|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-352 |
0e+00 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 771.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVF 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 QHYALFRHMTVFDNIAFGLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLL 160
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMGEV 240
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 241 NRLTGTVRGGQFHVGAHRWPLGYTPAYQGPVDLFLRPWEVDISRRTSLDSPLPVQVIEASPKGHYTQLVVQPLGWYHDPL 320
Cdd:PRK10851 241 NRLQGTIRGGQFHVGAHRWPLGYTPAYQGPVDLFLRPWEVDISRRTSLDSPLPVQVLEVSPKGHYWQLVVQPLGWYNEPL 320
|
330 340 350
....*....|....*....|....*....|...
gi 17865703 321 TVVMAGE-DVPVRGERLFVGLQKARLYNGDQRI 352
Cdd:PRK10851 321 TVVMHGDiDAPQRGERLFVGLQNARLYNGDERI 353
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-346 |
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: 528.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV-SRLHARERKVGFV 79
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 FQHYALFRHMTVFDNIAFGLTVLPrrdrPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILL 159
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRP----PSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMGE 239
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 240 VNRLTGTVRGGQFHVGAHRWPLGyTPAYQGPVDLFLRPWEVDISRRTSLDSPLPVQVIEASPKGHYTQLVVQPLGWYHDP 319
Cdd:COG1118 237 VNVLRGRVIGGQLEADGLTLPVA-EPLPDGPAVAGVRPHDIEVSREPEGENTFPATVARVSELGPEVRVELKLEDGEGQP 315
|
330 340 350
....*....|....*....|....*....|.
gi 17865703 320 LTVVM----AGEDVPVRGERLFVGLQKARLY 346
Cdd:COG1118 316 LEAEVtkeaWAELGLAPGDPVYLRPRPARVF 346
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
3-243 |
6.50e-152 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 427.29 E-value: 6.50e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQH 82
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAFGLTVLprrdRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIR----KHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMGEVNR 242
Cdd:TIGR00968 157 PFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNV 236
|
.
gi 17865703 243 L 243
Cdd:TIGR00968 237 L 237
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-345 |
1.77e-147 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 420.66 E-value: 1.77e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 2 SIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQ 81
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRHMTVFDNIAFGLtvlpRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLD 161
Cdd:COG3842 85 DYALFPHLTVAENVAFGL----RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMGEVN 241
Cdd:COG3842 161 EPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 242 RLTGTVR---GGQFHVGAHRWPLGYTPAYQ--GPVDLFLRPWEVDISrRTSLDSPLPVQVIEASPKGHYTQLVVQ-PLGw 315
Cdd:COG3842 241 LLPGTVLgdeGGGVRTGGRTLEVPADAGLAagGPVTVAIRPEDIRLS-PEGPENGLPGTVEDVVFLGSHVRYRVRlGDG- 318
|
330 340 350
....*....|....*....|....*....|..
gi 17865703 316 yhDPLTVVMAGEDV--PVRGERLFVGLQKARL 345
Cdd:COG3842 319 --QELVVRVPNRAAlpLEPGDRVGLSWDPEDV 348
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-239 |
2.74e-144 |
|
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: 408.27 E-value: 2.74e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVF 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 QHYALFRHMTVFDNIAFGLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLL 160
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMGE 239
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-346 |
1.14e-133 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 385.58 E-value: 1.14e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 2 SIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQ 81
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRHMTVFDNIAFGLTVlprRDRPtAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLD 161
Cdd:COG3839 83 SYALYPHMTVYENIAFPLKL---RKVP-KAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMGE-- 239
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSpp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 240 VNRLTGTVRGGQFHVGAHRWPL--GYTPAYQGPVDLFLRPwEvDISRRTSLDSPLPVQVIEASPKGHYTQLVVQPLGwyh 317
Cdd:COG3839 239 MNLLPGTVEGGGVRLGGVRLPLpaALAAAAGGEVTLGIRP-E-HLRLADEGDGGLEATVEVVEPLGSETLVHVRLGG--- 313
|
330 340
....*....|....*....|....*....
gi 17865703 318 DPLTVVMAGEDVPVRGERLFVGLQKARLY 346
Cdd:COG3839 314 QELVARVPGDTRLRPGDTVRLAFDPERLH 342
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-345 |
5.55e-110 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 325.45 E-value: 5.55e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQH 82
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAFGLTVlPRRDRptaAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:TIGR03265 85 YALFPNLTVADNIAYGLKN-RGMGR---AEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMGEVNR 242
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 243 LTGTVR-GGQFHVGAHRWPLGYTPAYQG-PVDLFLRPWEVDISRRTSLDSPLPVQVIEASPKGHYTQLVVQPLGwyhDPL 320
Cdd:TIGR03265 241 LPGTRGgGSRARVGGLTLACAPGLAQPGaSVRLAVRPEDIRVSPAGNAANLLLARVEDMEFLGAFYRLRLRLEG---LPG 317
|
330 340 350
....*....|....*....|....*....|..
gi 17865703 321 TVVMA------GEDVPVR-GERLFVGLQKARL 345
Cdd:TIGR03265 318 QALVAdvsaseVERLGIRaGQPIWIELPAERL 349
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-238 |
5.51e-109 |
|
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: 318.41 E-value: 5.51e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQH 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAFGLtvlpRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:cd03300 81 YALFPHLTVFENIAFGL----RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMG 238
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-219 |
1.73e-104 |
|
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: 305.98 E-value: 1.73e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQH 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAFGLtvlpRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:cd03259 81 YALFPHLTVAENIAFGL----KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQAD 219
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-247 |
3.45e-104 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 311.50 E-value: 3.45e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQH 82
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAFGLtvlpRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:PRK09452 95 YALFPHMTVFENVAFGL----RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMGEVNR 242
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINI 250
|
....*
gi 17865703 243 LTGTV 247
Cdd:PRK09452 251 FDATV 255
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-213 |
6.28e-98 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 291.22 E-value: 6.28e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARerkVGF 78
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD---RGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHMTVFDNIAFGLtvlPRRDRPTAAAiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQIL 158
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGL---ELRGVPKAER-RERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-261 |
4.81e-95 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 287.00 E-value: 4.81e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQH 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAFGLTVLPRrdrpTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGV----PKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMGEVNR 242
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANI 242
|
250
....*....|....*....
gi 17865703 243 LTGTVRGGQFHVGAHRWPL 261
Cdd:PRK11432 243 FPATLSGDYVDIYGYRLPR 261
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-211 |
3.58e-93 |
|
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: 277.43 E-value: 3.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARerkVGF 78
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHMTVFDNIAFGLtvlpRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQIL 158
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGL----ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17865703 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMS 211
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-239 |
2.14e-92 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 278.51 E-value: 2.14e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFV 79
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 FQHYALFRHMTVFDNIAfglTVlPRRDRPTAAAIKTKVTQLLEMVQL--AHLADRFPAQLSGGQKQRVALARALAVEPQI 157
Cdd:COG1125 82 IQQIGLFPHMTVAENIA---TV-PRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFM 237
Cdd:COG1125 158 LLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFV 237
|
..
gi 17865703 238 GE 239
Cdd:COG1125 238 GA 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-217 |
1.44e-89 |
|
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: 267.97 E-value: 1.44e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQH 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAFGLTVlprRDRPTAAaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKL---RKVPKDE-IDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQ 217
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-353 |
5.62e-87 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 266.71 E-value: 5.62e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 2 SIEIARIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVF 80
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 QHYALFRHMTVFDNIAFGLTV--LPRrdrptaAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQIL 158
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIrgMPK------AEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMG 238
Cdd:PRK11650 157 LFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 239 E--VNRLTGTVR--GGQFHVGAH-RWPLGYTPAYQGPVDLFL--RPwEVDISRRTSLDSPLPVQVIEaspkghytqlvvq 311
Cdd:PRK11650 237 SpaMNLLDGRVSadGAAFELAGGiALPLGGGYRQYAGRKLTLgiRP-EHIALSSAEGGVPLTVDTVE------------- 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 17865703 312 PLG--------WYHDPLTVVMAGEDVPVRGERLFVGLQKARL--YNGD--QRIE 353
Cdd:PRK11650 303 LLGadnlahgrWGGQPLVVRLPHQERPAAGSTLWLHLPANQLhlFDADtgRRIE 356
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-311 |
2.80e-86 |
|
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: 263.97 E-value: 2.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 33 LLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQHYALFRHMTVFDNIAFGLtvlpRRDRPTAAA 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGL----KMRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 113 IKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVF 192
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 193 VTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMGEVNRLTGTV--RGGQ---FHVGAHRWPLGYT--- 264
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVieRKSEqvvLAGVEGRRCDIYTdvp 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17865703 265 -PAYQgPVDLFLRPWEVDIS--RRTSLDSPLPVQVIEASPKGHYTQLVVQ 311
Cdd:TIGR01187 237 vEKDQ-PLHVVLRPEKIVIEeeDEANSSNAIIGHVIDITYLGMTLEVHVR 285
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-230 |
1.47e-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: 258.77 E-value: 1.47e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVS----RLHARERKVGF 78
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHMTVFDNIAFGLTVLPRRDRPTAAAIktkVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQIL 158
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEER---AMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 159 LLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPAT 230
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-222 |
3.21e-85 |
|
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: 257.99 E-value: 3.21e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE-----RKVG 77
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 78 FVFQHYALFRHMTVFDNIAFGL---TVLPRRDrptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVE 154
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLrehTDLSEAE------IRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPD 222
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
18-283 |
1.34e-83 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 257.70 E-value: 1.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQHYALFRHMTVFDNIAF 97
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 98 GLTV--LPRRDrptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKEL 175
Cdd:NF040840 96 GLKLrkVPKEE------IERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 176 RRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMGEVNRLTGTVR----GGQ 251
Cdd:NF040840 170 IREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENIIEGVAEkggeGTI 249
|
250 260 270
....*....|....*....|....*....|..
gi 17865703 252 FHVGAHRWPLgyTPAYQGPVDLFLRPWEVDIS 283
Cdd:NF040840 250 LDTGNIKIEL--PEEKKGKVRIGIRPEDITIS 279
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-215 |
9.39e-83 |
|
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: 250.87 E-value: 9.39e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARER---- 74
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 75 --KVGFVFQHYALFRHMTVFDNIAFGLTVLPRRDRptaaAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALA 152
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKK----ERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAtEVADRVVVMSQGNI 215
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-239 |
2.62e-82 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 250.68 E-value: 2.62e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFV 79
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 FQHYALFRHMTVFDNIAfgltVLPRRDRPTAAAIKTKVTQLLEMVQL--AHLADRFPAQLSGGQKQRVALARALAVEPQI 157
Cdd:cd03295 81 IQQIGLFPHMTVEENIA----LVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFM 237
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
..
gi 17865703 238 GE 239
Cdd:cd03295 237 GA 238
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-216 |
4.13e-82 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 249.58 E-value: 4.13e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARER---- 74
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 75 --KVGFVFQHYALFRHMTVFDNIAFGLTV--LPRRDRptaaaiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARA 150
Cdd:COG1136 85 rrHIGFVFQFFNLLPELTALENVALPLLLagVSRKER------RERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDqEEATEVADRVVVMSQGNIE 216
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-238 |
2.38e-79 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 243.01 E-value: 2.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQvLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQH 82
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAFGLTVLpRRDRPTaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKR-KVDKKE---IERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMG 238
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-213 |
3.69e-78 |
|
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: 237.86 E-value: 3.69e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLH----ARERKVGF 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHMTVFDNIAFGltvlprrdrptaaaiktkvtqllemvqlahladrfpaqLSGGQKQRVALARALAVEPQIL 158
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-222 |
4.12e-78 |
|
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: 239.71 E-value: 4.12e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE-----RKVG 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 78 FVFQHYALFRHMTVFDNIAFGL---TVLPRRDrptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVE 154
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLrehTRLSEEE------IREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPD 222
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-224 |
6.15e-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: 239.16 E-value: 6.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQH--YALFrH 88
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQNpdDQLF-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 89 MTVFDNIAFGLTVLPRrdrpTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:COG1122 91 PTVEEDVAFGPENLGL----PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 169 AQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRV 224
Cdd:COG1122 167 PRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-228 |
3.54e-77 |
|
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: 246.35 E-value: 3.54e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF-----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE---- 73
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 74 -RKVGFVFQH--YALFRHMTVFDNIAFGLTVLPRRDRptaAAIKTKVTQLLEMVQL-AHLADRFPAQLSGGQKQRVALAR 149
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSR---AERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREP 228
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-215 |
2.13e-76 |
|
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: 234.35 E-value: 2.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVS----RLHARERKVGF 78
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHMTVFDNIAFGLTVLprRDRPTAAAIKTkVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQIL 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKV--KGMSKAEAEER-ALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 159 LLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-248 |
1.37e-75 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 238.20 E-value: 1.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQH 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAFGLtvlpRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:PRK11607 100 YALFPHMTVEQNIAFGL----KQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMGEVNR 242
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
|
....*.
gi 17865703 243 LTGTVR 248
Cdd:PRK11607 256 FEGVLK 261
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-310 |
3.00e-74 |
|
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: 233.84 E-value: 3.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIaRIKKSFGRTQVlnDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGT---DVSRLH---ARER 74
Cdd:COG4148 1 MMLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARGIflpPHRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 75 KVGFVFQHYALFRHMTVFDNIAFGLTVLPRRDRPTAAAiktkvtQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVE 154
Cdd:COG4148 78 RIGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRISFD------EVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVL 234
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 235 EFMGEVNRLTGTVR--------------GGQFHVGAHRWPLGytpayqGPVDLFLRPWEVDISRR----TSLDSPLPVQV 296
Cdd:COG4148 232 GGEEAGSVLEATVAahdpdygltrlalgGGRLWVPRLDLPPG------TRVRVRIRARDVSLALEppegSSILNILPGRV 305
|
330
....*....|....
gi 17865703 297 IEASPKGHYTQLVV 310
Cdd:COG4148 306 VEIEPADGGQVLVR 319
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-240 |
3.16e-74 |
|
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: 3.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE----- 73
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 74 RKVGFVFQHYALFRHMTVFDNIAFGLTV--LPRrdrptaAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARAL 151
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIagVPK------AEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI-EQADAPDrVWREPAT 230
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIvEQGPVLD-VFANPQS 234
|
250
....*....|
gi 17865703 231 RFVLEFMGEV 240
Cdd:COG1135 235 ELTRRFLPTV 244
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-238 |
1.96e-73 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 232.23 E-value: 1.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 2 SIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQ 81
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRHMTVFDNIAFGLTvLPRRDRptaAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLD 161
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLK-LAGAKK---EEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMG 238
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIG 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-244 |
7.27e-73 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 227.53 E-value: 7.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE------RKVGFVFQ 81
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRHMTVFDNIAFGLTV--LPRRDRPTAAAiktkvtQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILL 159
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVqgVPRAEREERAA------EALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMGE 239
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
....*
gi 17865703 240 VNRLT 244
Cdd:cd03294 264 VDRAK 268
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-222 |
8.60e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 226.10 E-value: 8.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERK-VGFVFQ 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRHMTVFDNIAF--GLTVLPRRDRptaaaiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILL 159
Cdd:COG1131 81 EPALYPDLTVRENLRFfaRLYGLPRKEA------RERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPD 222
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGK-TVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-219 |
3.81e-72 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 223.71 E-value: 3.81e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 20 DISLDIPsGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGT--DVSR----LHARERKVGFVFQHYALFRHMTVFD 93
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRkkinLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 94 NIAFGLTVLPRRDRptaaaiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
Cdd:cd03297 95 NLAFGLKRKRNRED------RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17865703 174 ELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQAD 219
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-216 |
1.85e-71 |
|
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: 1.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE----- 73
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 74 RKVGFVFQHYALFRHMTVFDNIAFGLTV--LPRrdrptaAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARAL 151
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIagVPK------AEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIE 216
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
13-213 |
4.30e-71 |
|
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: 220.80 E-value: 4.30e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQH--YALFRH 88
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVFQNpdDQFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 89 mTVFDNIAFGltvlPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:cd03225 92 -TVEEEVAFG----LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17865703 169 AQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:cd03225 167 PAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-231 |
1.21e-69 |
|
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: 218.52 E-value: 1.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKV 76
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQHY--ALFRHMTVFDNIAFGLTVLPRRDRptaaaiKTKVTQLLEMVQL-AHLADRFPAQLSGGQKQRVALARALAV 153
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDR------EERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIE---QADAPDRVWREPAT 230
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVeelTVADLLAGPKHPYT 235
|
.
