGlrMKPKHQRPNESQIATK--VHELLNMVQLDWLADRYPEQLSGGQRQRIALARALA-- 152
Cdd:PRK13547 95 AFAF---------SAREIVLLG--RYPHARRAGALTHRDGeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAql 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 153 -------VEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDV 224
Cdd:PRK13547 164 wpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
3-195 |
2.65e-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: 80.66 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVS-KNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHgedvsghdvRDRNVGFVFQ 81
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP---------EGEDLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 H-YalfrhmtvfdnVAFG-LRmkpkhqrpneSQIAtkvhellnmvqldwladrYP--EQLSGGQRQRIALARALAVEPKV 157
Cdd:cd03223 72 RpY-----------LPLGtLR----------EQLI------------------YPwdDVLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 517442396 158 LLLDEPFGALDAKVRKELRRwLARLHEdinLTSVFVTH 195
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQ-LLKELG---ITVISVGH 146
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-248 |
4.52e-18 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 85.38 E-value: 4.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGletpdqgsivfHGEDVSGHDVRDRNVGFVFQHyALFRHMTVFDNVAF 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLA-----------EMDKVEGHVHMKGSVAYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 98 GLRMKPKHQRPNESQIAtkvheLLNMVQLDWLADRYP-----EQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVR 172
Cdd:TIGR00957 722 GKALNEKYYQQVLEACA-----LLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 173 KEL-RRWLARLHEDINLTSVFVTHDQEEAMEVaDRIVVMNKGVIEQIGSPGDVYENPAS--DFVYHFLGDSNRLHLGED 248
Cdd:TIGR00957 797 KHIfEHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDGAfaEFLRTYAPDEQQGHLEDS 874
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-168 |
5.30e-18 |
|
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: 84.60 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFhGEDVsghdvrdrNVGFVFQ- 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------KLAYVDQs 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 HYALFRHMTVFDNVAFGLRMKP--KHQRPNESQIAtkvheLLNMVQLDwlADRYPEQLSGGQRQRIALARALAVEPKVLL 159
Cdd:TIGR03719 394 RDALDPNKTVWEEISGGLDIIKlgKREIPSRAYVG-----RFNFKGSD--QQKKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
....*....
gi 517442396 160 LDEPFGALD 168
Cdd:TIGR03719 467 LDEPTNDLD 475
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-238 |
5.50e-18 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 84.96 E-value: 5.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEdvsghdvrdrnVGFVFQhYALFRHMTVFDNVAF 97
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQ-TSWIMPGTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 98 GLrmkpkhqrpneSQIATKVHELLNMVQLDWLADRYPEQ-----------LSGGQRQRIALARALAVEPKVLLLDEPFGA 166
Cdd:TIGR01271 510 GL-----------SYDEYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 167 LDAKVRKEL-RRWLARLHedINLTSVFVThDQEEAMEVADRIVVMNKGVIEQIGSPGDVyENPASDFVYHFLG 238
Cdd:TIGR01271 579 LDVVTEKEIfESCLCKLM--SNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSEL-QAKRPDFSSLLLG 647
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-229 |
6.36e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 82.85 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 17 ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPD---QGSIVFHGEDVSG------HDVRDRNVGFVFQH--YAL 85
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNlpekelNKLRAEQISMIFQDpmTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 86 FRHMTVFDNVAFGLRMkpkHQRPNESQIATKVHELLNMVQLDWLADR---YPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK09473 111 NPYMRVGEQLMEVLML---HKGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 163 PFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPA 229
Cdd:PRK09473 188 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-209 |
7.19e-18 |
|
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: 84.07 E-value: 7.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRaLDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFhgedvsghDVRdrnVGFVFQH 82
Cdd:COG1245 342 VEYPDLTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE--------DLK---ISYKPQY 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNvafgLRMKpkhqrpNESQIATKV--HELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:COG1245 410 ISPDYDGTVEEF----LRSA------NTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517442396 161 DEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQeeAME--VADRIVV 209
Cdd:COG1245 480 DEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDI--YLIdyISDRLMV 528
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-215 |
1.13e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.42 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 21 ISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDR-NVGFVF-----QHYALFRHMTVFDN 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAiRAGIMLcpedrKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 95 VAFGLRmkpKHQRPNESqiatkvheLLNMVQLDWLADRY----------PEQ----LSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK11288 352 INISAR---RHHLRAGC--------LINNRWEAENADRFirslniktpsREQlimnLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 161 DEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-213 |
1.71e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.92 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLeTPD---QGSIVFHGEDVSGHDVRD-RNVGFV 79
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCRFKDIRDsEALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 F--QHYALFRHMTVFDNVAFGlrmkpkHQRP-------NESQIATKvhELLNMVQLDWLADRYPEQLSGGQRQRIALARA 150
Cdd:NF040905 82 IihQELALIPYLSIAENIFLG------NERAkrgvidwNETNRRAR--ELLAKVGLDESPDTLVTDIGVGKQQLVEIAKA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517442396 151 LAVEPKVLLLDEPFGAL-DAKVRKELRRWLARLHEDInlTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:NF040905 154 LSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGI--TSIIISHKLNEIRRVADSITVLRDG 215
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-218 |
1.75e-17 |
|
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: 79.23 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 6 RNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPD---QGSIVFHGEDVSG-HDVRDRNVGFVFQ 81
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEfAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 HYALFRHMTVFDNVAFGLRMKpkhqrpnesqiatkvhellnmvqldwlADRYPEQLSGGQRQRIALARALAVEPKVLLLD 161
Cdd:cd03233 91 EDVHFPTLTVRETLDFALRCK---------------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 162 EPFGALDAKVRKELRRWLaRLHEDINLTSVFVTHDQ--EEAMEVADRIVVMNKGviEQI 218
Cdd:cd03233 144 NSTRGLDSSTALEILKCI-RTMADVLKTTTFVSLYQasDEIYDLFDKVLVLYEG--RQI 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-222 |
1.80e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.93 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRaLDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFhgedvsghDVRdrnVGFVFQH 82
Cdd:PRK13409 341 VEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--------ELK---ISYKPQY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 YALFRHMTVFDNVafglrmkpkhqrpneSQIATKV------HELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPK 156
Cdd:PRK13409 409 IKPDYDGTVEDLL---------------RSITDDLgssyykSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDAD 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517442396 157 VLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQeeAME--VADRIVVMnkgvieqIGSPG 222
Cdd:PRK13409 474 LYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDI--YMIdyISDRLMVF-------EGEPG 532
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-218 |
2.67e-17 |
|
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: 82.54 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSknFnAFRALDE--------ISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDV-- 71
Cdd:COG4615 327 TLELRGVT--Y-RYPGEDGdegftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNRea 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 72 -RDRnvgF--VFQHYALFRHMTVFDNVAfglrmkpkhqrpnesqIATKVHELLNMVQLD--------WLADRypeQLSGG 140
Cdd:COG4615 404 yRQL---FsaVFSDFHLFDRLLGLDGEA----------------DPARARELLERLELDhkvsvedgRFSTT---DLSQG 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 141 QRQRIALARALAVEPKVLLLDE------PfgaldakvrkELRRW-----LARLHEdINLTSVFVTHDqEEAMEVADRIVV 209
Cdd:COG4615 462 QRKRLALLVALLEDRPILVFDEwaadqdP----------EFRRVfytelLPELKA-RGKTVIAISHD-DRYFDLADRVLK 529
|
....*....
gi 517442396 210 MNKGVIEQI 218
Cdd:COG4615 530 MDYGKLVEL 538
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-228 |
3.28e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 81.11 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 15 FRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLeTPDQGSI-----VFHGEDVSGHDVRDR------NVGFVFQH- 82
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLKLSPRERrkiigrEIAMIFQEp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 -YALFRHMTVFDNVAFGLrmkPKH-------QRPNESQiaTKVHELLNMVQL---DWLADRYPEQLSGGQRQRIALARAL 151
Cdd:COG4170 99 sSCLDPSAKIGDQLIEAI---PSWtfkgkwwQRFKWRK--KRAIELLHRVGIkdhKDIMNSYPHELTEGECQKVMIAMAI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 152 AVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-168 |
4.24e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 78.45 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSghdvRDR-----NVGFVFQHYALFRHMTVF 92
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLctyqkQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 93 DNVAFGLRMkpkhqrpneSQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:PRK13540 93 ENCLYDIHF---------SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-238 |
7.23e-17 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 79.13 E-value: 7.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEdvsghdvrdrnVGFVFQhYALFRHMTVFDNVAF 97
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQ-FSWIMPGTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 98 GLrmkpkhqrpneSQIATKVHELLNMVQLDWLADRYPEQ-----------LSGGQRQRIALARALAVEPKVLLLDEPFGA 166
Cdd:cd03291 121 GV-----------SYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 167 LDAKVRKEL-RRWLARLHEdiNLTSVFVTHDQEEaMEVADRIVVMNKGVIEQIGSPGDVyENPASDFVYHFLG 238
Cdd:cd03291 190 LDVFTEKEIfESCVCKLMA--NKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSEL-QSLRPDFSSKLMG 258
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3-231 |
7.57e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.59 E-value: 7.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSknFNAFRAL-DEISLDIQSGELVALLGPSGCGKT----TLLRII-AGLeTPDQGSIVFHGEDVSGHDVRDRNV 76
Cdd:PRK10418 5 IELRNIA--LQAAQPLvHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGV-RQTAGRVLLDGKPVAPCALRGRKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHyalfrhmtvfDNVAFG-LRMKPKHQRpnESQIATKVH-------ELLNMVQLD---WLADRYPEQLSGGQRQRI 145
Cdd:PRK10418 82 ATIMQN----------PRSAFNpLHTMHTHAR--ETCLALGKPaddatltAALEAVGLEnaaRVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVY 225
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
....*.
gi 517442396 226 ENPASD 231
Cdd:PRK10418 230 NAPKHA 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-227 |
1.31e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.79 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGlETPdqgsivfHGEDVSGhDVRDrNVGFVFQHYALFrHMTVFDNVAF 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-ELS-------HAETSSV-VIRG-SVAYVPQVSWIF-NATVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 98 GLRMKPkhQRPNESQIATKVHELLNMV---QLDWLADRyPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKE 174
Cdd:PLN03232 702 GSDFES--ERYWRAIDVTALQHDLDLLpgrDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517442396 175 LRRWLARlHEDINLTSVFVThDQEEAMEVADRIVVMNKGVIEQIGSPGDVYEN 227
Cdd:PLN03232 779 VFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-221 |
1.39e-16 |
|
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: 77.07 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNF--NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVG 77
Cdd:cd03369 6 EIEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQHYALFRHmTVFDNVafglrmkPKHQRPNESQI--ATKVHEllnmvqldwladrYPEQLSGGQRQRIALARALAVEP 155
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNL-------DPFDEYSDEEIygALRVSE-------------GGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 156 KVLLLDEPFGAL----DAKVRKELRRwlarlhEDINLTSVFVTHDQEEAMEVaDRIVVMNKGVIEQIGSP 221
Cdd:cd03369 145 RVLVLDEATASIdyatDALIQKTIRE------EFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-220 |
1.81e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 80.55 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAG-LETPDQGSIVFHGedvsghdvrdrNVGFVFQHYALFrHMTVFDNVA 96
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRG-----------TVAYVPQVSWIF-NATVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 97 FGLRMKPkhQRPNESQIATKVH---ELLNMVQLDWLADRyPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKV-- 171
Cdd:PLN03130 701 FGSPFDP--ERYERAIDVTALQhdlDLLPGGDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgr 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 172 -------RKELRrwlarlhediNLTSVFVThDQEEAMEVADRIVVMNKGVIEQIGS 220
Cdd:PLN03130 778 qvfdkciKDELR----------GKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGT 822
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-211 |
2.93e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 79.69 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 55 DQGSIVFHGEDVSGHDVRD-RNVGFVFQHYALFRHMTVFDNVAFGLRMKPKHQRPNESQIATkVHELLNMV--QLDWLAD 131
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAA-IDEFIESLpnKYDTNVG 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 132 RYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHdQEEAMEVADRIVVMN 211
Cdd:PTZ00265 1354 PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFN 1432
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-218 |
4.29e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVSKNfnAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV---SGHDVRDRNVGFV- 79
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDAVKKGMAYIt 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 --------FQHYALFRHMTV---FDNVAFGLRMKPKHQRpNESQIATKVHELLNMVQLDwlADRYPEQLSGGQRQRIALA 148
Cdd:PRK09700 345 esrrdngfFPNFSIAQNMAIsrsLKDGGYKGAMGLFHEV-DEQRTAENQRELLALKCHS--VNQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQI 218
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
13-168 |
6.27e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.27 E-value: 6.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 13 NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDvRDRNVGFVFQHYALFRHMTVF 92
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLGHLPGLKADLSTL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517442396 93 DNVAF--GLRMKPKHQRPNESqiatkvhelLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:PRK13543 101 ENLHFlcGLHGRRAKQMPGSA---------LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-196 |
6.34e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 78.24 E-value: 6.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 6 RNVSKNFNAFRA-LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPdqgsivFHGEDVSGHDVRdrnVGFVFQHYA 84
Cdd:PRK11819 10 NRVSKVVPPKKQiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE------FEGEARPAPGIK---VGYLPQEPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 85 LFRHMTVFDNVAFGLR-MKPKHQRPNE-----------------------SQI-ATKVHELLNmvQLDWLAD--RYP--- 134