gi 17865703 231 R 231
Cdd:COG1124 236 R 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-220 |
2.20e-69 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 216.84 E-value: 2.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE-----RKV 76
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQHYALFRHMTVFDNIAFGLTVLPRRDRptaaAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQ 156
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRK----EIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865703 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNIEQADA 220
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGT-TVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-218 |
9.22e-69 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 215.45 E-value: 9.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHA-----RE 73
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrkiRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 74 RKVGFVFQHY--ALFRHMTVFDNIAFGLTVlpRRDRPTAAAIKTKVTQLLEMVQL-AHLADRFPAQLSGGQKQRVALARA 150
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRI--HGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI-EQA 218
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIvEEG 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
21-223 |
1.40e-68 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 215.00 E-value: 1.40e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQHYALFRHMTVFDNIAFGLT 100
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 101 vlPRRdRPTAAAiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLR 180
Cdd:COG3840 98 --PGL-KLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17865703 181 QLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDR 223
Cdd:COG3840 174 ELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-224 |
7.10e-68 |
|
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: 214.14 E-value: 7.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVF 80
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 QHYALFRHMTVFDNIAFGLTV-LPRRDRPTAAAIKtKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILL 159
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRYPhLGLFGRPSAEDRE-AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRV 224
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-240 |
4.46e-66 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 209.18 E-value: 4.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKV----GF 78
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHMTVFDNIAFGltvlPRRDRPTA-AAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQI 157
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFG----PLRVRGASkEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFM 237
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
...
gi 17865703 238 GEV 240
Cdd:PRK09493 237 QHV 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-240 |
1.28e-64 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 208.89 E-value: 1.28e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE----- 73
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 74 RKVGFVFQHYALFRHMTVFDNIAFGLTvLPRRDRptaAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAV 153
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLE-LAGTPK---AEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI-EQADAPDrVWREPATRF 232
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLvEQGTVSE-VFSHPKHPL 236
|
....*...
gi 17865703 233 VLEFMGEV 240
Cdd:PRK11153 237 TREFIQST 244
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-215 |
1.57e-64 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 205.29 E-value: 1.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE-----RKV 76
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQHYALFRHMTVFDNIAFG-----------LTVLPRRDRPTAAAiktkvtqLLEMVQLAHLADRFPAQLSGGQKQRV 145
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGrlgrtstwrslLGLFPPEDRERALE-------ALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-215 |
9.44e-64 |
|
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: 200.70 E-value: 9.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHAR-ERKVGFVFQ 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRHMTVFDNIafgltvlprrdrptaaaiktkvtqllemvqlahladrfpaQLSGGQKQRVALARALAVEPQILLLD 161
Cdd:cd03230 81 EPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17865703 162 EPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGK-TILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-220 |
1.82e-62 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 199.85 E-value: 1.82e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSG--HIRFHGTDVSR-LHARE---- 73
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGqlNIAGHQFDFSQkPSEKAirll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 74 -RKVGFVFQHYALFRHMTVFDNiafgLTVLPRR--DRPTAAAIKtKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARA 150
Cdd:COG4161 81 rQKVGMVFQQYNLWPHLTVMEN----LIEAPCKvlGLSKEQARE-KAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLhEELKFTSVFVTHDQEEATEVADRVVVMSQGNI-EQADA 220
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIiEQGDA 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-220 |
3.05e-62 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 199.47 E-value: 3.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHG--------TDVSRLHAR 72
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 73 ERKVGFVFQHYALFRHMTVFDNiafgLTVLPRR----DRPTAaaiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALA 148
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQN----LIEAPCRvlglSKDQA---LARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLhEELKFTSVFVTHDQEEATEVADRVVVMSQGNI-EQADA 220
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIvEQGDA 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-215 |
2.90e-61 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 196.62 E-value: 2.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSR--LHAReRKVGFVF 80
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKepREAR-RQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 QHYALFRHMTVFDNIAFGLTVLPRRDRptaaAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLL 160
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDE----ELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 161 DEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-213 |
1.78e-60 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 194.92 E-value: 1.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRlhaRERKVGFVFQHYALFRH-- 88
Cdd:COG1121 15 SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIGYVPQRAEVDWDfp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 89 MTVFDNIAFGLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:COG1121 92 ITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17865703 169 AQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:COG1121 172 AATEEALYELLRELRREGK-TILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-213 |
4.49e-60 |
|
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: 194.10 E-value: 4.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 4 EIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARER-KVGFV--F 80
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIArtF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 QHYALFRHMTVFDNIAFGLTVLPR-----------RDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALAR 149
Cdd:COG0411 86 QNPRLFPELTVLENVLVAAHARLGrgllaallrlpRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865703 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFG 229
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-230 |
1.02e-59 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 193.48 E-value: 1.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVS-------RLHARERK 75
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgELVPADRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 76 --------VGFVFQHYALFRHMTVFDNIAFG-LTVLprrDRPTAAAIkTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVA 146
Cdd:COG4598 89 qlqrirtrLGMVFQSFNLWSHMTVLENVIEApVHVL---GRPKAEAI-ERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWR 226
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG 243
|
....
gi 17865703 227 EPAT 230
Cdd:COG4598 244 NPKS 247
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-228 |
1.31e-59 |
|
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: 193.82 E-value: 1.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVS-----RLHARERKVGFVFQH--YALFR 87
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDLRKKVGLVFQFpeHQLFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 88 hMTVFDNIAFGltvlPRRDRPTAAAIKTKVTQLLEMVQL-AHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
Cdd:TIGR04521 98 -ETVYKDIAFG----PKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 167 LDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREP 228
Cdd:TIGR04521 173 LDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-236 |
1.55e-59 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 193.15 E-value: 1.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHArERKVgfVFQHYALFRHMTVF 92
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DRGV--VFQKDALLPWLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 93 DNIAFGLTV--LPRRDRPTAAAiktkvtQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
Cdd:COG4525 95 DNVAFGLRLrgVPKAERRARAE------ELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 171 VRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGnieqadaPDRVwrepATRFVLEF 236
Cdd:COG4525 169 TREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG-------PGRI----VERLELDF 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-224 |
1.59e-59 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 191.63 E-value: 1.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ-----SSGHIRFHGTDV-----SRLHAR 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydldvDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 73 eRKVGFVFQHYALFRhMTVFDNIAFGLTVLPRRDRptaAAIKTKVTQLLEMVQL-AHLADRFPA-QLSGGQKQRVALARA 150
Cdd:cd03260 81 -RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLK---EELDERVEEALRKAALwDEVKDRLHAlGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865703 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRV 224
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-229 |
1.68e-59 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 200.13 E-value: 1.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 2 SIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL---EHQSSGHIRFHGTDVSRLHARER--KV 76
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRgrRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQHY-ALFRHMTVFDNIAFGLtvlpRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEP 155
Cdd:COG1123 86 GMVFQDPmTQLNPVTVGDQIAEAL----ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865703 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPA 229
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-215 |
4.05e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 190.03 E-value: 4.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVF 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 QHYALFrHMTVFDNIAFGLTVLPRRDRPTaaaiktKVTQLLEMVQLAH-LADRFPAQLSGGQKQRVALARALAVEPQILL 159
Cdd:COG4619 81 QEPALW-GGTVRDNLPFPFQLRERKFDRE------RALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-223 |
4.41e-59 |
|
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: 190.72 E-value: 4.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL------HAR 72
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedaraRLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 73 ERKVGFVFQHYALFRHMTVFDNIAfglTVLPRRDRPTAAAiktKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALA 152
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTALENVM---LPLELAGRRDARA---RARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAtEVADRVVVMSQGNIEQADAPDR 223
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDTAATA 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-224 |
2.33e-57 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 187.64 E-value: 2.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF--GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV---SRLHARERKVG 77
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 78 FVFQH-----YAlfrhMTVFDNIAFGLTVL--PRRDrptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARA 150
Cdd:TIGR04520 81 MVFQNpdnqfVG----ATVEDDVAFGLENLgvPREE------MRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865703 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEvADRVVVMSQGNIEQADAPDRV 224
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREI 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-229 |
4.92e-57 |
|
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: 185.72 E-value: 4.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERK-VGFV 79
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLppHEIARLgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 FQHYALFRHMTVFDNIAFGL------TVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAV 153
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPA 229
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
13-210 |
6.70e-57 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 184.61 E-value: 6.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-LEH--QSSGHIRFHGTDVSRLHARERKVGFVFQHYALFRHM 89
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPafSASGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 90 TVFDNIAFGL-TVLPRRDRptaaaiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:COG4136 92 SVGENLAFALpPTIGRAQR------RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17865703 169 AQVRKELRRWLRQLHEELKFTSVFVTHDQEEAtEVADRVVVM 210
Cdd:COG4136 166 AALRAQFREFVFEQIRQRGIPALLVTHDEEDA-PAAGRVLDL 206
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-220 |
3.02e-56 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 184.18 E-value: 3.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MS-IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGT--DVSR--------L 69
Cdd:PRK11264 1 MSaIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItiDTARslsqqkglI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 70 HARERKVGFVFQHYALFRHMTVFDNIAFGLTVLPRRDRPTAAAiktKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALAR 149
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATA---RARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNI-EQADA 220
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIvEQGPA 228
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-213 |
6.26e-56 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 182.06 E-value: 6.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE-----RKV 76
Cdd:TIGR02673 2 IEFHNVSKAYPGgVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQHYALFRHMTVFDNIAFGLTVlprrDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQ 156
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEV----RGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 157 ILLLDEPFGALDAQVRKELRRWLRQLHeELKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLN-KRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
5-229 |
1.13e-55 |
|
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: 186.09 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 5 IARIKKSFGRTQVlnDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV--SR----LHARERKVGF 78
Cdd:TIGR02142 2 SARFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdSRkgifLPPEKRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHMTVFDNIAFGLTvlpRRDRPTAAAIKTKVTQLLemvQLAHLADRFPAQLSGGQKQRVALARALAVEPQIL 158
Cdd:TIGR02142 80 VFQEARLFPHLSVRGNLRYGMK---RARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPA 229
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-213 |
1.24e-55 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 181.90 E-value: 1.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRlHARERKVgfVFQHYALFRHMTVFDNIAF 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 98 GL-TVLPRRDRPTAAAIktkVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELR 176
Cdd:TIGR01184 78 AVdRVLPDLSKSERRAI---VEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 17865703 177 RWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-215 |
6.00e-55 |
|
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: 180.46 E-value: 6.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV-----SRLHARERKV 76
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQHYALFRHMTVFDNIAFG-----------LTVLPRRDRPTAAAiktkvtqLLEMVQLAHLADRFPAQLSGGQKQRV 145
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstwrslFGLFPKEEKQRALA-------ALERVGLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-215 |
7.61e-55 |
|
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: 178.01 E-value: 7.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVfqhyalfrh 88
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYV--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 89 mtvfdniafgltvlprrdrptaaaiktkvTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:cd03214 79 -----------------------------PQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17865703 169 AQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:cd03214 130 IAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-229 |
1.94e-54 |
|
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: 181.40 E-value: 1.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLE---HQSSGHIRFHGTDVSRLHARE-- 73
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 74 ----RKVGFVFQH-Y-ALFRHMTVFDNIAFGLTVLPRRDRptaAAIKTKVTQLLEMVQL---AHLADRFPAQLSGGQKQR 144
Cdd:COG0444 82 kirgREIQMIFQDpMtSLNPVMTVGDQIAEPLRIHGGLSK---AEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 145 VALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI-EQADApDR 223
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIvEEGPV-EE 237
|
....*.
gi 17865703 224 VWREPA 229
Cdd:COG0444 238 LFENPR 243
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-208 |
2.06e-54 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 177.81 E-value: 2.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARER------KVGFVFQ 81
Cdd:TIGR03608 4 ISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKAskfrreKLGYLFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRHMTVFDNIAFGL--TVLPRRDRptaaaiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILL 159
Cdd:TIGR03608 84 NFALIENETVEENLDLGLkyKKLSKKEK------REKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQeEATEVADRVV 208
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDEGK-TIIIVTHDP-EVAKQADRVI 204
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-215 |
3.71e-54 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 179.10 E-value: 3.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 5 IARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSrlHARErKVGFVFQHYA 84
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA--EARE-DTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 85 LFRHMTVFDNIAFGLTvlprrdrptaAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
Cdd:PRK11247 92 LLPWKKVIDNVGLGLK----------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17865703 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-215 |
6.39e-54 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 176.96 E-value: 6.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARerkVGFVFQHYALFRHM- 89
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR---IGYVPQRRSIDRDFp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 90 -TVFDNIAFGLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:cd03235 85 iSVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17865703 169 AQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:cd03235 165 PKTQEDIYELLRELRREGM-TILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-212 |
9.77e-54 |
|
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: 176.13 E-value: 9.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERK-VGFV 79
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 FQHYALFRHMTVFDNIAFGLTVLPRRDRPTAaaiktkVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILL 159
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADREA------IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQlHEELKFTSVFVTHDQEEATevADRVVVMSQ 212
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLELA--AARVLDLGD 204
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-215 |
3.69e-53 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 175.60 E-value: 3.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERK-VG 77
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmHKRARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 78 FVFQHYALFRHMTVFDNIafgLTVLPRRdRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQI 157
Cdd:COG1137 82 YLPQEASIFRKLTVEDNI---LAVLELR-KLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 158 LLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVT-HDQEEATEVADRVVVMSQGNI 215
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHLKE--RGIGVLITdHNVRETLGICDRAYIISEGKV 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-164 |
7.61e-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: 171.68 E-value: 7.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSR--LHARERKVGFVFQHYALFRHMTVFDNI 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 96 AFGLTVLprrdRPTAAAIKTKVTQLLEMVQLAHLADR----FPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
Cdd:pfam00005 81 RLGLLLK----GLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-215 |
2.15e-52 |
|
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: 174.02 E-value: 2.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE-----RKV 76
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQHYALFRHMTVFDNIAFG-----------LTVLPRRDrptaaaiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRV 145
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGrlgykptwrslLGRFSEED-------KERALSALERVGLADKAYQRADQLSGGQQQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-231 |
2.66e-52 |
|
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: 173.11 E-value: 2.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERK-VGFV 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 FQHYALFRHMTVFDNIafgLTVLPRRDRPTaAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILL 159
Cdd:cd03218 81 PQEASIFRKLTVEENI---LAVLEIRGLSK-KEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVT-HDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATR 231
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKD--RGIGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
12-229 |
3.66e-52 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 176.08 E-value: 3.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 12 FGRT----QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE-----RKVGFVFQH 82
Cdd:COG4608 24 FGRTvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 -YA-LFRHMTVFDNIAFGL---TVLPRRDRptaaaiKTKVTQLLEMVQL-AHLADRFPAQLSGGQKQRVALARALAVEPQ 156
Cdd:COG4608 104 pYAsLNPRMTVGDIIAEPLrihGLASKAER------RERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865703 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI-EQADApDRVWREPA 229
Cdd:COG4608 178 LIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIvEIAPR-DELYARPL 250
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-215 |
1.43e-51 |
|
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: 170.48 E-value: 1.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQH 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAFGLTVLPRRDRptaaaiktKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKK--------RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEELKftSVFV-THDQEEATEVADRVVVMSQGNI 215
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGI--TVLIsSHLLSEIQKVADRIGIINKGKL 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-238 |
2.58e-51 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 172.54 E-value: 2.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARI-----KKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVS----RLHA 71
Cdd:PRK13637 1 MSIKIENLthiymEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 72 RERKVGFVFQH--YALFRHmTVFDNIAFGltvlPRRDRPTAAAIKTKVTQLLEMVQLAH--LADRFPAQLSGGQKQRVAL 147
Cdd:PRK13637 81 IRKKVGLVFQYpeYQLFEE-TIEKDIAFG----PINLGLSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWRE 227
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
250
....*....|.
gi 17865703 228 PATrfvLEFMG 238
Cdd:PRK13637 236 VET---LESIG 243
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-215 |
4.16e-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: 169.81 E-value: 4.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE----- 73
Cdd:TIGR02982 2 ISIRNLNHYYGhgslRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQlvqlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 74 RKVGFVFQHYALFRHMTVFDNIAFGLTVLPRRdrpTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAV 153
Cdd:TIGR02982 82 RRIGYIFQAHNLLGFLTARQNVQMALELQPNL---SYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVH 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQeEATEVADRVVVMSQGNI 215
Cdd:TIGR02982 159 HPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDN-RILDVADRILQMEDGKL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-213 |
6.08e-51 |
|
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: 167.04 E-value: 6.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 4 EIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSR--LHARERKVGFVFQ 81
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlpLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 hyalfrhmtvfdniafgltvlprrdrptaaaiktkvtqllemvqlahladrfpaqLSGGQKQRVALARALAVEPQILLLD 161
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17865703 162 EPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-213 |
1.29e-50 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 169.88 E-value: 1.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHArERkvGFVFQH 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-ER--GVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAFGLTV--LPRRDRPTAAAiktkvtQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLL 160
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLagVEKMQRLEIAH------QMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17865703 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-215 |
1.82e-50 |
|
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: 168.06 E-value: 1.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVlnDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQH 82
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAFGLTvlPR-RDRPTAaaiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLD 161
Cdd:cd03298 79 NNLFAHLTVEQNVGLGLS--PGlKLTAED---RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17865703 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
17-224 |
1.33e-49 |
|
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: 176.95 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHYALFrHMTVFDN 94
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SGTIREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGltvlprRDRPTAAAIKtkvtQLLEMVQLAHLADRFP-----------AQLSGGQKQRVALARALAVEPQILLLDEP 163
Cdd:COG2274 569 ITLG------DPDATDEEII----EAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 164 FGALDAQVRKELRRWLRQLHEELkfTSVFVTHDqEEATEVADRVVVMSQGNIEQADAPDRV 224
Cdd:COG2274 639 TSALDAETEAIILENLRRLLKGR--TVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-215 |
1.90e-49 |
|
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: 165.27 E-value: 1.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE-----RKV 76
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQHYALFRHMTVFDNIAFGLTVL--PRRDrptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVE 154
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTgvPPRE------IRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-217 |
2.44e-49 |
|
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: 165.03 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 22 SLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQHYALFRHMTVFDNIAFGLtv 101
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 102 lprrdRPT---AAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRW 178
Cdd:TIGR01277 96 -----HPGlklNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 17865703 179 LRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQ 217
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKV 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-215 |
1.10e-48 |
|
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: 164.49 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSG---HI---RFHGTDVSRLHareRKV 76
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLfgeRRGGEDVWELR---KRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFV--FQHYALFRHMTVFDNIAFGLT-VLPRRDRPTAAAIKtKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAV 153
Cdd:COG1119 81 GLVspALQLRFPRDETVLDVVLSGFFdSIGLYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
8-243 |
1.20e-48 |
|
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: 163.98 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERK-VGFVFQHYA 84
Cdd:TIGR04406 7 LIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpmHERARLgIGYLPQEAS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 85 LFRHMTVFDNIafgLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
Cdd:TIGR04406 87 IFRKLTVEENI---MAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 165 GALDAQVRKELRRWLRQLHEelKFTSVFVT-HDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVleFMGEVNRL 243
Cdd:TIGR04406 164 AGVDPIAVGDIKKIIKHLKE--RGIGVLITdHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRV--YLGEQFRL 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-213 |
2.38e-48 |
|
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: 161.01 E-value: 2.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERKVGFVFQHYALFrHMTVFD 93
Cdd:cd03228 16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLdlESLRKNIAYVPQDPFLF-SGTIRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 94 NIafgltvlprrdrptaaaiktkvtqllemvqlahladrfpaqLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
Cdd:cd03228 95 NI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17865703 174 ELRRWLRQLHEELkfTSVFVTHDqEEATEVADRVVVMSQG 213
Cdd:cd03228 134 LILEALRALAKGK--TVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-219 |
3.83e-48 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 163.28 E-value: 3.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLR-------IIAGLEHqsSGHIRFHGTDVsrlHARE-------RKVG 77
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGEDI---YDPDvdvvelrRRVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 78 FVFQHYALFRhMTVFDNIAFGLTVLPRRDRPTAAAIktkVTQLLEMVQL-AHLADRF--PAQ-LSGGQKQRVALARALAV 153
Cdd:COG1117 96 MVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEI---VEESLRKAALwDEVKDRLkkSALgLSGGQQQRLCIARALAV 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 154 EPQILLLDEPFGALD----AQVrkElrrwlrQLHEELK--FTSVFVTHDQEEATEVADRVVVMSQGN-IEQAD 219
Cdd:COG1117 172 EPEVLLMDEPTSALDpistAKI--E------ELILELKkdYTIVIVTHNMQQAARVSDYTAFFYLGElVEFGP 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-227 |
4.32e-48 |
|
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: 161.83 E-value: 4.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERK-VGFVFQHYALFRHM 89
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLppHERARAgIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 90 TVFDNIAFGLTVLPRRDRPTaaaiktkvtqllemvQLAHLADRFPA----------QLSGGQKQRVALARALAVEPQILL 159
Cdd:cd03224 91 TVEENLLLGAYARRRAKRKA---------------RLERVYELFPRlkerrkqlagTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWRE 227
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-215 |
5.37e-48 |
|
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: 161.27 E-value: 5.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 4 EIARIKKSFGR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRlHARERKVGFVFQH 82
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 --YALFRHmTVFDNIAFGLtvlprrdrPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLL 160
Cdd:cd03226 80 vdYQLFTD-SVREELLLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 161 DEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-215 |
1.32e-47 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 161.29 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 22 SLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQHYALFRHMTVFDNIAFGLTV 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 102 LPRRDrptaAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQ 181
Cdd:PRK10771 99 GLKLN----AAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190
....*....|....*....|....*....|....
gi 17865703 182 LHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-230 |
3.03e-47 |
|
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: 167.94 E-value: 3.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 8 IKKS-FGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLeHQSSGHIRFHGTDVSRLHARE-----RKVG 77
Cdd:COG4172 287 IKRGlFRRTVghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAlrplrRRMQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 78 FVFQH-YALF--RhMTVFDNIAFGLTVLprRDRPTAAAIKTKVTQLLEMVQL-AHLADRFPAQLSGGQKQRVALARALAV 153
Cdd:COG4172 366 VVFQDpFGSLspR-MTVGQIIAEGLRVH--GPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI-EQADApDRVWREPAT 230
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVvEQGPT-EQVFDAPQH 519
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
8-231 |
7.56e-47 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 162.74 E-value: 7.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 8 IKKSFGRTQVlnDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGT---DVSR---LHARERKVGFVFQ 81
Cdd:PRK11144 6 FKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgicLPPEKRRIGYVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRHMTVFDNIAFGLtvlprrdRPTAAAIKTKVTQLLemvQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLD 161
Cdd:PRK11144 84 DARLFPHYKVRGNLRYGM-------AKSMVAQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATR 231
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-215 |
2.00e-46 |
|
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: 157.35 E-value: 2.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGqMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERK-VGFVFQ 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRHMTVFDNIAFgLTVLPRRDRPTAaaiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLD 161
Cdd:cd03264 80 EFGVYPNFTVREFLDY-IAWLKGIPSKEV---KARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17865703 162 EPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-217 |
2.95e-46 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 166.11 E-value: 2.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHYALFrHMT 90
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAFGltvlprrdRPTAAaiKTKVTQLLEMVQLAHLADRFP-----------AQLSGGQKQRVALARALAVEPQILL 159
Cdd:COG1132 430 IRENIRYG--------RPDAT--DEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTH------DqeeatevADRVVVMSQGNIEQ 217
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLMKGR--TTIVIAHrlstirN-------ADRILVLDDGRIVE 554
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-222 |
3.10e-46 |
|
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: 157.15 E-value: 3.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRlHARE--RKVGFVF 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREvrRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 QHYALFRHMTVFDNIAF--GLTVLPRRDRptaaaiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQIL 158
Cdd:cd03265 80 QDLSVDDELTGWENLYIhaRLYGVPGAER------RERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865703 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPD 222
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-215 |
3.32e-46 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 156.90 E-value: 3.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV-SRLHARERKVGFV 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 FQHYALFRHMTVFDNIAF--GLTVLPRRDrptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQI 157
Cdd:cd03263 81 PQFDALFDELTVREHLRFyaRLKGLPKSE------IKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 158 LLLDEPFGALDAQVRKELrrWlRQLHEELKFTSV-FVTHDQEEATEVADRVVVMSQGNI 215
Cdd:cd03263 155 LLLDEPTSGLDPASRRAI--W-DLILEVRKGRSIiLTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-224 |
4.92e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 158.23 E-value: 4.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGR--TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGF 78
Cdd:PRK13632 8 IKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHY-ALFRHMTVFDNIAFGL--TVLPRRDrptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEP 155
Cdd:PRK13632 88 IFQNPdNQFIGATVEDDIAFGLenKKVPPKK------MKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATeVADRVVVMSQGNIEQADAPDRV 224
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-224 |
8.41e-46 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 157.20 E-value: 8.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVF 80
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 QHYALFRHMTVFDNIAFGLTVLPRRDRPTAAAIKtkvtQLLEMVQLAHLADRFPAQLSGGQKQRVALARALA-------V 153
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVR----EALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 154 EPQILLLDEPFGALD----AQVRKELRRWLRQlheelKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRV 224
Cdd:COG4559 158 GPRWLFLDEPTSALDlahqHAVLRLARQLARR-----GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-224 |
1.06e-45 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 156.86 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGF 78
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHMTVFDNIAFGLTVLPRRDRPTAAAiktkVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALA------ 152
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDAL----VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRV 224
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEV 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-228 |
1.11e-45 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 156.78 E-value: 1.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVF 80
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 QHYALFRHMTVFDNIAFGltvlpR----RDRPTAAAiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQ 156
Cdd:COG4604 82 QENHINSRLTVRELVAFG-----RfpysKGRLTAED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREP 228
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-215 |
1.35e-45 |
|
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: 155.59 E-value: 1.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARER---- 74
Cdd:TIGR02211 2 LKCENLGKRYQEgkldTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 75 --KVGFVFQHYALFRHMTVFDNIAfgLTVLPRRDRPTAAaiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALA 152
Cdd:TIGR02211 82 nkKLGFIYQFHHLLPDFTALENVA--MPLLIGKKSVKEA--KERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAtEVADRVVVMSQGNI 215
Cdd:TIGR02211 158 NQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELA-KKLDRVLEMKDGQL 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
13-235 |
1.85e-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: 156.50 E-value: 1.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERK-----VGFVFQ--HYAL 85
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRafrrdVQLVFQdsPSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 86 FRHMTVFDNIAFGLTVLPRRDrptAAAIKTKVTQLLEMVQL-AHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
Cdd:TIGR02769 102 NPRMTVRQIIGEPLRHLTSLD---ESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI--EQADAPDRVWREPATRFVLE 235
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIveECDVAQLLSFKHPAGRNLQS 251
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-215 |
2.65e-45 |
|
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: 155.14 E-value: 2.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERK-VGFVFQHYALFRHM 89
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLppHRIARLgIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 90 TVFDNIAFGLtvLPRRDRPTAAAIktkvtqlLEMVqlahlADRFP----------AQLSGGQKQRVALARALAVEPQILL 159
Cdd:COG0410 94 TVEENLLLGA--YARRDRAEVRAD-------LERV-----YELFPrlkerrrqraGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRI 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-241 |
4.74e-45 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 159.43 E-value: 4.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 8 IKKSFGRTQVLN---------DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL------HAR 72
Cdd:PRK10070 25 IEQGLSKEQILEktglslgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelrEVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 73 ERKVGFVFQHYALFRHMTVFDNIAFGLTV--LPRRDRptaaaiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARA 150
Cdd:PRK10070 105 RKKIAMVFQSFALMPHMTVLDNTAFGMELagINAEER------REKALDALRQVGLENYAHSYPDELSGGMRQRVGLARA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPAT 230
Cdd:PRK10070 179 LAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
250
....*....|.
gi 17865703 231 RFVLEFMGEVN 241
Cdd:PRK10070 259 DYVRTFFRGVD 269
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-222 |
1.05e-44 |
|
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: 161.46 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHYALFrHMT 90
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWVPQNPYLF-AGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAFGltvlprRDRPTAAAIKtkvtQLLEMVQLAHLADRFP-----------AQLSGGQKQRVALARALAVEPQILL 159
Cdd:COG4988 427 IRENLRLG------RPDASDEELE----AALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEATEvADRVVVMSQGNIEQADAPD 222
Cdd:COG4988 497 LDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIVEQGTHE 556
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-242 |
2.51e-44 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 153.25 E-value: 2.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGF 78
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHMTVFDNIAFG----LTV---LPRRDRptaaaikTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARAL 151
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGrspwLSLwgrLSAEDN-------ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATR 231
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLR 232
|
250
....*....|.
gi 17865703 232 FVLEFMGEVNR 242
Cdd:PRK11231 233 TVFDVEAEIHP 243
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-215 |
3.41e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 154.11 E-value: 3.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 2 SIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHAreRKVGFVFQ 81
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR--RRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRHMTVFDNIAF-----GLtvlprrdrpTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQ 156
Cdd:COG4152 79 ERGLYPKMKVGEQLVYlarlkGL---------SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAKGT-TVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-222 |
1.17e-43 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 151.84 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV-----SRLHARERKVG 77
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 78 FVFQHYALFRHMTVFDNIAFGL---TVLPrrdrptAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVE 154
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLrehTQLP------APLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRV-VVMSQGNIEQADAPD 222
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAyIVADKKIVAHGSAQA 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
13-231 |
1.57e-43 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 151.76 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERK-----VGFVFQHY--AL 85
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafrrdIQMVFQDSisAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 86 FRHMTVFDNIAFGLTVLPRRDRPTAAAiktKVTQLLEMVQLA-HLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
Cdd:PRK10419 103 NPRKTVREIIREPLRHLLSLDKAERLA---RASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI--EQADAPDRVWREPATR 231
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIveTQPVGDKLTFSSPAGR 248
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-215 |
2.00e-43 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 149.98 E-value: 2.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 4 EIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERK-VGFVF 80
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLppHERARAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 QHYALFRHMTVFDNIAFGLTVLPRRDRPTAAAIKTKVTQLLEMvqlahlADRFPAQLSGGQKQRVALARALAVEPQILLL 160
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVLKEM------LGRRGGDLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-210 |
2.03e-43 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 156.72 E-value: 2.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV---SRLHARERKVGFV 79
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrSPRDAQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 FQHYALFRHMTVFDNIAFGLtvLPRR----DRptaAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEP 155
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGR--EPRRggliDW---RAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVM 210
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGV-AIIYISHRLDEVFEIADRVTVL 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-237 |
2.39e-43 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 150.89 E-value: 2.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVS--------------- 67
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 68 RLHARERKVGFVFQHYALFRHMTVFDNI------AFGLTVLPRRDRPTAAAIKTKVTQLLEmvqlahlaDRFPAQLSGGQ 141
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmeapiqVLGLSKQEARERAVKYLAKVGIDERAQ--------GKYPVHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 142 KQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAP 221
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
250
....*....|....*.
gi 17865703 222 DRVWREPATRFVLEFM 237
Cdd:PRK10619 237 EQLFGNPQSPRLQQFL 252
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-229 |
6.86e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 150.56 E-value: 6.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRF------HGTDVSRLHARERKVGFVFQ--HYALFRHm 89
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKPLRKKVGIVFQfpEHQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 90 TVFDNIAFGltvlPRRDRPTAAAIKTKVTQLLEMVQLAH-LADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:PRK13634 102 TVEKDICFG----PMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 169 AQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPA 229
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-213 |
1.04e-42 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 146.03 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV---SRLHARERKVGFV 79
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVsfaSPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 FqhyalfrhmtvfdniafgltvlprrdrptaaaiktkvtqllemvqlahladrfpaQLSGGQKQRVALARALAVEPQILL 159
Cdd:cd03216 81 Y-------------------------------------------------------QLSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGV-AVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-213 |
1.80e-42 |
|
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: 147.04 E-value: 1.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHarERKVGFVFQH 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA--RNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAF--GLTVLPRRDrptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLL 160
Cdd:cd03269 79 RGLYPKMKVIDQLVYlaQLKGLKKEE------ARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17865703 161 DEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-215 |
8.13e-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: 145.59 E-value: 8.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSR--LHAReRKV 76
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepAEAR-RRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQHYALFRHMTVFDNIAF--GLTVLPRRdrptaaAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVE 154
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYfaGLYGLKGD------ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-222 |
4.09e-41 |
|
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: 151.84 E-value: 4.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHYALFrHMT 90
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQRPHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAFGltvlprrdRPTAAaiKTKVTQLLEMVQLAHLADRFP-----------AQLSGGQKQRVALARALAVEPQILL 159
Cdd:COG4987 425 LRENLRLA--------RPDAT--DEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865703 160 LDEPFGALDAQVRKELrrwLRQLHEELK-FTSVFVTHDQEEAtEVADRVVVMSQGNIEQADAPD 222
Cdd:COG4987 495 LDEPTEGLDAATEQAL---LADLLEALAgRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHE 554
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-213 |
8.37e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 149.79 E-value: 8.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV---SRLHARERKVGFV 79
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirSPRDAIALGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 FQHYALFRHMTVFDNIAFGLTVLPRRDRPTAAAIKtkvtqllemvQLAHLADRFP---------AQLSGGQKQRVALARA 150
Cdd:COG3845 86 HQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARA----------RIRELSERYGldvdpdakvEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAEGK-SIIFITHKLREVMAIADRVTVLRRG 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-226 |
3.82e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 143.23 E-value: 3.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHY-ALFRHMTV 91
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGMVFQNPdNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 92 FDNIAFGL--TVLPRRDrptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
Cdd:PRK13635 100 QDDVAFGLenIGVPREE------MVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 170 QVRKELRRWLRQLHEELKFTSVFVTHDQEEATEvADRVVVMSQGNIEQADAPDRVWR 226
Cdd:PRK13635 174 RGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-221 |
7.51e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 142.18 E-value: 7.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVG 77
Cdd:PRK13650 5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDirHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 78 FVFQHY-ALFRHMTVFDNIAFGLTV--LPRRDrptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVE 154
Cdd:PRK13650 85 MVFQNPdNQFVGATVEDDVAFGLENkgIPHEE------MKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATeVADRVVVMSQGNIEQADAP 221
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTP 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-225 |
1.29e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 141.43 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE-RK-VGFVFQH-YALFRHMTVFDN 94
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlRKhIGIVFQNpDNQFVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGLT--VLPRRDrptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVR 172
Cdd:PRK13648 105 VAFGLEnhAVPYDE------MHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17865703 173 KELRRWLRQLHEELKFTSVFVTHDQEEATEvADRVVVMSQGNIEQADAPDRVW 225
Cdd:PRK13648 179 QNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-229 |
1.98e-39 |
|
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: 146.75 E-value: 1.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 7 RIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKT----TLLRIIAGLEHQSSGHIRFHGTDVSRLHARE------RKV 76
Cdd:COG4172 15 AFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQH--YALFRHMTVFDNIAfglTVLPRRDRPTAAAIKTKVTQLLEMVQL---AHLADRFPAQLSGGQKQRVALARAL 151
Cdd:COG4172 95 AMIFQEpmTSLNPLHTIGKQIA---EVLRLHRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI-EQADApDRVWREPA 229
Cdd:COG4172 172 ANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIvEQGPT-AELFAAPQ 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-243 |
7.09e-39 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 138.49 E-value: 7.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIAR-IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVS--RLHARERK-V 76
Cdd:PRK10895 1 MATLTAKnLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQHYALFRHMTVFDNIafgLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQ 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNL---MAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 157 ILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVT-HDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVle 235
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRD--SGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV-- 233
|
....*...