Cdd:PRK11819 81 LDPEKTVRENVEEGVAeVKAALDRFNEiyaayaepdadfdalaaeqgelqEIIdAADAWDLDS--QLEIAMDalRCPpwd 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 135 ---EQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAkvrkELRRWLARLHEDINLTSVFVTHD 196
Cdd:PRK11819 159 akvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-168 |
3.29e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 76.31 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAfRAL-DEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFhGEDVSghdvrdrnVGFVFQ 81
Cdd:PRK11819 325 IEAENLSKSFGD-RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK--------LAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 -HYALFRHMTVFDNVAFGLRMKP--KHQRPNESQIAT----------KVhellnmvqldwladrypEQLSGGQRQRIALA 148
Cdd:PRK11819 395 sRDALDPNKTVWEEISGGLDIIKvgNREIPSRAYVGRfnfkggdqqkKV-----------------GVLSGGERNRLHLA 457
|
170 180
....*....|....*....|
gi 517442396 149 RALAVEPKVLLLDEPFGALD 168
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLD 477
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-213 |
3.32e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 73.52 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHG---EDVSGHDVRDRN---VGFVFQHYALFrHMTV 91
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNkneSEPSFEATRSRNrysVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 92 FDNVAFGLRM-KPKHQRPNESQIATKVHELLNMVQLDWLADRyPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAK 170
Cdd:cd03290 96 EENITFGSPFnKQRYKAVTDACSLQPDIDLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517442396 171 VRKEL-RRWLARLHEDINLTSVFVTHdQEEAMEVADRIVVMNKG 213
Cdd:cd03290 175 LSDHLmQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-215 |
3.53e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.81 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNfnafrALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDR-NVGFVF 80
Cdd:PRK10762 257 RLKVDNLSGP-----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 -----QHYALFRHMTVFDNVA---------FGLRMKpkHQRpnESQIATKVHELLNMvqldwladRYP--EQ----LSGG 140
Cdd:PRK10762 332 isedrKRDGLVLGMSVKENMSltalryfsrAGGSLK--HAD--EQQAVSDFIRLFNI--------KTPsmEQaiglLSGG 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 141 QRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-182 |
1.78e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.15 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 28 GELVALLGPSGCGKTTLLRIIAGLETPD--QGSIVFHGEDVSGHDVRdrNVGFVFQHYALFRHMTVFDNVAFG--LRMKP 103
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILK--RTGFVTQDDILYPHLTVRETLVFCslLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 104 KHQRPNESQIATKVHELLNMVQLD--WLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLAR 181
Cdd:PLN03211 172 SLTKQEKILVAESVISELGLTKCEntIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
.
gi 517442396 182 L 182
Cdd:PLN03211 252 L 252
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-213 |
2.51e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.99 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 15 FRALDEISLDIQSGELVALLGPSGCGKTTLLRIIA----GLETPDQGSIVFHGedVSGHDVRDRNVGFVF---QHYALFR 87
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDG--ITPEEIKKHYRGDVVynaETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 88 HMTVFDNVAFGLRMKPKHQRPN----ESQIATKVHELLNMVQLDW-----LADRYPEQLSGGQRQRIALARALAVEPKVL 158
Cdd:TIGR00956 152 HLTVGETLDFAARCKTPQNRPDgvsrEEYAKHIADVYMATYGLSHtrntkVGNDFVRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 159 LLDEPFGALDAKVRKELRRWLaRLHEDINLTSVFVTHDQ--EEAMEVADRIVVMNKG 213
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRAL-KTSANILDTTPLVAIYQcsQDAYELFDKVIVLYEG 287
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-195 |
2.67e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALD---EISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHgedvSGHDVRDRN---- 75
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN----DSHNLKDINlkww 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 76 ---VGFVFQHYALFRHmTVFDNVAFGL---------------------------------------------------RM 101
Cdd:PTZ00265 459 rskIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliEM 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 102 KPKHQRPNESQIATKVHELLNMVQLDWLADRY-------PEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKE 174
Cdd:PTZ00265 538 RKNYQTIKDSEVVDVSKKVLIHDFVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
250 260
....*....|....*....|.
gi 517442396 175 LRRWLARLHEDINLTSVFVTH 195
Cdd:PTZ00265 618 VQKTINNLKGNENRITIIIAH 638
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
13-215 |
3.82e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 13 NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSgHDVRDRNVGFVFQHYALFRHMTVF 92
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-QALQKNLVAYVPQSEEVDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 93 --DNVAFG-------LRMKPKHQRpnesQIATKVHELLNMVQLdwlADRYPEQLSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:PRK15056 97 veDVVMMGryghmgwLRRAKKRDR----QIVTAALARVDMVEF---RHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517442396 164 FGALDAKVRKELRRWLARLhEDINLTSVFVTHDQEEAMEVADrIVVMNKGVI 215
Cdd:PRK15056 170 FTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTV 219
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-196 |
4.92e-14 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 70.86 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 26 QSGELVALLGPSGCGKTTLLRIIAGLETPDQGSivfHGEDVSGHDVRDRNVGFVFQHYalfrhMTVFDNVAFGLRMKPKH 105
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPPDWDEILDEFRGSELQNY-----FTKLLEGDVKVIVKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 106 --QRPNE-----SQIATKVHE------LLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVR 172
Cdd:cd03236 96 vdLIPKAvkgkvGELLKKKDErgkldeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180
....*....|....*....|....
gi 517442396 173 KELRRWLARLHEDINLTSVfVTHD 196
Cdd:cd03236 176 LNAARLIRELAEDDNYVLV-VEHD 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-215 |
5.71e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 72.23 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFhGEDVsghdvrdrNVGFVFQ- 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-SENA--------NIGYYAQd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 82 HYALF-RHMTVFDnvAFGLRMKPKHqrpNESQIATKVHELLnMVQLDwlADRYPEQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:PRK15064 391 HAYDFeNDLTLFD--WMSQWRQEGD---DEQAVRGTLGRLL-FSQDD--IKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 161 DEPFGALDAKVRKELRRWLarlhEDINLTSVFVTHDQEEAMEVADRIV-VMNKGVI 215
Cdd:PRK15064 463 DEPTNHMDMESIESLNMAL----EKYEGTLIFVSHDREFVSSLATRIIeITPDGVV 514
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-207 |
7.91e-14 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 67.78 E-value: 7.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 27 SGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDRNVGFVFqhyalfrhmtvfdnvafglrmkpkhq 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 107 rpnesqiatkvhellnmvqldwlaDRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELR-----RWLAR 181
Cdd:smart00382 55 ------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLL 110
|
170 180
....*....|....*....|....*.