gi 17865703 236 FMGEVNRL 243
Cdd:PRK10895 234 YLGEDFRL 241
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-228 |
1.14e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 139.16 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL---EHQSSGHIRFHGTDVSR---LHARErKVGFVFQHY-ALFRHM 89
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAktvWDIRE-KVGIVFQNPdNQFVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 90 TVFDNIAFGLTvlpRRDRPTAAAIKTkVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
Cdd:PRK13640 101 TVGDDVAFGLE---NRAVPRPEMIKI-VRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 170 QVRKELRRWLRQLHEELKFTSVFVTHDQEEAtEVADRVVVMSQGNIEQADAPDRVWREP 228
Cdd:PRK13640 177 AGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-229 |
3.40e-38 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 144.48 E-value: 3.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHA------R 72
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalaqlR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 73 ERKVGFVFQHYALFRHMTVFDNIAF-----GLTVLPRRDRPTAaaiktkvtqLLEMVQLAHLADRFPAQLSGGQKQRVAL 147
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVpavyaGLERKQRLLRAQE---------LLQRLGLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEvADRVVVMSQGNIeQADAPDRVWRE 227
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEI-VRNPPAQEKVN 232
|
..
gi 17865703 228 PA 229
Cdd:PRK10535 233 VA 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-213 |
7.08e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 136.79 E-value: 7.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHY--ALFRhMT 90
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGLVFQDPddQVFS-ST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAFGltvlPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
Cdd:PRK13647 97 VWDDVAFG----PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17865703 171 VRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:PRK13647 173 GQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-228 |
1.39e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 136.47 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHY--ALFRh 88
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLVFQNPddQIFS- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 89 MTVFDNIAFGLTVLPRRDrptaAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:PRK13652 94 PTVEQDIAFGPINLGLDE----ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 169 AQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREP 228
Cdd:PRK13652 170 PQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-210 |
1.92e-37 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 133.13 E-value: 1.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRfhgtdvsrlHARERKVGFVFQHYALFRHM- 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR---------RAGGARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 90 -TVFDNIAFGLtvLPRRD--RPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
Cdd:NF040873 72 lTVRDLVAMGR--WARRGlwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17865703 167 LDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEvADRVVVM 210
Cdd:NF040873 150 LDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-215 |
2.10e-37 |
|
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: 134.25 E-value: 2.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHYALFrHMTVFDN 94
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQDVTLF-YGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGLTvlprrdrptaAAIKTKVTQLLEMVQLAHLADRFP-----------AQLSGGQKQRVALARALAVEPQILLLDEP 163
Cdd:cd03245 98 ITLGAP----------LADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 164 FGALD----AQVRKELRRWLRQLheelkfTSVFVTHDQeEATEVADRVVVMSQGNI 215
Cdd:cd03245 168 TSAMDmnseERLKERLRQLLGDK------TLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
16-215 |
2.28e-37 |
|
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: 134.28 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSR--LHARERKVGFVFQHYALFrHMTVFD 93
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtLDSLRRAIGVVPQDTVLF-NDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 94 NIAFGltvlprrdRPTAAAIktkvtQLLEMVQLAHLAD---RFPAQ-----------LSGGQKQRVALARALAVEPQILL 159
Cdd:cd03253 94 NIRYG--------RPDATDE-----EVIEAAKAAQIHDkimRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEATEvADRVVVMSQGNI 215
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-218 |
5.19e-37 |
|
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: 133.51 E-value: 5.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVS--RLHARERKVGFVFQHYALFrHMTVFDN 94
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASLRRQIGLVSQDVFLF-NDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGltvlprRDRPTAAAIktkvtqlLEMVQLAHLAD---RFP-----------AQLSGGQKQRVALARALAVEPQILLL 160
Cdd:cd03251 96 IAYG------RPGATREEV-------EEAARAANAHEfimELPegydtvigergVKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 161 DEPFGALDAQVRKELRRWLRQLheeLKFTSVFVTHDQEEATEVADRVVVMSQGNIEQA 218
Cdd:cd03251 163 DEATSALDTESERLVQAALERL---MKNRTTFVIAHRLSTIENADRIVVLEDGKIVER 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
9-215 |
9.59e-37 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 132.31 E-value: 9.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 9 KKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE-----RKVGFVFQHY 83
Cdd:PRK10908 9 KAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 84 ALFRHMTVFDNIAFGLTVlprrDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEP 163
Cdd:PRK10908 89 HLLMDRTVYDNVAIPLII----AGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 164 FGALDAQVRKELRRwlrqLHEELKFTSVFV---THDQEEATEVADRVVVMSQGNI 215
Cdd:PRK10908 165 TGNLDDALSEGILR----LFEEFNRVGVTVlmaTHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-215 |
1.33e-36 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 133.21 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL---EHQSSGHIRFHGTDVSRLHARERKV--- 76
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIrks 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 ----GFVFQHYALFRHMTVFDNI---AFGLTVLPRRD-RPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALA 148
Cdd:PRK09984 85 rantGYIFQQFNLVNRLSVLENVligALGSTPFWRTCfSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-228 |
1.49e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 132.73 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-----EHQSSGHIRFHGTDVSRLHARE--RK 75
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIElrRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 76 VGFVFQHYALFRHMTVFDNIAFGLTVlpRRDRPTAAAIKTKVTQLLEMVQL-AHLADRFPA---QLSGGQKQRVALARAL 151
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKL--NRLVKSKKELQERVRWALEKAQLwDEVKDRLDApagKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREP 228
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-228 |
1.69e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 132.66 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 2 SIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-----EHQSSGHIRFHG-----TDVSRLHA 71
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGrniysPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 72 ReRKVGFVFQHYALFRHMTVFDNIAFGLT----VLPRRDRPTAAAIKTKVTQLLEMVQlAHLADrFPAQLSGGQKQRVAL 147
Cdd:PRK14267 84 R-REVGMVFQYPNPFPHLTIYDNVAIGVKlnglVKSKKELDERVEWALKKAALWDEVK-DRLND-YPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWRE 227
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
.
gi 17865703 228 P 228
Cdd:PRK14267 239 P 239
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-200 |
3.59e-36 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 131.05 E-value: 3.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHA------R 72
Cdd:PRK10584 7 VEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearaklR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 73 ERKVGFVFQHYALFRHMTVFDNIAFGLTVLPRRDRPTaaaiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALA 152
Cdd:PRK10584 87 AKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQS----RNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17865703 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEA 200
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
17-215 |
7.07e-36 |
|
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: 128.49 E-value: 7.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHYALFRHmTVFDN 94
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IafgltvlprrdrptaaaiktkvtqllemvqlahladrfpaqLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKE 174
Cdd:cd03246 96 I-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17865703 175 LRRWLRQLhEELKFTSVFVTHdQEEATEVADRVVVMSQGNI 215
Cdd:cd03246 135 LNQAIAAL-KAAGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
3-215 |
2.38e-35 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 128.67 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSR--LHarerKVGFVF 80
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRkdLH----KIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 QHYALFRHMTVFDNIAFGLTVLPRRDrptaaaikTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLL 160
Cdd:TIGR03740 77 ESPPLYENLTARENLKVHTTLLGLPD--------SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLIL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 161 DEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:TIGR03740 149 DEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-213 |
2.94e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 129.08 E-value: 2.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERK-VGFVFQHYA 84
Cdd:COG4674 16 LTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLdeHEIARLgIGRKFQKPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 85 LFRHMTVFDNIAFGLtvlPRRDRPTA-------AAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQI 157
Cdd:COG4674 96 VFEELTVFENLELAL---KGDRGVFAslfarltAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 158 LLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:COG4674 173 LLLDEPVAGMTDAETERTAELLKSLAG--KHSVVVVEHDMEFVRQIARKVTVLHQG 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-224 |
6.23e-35 |
|
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: 134.49 E-value: 6.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHYALFRHmT 90
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAfgltvlpRRDRPTAAAIktkvtqllemVQLAHLAD------RFP-----------AQLSGGQKQRVALARALAV 153
Cdd:COG4618 422 IAENIA-------RFGDADPEKV----------VAAAKLAGvhemilRLPdgydtrigeggARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQeEATEVADRVVVMSQGNIEQADAPDRV 224
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-213 |
6.27e-35 |
|
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: 127.20 E-value: 6.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTdvsrlharerkVGFVFQhYALFRHMTVFDNIA 96
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQ-EPWIQNGTIRENIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 97 FGLTVLPRRDRptaAAIKtkVTQLLEMVQLahladrFPAQ-----------LSGGQKQRVALARALAVEPQILLLDEPFG 165
Cdd:cd03250 88 FGKPFDEERYE---KVIK--ACALEPDLEI------LPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17865703 166 ALDAQVRKEL-RRWLRQLHEELKfTSVFVTHdQEEATEVADRVVVMSQG 213
Cdd:cd03250 157 AVDAHVGRHIfENCILGLLLNNK-TRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
15-217 |
6.84e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 128.01 E-value: 6.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHA------RERKVGFVFQHYALFRH 88
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 89 MTVFDNIAFGLTVLPRRdrptAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:PRK11629 102 FTALENVAMPLLIGKKK----PAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17865703 169 AQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVaDRVVVMSQGNIEQ 217
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-231 |
6.88e-35 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 131.89 E-value: 6.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGF 78
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHMTVFDNIAFGLTvlPRRDR--PTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQ 156
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGRT--PHRSRfdTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 157 ILLLDEPFGALDA--QVRK-ELrrwLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATR 231
Cdd:PRK09536 160 VLLLDEPTASLDInhQVRTlEL---VRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-213 |
7.01e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 130.72 E-value: 7.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV-SRLHARERKVGFV 79
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 FQHYALFRHMTVFDNiafgLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILL 159
Cdd:PRK13536 120 PQFDNLDLEFTVREN----LLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-215 |
7.31e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 128.66 E-value: 7.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGR-----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERK 75
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 76 VGFVFQHYAL--FRHMTVFDNIA--------FGLTV-LPRRDRptaAAIKTKVTQL---LEmvqlAHLADRFpAQLSGGQ 141
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRgLTKKRR---ELFRELLATLglgLE----NRLDTKV-GLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 142 KQRVALARALAVEPQILLLDEPFGALD---AQVRKELRrwlRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDpktAALVLELT---EKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
17-221 |
1.16e-34 |
|
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: 134.61 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHYALFrHMTVFDN 94
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTLRDN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGltvlprrdrpTAAAIKTKVTQLLEMVQLAHLADRFP-----------AQLSGGQKQRVALARALAVEPQILLLDEP 163
Cdd:TIGR03375 559 IALG----------APYADDEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILLLDEP 628
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 164 FGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQeEATEVADRVVVMSQGNIeQADAP 221
Cdd:TIGR03375 629 TSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRT-SLLDLVDRIIVMDNGRI-VADGP 682
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-215 |
1.52e-34 |
|
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: 126.62 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQS---SGHIRFHGTDVSRLHARERkVGFVFQHYALFRHMTVF 92
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 93 DNIAFglTVLPRRDRPTAAAIKTKVTQLLEMVQLAH--LADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
Cdd:cd03234 100 ETLTY--TAILRLPRKSSDAIRKKRVEDVLLRDLALtrIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17865703 171 VRKELRRWLRQLHEELKFtsVFVTHDQ--EEATEVADRVVVMSQGNI 215
Cdd:cd03234 178 TALNLVSTLSQLARRNRI--VILTIHQprSDLFRLFDRILLLSSGEI 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-236 |
2.25e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 128.02 E-value: 2.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFG-----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHG------TDVSRL 69
Cdd:PRK13641 1 MSIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpeTGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 70 HARERKVGFVFQ--HYALFRHmTVFDNIAFGltvlPRRDRPTAAAIKTKVTQLLEMVQLAH-LADRFPAQLSGGQKQRVA 146
Cdd:PRK13641 81 KKLRKKVSLVFQfpEAQLFEN-TVLKDVEFG----PKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQlHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAP----- 221
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKD-YQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPkeifs 234
|
250 260
....*....|....*....|..
gi 17865703 222 DRVW------REPAT-RFVLEF 236
Cdd:PRK13641 235 DKEWlkkhylDEPATsRFASKL 256
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
2.86e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 128.28 E-value: 2.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRT-----QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE-- 73
Cdd:PRK13651 1 MQIKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 74 ------------------------RKVGFVFQ--HYALFRHmTVFDNIAFGltvlPRRDRPTAAAIKTKVTQLLEMVQL- 126
Cdd:PRK13651 81 ekvleklviqktrfkkikkikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFG----PVSMGVSKEEAKKRAAKYIELVGLd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 127 AHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADR 206
Cdd:PRK13651 156 ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKR 234
|
....*....
gi 17865703 207 VVVMSQGNI 215
Cdd:PRK13651 235 TIFFKDGKI 243
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-237 |
3.09e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 127.09 E-value: 3.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 5 IARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL------EHQSSGHIRFHGTDVSRLHARE--RKV 76
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKlrKEV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQHYALFRHMTVFDNIAFGLTVLPRRDRptaAAIKTKVTQLLEMVQL-AHLADRF--PA-QLSGGQKQRVALARALA 152
Cdd:PRK14246 93 GMVFQQPNPFPHLSIYDNIAYPLKSHGIKEK---REIKKIVEECLRKVGLwKEVYDRLnsPAsQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRF 232
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
....*
gi 17865703 233 VLEFM 237
Cdd:PRK14246 248 TEKYV 252
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
9-215 |
8.00e-34 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 123.82 E-value: 8.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 9 KKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL--EHQSSGHIRFHGTDVSRLHAReRKVGFVFQHYALF 86
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFR-KIIGYVPQDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 87 RHMTVFDNIAFgltvlprrdrptAAAIKtkvtqllemvqlahladrfpaQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
Cdd:cd03213 95 PTLTVRETLMF------------AAKLR---------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17865703 167 LDA----QVRKELRRwLRQLHEelkfTSVFVTHD-QEEATEVADRVVVMSQGNI 215
Cdd:cd03213 142 LDSssalQVMSLLRR-LADTGR----TIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-215 |
1.19e-33 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 124.75 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTD-VSRLHARERKVGFVF-QHYALFRHMTVFDn 94
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpWKRRKKFLRRIGVVFgQKTQLWWDLPVID- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 iafGLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKE 174
Cdd:cd03267 115 ---SFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17865703 175 LRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-213 |
1.37e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 126.46 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV-SRLHARERKVGFVFQ 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRHMTVFDNiafgLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLD 161
Cdd:PRK13537 88 FDNLDPDFTVREN----LLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17865703 162 EPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-230 |
2.11e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.19 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV-----SRLHAReRKVGFVFQHY--ALFR 87
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkkSLLEVR-KTVGIVFQNPddQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 88 HmTVFDNIAFG-LTV-LPRRDrptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
Cdd:PRK13639 94 P-TVEEDVAFGpLNLgLSKEE------VEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 166 ALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPAT 230
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
7-228 |
2.93e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 124.56 E-value: 2.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 7 RIKKSFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGT-----DVSRlhaRERKVGF 78
Cdd:COG4167 15 KYRTGLFRRQqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygDYKY---RCKHIRM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHyalfrhmtvfDNIAF--GLTVLPRRDRP-------TAAAIKTKVTQLLEMVQL--AHlADRFPAQLSGGQKQRVAL 147
Cdd:COG4167 92 IFQD----------PNTSLnpRLNIGQILEEPlrlntdlTAEEREERIFATLRLVGLlpEH-ANFYPHMLSSGQKQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWRE 227
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
.