gi 517442396 182 LHEDINLTSVFVTHDQEEAMEVADRI 207
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-228 |
1.01e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.12 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLriiagletpdqGSIVFHGEDVSGHDVRDRNVGFVFQHyALFRHMTVFDNVAF 97
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLL-----------QSLLSQFEISEGRVWAERSIAYVPQQ-AWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 98 GlrmkpKHQRPNESQIATKVHEL-LNMVQLD-WLADRYPEQ---LSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVR 172
Cdd:PTZ00243 744 F-----DEEDAARLADAVRVSQLeADLAQLGgGLETEIGEKgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517442396 173 KELRR--WLARLHEDinlTSVFVTHdQEEAMEVADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:PTZ00243 819 ERVVEecFLGALAGK---TRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
10-208 |
1.60e-13 |
|
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: 68.40 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 10 KNFNAFRALDEISLDiqsGELVALLGPSGCGKTTLLR-IIAGL--ETPDQGSIVFHGEDVSGHDVRDRNVGFVFQH---- 82
Cdd:cd03240 7 RNIRSFHERSEIEFF---SPLTLIVGQNGAGKTTIIEaLKYALtgELPPNSKGGAHDPKLIREGEVRAQVKLAFENangk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 83 -YALFRHMTVFDNVAFglrmkpKHQRpnesqiatkvhellnmvQLDWLADRYPEQLSGGQRQ------RIALARALAVEP 155
Cdd:cd03240 84 kYTITRSLAILENVIF------CHQG-----------------ESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNC 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 156 KVLLLDEPFGALDakvRKELRRWLARLHEDINLTSVF----VTHDqEEAMEVADRIV 208
Cdd:cd03240 141 GILALDEPTTNLD---EENIEESLAEIIEERKSQKNFqlivITHD-EELVDAADHIY 193
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-215 |
2.11e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 70.15 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTtllriiagletpdQGSIVFHgedVSGHDVRDRNVGFVF- 80
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**-------------RGALPAH---V*GPDAGRRPWRF*Tw 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 --QHYALFRHMTVFDNVAFGLR----------MKPKHQRPNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALA 148
Cdd:NF000106 77 caNRRALRRTIG*HRPVR*GRResfsgrenlyMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:NF000106 157 ASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
3-228 |
2.27e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.83 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLeTPDQGSIV-----FHGEDVSGHDVRD 73
Cdd:PRK15093 4 LDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTadrmrFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 74 R------NVGFVFQHyalfrHMTVFD-NVAFGLRMKPK----------HQRPNESQiaTKVHELLNMVQLDWLAD---RY 133
Cdd:PRK15093 83 RrklvghNVSMIFQE-----PQSCLDpSERVGRQLMQNipgwtykgrwWQRFGWRK--RRAIELLHRVGIKDHKDamrSF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 134 PEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:PRK15093 156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCG 235
|
250
....*....|....*
gi 517442396 214 VIEQIGSPGDVYENP 228
Cdd:PRK15093 236 QTVETAPSKELVTTP 250
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-200 |
3.43e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.04 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGlETPdQGS----IVFHGEDVSGHDVRD--RNV 76
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHP-QGYsndlTLFGRRRGSGETIWDikKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHYAL-FRHMTVFDNV-------AFGL-RMKPKHQRpnesQIATKVHELLNMVqlDWLADRYPEQLSGGQrQRIAL 147
Cdd:PRK10938 339 GYVSSSLHLdYRVSTSVRNVilsgffdSIGIyQAVSDRQQ----KLAQQWLDILGID--KRTADAPFHSLSWGQ-QRLAL 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517442396 148 -ARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINLTSVFVTHDQEEA 200
Cdd:PRK10938 412 iVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-213 |
4.41e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.14 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 16 RALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETpdqGSIVFHGEDVSGHDVRD----RNVGFVFQHYALFRHMTV 91
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT---TGVITGGDRLVNGRPLDssfqRSIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 92 FDNVAFGLRMKpkhqRPNESQIATK---VHELLNMVQLDWLADRY----PEQLSGGQRQRIALARALAVEPKVLL-LDEP 163
Cdd:TIGR00956 854 RESLRFSAYLR----QPKSVSKSEKmeyVEEVIKLLEMESYADAVvgvpGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517442396 164 FGALDAKVRKELRRWLARLHEdiNLTSVFVTHDQEEA--MEVADRIVVMNKG 213
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLAD--HGQAILCTIHQPSAilFEEFDRLLLLQKG 979
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-220 |
5.76e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.04 E-value: 5.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 17 ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDV--SGHDVRdRNVGFVFQHYALFRHMTVFDN 94
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltNISDVH-QNMGYCPQFDAIDDLLTGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 95 VAFGLRMKpkhQRPNEsQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKE 174
Cdd:TIGR01257 2033 LYLYARLR---GVPAE-EIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517442396 175 LrrW-----LARLHEDINLTSvfvtHDQEEAMEVADRIVVMNKGVIEQIGS 220
Cdd:TIGR01257 2109 L--WntivsIIREGRAVVLTS----HSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-224 |
8.77e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.20 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHG---EDVSGHDVRDRnVGFVFQHYALFrhmtvfdn 94
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniAKIGLHDLRFK-ITIIPQDPVLF-------- 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 95 vAFGLRMK--PKHQRPNES-QIATKVHELLNMV-----QLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGA 166
Cdd:TIGR00957 1373 -SGSLRMNldPFSQYSDEEvWWALELAHLKTFVsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517442396 167 LDAKVRKELRRWLARLHEDInlTSVFVTHDQEEAMEVAdRIVVMNKGVIEQIGSPGDV 224
Cdd:TIGR00957 1452 VDLETDNLIQSTIRTQFEDC--TVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-175 |
6.89e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 63.35 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 35 GPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVsgHDVRDRNVGFVFQHYALFRHMTVFDNVAFGlrmkpkhqrpneSQI- 113
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI--NNIAKPYCTYIGHNLGLKLEMTVFENLKFW------------SEIy 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517442396 114 --ATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKEL 175
Cdd:PRK13541 99 nsAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
13-232 |
7.44e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.45 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 13 NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEdvsghdvrdrnVGFVFQHYALFRHMTVF 92
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------VSVIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 93 DNVAFG---LRMKPKhqrpnesQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEpfgALDA 169
Cdd:PRK13546 104 ENIEFKmlcMGFKRK-------EIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517442396 170 KVRKELRRWLARLHE--DINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDV---YENPASDF 232
Cdd:PRK13546 174 GDQTFAQKCLDKIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlpkYEAFLNDF 241
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
9-209 |
9.51e-12 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 62.59 E-value: 9.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 9 SKNFNAFRALDEISlDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSghdvrdrnvgfvfqhyalfrh 88
Cdd:cd03222 7 VKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV--------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 89 mtvfdnvafglrMKPKHQrpnesqiatkvhellnmvqldwladrypeQLSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:cd03222 65 ------------YKPQYI-----------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517442396 169 AKVRKELRRWLARLHEDINLTSVFVTHDQEEAMEVADRIVV 209
Cdd:cd03222 104 IEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-198 |
1.72e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.97 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 4 EVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIvfhgedvsgHDVRDRNVGFVFQHY 83
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI---------HCGTKLEVAYFDQHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 84 A-LFRHMTVFDNVAFGlrmkpkhqrPNESQIATKVHELLNMVQlDWLAD----RYP-EQLSGGQRQRIALARALAVEPKV 157
Cdd:PRK11147 392 AeLDPEKTVMDNLAEG---------KQEVMVNGRPRHVLGYLQ-DFLFHpkraMTPvKALSGGERNRLLLARLFLKPSNL 461
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517442396 158 LLLDEPFGALDAKVRkELrrwLARLHEDINLTSVFVTHDQE 198
Cdd:PRK11147 462 LILDEPTNDLDVETL-EL---LEELLDSYQGTVLLVSHDRQ 498
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-213 |
1.92e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 62.26 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 16 RALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETpdQGSIvfHGE-DVSGHDVRD---RNVGFVFQHYALFRHMTV 91
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT--AGVI--TGEiLINGRPLDKnfqRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 92 FDNVAFG--LRmkpkhqrpnesqiatkvhellnmvqldwladrypeQLSGGQRQRIALARALAVEPKVLLLDEPFGALDA 169
Cdd:cd03232 97 REALRFSalLR-----------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517442396 170 KVRKELRRWLARLHEDINltSVFVTHDQEEA--MEVADRIVVMNKG 213
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQ--AILCTIHQPSAsiFEKFDRLLLLKRG 185
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-196 |
2.87e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 25 IQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSivfHGEDVSGHDVRDRNVGFVFQHYalfrhmtvFDNVAFGlRMKPK 104
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD---YEEEPSWDEVLKRFRGTELQNY--------FKKLYNG-EIKVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 105 HQ--------------------RPNESQIATKVHELLNmvqLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:PRK13409 164 HKpqyvdlipkvfkgkvrellkKVDERGKLDEVVERLG---LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190
....*....|....*....|....*....|..
gi 517442396 165 GALDAKVRKELRRWLARLHEDINLtsVFVTHD 196
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELAEGKYV--LVVEHD 270
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-220 |
4.07e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.35 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGleTPD----QGSIVFHGEDVSGHDVRDR-NVG 77
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERaHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 --FVFQhYALfrHMTVFDNVAFgLRM----KPKHQRPNES---QIATKVHELLNMVQLD--WLADRYPEQLSGGQRQRIA 146
Cdd:CHL00131 86 ifLAFQ-YPI--EIPGVSNADF-LRLaynsKRKFQGLPELdplEFLEIINEKLKLVGMDpsFLSRNVNEGFSGGEKKRNE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517442396 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDINlTSVFVTHDQeEAME--VADRIVVMNKGVIEQIGS 220
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQ-RLLDyiKPDYVHVMQNGKIIKTGD 235
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-225 |
1.18e-10 |
|
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: 62.49 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 26 QSGELVALLGPSGCGKTTLLRIIAGLETPDQGSivfHGEDVSGHDVRDRNVGFVFQHYalfrhmtvFDNVAFG-LR--MK 102
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGD---YDEEPSWDEVLKRFRGTELQDY--------FKKLANGeIKvaHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 103 PKH----------------QRPNESQIATKVHELLNmvqLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGA 166
Cdd:COG1245 166 PQYvdlipkvfkgtvrellEKVDERGKLDELAEKLG---LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517442396 167 LDAKVRKELRRWLARLHEDiNLTSVFVTHDQeeAM--EVADRIVVMnkgvieqIGSPGdVY 225
Cdd:COG1245 243 LDIYQRLNVARLIRELAEE-GKYVLVVEHDL--AIldYLADYVHIL-------YGEPG-VY 292
|
|
| TOBE_3 |
pfam12857 |
TOBE-like domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
270-321 |
1.28e-10 |
|
TOBE-like 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 sulfate. Found in ABC transporters immediately after the ATPase domain.
Pssm-ID: 432835 Cd Length: 59 Bit Score: 56.10 E-value: 1.28e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 517442396 270 AAEVRDIRPLGATTRVTLKVEGQSELIEAEVVKDHDSLVGLAKGETLFFKPK 321
Cdd:pfam12857 8 PATVRRIRRVGPIVRLELERLDTGELIEIELPRDRFRELGLAEGETVRLRPR 59
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-197 |
1.09e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.88 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNAFraLDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLE--TPDQGSIVFHGEDVSGHDVRDR---N 75
Cdd:PRK09580 2 LSIKDLHVSVEDKAI--LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 76 VGFVFQHYALFRHMT--VFDNVAFGLRMKPKHQRP-----NESQIATKVhELLNMVQlDWLADRYPEQLSGGQRQRIALA 148
Cdd:PRK09580 80 IFMAFQYPVEIPGVSnqFFLQTALNAVRSYRGQEPldrfdFQDLMEEKI-ALLKMPE-DLLTRSVNVGFSGGEKKRNDIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517442396 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLARLhEDINLTSVFVTHDQ 197
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQ 205
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-232 |
1.67e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 2 SIEVRNVSKNF--NAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVG 77
Cdd:PLN03130 1237 SIKFEDVVLRYrpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlrKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 78 FVFQHYALFRhmtvfDNVAFGLRMKPKHQRPNESQIATKVHeLLNMVQ-----LDWLADRYPEQLSGGQRQRIALARALA 152
Cdd:PLN03130 1317 IIPQAPVLFS-----GTVRFNLDPFNEHNDADLWESLERAH-LKDVIRrnslgLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 153 VEPKVLLLDEPFGAL----DAKVRKELRrwlarlHEDINLTSVFVTHDQEEAMEvADRIVVMNKGVIEQIGSPGDVYENP 228
Cdd:PLN03130 1391 RRSKILVLDEATAAVdvrtDALIQKTIR------EEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNE 1463
|
....