gi 17865703 228 P 228
Cdd:COG4167 241 P 241
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-213 |
4.11e-33 |
|
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: 122.93 E-value: 4.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSF------GRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFH----GTDVSR--- 68
Cdd:COG4778 5 LEVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQasp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 69 ---LHARERKVGFVFQHyalfrhmtvfdniafgLTVLPR-----------RDRPTAAAI-KTKVTQLLEMVQLA-HLADR 132
Cdd:COG4778 85 reiLALRRRTIGYVSQF----------------LRVIPRvsaldvvaeplLERGVDREEaRARARELLARLNLPeRLWDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 133 FPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVrkelRRWLRQLHEELK---FTSVFVTHDQEEATEVADRVVV 209
Cdd:COG4778 149 PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAAN----RAVVVELIEEAKargTAIIGIFHDEEVREAVADRVVD 224
|
....
gi 17865703 210 MSQG 213
Cdd:COG4778 225 VTPF 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-219 |
5.23e-33 |
|
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: 122.64 E-value: 5.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLharERKVGFvf 80
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL---GLGGGF-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 qHYALfrhmTVFDNIAFGLTVLPRrdrpTAAAIKTKVTqllEMVQLAHLADRFPAQL---SGGQKQRVALARALAVEPQI 157
Cdd:cd03220 96 -NPEL----TGRENIYLNGRLLGL----SRKEIDEKID---EIIEFSELGDFIDLPVktySSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNIEQAD 219
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-215 |
6.09e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 124.19 E-value: 6.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHG--TDVSR---LHARErKVGFVFQH--YALFR 87
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRkglMKLRE-SVGMVFQDpdNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 88 hMTVFDNIAFGLT--VLPRRDrptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
Cdd:PRK13636 98 -ASVYQDVSFGAVnlKLPEDE------VRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17865703 166 ALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-215 |
1.22e-32 |
|
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: 121.88 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHYALFrHMTVFD 93
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLF-DGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 94 NIAFGltvlpRRDRPTAAAIK-TKVTQLLEMVqlAHLADRFP-------AQLSGGQKQRVALARALAVEPQILLLDEPFG 165
Cdd:cd03249 96 NIRYG-----KPDATDEEVEEaAKKANIHDFI--MSLPDGYDtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17865703 166 ALDAQVRKELRRWLRQLHEElkFTSVFVTHdQEEATEVADRVVVMSQGNI 215
Cdd:cd03249 169 ALDAESEKLVQEALDRAMKG--RTTIVIAH-RLSTIRNADLIAVLQNGQV 215
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-225 |
1.60e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 122.89 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGtdvSRLHAR-----ERKVGFVFQHY-ALFRHMTV 91
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAEnvwnlRRKIGMVFQNPdNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 92 FDNIAFGLTvlpRRDRPTAAAIKtKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
Cdd:PRK13642 100 EDDVAFGME---NQGIPREEMIK-RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17865703 172 RKELRRWLRQLHEELKFTSVFVTHDQEEATEvADRVVVMSQGNIEQADAPDRVW 225
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
13-234 |
1.61e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 123.92 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSR-----LHARERKVGFVFQH-YA-L 85
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpeaQKLLRQKIQIVFQNpYGsL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 86 FRHMTVFDNIAFGL---TVLPRRDRptaaaiKTKVTQLLEMVQL-AHLADRFPAQLSGGQKQRVALARALAVEPQILLLD 161
Cdd:PRK11308 106 NPRKKVGQILEEPLlinTSLSAAER------REKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGN-IEQADApDRVW---REPATRFVL 234
Cdd:PRK11308 180 EPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRcVEKGTK-EQIFnnpRHPYTQALL 255
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
12-239 |
3.37e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 121.25 E-value: 3.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERKvGFV--FQHYALFR 87
Cdd:PRK11300 15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpgHQIARM-GVVrtFQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 88 HMTVFDNIAF------------GLTVLPRRDRPTAAAIkTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEP 155
Cdd:PRK11300 94 EMTVIENLLVaqhqqlktglfsGLLKTPAFRRAESEAL-DRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPatRFVLE 235
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP--DVIKA 250
|
....
gi 17865703 236 FMGE 239
Cdd:PRK11300 251 YLGE 254
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-240 |
3.67e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 121.78 E-value: 3.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSR------LHARERKVGFVFQ--HYALFRHm 89
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkdIKQIRKKVGLVFQfpESQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 90 TVFDNIAFGltvlPRRDRPTAAAIKTKVTQLLEMVQLAH-LADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:PRK13649 102 TVLKDVAFG----PQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 169 AQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREpatrfvLEFMGEV 240
Cdd:PRK13649 178 PKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD------VDFLEEK 242
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-211 |
3.97e-32 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 120.20 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERKVGFVFQHYALFRHmT 90
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLkpEIYRQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAFGLTVlpRRDRPTAAAIKTKVTQLlEMVQlaHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
Cdd:PRK10247 97 VYDNLIFPWQI--RNQQPDPAIFLDDLERF-ALPD--TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17865703 171 VRKELRRWLRQLHEELKFTSVFVTHDQEEATEvADRVVVMS 211
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQ 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-215 |
8.81e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 125.18 E-value: 8.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 5 IARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRfhgtdvsrlHARERKVGFVFQHYA 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS---------IPKGLRIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 85 LFRHMTVFDNIAFGLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQ---------------------------- 136
Cdd:COG0488 72 LDDDLTVLDTVLDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALggweaearaeeilsglgfpeedldrpvs 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 137 -LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQlheeLKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:COG0488 152 eLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN----YPGTVLVVSHDRYFLDRVATRILELDRGKL 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-210 |
1.44e-31 |
|
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: 124.71 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERKVGFVFQHYALFRHmT 90
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAdaDSWRDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAFGltvlpRRDrPTAAAIKTKVTQ--LLEMVQ-----LAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEP 163
Cdd:TIGR02857 412 IAENIRLA-----RPD-ASDAEIREALERagLDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17865703 164 FGALDAQVRKELRRWLRQLHEelKFTSVFVTHDqEEATEVADRVVVM 210
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
13-215 |
1.64e-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: 124.77 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHYALFRHmT 90
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIA-FGLTVLPRRdrPTAAAiktKVTQLLEMVQlahladRFP-----------AQLSGGQKQRVALARALAVEPQIL 158
Cdd:TIGR01842 408 VAENIArFGENADPEK--IIEAA---KLAGVHELIL------RLPdgydtvigpggATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 159 LLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHdQEEATEVADRVVVMSQGNI 215
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRI 531
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-224 |
3.25e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 118.26 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 5 IARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTdVSRLHArerkVGFVFQHya 84
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSALLE----LGAGFHP-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 85 lfrHMTVFDNIAFGLTVL--PRRDrptaaaIKTKVTqllEMVQLAHLADRF--PAQ-LSGGQKQRVALARALAVEPQILL 159
Cdd:COG1134 102 ---ELTGRENIYLNGRLLglSRKE------IDEKFD---EIVEFAELGDFIdqPVKtYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRV 224
Cdd:COG1134 170 VDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-215 |
3.97e-31 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 124.06 E-value: 3.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVS--RLHARERKVGFVFQHYALFRHmTVFDN 94
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdyTLASLRRQVALVSQDVVLFND-TIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGltvlprrdrPTAAAIKTKVTQLLEMVQLAHLADRFP-----------AQLSGGQKQRVALARALAVEPQILLLDEP 163
Cdd:TIGR02203 426 IAYG---------RTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17865703 164 FGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEATEVADRVVVMSQGNI 215
Cdd:TIGR02203 497 TSALDNESERLVQAALERLMQGR--TTLVIAH-RLSTIEKADRIVVMDDGRI 545
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-227 |
4.23e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 119.04 E-value: 4.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVS---RLHARERKVGFVFQH-----YAL 85
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeeNLWDIRNKAGMVFQNpdnqiVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 86 FrhmtVFDNIAFG---LTVLPRRdrptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:PRK13633 102 I----VEEDVAFGpenLGIPPEE-------IRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEvADRVVVMSQGNIEQADAPDRVWRE 227
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-227 |
4.47e-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: 123.37 E-value: 4.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRF----HGTDVSRLHARERK-----VGFVFQHY 83
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRGrakryIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 84 ALFRHMTVFDNI--AFGLTvLPRRDRPTAAAIKTKVTQLLEMvQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLD 161
Cdd:TIGR03269 375 DLYPHRTVLDNLteAIGLE-LPDELARMKAVITLKMVGFDEE-KAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWRE 227
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-229 |
5.24e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.95 E-value: 5.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKK---SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-----EHQSSGHIRFHG-------TD 65
Cdd:PRK14239 1 MTEPILQVSDlsvYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGhniysprTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 66 VSRLharERKVGFVFQHYALFRhMTVFDNIAFGLTVLPRRDRPT----------AAAIKTKVTQLLEMVQLAhladrfpa 135
Cdd:PRK14239 81 TVDL---RKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVldeavekslkGASIWDEVKDRLHDSALG-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 136 qLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PRK14239 149 -LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
250
....*....|....
gi 17865703 216 EQADAPDRVWREPA 229
Cdd:PRK14239 226 IEYNDTKQMFMNPK 239
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-233 |
5.77e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 118.55 E-value: 5.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV---SRLHARERKVGFVFQH-YALFRHMT 90
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfSKLQGIRKLVGIVFQNpETQFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAFGLT--VLPrrdrPTAaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:PRK13644 95 VEEDLAFGPEnlCLP----PIE--IRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 169 AQVRKELRRWLRQLHEELKfTSVFVTHDQEEaTEVADRVVVMSQGNIEQADAPDRVWREPATRFV 233
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGK-TIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-228 |
6.37e-31 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 119.81 E-value: 6.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERK-----VGFVFQH--YALFRHMTV 91
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrsdIQMIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 92 FDNIAFGL-TVLPRRDRptaAAIKTKVTQLLEMVQL-AHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
Cdd:PRK15079 118 GEIIAEPLrTYHPKLSR---QEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 170 QVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREP 228
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-215 |
6.40e-31 |
|
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: 115.61 E-value: 6.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARER---KVGFV---FQHYALFRHMT 90
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAFgltvlprrdrptaaaiktkvtqllemvqlahladrfPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
Cdd:cd03215 95 VAENIAL------------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17865703 171 VRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:cd03215 139 AKAEIYRLIRELADAGK-AVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-224 |
2.99e-30 |
|
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: 121.06 E-value: 2.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLE--HQSSGHIRFH------------------ 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 63 -----------------GTDVSRLHARERKVGFVFQH-YALFRHMTVFDNIafgLTVLPRRDRPTAAAIKtKVTQLLEMV 124
Cdd:TIGR03269 81 pcpvcggtlepeevdfwNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNV---LEALEEIGYEGKEAVG-RAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 125 QLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVA 204
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|
gi 17865703 205 DRVVVMSQGNIEQADAPDRV 224
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEV 256
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-240 |
3.19e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 116.73 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHiRFHGtDV-----SRLHARE-----RKVGFVFQ 81
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-RYSG-DVllggrSIFNYRDvlefrRRVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRhMTVFDNIAFGL---TVLPRRDRPTAAAIKTKVTQLLEMVQlAHLADRfPAQLSGGQKQRVALARALAVEPQIL 158
Cdd:PRK14271 109 RPNPFP-MSIMDNVLAGVrahKLVPRKEFRGVAQARLTEVGLWDAVK-DRLSDS-PFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 159 LLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREP----ATRFVL 234
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPkhaeTARYVA 263
|
....*.
gi 17865703 235 EFMGEV 240
Cdd:PRK14271 264 GLSGDV 269
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-205 |
4.79e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 115.65 E-value: 4.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLR-------IIAGLehQSSGHIRFHGTDV--SRLHARE--RKVGFVF 80
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF--RVEGKVTFHGKNLyaPDVDPVEvrRRIGMVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 QHYALFRHmTVFDNIAFGLTV----------LPRRDRptAAAIKTKVTQLLEMVQLAhladrfpaqLSGGQKQRVALARA 150
Cdd:PRK14243 98 QKPNPFPK-SIYDNIAYGARIngykgdmdelVERSLR--QAALWDEVKDKLKQSGLS---------LSGGQQQRLCIARA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkFTSVFVTHDQEEATEVAD 205
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-227 |
5.81e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 116.37 E-value: 5.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE------RKVGFVFQ--HYALF 86
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrKKVGVVFQfpESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 87 RHmTVFDNIAFGltvlPRRDRPTAAAIKTKVTQLLEMVQLA-HLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
Cdd:PRK13643 99 EE-TVLKDVAFG----PQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 166 ALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWRE 227
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-237 |
6.39e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 120.20 E-value: 6.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTT----LLRIIAglehqSSGHIRFHGTDVSRLHARE-----RKVGF 78
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQ--HYALFRHMTVFDNIAFGLTVlpRRDRPTAAAIKTKVTQLLEMVQL-AHLADRFPAQLSGGQKQRVALARALAVEP 155
Cdd:PRK15134 367 VFQdpNSSLNPRLNVLQIIEEGLRV--HQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGN-IEQADApDRVWREPATRFVL 234
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEvVEQGDC-ERVFAAPQQEYTR 523
|
...
gi 17865703 235 EFM 237
Cdd:PRK15134 524 QLL 526
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-169 |
2.28e-29 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 112.27 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERkvgfvfQHY-----ALFRHMTV 91
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA------CHYlghrnAMKPALTV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 92 FDNIAFGLTVLPRRDRPTAAAiktkvtqlLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
Cdd:PRK13539 91 AENLEFWAAFLGGEELDIAAA--------LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-222 |
2.68e-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: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 20 DISLDIPSGQMVALLGPSGSGKTT----LLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFQHyalfrHMTVFD-- 93
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQN-----PRTAFNpl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 94 -NIAFGLT-VLPRRDRPTAAAiKTKVTQLLEMVQLAH---LADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:TIGR02770 79 fTMGNHAIeTLRSLGKLSKQA-RALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 169 AQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI-EQADAPD 222
Cdd:TIGR02770 158 VVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIvERGTVKE 212
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
9-221 |
4.31e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 113.95 E-value: 4.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 9 KKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGH-------IRFHGTDVSRLHARERKVGFVFQ 81
Cdd:PRK13645 18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaIPANLKKIKEVKRLRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 --HYALFRHmTVFDNIAFGltvlPRRDRPTAAAIKTKVTQLLEMVQLAH-LADRFPAQLSGGQKQRVALARALAVEPQIL 158
Cdd:PRK13645 98 fpEYQLFQE-TIEKDIAFG----PVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAP 221
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-216 |
7.68e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 116.70 E-value: 7.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRfHGTDVsrlharerKVGFVFQH 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETV--------KIGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFR-HMTVFDNIafgltvlpRRDRPTAAaiKTKVTQLLEmvqlahladRF---PAQ-------LSGGQKQRVALARAL 151
Cdd:COG0488 387 QEELDpDKTVLDEL--------RDGAPGGT--EQEVRGYLG---------RFlfsGDDafkpvgvLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 152 AVEPQILLLDEPFGALDAQVRKELrrwlrqlhEEL--KF--TSVFVTHDQEEATEVADRVVVMSQGNIE 216
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEAL--------EEAldDFpgTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-228 |
7.87e-29 |
|
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: 112.23 E-value: 7.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRF-----HGTDVSRLHARERKV- 76
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERRRl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 -----GFVFQHYALFRHMTVFDNIAFGLTVLPRRDRpTAAAIKTKVTQLLEMVQL-AHLADRFPAQLSGGQKQRVALARA 150
Cdd:TIGR02323 84 mrtewGFVHQNPRDGLRMRVSAGANIGERLMAIGAR-HYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREP 228
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-215 |
1.02e-28 |
|
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: 111.16 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERKVGFVFQHYALFRHmTVFD 93
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrKSLRSMIGVVLQDTFLFSG-TIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 94 NIAFGltvlprrdRPTAAaiKTKVTQLLEMVQLAHLADRFP-----------AQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:cd03254 96 NIRLG--------RPNAT--DEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEATEVADRVVVMSQGNI 215
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMK--GRTSIIIAH-RLSTIKNADKILVLDDGKI 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-228 |
1.03e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 111.94 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHG-----TDVSRLHARERKV------ 76
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRllrtew 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQHYALFRHMTVF--DNIAFGLTVLPRRDRptaAAIKTKVTQLLEMVQLAhlADR---FPAQLSGGQKQRVALARAL 151
Cdd:PRK11701 92 GFVHQHPRDGLRMQVSagGNIGERLMAVGARHY---GDIRATAGDWLERVEID--AARiddLPTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREP 228
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDP 243
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-215 |
1.22e-28 |
|
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: 111.02 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHAR--ERKVGFVFQHYALFRHmTVF 92
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 93 DNIAFGLTVLPRrDRPTAAAIKTKVTQLLEMVQLAHL--ADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
Cdd:cd03248 106 DNIAYGLQSCSF-ECVKEAAQKAHAHSFISELASGYDteVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17865703 171 VRKELRRWLRQLHEElkfTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:cd03248 185 SEQQVQQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-213 |
2.44e-28 |
|
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: 107.53 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTdvsrlharerkvgfvfqh 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 yalfrhmtvfdniafgltvlprrdrptaaaiktkvtqllemVQLAHLAdrfpaQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:cd03221 63 -----------------------------------------VKIGYFE-----QLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17865703 163 PFGALDAQVRKELRRWLRqlheELKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:cd03221 97 PTNHLDLESIEALEEALK----EYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-196 |
3.88e-28 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 115.15 E-value: 3.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHYALFrHMTVFDN 94
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQDAHLF-DTTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGltvlprrdRPTAAaiKTKVTQLLEMVQLAHLADRFP-----------AQLSGGQKQRVALARALAVEPQILLLDEP 163
Cdd:TIGR02868 429 LRLA--------RPDAT--DEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|...