gi 517442396 229 ASDF 232
Cdd:PLN03130 1464 GSAF 1467
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
86-230 |
1.79e-09 |
|
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: 58.87 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 86 FRHMTVFDNVAFglrMKPKHQRPNESQIATKVHE--------LLNmVQLDWLA-DRYPEQLSGGQRQRIALARALAVE-P 155
Cdd:TIGR00630 433 VSELSIREAHEF---FNQLTLTPEEKKIAEEVLKeirerlgfLID-VGLDYLSlSRAAGTLSGGEAQRIRLATQIGSGlT 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 156 KVL-LLDEPFGALDAKVRKELRRWLARLhEDINLTSVFVTHDqEEAMEVADRIVVMNKG-------VIEQiGSPGDVYEN 227
Cdd:TIGR00630 509 GVLyVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYVIDIGPGagehggeVVAS-GTPEEILAN 585
|
...
gi 517442396 228 PAS 230
Cdd:TIGR00630 586 PDS 588
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-213 |
3.35e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.32 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 1 MSIEVRNVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETpdqGSIVFHGEDVSG----HDVRDRNV 76
Cdd:PLN03140 879 MPAEMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKT---GGYIEGDIRISGfpkkQETFARIS 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 77 GFVFQHYALFRHMTVFDNVAFG--LRMkPKHQRPNESQIAtkVHELLNMVQLDWLADR---YP--EQLSGGQRQRIALAR 149
Cdd:PLN03140 956 GYCEQNDIHSPQVTVRESLIYSafLRL-PKEVSKEEKMMF--VDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAV 1032
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 150 ALAVEPKVLLLDEPFGALDAKVRKELRRwLARLHEDINLTSVFVTHDQE-EAMEVADRIVVMNKG 213
Cdd:PLN03140 1033 ELVANPSIIFMDEPTSGLDARAAAIVMR-TVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRG 1096
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-208 |
3.63e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.87 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGedvsghdvrDRNVGFVFQHY-ALfrHMTVFDNVA 96
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG---------NWQLAWVNQETpAL--PQPALEYVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 97 FGLR--------MKPKHQRPNESQIATkVHELLNMVQLDWLADRYP----------EQL-------SGGQRQRIALARAL 151
Cdd:PRK10636 86 DGDReyrqleaqLHDANERNDGHAIAT-IHGKLDAIDAWTIRSRAAsllhglgfsnEQLerpvsdfSGGWRMRLNLAQAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 152 AVEPKVLLLDEPFGALDAKVRKELRRWLarlhEDINLTSVFVTHDQEEAMEVADRIV 208
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWL----KSYQGTLILISHDRDFLDPIVDKII 217
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-277 |
3.88e-09 |
|
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: 56.79 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNF----NAfrALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDqGSIVFHG---EDVSGHDVRdRN 75
Cdd:cd03289 3 MTVKDLTAKYteggNA--VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGvswNSVPLQKWR-KA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 76 VGFVFQHYALFrhmtvfdNVAFGLRMKPKHQRPNEsqiatKVHELLNMVQLDWLADRYPEQL-----------SGGQRQR 144
Cdd:cd03289 79 FGVIPQKVFIF-------SGTFRKNLDPYGKWSDE-----EIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 145 IALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDinlTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDV 224
Cdd:cd03289 147 MCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFAD---CTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 517442396 225 YENpaSDFVYHFLGDSNRLHLGEDRHVLFRPHEVSLSRSELEDHHAAEVRDIR 277
Cdd:cd03289 224 LNE--KSHFKQAISPSDRLKLFPRRNSSKSKRKPRPQIQALQEETEEEVQDTR 274
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-245 |
4.51e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRD--RNVGFVFQHYALFRhmtvfDNV 95
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFS-----GTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 96 AFGLRMKPKHqrpNESQIatkvHELLNMVQLDWLADRYP-----------EQLSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:PLN03232 1327 RFNIDPFSEH---NDADL----WEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 165 GALDAKVRKELRRwlaRLHEDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIGSPGDVYENPASDF--VYHFLGDSNR 242
Cdd:PLN03232 1400 ASVDVRTDSLIQR---TIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFfrMVHSTGPANA 1476
|
...
gi 517442396 243 LHL 245
Cdd:PLN03232 1477 QYL 1479
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-195 |
6.00e-09 |
|
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: 57.07 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 20 EISLDIQSGELVALLGPSGCGKTTLLRIIAGL--------ETPDQGSIVFHGED--VSGHDVRDRNVgfvfqhYAlfrhM 89
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFYVPQRpyMTLGTLRDQII------YP----D 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 90 TVFDnvafglrMKPKHQRPNEsqiatkVHELLNMVQLDWLADR---------YPEQLSGGQRQRIALARALAVEPKVLLL 160
Cdd:TIGR00954 540 SSED-------MKRRGLSDKD------LEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*
gi 517442396 161 DEPFGAldakVRKELRRWLARLHEDINLTSVFVTH 195
Cdd:TIGR00954 607 DECTSA----VSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-218 |
4.94e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 10 KNFNAFR--ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHDVRDR-NVGFvfqhyALF 86
Cdd:PRK10982 254 RNLTSLRqpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAiNHGF-----ALV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 87 ----RHMTVFDNVAFGLRMKPKHQRPNESQIAtkvheLLNMVQL----DWLAD----RYPEQ------LSGGQRQRIALA 148
Cdd:PRK10982 329 teerRSTGIYAYLDIGFNSLISNIRNYKNKVG-----LLDNSRMksdtQWVIDsmrvKTPGHrtqigsLSGGNQQKVIIG 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVIEQI 218
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-209 |
6.86e-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: 54.15 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDqGSIVFHG---EDVSGHDVRdRNVGFVFQHYALFrhmtvfdN 94
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvswNSVTLQTWR-KAFGVIPQKVFIF-------S 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 95 VAFGLRMKPkHQRPNESQIATKVHEllnmVQLDWLADRYPEQ-----------LSGGQRQRIALARALAVEPKVLLLDEP 163
Cdd:TIGR01271 1306 GTFRKNLDP-YEQWSDEEIWKVAEE----VGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517442396 164 FGALDAKVRKELRRWLArlHEDINLTSVFVTHDQEEAMEVADRIVV 209
Cdd:TIGR01271 1381 SAHLDPVTLQIIRKTLK--QSFSNCTVILSEHRVEALLECQQFLVI 1424
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
137-213 |
1.28e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.90 E-value: 1.28e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 137 LSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
8-224 |
2.14e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 8 VSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFhgedvsghdVRDRNVGFVFQHYALFr 87
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIKLGYFAQHQLEF- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 88 hmtvfdnvafglrmkpkhQRPNES------QIATKVHELlnmvQL-DWLA------DRYPE---QLSGGQRQRIALARAL 151
Cdd:PRK10636 388 ------------------LRADESplqhlaRLAPQELEQ----KLrDYLGgfgfqgDKVTEetrRFSGGEKARLVLALIV 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517442396 152 AVEPKVLLLDEPFGALDAKVRKELRRWLArlheDINLTSVFVTHDQEEAMEVADRIVVMNKGVIEQIgsPGDV 224
Cdd:PRK10636 446 WQRPNLLLLDEPTNHLDLDMRQALTEALI----DFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPF--DGDL 512
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-221 |
2.19e-07 |
|
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: 51.06 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSG---HDVRDRnVGFVFQHYALFRHMTVFDn 94
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlplHTLRSR-LSIILQDPILFSGSIRFN- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 95 vafglrMKPKHQRPNESQI-ATKVHELLNMVQ-----LDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:cd03288 115 ------LDPECKCTDDRLWeALEIAQLKNMVKslpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASID 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517442396 169 AKVRKELRRWLARLHEDinLTSVFVTHDQEEAMEvADRIVVMNKGVIEQIGSP 221
Cdd:cd03288 189 MATENILQKVVMTAFAD--RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTP 238
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-210 |
2.53e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 22 SLDIQSGELVALLGPSGCGKTTLLRIIAGlETPdqgsiVFHGEDVSGhdvrdrnvgfvFQHYAL-------------FRH 88
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG-ELP-----LLSGERQSQ-----------FSHITRlsfeqlqklvsdeWQR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 89 ----MTVFDNVAFGLRMKPKHQrpNESQIATKVHELLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEPKVLLLDEPF 164
Cdd:PRK10938 86 nntdMLSPGEDDTGRTTAEIIQ--DEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517442396 165 GALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVM 210
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
3-213 |
4.30e-07 |
|
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: 49.95 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 3 IEVRNVSKNfnafrALDEISLDIQSGELVALLGPSGCGKTTLL---------------------RIIAGLETPDQGSIVF 61
Cdd:cd03270 1 IIVRGAREH-----NLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 62 HGEDVS------GHDVRDrNVGFVFQHYALFRhmTVFDNVAFGLRMKpkhqrpnesqiatkvheLLNMVQLDWLA-DRYP 134
Cdd:cd03270 76 LSPAIAidqkttSRNPRS-TVGTVTEIYDYLR--LLFARVGIRERLG-----------------FLVDVGLGYLTlSRSA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 135 EQLSGGQRQRIALARALAVEPKVLL--LDEPFGALDAKVRKELRRWLARLhEDINLTSVFVTHDqEEAMEVADRIVVMNK 212
Cdd:cd03270 136 PTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD-EDTIRAADHVIDIGP 213
|
.
gi 517442396 213 G 213
Cdd:cd03270 214 G 214
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
10-196 |
4.66e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 49.62 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 10 KNFNAFRALDEISLDiqsGELVALLGPSGCGKTTLLRIIAgletpdqgsIVFHGEDVSGHDVRDR---------NVGFVF 80
Cdd:COG0419 8 ENFRSYRDTETIDFD---DGLNLIVGPNGAGKSTILEAIR---------YALYGKARSRSKLRSDlinvgseeaSVELEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 81 QH----YALFRH---------------MTVFDNVaFGL--------RMKPKHQRPNESQIATKVHELLNMVQLDWLADRY 133
Cdd:COG0419 76 EHggkrYRIERRqgefaefleakpserKEALKRL-LGLeiyeelkeRLKELEEALESALEELAELQKLKQEILAQLSGLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517442396 134 P-EQLSGGQRQRIALARALAvepkvLLLDepFGALDAKVRKELRRWLARLHedinltsvFVTHD 196
Cdd:COG0419 155 PiETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
136-215 |
6.37e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 136 QLSGGQRQRIALARALAVEPKVLLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGVI 215
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
16-213 |
6.57e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 16 RALDEISLDIQSGELVALLGPSGCGKTTLLRiiAGLETPDQGSIVfhgEDVSghdvrdrnvgfvfqhyALFRHMTVFdnv 95
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLI---SFLP----------------KFSRNKLIF--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 96 afglrmkpkhqrpnESQIATKVHELLNMVQLDwladRYPEQLSGGQRQRIALARALAVEPK--VLLLDEPFGALDAKVRK 173
Cdd:cd03238 65 --------------IDQLQFLIDVGLGYLTLG----QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517442396 174 ELRRWLARLhEDINLTSVFVTHDqEEAMEVADRIVVMNKG 213
Cdd:cd03238 127 QLLEVIKGL-IDLGNTVILIEHN-LDVLSSADWIIDFGPG 164
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
132-168 |
9.58e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 9.58e-07
10 20 30
....*....|....*....|....*....|....*..