gi 17865703 164 FGALDAQVRKELRRWLRQLHEELkfTSVFVTHD 196
Cdd:TIGR02868 499 TEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-215 |
9.30e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 110.95 E-value: 9.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRlhaRE----RKVGFVF-QHYALFRHMTVF 92
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK---RRkefaRRIGVVFgQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 93 DNiafgLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVR 172
Cdd:COG4586 115 DS----FRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17865703 173 KELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:COG4586 191 EAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-229 |
1.50e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 110.33 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSG-----------HIRFHGTDVSRLHAR-------ERKVGF 78
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdKKNNHELITNPYSKKiknfkelRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQ--HYALFRHmTVFDNIAFGltvlprrdrPTAAAI-KTKVTQL----LEMVQLAH-LADRFPAQLSGGQKQRVALARA 150
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFG---------PVALGVkKSEAKKLakfyLNKMGLDDsYLERSPFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPA 229
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-216 |
2.59e-27 |
|
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: 105.86 E-value: 2.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLH-ARERKVGFVFQHYALFrHMTVFD 93
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEkALSSLISVLNQRPYLF-DTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 94 NIAfgltvlprrdrptaaaiktkvtqllemvqlahladrfpAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
Cdd:cd03247 94 NLG--------------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17865703 174 ELrrwLRQLHEELK-FTSVFVTHdQEEATEVADRVVVMSQGNIE 216
Cdd:cd03247 136 QL---LSLIFEVLKdKTLIWITH-HLTGIEHMDKILFLENGKII 175
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-224 |
3.87e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 108.15 E-value: 3.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKK-----SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE-- 73
Cdd:PRK10253 1 MTESVARLRGeqltlGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEva 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 74 RKVGFVFQHYALFRHMTVFDNIAFG----LTVLPRRDRPTAAAiktkVTQLLEMVQLAHLADRFPAQLSGGQKQRVALAR 149
Cdd:PRK10253 81 RRIGLLAQNATTPGDITVQELVARGryphQPLFTRWRKEDEEA----VTKAMQATGITHLADQSVDTLSGGQRQRAWIAM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRV 224
Cdd:PRK10253 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-215 |
4.20e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 111.68 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL---HARERKVGFV 79
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpaKAHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 FQHYALFRHMTVFDNIAFGLtvlprrdrPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILL 159
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGL--------PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 160 LDEPFGALDAQvrkELRRWLRQLHEELK--FTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PRK15439 164 LDEPTASLTPA---ETERLFSRIRELLAqgVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-227 |
6.83e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.94 E-value: 6.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRF------HGTDVSRLHARERKVGFVFQ--HYALFR 87
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVddititHKTKDKYIRPVRKRIGMVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 88 HmTVFDNIAFGltvlPRRDRPTAAAIKTKVTQLLemVQLAHLAD---RFPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
Cdd:PRK13646 101 D-TVEREIIFG----PKNFKMNLDEVKNYAHRLL--MDLGFSRDvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWRE 227
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-205 |
1.05e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 106.66 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 2 SIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-----EHQSSGHIRFHGTDVSR----LHAR 72
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYErrvnLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 73 ERKVGFVFQHYALFRhMTVFDNIAFGLTVLPRRDRPTAAAIKTKVTQLLEMV-QLAHLADRFPAQLSGGQKQRVALARAL 151
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWdEIKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17865703 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVAD 205
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-215 |
2.25e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.72 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 10 KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARER-KVGFVF-----QHY 83
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAiRAGIAYvpedrKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 84 ALFRHMTVFDNIAfgLTVLPRRDRP---TAAAIKTKVTQLLEMVQL-AHLADRFPAQLSGGQKQRVALARALAVEPQILL 159
Cdd:COG1129 340 GLVLDLSIRENIT--LASLDRLSRGgllDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 160 LDEPF-----GAldaqvRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:COG1129 418 LDEPTrgidvGA-----KAEIYRLIRELAAEGK-AVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-227 |
2.58e-26 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 104.88 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHAR--ERKVGFVFQHYALFRHmTVFDN 94
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLFNR-SIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGLTVLPRRDRPTAAAIKTKVTQLLEMVQ-LAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
Cdd:cd03252 96 IALADPGMSMERVIEAAKLAGAHDFISELPEgYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17865703 174 ELrrwLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWRE 227
Cdd:cd03252 176 AI---MRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-170 |
3.92e-26 |
|
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: 103.59 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHA-RERKVGFVFQHYALFRHMTV 91
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDePHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 92 FDNIAFGLTVLPRRDRptaaaiktKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
Cdd:TIGR01189 91 LENLHFWAAIHGGAQR--------TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-213 |
4.06e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 109.10 E-value: 4.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLH---ARERKVGFV 79
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 FQHYALFRHMTVFDNIAFGLtvLPRR-----DRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVE 154
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGR--HLTKkvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-217 |
4.54e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 109.81 E-value: 4.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTllrIIAGLEH---QSSGHIRFHGTDVSRL--HARERKVGFVFQHYALFRHmT 90
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlyqPTGGQVLLDGVPLVQYdhHYLHRQVALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAFGLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHL-ADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTeVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17865703 170 QVRKELRRWLRQLHEelkfTSVFVTHdQEEATEVADRVVVMSQGNIEQ 217
Cdd:TIGR00958 651 ECEQLLQESRSRASR----TVLLIAH-RLSTVERADQILVLKKGSVVE 693
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-212 |
4.54e-26 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 104.81 E-value: 4.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRfhgtdvsrlHARERKVGFVFQH 82
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLRIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALfrhmtvfdNIAFGLTVlPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:PRK09544 76 LYL--------DTTLPLTV-NRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQ 212
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-229 |
4.72e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.02 E-value: 4.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKT-TLLRIIAGLEHQS----SGHIRFHGTDVsrLHARER--------KVGFVFQH 82
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESL--LHASEQtlrgvrgnKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 --YALFRHMTVFDNIAFGLTvLPRRDRPTAAaiKTKVTQLLEMVQLAHLADR---FPAQLSGGQKQRVALARALAVEPQI 157
Cdd:PRK15134 101 pmVSLNPLHTLEKQLYEVLS-LHRGMRREAA--RGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPA 229
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-217 |
6.29e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.78 E-value: 6.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAG-LEHQssGHIRFHGTDVSRLHARE--RKVGFVFQHYALFrHMTVFDNIAF 97
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGfLPYQ--GSLKINGIELRELDPESwrKHLSWVGQNPQLP-HGTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 98 GltvlprrdRPTAAaiKTKVTQLLEMVQLAHLADRFP-----------AQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
Cdd:PRK11174 446 G--------NPDAS--DEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17865703 167 LDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEATEVADRVVVMSQGNIEQ 217
Cdd:PRK11174 516 LDAHSEQLVMQALNAASRRQ--TTLMVTH-QLEDLAQWDQIWVMQDGQIVQ 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
11-217 |
6.41e-26 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 108.75 E-value: 6.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 11 SFG---RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERKVGFVFQHYAL 85
Cdd:COG5265 364 SFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVtqASLRAAIGIVPQDTVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 86 FrHMTVFDNIAFGltvlprrdRPTA------AAIKtkvtqllemvqLAHLaDRFPAQ---------------LSGGQKQR 144
Cdd:COG5265 444 F-NDTIAYNIAYG--------RPDAseeeveAAAR-----------AAQI-HDFIESlpdgydtrvgerglkLSGGEKQR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 145 VALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTH------DqeeatevADRVVVMSQGNI-EQ 217
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHrlstivD-------ADEILVLEAGRIvER 573
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-215 |
1.85e-25 |
|
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: 107.90 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 2 SIEIARIKKSFG-RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERKVGF 78
Cdd:TIGR01193 473 DIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIdrHTLRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHmTVFDNIAFGltvlprrdrptaaaIKTKVTQ--LLEMVQLAHLAD---RFP-----------AQLSGGQK 142
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLG--------------AKENVSQdeIWAACEIAEIKDdieNMPlgyqtelseegSSISGGQK 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 143 QRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkfTSVFVTHDQEEATEVaDRVVVMSQGNI 215
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKI 686
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-217 |
6.30e-25 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 105.95 E-value: 6.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVS--RLHARERKVGFVFQHYALFRHmTVFDN 94
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklQLDSWRSRLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGltvlprrdRPTAAAiktkvTQLLEMVQLAHLAD---RFP-----------AQLSGGQKQRVALARALAVEPQILLL 160
Cdd:PRK10789 409 IALG--------RPDATQ-----QEIEHVARLASVHDdilRLPqgydtevgergVMLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 161 DEPFGALDA----QVRKELRRWLRQLheelkfTSVFVTHDQEEATEvADRVVVMSQGNIEQ 217
Cdd:PRK10789 476 DDALSAVDGrtehQILHNLRQWGEGR------TVIISAHRLSALTE-ASEILVMQHGHIAQ 529
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-195 |
1.14e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 99.49 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL-HARERKVGFVFQHYALFRHMTVFDNIAFG 98
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrDEYHQDLLYLGHQPGIKTELTALENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 99 LTVlprRDRPTAAAIktkvTQLLEMVQLAHLADRFPAQLSGGQKQRVALARaLAVEPQIL-LLDEPFGALDAQVRKELRR 177
Cdd:PRK13538 99 QRL---HGPGDDEAL----WEALAQVGLAGFEDVPVRQLSAGQQRRVALAR-LWLTRAPLwILDEPFTAIDKQGVARLEA 170
|
170
....*....|....*...
gi 17865703 178 WLRQlHEELKFTSVFVTH 195
Cdd:PRK13538 171 LLAQ-HAEQGGMVILTTH 187
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-217 |
1.41e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 104.80 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 2 SIEIARIKKSFGRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL-HARERK-VGF 78
Cdd:PRK10790 340 RIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLsHSVLRQgVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHmTVFDNIAFGltvlprRDrptaaAIKTKVTQLLEMVQLAHLADRFPA-----------QLSGGQKQRVAL 147
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLG------RD-----ISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLAL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEATEvADRVVVMSQGN-IEQ 217
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQaVEQ 555
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-224 |
3.88e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 99.53 E-value: 3.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLeHQSSGHIRFHGTDVSRLHARE--RKVGFVFQHYALFRHMTVFDNI 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 96 AFGLtvlprRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARA-LAVEPQI------LLLDEPFGALD 168
Cdd:COG4138 91 ALHQ-----PAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVlLQVWPTInpegqlLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 169 AQVRKELRRWLRQLHeELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRV 224
Cdd:COG4138 166 VAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-213 |
9.21e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.58 E-value: 9.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRfhgtdvsrLHARERkvgfvfqhyALFrhmtvf 92
Cdd:COG4178 375 GRP-LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA--------RPAGAR---------VLF------ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 93 dniafgltvLPRR------------------DRPTAAAIKtkvtQLLEMVQLAHLADRF------PAQLSGGQKQRVALA 148
Cdd:COG4178 431 ---------LPQRpylplgtlreallypataEAFSDAELR----EALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 149 RALAVEPQILLLDEPFGALDAQVRKELrrwLRQLHEEL-KFTSVFVTHdQEEATEVADRVVVMSQG 213
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAAL---YQLLREELpGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-240 |
2.07e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 101.47 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV-----SRLHARERKVGFVFQ--HYALFRHMTVF 92
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspGKLQALRRDIQFIFQdpYASLDPRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 93 DNIAFGLTVLPRRDRPTAAAiktKVTQLLEMVQL-AHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
Cdd:PRK10261 422 DSIMEPLRVHGLLPGKAAAA---RVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 172 RKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVLEFMGEV 240
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
16-215 |
2.87e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.06 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ--SSGHIRFHGTDVSRL--HARERK-VGFVFQHYALFRHMT 90
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYevTSGSILLDGEDILELspDERARAgIFLAFQYPVEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFD--NIAFGLTvlpRRDRPTAAAIKTKVTQLLEMVQLAH-LADR-----FpaqlSGGQKQRVALARALAVEPQILLLDE 162
Cdd:COG0396 94 VSNflRTALNAR---RGEELSAREFLKLLKEKMKELGLDEdFLDRyvnegF----SGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEElKFTSVFVTHdQEEATE--VADRVVVMSQGNI 215
Cdd:COG0396 167 TDSGLDIDALRIVAEGVNKLRSP-DRGILIITH-YQRILDyiKPDFVHVLVDGRI 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-196 |
5.07e-23 |
|
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: 100.01 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 7 RIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFhgtdvsrlhARERKVGFVFQHYAL 85
Cdd:TIGR03719 9 RVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP---------QPGIKVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 86 FRHMTVFDNIAFGLT----VLPRRDRPTAA---------AIKTKVTQLLEMVQ------------LAHLADRFP------ 134
Cdd:TIGR03719 80 DPTKTVRENVEEGVAeikdALDRFNEISAKyaepdadfdKLAAEQAELQEIIDaadawdldsqleIAMDALRCPpwdadv 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 135 AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHD 196
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHD 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-215 |
6.14e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.72 E-value: 6.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARER---KVGFV---FQHYALFRHMT 90
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYIpedRLGRGLVPDMS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAFGltvlpRRDRPTAA--------AIKTKVTQLLEM--VQLAHLADRFpAQLSGGQKQRVALARALAVEPQILLL 160
Cdd:COG3845 353 VAENLILG-----RYRRPPFSrggfldrkAIRAFAEELIEEfdVRTPGPDTPA-RSLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 161 DEPFGALD----AQVRKELRRwLRQlheelKFTSV-FVTHDQEEATEVADRVVVMSQGNI 215
Cdd:COG3845 427 AQPTRGLDvgaiEFIHQRLLE-LRD-----AGAAVlLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-219 |
6.20e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.90 E-value: 6.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLH--ARERKVGFVFQHYALFRHmTVFD 93
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeaALRQAISVVSQRVHLFSA-TLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 94 NIAFGLtvlprrdrptAAAIKTKVTQLLEMVQLAHLADRFPA----------QLSGGQKQRVALARALAVEPQILLLDEP 163
Cdd:PRK11160 433 NLLLAA----------PNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEP 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 164 FGALDAQVRKELRRWLRQlHEELKfTSVFVTHdQEEATEVADRVVVMSQGNI-EQAD 219
Cdd:PRK11160 503 TEGLDAETERQILELLAE-HAQNK-TVLMITH-RLTGLEQFDRICVMDNGQIiEQGT 556
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-222 |
1.14e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 99.81 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERkvgfVFQH 82
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRA----VCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YA---------LFRHMTVFDNIAF-----GLTVLPRRDRptaaaiktkVTQLLEMVQLAHLADRfPA-QLSGGQKQRVAL 147
Cdd:NF033858 78 IAympqglgknLYPTLSVFENLDFfgrlfGQDAAERRRR---------IDELLRATGLAPFADR-PAgKLSGGMKQKLGL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 148 ARALAVEPQILLLDEPFGALDAQVRK---ELRRWLRQLHEELkftSVFV-THDQEEAtEVADRVVVMSQGNIEQADAPD 222
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPLSRRqfwELIDRIRAERPGM---SVLVaTAYMEEA-ERFDWLVAMDAGRVLATGTPA 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-231 |
1.34e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 94.95 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHA----RErKVGF 78
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakimRE-AVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHMTVFDNIAFGltvlprrdrpTAAAIKTKVTQLLEMV-----QLAHLADRFPAQLSGGQKQRVALARALAV 153
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMG----------GFFAERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATR 231
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVR 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-213 |
2.27e-22 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 97.97 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-EHQS-SGHIRFHGTDVSRLHAR--ERK-VG 77
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyPHGTwDGEIYWSGSPLKASNIRdtERAgIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 78 FVFQHYALFRHMTVFDNIAFGLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFP-AQLSGGQKQRVALARALAVEPQ 156
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 157 ILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-215 |
4.06e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.78 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVS--RLHARERKVGFVFQHYALFRHmTVF 92
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQVALVSQNVHLFND-TIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 93 DNIAFgltvlPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFP-------AQLSGGQKQRVALARALAVEPQILLLDEPFG 165
Cdd:PRK11176 435 NNIAY-----ARTEQYSREQIEEAARMAYAMDFINKMDNGLDtvigengVLLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17865703 166 ALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEATEVADRVVVMSQGNI 215
Cdd:PRK11176 510 ALDTESERAIQAALDELQKNR--TSLVIAH-RLSTIEKADEILVVEDGEI 556
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-213 |
5.42e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.92 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-EHQS-SGHIRFHGTDVSRLHAR--ERK-VG 77
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyPHGTyEGEIIFEGEELQASNIRdtERAgIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 78 FVFQHYALFRHMTVFDNIAFGLTVLP--RRDRPtaaAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEP 155
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGNEITPggIMDYD---AMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 156 QILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-261 |
6.52e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.23 E-value: 6.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHG----------------TDVSRLHARERKV 76
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvielseqSAAQMRHVRGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQH--YALFRHMTVFDNIAFGLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVE 154
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRFVL 234
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTR 266
|
250 260
....*....|....*....|....*..