gi 517442396 132 RYPEQLSGGQRQRIALARALAVEPKVLLLDEPFGALD 168
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-162 |
2.65e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 17 ALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIvfhgeDVSGhdvrdrNVGFVFQHYALFRHMTVFDNVA 96
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKG------SAALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517442396 97 F-GLRMKPKHQRPNEsqIATKVHELLNMVQldwLADRYPEQLSGGQRQRIALARALAVEPKVLLLDE 162
Cdd:PRK13545 108 LkGLMMGLTKEKIKE--IIPEIIEFADIGK---FIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
18-210 |
4.58e-06 |
|
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: 46.20 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFHGEDVSGHdvrdrNVGFVFQHYALFRHmtvfdnvaf 97
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGC-----IVAAVSAELIFTRL--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 98 glrmkpkhqrpnesqiatkvhellnmvqldwladrypeQLSGGQRQRIALARALA---VEPKVL-LLDEPFGALDAKVRK 173
Cdd:cd03227 77 --------------------------------------QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQ 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 517442396 174 ELrRWLARLHEDINLTSVFVTHDqEEAMEVADRIVVM 210
Cdd:cd03227 119 AL-AEAILEHLVKGAQVIVITHL-PELAELADKLIHI 153
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-213 |
4.67e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 15 FRALDeISLDIQSgeLVALLGPSGCGKTTLLRIIAGLETPDQGSI---------VFHGEDVSGHDVRDRNVGFVFQHYA- 84
Cdd:PLN03073 525 FKNLN-FGIDLDS--RIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmaVFSQHHVDGLDLSSNPLLYMMRCFPg 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 85 -----LFRHMTVFdNVAFGLRMKPKHQrpnesqiatkvhellnmvqldwladrypeqLSGGQRQRIALARALAVEPKVLL 159
Cdd:PLN03073 602 vpeqkLRAHLGSF-GVTGNLALQPMYT------------------------------LSGGQKSRVAFAKITFKKPHILL 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517442396 160 LDEPFGALDAKVRKELRRWLARLHEDInltsVFVTHDQEEAMEVADRIVVMNKG 213
Cdd:PLN03073 651 LDEPSNHLDLDAVEALIQGLVLFQGGV----LMVSHDEHLISGSVDELWVVSEG 700
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
10-214 |
1.01e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 45.72 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 10 KNFNAFRALDEISL-DIQSGELVALLGPSGCGKTTLLRIIA------GLETPDQG---SIVFHGEDVSghdvrdrNVGFV 79
Cdd:cd03279 9 KNFGPFREEQVIDFtGLDNNGLFLICGPTGAGKSTILDAITyalygkTPRYGRQEnlrSVFAPGEDTA-------EVSFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 80 FQ----HYALFRHmtvfdnvaFGLrmkpkhqrpNESQIATKVheLLNMVQLDWLADRYPEQLSGGQRQRIALARALAVEP 155
Cdd:cd03279 82 FQlggkKYRVERS--------RGL---------DYDQFTRIV--LLPQGEFDRFLARPVSTLSGGETFLASLSLALALSE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 156 KV----------LLLDEPFGALDAKVRKELRRWLARLHEDiNLTSVFVTHDQEEAMEVADRIVVMNKGV 214
Cdd:cd03279 143 VLqnrggarleaLFIDEGFGTLDPEALEAVATALELIRTE-NRMVGVISHVEELKERIPQRLEVIKTPG 210
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
108-230 |
6.27e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 108 PNESQIATKVHE-------LLNMVQLDWLA-DRYPEQLSGGQRQRIALARALA---VEpkVL-LLDEP------------ 163
Cdd:COG0178 449 EREAEIAERILKeirsrlgFLVDVGLDYLTlDRSAGTLSGGEAQRIRLATQIGsglVG--VLyVLDEPsiglhqrdndrl 526
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517442396 164 FGALdakvrKELRrwlarlheDINLTSVFVTHDqEEAMEVADRIVVMNKG-------VIEQiGSPGDVYENPAS 230
Cdd:COG0178 527 IETL-----KRLR--------DLGNTVIVVEHD-EDTIRAADYIIDIGPGagehggeVVAQ-GTPEEILKNPDS 585
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-232 |
1.02e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLL----RIIaglETPDqGSIVFHGEDVSGHDVRD--RNVGFVFQHYALFRHmTV 91
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMV---EVCG-GEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 92 FDNVAFGLRMKPkhqrpnesqiaTKVHELLNMVQL--------DWLADRYPE---QLSGGQRQRIALARALAVE-PKVLL 159
Cdd:PTZ00243 1401 RQNVDPFLEASS-----------AEVWAALELVGLrervasesEGIDSRVLEggsNYSVGQRQLMCMARALLKKgSGFIL 1469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517442396 160 LDEPFG----ALDAKVRKELRRWLArlhediNLTSVFVTHdqeEAMEVA--DRIVVMNKGVIEQIGSPGDVYENPASDF 232
Cdd:PTZ00243 1470 MDEATAnidpALDRQIQATVMSAFS------AYTVITIAH---RLHTVAqyDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-196 |
2.74e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 7 NVSKNFNAFRALDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIVFhgedvsghDVRDRnVGFVFQHYALF 86
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL--------DPNER-LGKLRQDQFAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 87 RHMTVFDNVAFGLR--MKPKHQR------PN------------ESQIA--------TKVHELLNMVQLDwladryPEQLS 138
Cdd:PRK15064 77 EEFTVLDTVIMGHTelWEVKQERdriyalPEmseedgmkvadlEVKFAemdgytaeARAGELLLGVGIP------EEQHY 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517442396 139 G-------GQRQRIALARALAVEPKVLLLDEPFGALDAKVrkelRRWLARLHEDINLTSVFVTHD 196
Cdd:PRK15064 151 GlmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISHD 211
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-301 |
3.75e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 131 DRYPEQLSGGQRQRIALARALAVEPK--VLLLDEPFGALDAKVRKELRRWLARLHEDINlTSVFVTHDqEEAMEVADRIV 208
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHD-EQMISLADRII 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 209 VMNKGV------IEQIGSPGDvyenpasdfvyhFLGDSNRLHLGEDRHVLF------RPHEVS-LSRSELEDHHAAEVRD 275
Cdd:PRK00635 549 DIGPGAgifggeVLFNGSPRE------------FLAKSDSLTAKYLRQELTipipekRTNSLGtLTLSKATKHNLKDLTI 616
|
170 180
....*....|....*....|....*..
gi 517442396 276 IRPLGATTRVT-LKVEGQSELIEAEVV 301
Cdd:PRK00635 617 SLPLGRLTVVTgVSGSGKSSLINDTLV 643
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
25-50 |
2.89e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 39.30 E-value: 2.89e-03
10 20
....*....|....*....|....*...
gi 517442396 25 IQSGELVALL--GPSGCGKTTLLRIIAG 50
Cdd:PRK13342 31 IEAGRLSSMIlwGPPGTGKTTLARIIAG 58
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
31-54 |
4.73e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 37.09 E-value: 4.73e-03
10 20
....*....|....*....|....
gi 517442396 31 VALLGPSGCGKTTLLRIIAGLETP 54
Cdd:COG4917 4 IMLIGRSGAGKTTLTQALNGEELE 27
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
116-207 |
8.28e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 37.24 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517442396 116 KVHELLNMVQLDwlaDRYPEQLSGGQRQRIALARALA---VEPK-VLLLDEPFGALDAKVRKELRRWLARLHEDinlTSV 191
Cdd:cd03272 141 KINSLTNMKQDE---QQEMQQLSGGQKSLVALALIFAiqkCDPApFYLFDEIDAALDAQYRTAVANMIKELSDG---AQF 214
|
90
....*....|....*.
gi 517442396 192 FVTHDQEEAMEVADRI 207
Cdd:cd03272 215 ITTTFRPELLEVADKF 230
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
18-60 |
9.18e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 36.96 E-value: 9.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 517442396 18 LDEISLDIQSGELVALLGPSGCGKTTLLRIIAGLETPDQGSIV 60
Cdd:PRK15177 3 LDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFI 45
|
|
| |