gi 17865703 235 EFMGEVNRLtGTVRGGQFhvgAHRWPL 261
Cdd:PRK10261 267 ALLAAVPQL-GAMKGLDY---PRRFPL 289
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
13-215 |
9.49e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 96.65 E-value: 9.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIA-----GLEHQSSGHIRFHGTDVSRLHARErkvGFVFQHYALFR 87
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkGVKGSGSVLLNGMPIDAKEMRAIS---AYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 88 HMTVFDNIAFGLTVlpRRDRPTAAAIK-TKVTQLLEMVQLAHLADRF---PAQ---LSGGQKQRVALARALAVEPQILLL 160
Cdd:TIGR00955 113 TLTVREHLMFQAHL--RMPRRVTKKEKrERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 161 DEPFGALDA----QVRKELRRwLRQlheelKFTSVFVTHDQEEAT--EVADRVVVMSQGNI 215
Cdd:TIGR00955 191 DEPTSGLDSfmaySVVQVLKG-LAQ-----KGKTIICTIHQPSSElfELFDKIILMAEGRV 245
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-215 |
1.53e-21 |
|
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: 91.17 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 7 RIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEH---QSSGHIRFHGTDVSRLHAR-ERKVGFVFQH 82
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFAEKyPGEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAFgltvlprrdrptaaAIKTKvtqllemvqlahlADRFPAQLSGGQKQRVALARALAVEPQILLLDE 162
Cdd:cd03233 92 DVHFPTLTVRETLDF--------------ALRCK-------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 163 PFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQ--EEATEVADRVVVMSQGNI 215
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADVLK-TTTFVSLYQasDEIYDLFDKVLVLYEGRQ 198
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
13-228 |
1.71e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.54 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHAR--ERKVGFVFQHYALFRHMT 90
Cdd:PRK10575 23 GRT-LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAFG-------LTVLPRRDRptaaaikTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEP 163
Cdd:PRK10575 102 VRELVAIGrypwhgaLGRFGAADR-------EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 164 FGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREP 228
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-198 |
2.83e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 90.79 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 2 SIEIARIKKSFG------RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFhgtdvsrlharerk 75
Cdd:COG2401 24 SERVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 76 vgfVFQHYALFRHMTVFDNIAfgltvlprRDRPTAAAIKtkvtqLLEMVQL--AHLADRFPAQLSGGQKQRVALARALAV 153
Cdd:COG2401 90 ---DVPDNQFGREASLIDAIG--------RKGDFKDAVE-----LLNAVGLsdAVLWLRRFKELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17865703 154 EPQILLLDEpFGA-LDAQVRKELRRWLRQLHEELKFTSVFVTHDQE 198
Cdd:COG2401 154 RPKLLVIDE-FCShLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-221 |
1.00e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 94.31 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 5 IARIKKSFGRTQVlNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV-SRLHARERKVGFVFQHY 83
Cdd:TIGR01257 934 LVKIFEPSGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 84 ALFRHMTVFDNIAFgLTVLPRRDRPTAaaiKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEP 163
Cdd:TIGR01257 1013 ILFHHLTVAEHILF-YAQLKGRSWEEA---QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 164 FGALDAQVRKELrrWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAP 221
Cdd:TIGR01257 1089 TSGVDPYSRRSI--WDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-213 |
1.60e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 92.67 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHAR---ERKVGFVFQHYA 84
Cdd:PRK11288 10 IGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaalAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 85 LFRHMTVFDNIAFGLtvLPRRdrptAAAIKTKVTQLLEMVQLAHLADRF-PAQ----LSGGQKQRVALARALAVEPQILL 159
Cdd:PRK11288 90 LVPEMTVAENLYLGQ--LPHK----GGIVNRRLLNYEAREQLEHLGVDIdPDTplkyLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTsVFVTHDQEEATEVADRVVVMSQG 213
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRVI-LYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-215 |
1.75e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 92.72 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHAR--ERKVGFVFQHYALFRHmT 90
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVVFQDAGLFNR-S 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAFGltvlprrdRPTAAaiKTKVTQLLEMVQLAHLADRFPA-----------QLSGGQKQRVALARALAVEPQILL 159
Cdd:PRK13657 425 IEDNIRVG--------RPDAT--DEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 160 LDEPFGALDAQVRKELRRWLRQLheeLKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDEL---MKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-215 |
2.80e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.17 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLhARERKVGFVFQHYALFRHMTVF--DNI 95
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-LQKNLVAYVPQSEEVDWSFPVLveDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 96 A---FGLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHladRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVR 172
Cdd:PRK15056 102 MmgrYGHMGWLRRAKKRDRQIVTAALARVDMVEFRH---RQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17865703 173 KELRRWLRQLHEELKfTSVFVTHDQEEATEVADrVVVMSQGNI 215
Cdd:PRK15056 179 ARIISLLRELRDEGK-TMLVSTHNLGSVTEFCD-YTVMVKGTV 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
15-209 |
4.02e-20 |
|
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: 88.23 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSG-----QMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSrlharerkvgFVFQHYALFRHM 89
Cdd:cd03237 7 KKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS----------YKPQYIKADYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 90 TVfDNIAFGLTvlprRDRPTAAAIKTKVTQLLemvQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
Cdd:cd03237 77 TV-RDLLSSIT----KDFYTHPYFKTEIAKPL---QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17865703 170 QVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVV 209
Cdd:cd03237 149 EQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-168 |
4.86e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 86.93 E-value: 4.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSR-LHARERKVGFVFQHYALFRHMTVFDNI 95
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGHRSGINPYLTLRENC 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865703 96 AFGLTVlprrdrptaAAIKTKVTQLLEMVQLAHLADrFP-AQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:PRK13540 96 LYDIHF---------SPGAVGITELCRLFSLEHLID-YPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-228 |
5.09e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 89.42 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGL----EHQSSGHIRFHGTDVSRLHARERK------VGFVFQH--YALFRH 88
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERRnlvgaeVAMIFQDpmTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 89 MTVFDNIAFGLTVLPRRDRPTAaaiKTKVTQLLEMVQLAHLADR---FPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
Cdd:PRK11022 106 YTVGFQIMEAIKVHQGGNKKTR---RQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 166 ALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREP 228
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-170 |
5.62e-20 |
|
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: 86.78 E-value: 5.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHAR-ERKVGFVFQHYALFRHMTVFDNI 95
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 96 AFGltvlpRRDRPTAAaiktkVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
Cdd:cd03231 95 RFW-----HADHSDEQ-----VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-221 |
7.33e-20 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 86.78 E-value: 7.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSR--LHARERKVGFVFQHYALFRHmTVFDN 94
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKigLHDLRSRISIIPQDPVLFSG-TIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAfgltvlprrdrPTAAAIKTKVTQLLEMVQLAHLADRFP-----------AQLSGGQKQRVALARALAVEPQILLLDEP 163
Cdd:cd03244 98 LD-----------PFGEYSDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 164 FGALDAQVRKELRRWLRqlhEELKFTSVF-VTHDQEEATEvADRVVVMSQGNIEQADAP 221
Cdd:cd03244 167 TASVDPETDALIQKTIR---EAFKDCTVLtIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-225 |
2.39e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.60 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGT--DVSR--LHARERKVGFVFQ--HYALFrHM 89
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKrgLLALRQQVATVFQdpEQQIF-YT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 90 TVFDNIAFGLtvlpRRDRPTAAAIKTKVTQLLEMVQLAHLADRfPAQ-LSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:PRK13638 94 DIDSDIAFSL----RNLGVPEAEITRRVDEALTLVDAQHFRHQ-PIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 169 AQVRKELRRWLRQLHEELKFTsVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVW 225
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-217 |
2.53e-19 |
|
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: 90.00 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTdvsrlharerkVGFVFQHyALFRHMTVFDNIAF 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------VAYVPQQ-AWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 98 GLTVLPRRDRPTAAAiktkvTQLLEMVQLAHLADRFP-----AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVR 172
Cdd:TIGR00957 722 GKALNEKYYQQVLEA-----CALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17865703 173 KELRRWLRQLHEELKF-TSVFVTHDQEEATEVaDRVVVMSQGNIEQ 217
Cdd:TIGR00957 797 KHIFEHVIGPEGVLKNkTRILVTHGISYLPQV-DVIIVMSGGKISE 841
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-228 |
2.61e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 86.14 E-value: 2.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEhQSSGHIRFHGTDVSRLHARE---RKVGFVFQHYALFrHMTVFDNIAf 97
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAElarHRAYLSQQQTPPF-AMPVFQYLT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 98 gltvLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARA-LAVEP------QILLLDEPFGALDAQ 170
Cdd:PRK03695 92 ----LHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPdinpagQLLLLDEPMNSLDVA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 171 VRKELRRWLRQLhEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREP 228
Cdd:PRK03695 168 QQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-215 |
3.88e-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: 84.50 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ--SSGHIRFHGTDVSRLHARER-KVGfvfqhyaLFrhmtvf 92
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDITDLPPEERaRLG-------IF------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 93 dnIAFgltvlprrDRPtaAAIktkvtqllEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVR 172
Cdd:cd03217 81 --LAF--------QYP--PEI--------PGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17865703 173 KELRRWLRQLHEElKFTSVFVTHDQEEATEV-ADRVVVMSQGNI 215
Cdd:cd03217 141 RLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRI 183
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-217 |
4.54e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 89.03 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-LEHQSSGHIRFHGTdvsrlharerkVGFVFQHYALFrHMTVFDNIA 96
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT-----------VAYVPQVSWIF-NATVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 97 FGLTVLPRR-DRPTAAAIKTKVTQLLEMVQLAHLADRfPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKEL 175
Cdd:PLN03130 701 FGSPFDPERyERAIDVTALQHDLDLLPGGDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV 779
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17865703 176 rrWLRQLHEELKF-TSVFVTHDQEEATEVaDRVVVMSQGNIEQ 217
Cdd:PLN03130 780 --FDKCIKDELRGkTRVLVTNQLHFLSQV-DRIILVHEGMIKE 819
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-217 |
4.55e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 88.88 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-LEHQSSGHIRFHGTdvsrlharerkVGFVFQHYALFrHMTVFDNIA 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS-----------VAYVPQVSWIF-NATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 97 FGLTVLPRRdrptaaaiktkVTQLLEMVQLAHLADRFPAQ-----------LSGGQKQRVALARALAVEPQILLLDEPFG 165
Cdd:PLN03232 701 FGSDFESER-----------YWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17865703 166 ALDAQVRKELrrWLRQLHEELK-FTSVFVThDQEEATEVADRVVVMSQGNIEQ 217
Cdd:PLN03232 770 ALDAHVAHQV--FDSCMKDELKgKTRVLVT-NQLHFLPLMDRIILVSEGMIKE 819
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-195 |
7.04e-19 |
|
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: 82.59 E-value: 7.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIrfhgtdvsrlharerkvgfvfqhyalfrHMTVFDNIA 96
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------------------------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 97 FgltvLPRRdrptaaaikTKVTQLLEMVQLAHLADRfpaQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVrkeLR 176
Cdd:cd03223 68 F----LPQR---------PYLPLGTLREQLIYPWDD---VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES---ED 128
|
170
....*....|....*....
gi 17865703 177 RWLRQLHEELkFTSVFVTH 195
Cdd:cd03223 129 RLYQLLKELG-ITVISVGH 146
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-223 |
7.10e-19 |
|
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: 87.93 E-value: 7.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHG---TDVSRLHARERkvgF--VFQHYALFRHMtvfdni 95
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGqpvTADNREAYRQL---FsaVFSDFHLFDRL------ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 96 aFGLTVLPRRDRptaaaiktkVTQLLEMVQLAHL----ADRF-PAQLSGGQKQRVALARALAVEPQILLLDE------Pf 164
Cdd:COG4615 422 -LGLDGEADPAR---------ARELLERLELDHKvsveDGRFsTTDLSQGQRKRLALLVALLEDRPILVFDEwaadqdP- 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 165 galdaqvrkELRRWL-RQLHEELK---FTSVFVTHDqEEATEVADRVVVMSQGNIEQADAPDR 223
Cdd:COG4615 491 ---------EFRRVFyTELLPELKargKTVIAISHD-DRYFDLADRVLKMDYGKLVELTGPAA 543
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-196 |
9.42e-19 |
|
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: 87.30 E-value: 9.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFhGTDVsrlharerKVGFVFQ- 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------KLAYVDQs 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRHMTVFDNIAFGLTVLPRRDRptaaaiktkvtqllEMVQLAHLAdRFP----------AQLSGGQKQRVALARAL 151
Cdd:TIGR03719 394 RDALDPNKTVWEEISGGLDIIKLGKR--------------EIPSRAYVG-RFNfkgsdqqkkvGQLSGGERNRVHLAKTL 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17865703 152 AVEPQILLLDEPFGALDAQVrkelrrwLRQLHEEL-KF--TSVFVTHD 196
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVET-------LRALEEALlNFagCAVVISHD 499
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-213 |
1.05e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.98 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVS---RLHARERKVGFV 79
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKSSQEAGIGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 FQHYALFRHMTVFDNIAFGltvlpRRDRPTAAAIKTK-----VTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVE 154
Cdd:PRK10762 85 HQELNLIPQLTIAENIFLG-----REFVNRFGRIDWKkmyaeADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-213 |
1.48e-18 |
|
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: 84.52 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGtdvsrlharerKVGFVFQhYALFRHMTVFDN 94
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------RISFSSQ-FSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGLTVLPRRDRPTAAAiktkvtqllemVQLAHLADRFPAQ-----------LSGGQKQRVALARALAVEPQILLLDEP 163
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKA-----------CQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17865703 164 FGALDAQVRKEL-RRWLRQLHEELkfTSVFVTHDQEEaTEVADRVVVMSQG 213
Cdd:cd03291 187 FGYLDVFTEKEIfESCVCKLMANK--TRILVTSKMEH-LKKADKILILHEG 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-213 |
1.72e-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: 87.27 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGtdvsrlharerKVGFVFQhYALFRHMTVFDN 94
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------RISFSPQ-TSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGLTVLPRRDRPTaaaikTKVTQLLEMVQLAHLADRFP-----AQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
Cdd:TIGR01271 507 IIFGLSYDEYRYTSV-----IKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17865703 170 QVRKEL-RRWLRQLHEELkfTSVFVTHDQEEATEvADRVVVMSQG 213
Cdd:TIGR01271 582 VTEKEIfESCLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-196 |
1.91e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 86.71 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 7 RIKKSFG-RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFhgtdvsrlhARERKVGFVFQHYAL 85
Cdd:PRK11819 11 RVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP---------APGIKVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 86 FRHMTVFDNIAFGL----TVLPRRDRPTAA---------AIKTKVTQLLEMVQLAHLAD------------RFP------ 134
Cdd:PRK11819 82 DPEKTVRENVEEGVaevkAALDRFNEIYAAyaepdadfdALAAEQGELQEIIDAADAWDldsqleiamdalRCPpwdakv 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 135 AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHD 196
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-215 |
2.13e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 83.69 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 12 FGRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRF--HGTDVSRLHARERKVGFVFQHYAlfr 87
Cdd:PRK15112 21 FRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddHPLHFGDYSYRSQRIRMIFQDPS--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 88 hmtvfdniafglTVL-PRR------DRP-------TAAAIKTKVTQLLEMVQL-AHLADRFPAQLSGGQKQRVALARALA 152
Cdd:PRK15112 98 ------------TSLnPRQrisqilDFPlrlntdlEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PRK15112 166 LRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-218 |
4.33e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.49 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARER-KVGFVF-----QHYALFRHMTVFD 93
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 94 NIA------FGLTVLPRRDRPTA----AAIKTKVTQllemvqlahlADRFPAQLSGGQKQRVALARALAVEPQILLLDEP 163
Cdd:PRK15439 361 NVCalthnrRGFWIKPARENAVLeryrRALNIKFNH----------AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 164 FGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNIEQA 218
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGA 484
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
10-213 |
4.34e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 85.70 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 10 KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSghirFHGTDVS--RLHARE--RKVGFVFQHYAL 85
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILAnnRKPTKQilKRTGFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 86 FRHMTVFDNIAF-GLTVLPR---RDRPTAAAiKTKVTQL-LEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLL 160
Cdd:PLN03211 152 YPHLTVRETLVFcSLLRLPKsltKQEKILVA-ESVISELgLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17865703 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
11-168 |
1.12e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 80.66 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 11 SFGR--TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHaRERKVGFVFQHYALFRH 88
Cdd:PRK13543 18 AFSRneEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 89 MTVFDNIAFGLTVLPRRDRPTAAAIktkvtqlLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:PRK13543 97 LSTLENLHFLCGLHGRRAKQMPGSA-------LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-213 |
2.62e-17 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 79.68 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSR-----LHARER-KVGFVFQHYALFrHMTV 91
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEpsfeaTRSRNRySVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 92 FDNIAFGLTVLPRRDRPTAAAIKTKV-TQLLEMVQLAHLADRfPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDACSLQPdIDLLPFGDQTEIGER-GINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17865703 171 VRKEL-RRWLRQLHEELKFTSVFVTHDQEEATEvADRVVVMSQG 213
Cdd:cd03290 175 LSDHLmQEGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-217 |
3.34e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.52 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 8 IKKSFGRTQvlnDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV---SRLHARERKVGFV----- 79
Cdd:PRK09700 272 TSRDRKKVR---DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDAVKKGMAYItesrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 ----FQHYALFRHMTVFDNI-------AFGLtVLPRRDRPTAAAIKtkvtqllEMVQL-AHLADRFPAQLSGGQKQRVAL 147
Cdd:PRK09700 349 dngfFPNFSIAQNMAISRSLkdggykgAMGL-FHEVDEQRTAENQR-------ELLALkCHSVNQNITELSGGNQQKVLI 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNIEQ 217
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-210 |
5.02e-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: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIariKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLeHQSSGHI-----RFHGTDVSRLHARERK 75
Cdd:COG4170 9 LTIEI---DTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVtadrfRWNGIDLLKLSPRERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 76 ------VGFVFQH--YALFRHMTVFDNIAFgltVLPRR-------DRPTAAaiKTKVTQLLEMVQL---AHLADRFPAQL 137
Cdd:COG4170 85 kiigreIAMIFQEpsSCLDPSAKIGDQLIE---AIPSWtfkgkwwQRFKWR--KKRAIELLHRVGIkdhKDIMNSYPHEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVM 210
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-226 |
6.08e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.87 E-value: 6.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG--LEHQSSGHIRFHG-----------TDVSRLhARERKV------- 76
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGdvtlngeplaaIDAPRL-ARLRAVlpqaaqp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFqhyalfrhmTVFDNIAFGLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALA---- 152
Cdd:PRK13547 95 AFAF---------SAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 153 -----VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWR 226
Cdd:PRK13547 166 phdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-245 |
6.95e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.54 E-value: 6.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQS---SGHIRFHGTDVSRLHARE------RKVGFVFQH--YALFR 87
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKElnklraEQISMIFQDpmTSLNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 88 HMTVFDNIAFGLTVLPRRDRPTAAAIKTKvtqLLEMVQLAHLADR---FPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
Cdd:PRK09473 113 YMRVGEQLMEVLMLHKGMSKAEAFEESVR---MLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQG-NIEQADAPDrVWREPATRFVLEFMGEVNRL 243
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGrTMEYGNARD-VFYQPSHPYSIGLLNAVPRL 268
|
..
gi 17865703 244 TG 245
Cdd:PRK09473 269 DA 270
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-213 |
7.39e-17 |
|
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: 77.67 E-value: 7.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQS--SGHIRFHGTDVSRLHARErkVGFVFQHYALFRHMT 90
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQRS--TGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAFgltvlprrdrptAAAIKtkvtqllemvqlahladrfpaQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
Cdd:cd03232 96 VREALRF------------SALLR---------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17865703 171 VRKELRRWLRQLHEELKftSVFVTHDQEEAT--EVADRVVVMSQG 213
Cdd:cd03232 143 AAYNIVRFLKKLADSGQ--AILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-216 |
3.74e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.21 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGhirfhgtdvsRLHArERKVGFVFQHyALFRHMTVFDNIA 96
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG----------RVWA-ERSIAYVPQQ-AWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 97 FgltVLPRRDRPTAAAIKtkVTQLleMVQLAHLADRFPAQ-------LSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
Cdd:PTZ00243 743 F---FDEEDAARLADAVR--VSQL--EADLAQLGGGLETEigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17865703 170 QVRKELRR--WLRQLHEElkfTSVFVTHdQEEATEVADRVVVMSQGNIE 216
Cdd:PTZ00243 816 HVGERVVEecFLGALAGK---TRVLATH-QVHVVPRADYVVALGDGRVE 860
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
18-232 |
4.23e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 79.25 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVS--RLHARERKVGFVFQHYALFRHMtvfdni 95
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaeQPEDYRKLFSAVFTDFHLFDQL------ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 96 afgltvLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPA--QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
Cdd:PRK10522 413 ------LGPEGKPANPALVEKWLERLKMAHKLELEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 174 ELRRWLRQLHEELKFTSVFVTHDqEEATEVADRVVVMSQGNIEQ--ADAPDRVWREPATRF 232
Cdd:PRK10522 487 EFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSEltGEERDAASRDAVART 546
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-234 |
9.06e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.28 E-value: 9.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 20 DISLDIPSGQMVALLGPSGSGKT----TLLRII-AGLEhQSSGHIRFHGTDVSRLHARERKVGFVFQH----YALFRHMT 90
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVR-QTAGRVLLDGKPVAPCALRGRKIATIMQNprsaFNPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 vfdniAFGLTVLPRRDRPTAAAiktKVTQLLEMVQL---AHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
Cdd:PRK10418 100 -----THARETCLALGKPADDA---TLTAALEAVGLenaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 168 DAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI-EQADAPD--RVWREPATRFVL 234
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIvEQGDVETlfNAPKHAVTRSLV 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-213 |
1.05e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 78.61 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQS----SGHIRFHGTDVSRLHARER-KVGFVFQHYALFRHMT 90
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAFgltvlprrdrptAAAIKT---KVTQLLEMVQLAHLADRFPAQL------------------SGGQKQRVALAR 149
Cdd:TIGR00956 155 VGETLDF------------AARCKTpqnRPDGVSREEYAKHIADVYMATYglshtrntkvgndfvrgvSGGERKRVSIAE 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQ--EEATEVADRVVVMSQG 213
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILD-TTPLVAIYQcsQDAYELFDKVIVLYEG 287
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-196 |
2.54e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.08 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFhGTDVsrlharerKVGFVFQ- 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--------KLAYVDQs 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRHMTVFDNIAFGLTVLPRRDRptaaaiktkvtqllEMVQLAHLAdRF----PAQ------LSGGQKQRVALARAL 151
Cdd:PRK11819 396 RDALDPNKTVWEEISGGLDIIKVGNR--------------EIPSRAYVG-RFnfkgGDQqkkvgvLSGGERNRLHLAKTL 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17865703 152 AVEPQILLLDEPFGALDAQVrkelrrwLRQLHEEL-KF--TSVFVTHD 196
Cdd:PRK11819 461 KQGGNVLLLDEPTNDLDVET-------LRALEEALlEFpgCAVVISHD 501
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-221 |
5.29e-15 |
|
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: 72.83 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSR--LHARERKVGFVFQHYALFRHmTVFD 93
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTipLEDLRSSLTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 94 NiafgltvLPRRDRPTAAaiktkvtQLLEMVQLAHLADrfpaQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
Cdd:cd03369 101 N-------LDPFDEYSDE-------EIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17865703 174 ELRRWLRqlhEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAP 221
Cdd:cd03369 163 LIQKTIR---EEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-215 |
9.34e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.33 E-value: 9.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE------------RKV-GFVFQHyal 85
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairagimlcpedRKAeGIIPVH--- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 86 frhmTVFDNIA---------FGLTVLPRRDRPTAA------AIKTKVTQLLEMvqlahladrfpaQLSGGQKQRVALARA 150
Cdd:PRK11288 347 ----SVADNINisarrhhlrAGCLINNRWEAENADrfirslNIKTPSREQLIM------------NLSGGNQQKAILGRW 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-223 |
1.52e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.16 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHG--TDVSRLHAReRKVGFVFQHYALFRHMTVFDNIA 96
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIATR-RRVGYMSQAFSLYGELTVRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 97 -----FGLTvlprrdrptAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
Cdd:NF033858 362 lharlFHLP---------AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17865703 172 RKELRRWLRQLHEELKFTsVFV-THDQEEAtEVADRVVVMSQGNIEQADAPDR 223
Cdd:NF033858 433 RDMFWRLLIELSREDGVT-IFIsTHFMNEA-ERCDRISLMHAGRVLASDTPAA 483
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-215 |
2.31e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHgTD--VSRLHARERkvgfvfqhyalfRH 88
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDliVARLQQDPP------------RN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 89 M--TVFDNIAFGLTVLprrdrptAAAIKT--KVTQLLE-------MVQLAHL--------------------------AD 131
Cdd:PRK11147 79 VegTVYDFVAEGIEEQ-------AEYLKRyhDISHLVEtdpseknLNELAKLqeqldhhnlwqlenrinevlaqlgldPD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 132 RFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMS 211
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLD 227
|
....
gi 17865703 212 QGNI 215
Cdd:PRK11147 228 RGKL 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-219 |
4.10e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARER-KVGFVF-----QHYALFRHMTV 91
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYisedrKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 92 FDNIAfgLTVLPRRDRpTAAAIKTKVTQLL--EMVQLAHL----ADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
Cdd:PRK10762 348 KENMS--LTALRYFSR-AGGSLKHADEQQAvsDFIRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 166 ALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNI------EQAD 219
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRIsgeftrEQAT 483
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-209 |
8.03e-14 |
|
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: 72.51 E-value: 8.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGrtqvlnDISLDIPSGQM-----VALLGPSGSGKTTLLRIIAGLEHQSSGHIRFhgtdvsrlharERKVG 77
Cdd:COG1245 342 VEYPDLTKSYG------GFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-----------DLKIS 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 78 FVFQHYALFRHMTVFDNIAFGLTvlprrDRPTAAAIKTKVTQLLemvQLAHLADRFPAQLSGGQKQRVALARALAVEPQI 157
Cdd:COG1245 405 YKPQYISPDYDGTVEEFLRSANT-----DDFGSSYYKTEIIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17865703 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVV 209
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-213 |
1.34e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.68 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDV---SRLHARERKVGFVFQHYA 84
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 85 LFRHMTVFDNIAFGLtvLPRRD---------RPTAAAI---------KTKVtqllemvqlahladrfpAQLSGGQKQRVA 146
Cdd:PRK10982 84 LVLQRSVMDNMWLGR--YPTKGmfvdqdkmyRDTKAIFdeldididpRAKV-----------------ATLSVSQMQMIE 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-175 |
3.31e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 67.59 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHarERKVGFVFQHYALFRHMTVFDNI 95
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--KPYCTYIGHNLGLKLEMTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 96 AFGLTVLPRRDRPTAAAIKTKVTQLLemvqlahlaDRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKEL 175
Cdd:PRK13541 92 KFWSEIYNSAETLYAAIHYFKLHDLL---------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-228 |
3.81e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.45 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIariKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ----SSGHIRFHGTDVSRLHARERKv 76
Cdd:PRK15093 9 LTIEF---KTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 gfvfqhyALFRH--MTVFDNIAFGLTVLPRRDRPTAAAI----------------KTKVTQLLEMVQLAHLAD---RFPA 135
Cdd:PRK15093 85 -------KLVGHnvSMIFQEPQSCLDPSERVGRQLMQNIpgwtykgrwwqrfgwrKRRAIELLHRVGIKDHKDamrSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 136 QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250
....*....|...
gi 17865703 216 EQADAPDRVWREP 228
Cdd:PRK15093 238 VETAPSKELVTTP 250
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-210 |
3.94e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.43 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERKVGFVFQHyaLFRHMTVF 92
Cdd:PRK10938 16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLsfEQLQKLVSDEWQR--NNTDMLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 93 DNIAFGLTvlprrdrpTAAAIKTKVT------QLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
Cdd:PRK10938 94 GEDDTGRT--------TAEIIQDEVKdparceQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17865703 167 LDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVM 210
Cdd:PRK10938 166 LDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-209 |
4.26e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGrtqvlnDISLDIPSGQM-----VALLGPSGSGKTTLLRIIAGLEHQSSGHIrfhGTDVsrlharerKVG 77
Cdd:PRK13409 341 VEYPDLTKKLG------DFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPEL--------KIS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 78 FVFQHYALFRHMTVFDNIAfgltvlprrdrptaaAIKTKV------TQLLEMVQLAHLADRFPAQLSGGQKQRVALARAL 151
Cdd:PRK13409 404 YKPQYIKPDYDGTVEDLLR---------------SITDDLgssyykSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACL 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEATEVADRVVV 209
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-223 |
5.96e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 54 QSSGHIRFHGTDVSRLHARERKVGF--VFQHYALFrHMTVFDNIAFGLTVLPRRDRPTAAAIKTkVTQLLEMVQLAHLAD 131
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNLKDLRNLFsiVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAA-IDEFIESLPNKYDTN 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 132 RFP--AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHdQEEATEVADRVVV 209
Cdd:PTZ00265 1352 VGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVV 1430
|
170
....*....|....
gi 17865703 210 MSQgnieqadaPDR 223
Cdd:PTZ00265 1431 FNN--------PDR 1436
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-213 |
6.86e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.43 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 4 EIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-EHQS-SGHIRFHGTDV--SRLHARERKvGFV 79
Cdd:NF040905 3 EMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyPHGSyEGEILFDGEVCrfKDIRDSEAL-GIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 80 F--QHYALFRHMTVFDNIAFGltvlprRDRPTAAAI-----KTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALA 152
Cdd:NF040905 82 IihQELALIPYLSIAENIFLG------NERAKRGVIdwnetNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-215 |
1.51e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.38 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFhgtdvsrlhARERKVGFVFQ- 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW---------SENANIGYYAQd 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALF-RHMTVFDNIAfgltvLPRRDRPTAAAIKTKVTQLLemvqlaHLADRFPAQ---LSGGQKQRVALARALAVEPQI 157
Cdd:PRK15064 391 HAYDFeNDLTLFDWMS-----QWRQEGDDEQAVRGTLGRLL------FSQDDIKKSvkvLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17865703 158 LLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PRK15064 460 LVMDEPTNHMDMESIESLNMAL----EKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-227 |
1.66e-12 |
|
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: 66.80 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHqSSGHIRFHGTDVSRLHARE-RKV-GF 78
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKwRKAfGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHmTVFDNIafgltvlprrdRPTAAAIKTKVTQLLEMVQLAHLADRFPAQL-----------SGGQKQRVAL 147
Cdd:cd03289 82 IPQKVFIFSG-TFRKNL-----------DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWRE 227
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFAD---CTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-216 |
4.04e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.16 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-EHQSSGHIRFHGTDV---SRLHARERKVGFV---FQHYALFRHMT 90
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdirNPAQAIRAGIAMVpedRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 91 VFDNIAfgLTVLPR---RDRPTAAAiktKVTQLLEMVQLAHLADRFP----AQLSGGQKQRVALARALAVEPQILLLDEP 163
Cdd:TIGR02633 356 VGKNIT--LSVLKSfcfKMRIDAAA---ELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17865703 164 FGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNIE 216
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-213 |
4.28e-12 |
|
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: 67.73 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 28 GQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHG----TDVSRLHareRKVGFVFQHYALFRHMTVFDNIafgltVLP 103
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksilTNISDVH---QNMGYCPQFDAIDDLLTGREHL-----YLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 104 RRDRPTAAAIKTKVTQL-LEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQL 182
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
170 180 190
....*....|....*....|....*....|.
gi 17865703 183 HEELKfTSVFVTHDQEEATEVADRVVVMSQG 213
Cdd:TIGR01257 2117 IREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-200 |
4.76e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.96 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQS-------------SGH----IRFH-GTDVSRLH-- 70
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGysndltlfgrrrgSGEtiwdIKKHiGYVSSSLHld 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 71 ----ARERKV---GFvfqhyalfrhmtvFDNIAFGLTVlPRRDRPTAAaiktkvtQLLEMVQL-AHLADRFPAQLSGGQk 142
Cdd:PRK10938 349 yrvsTSVRNVilsGF-------------FDSIGIYQAV-SDRQQKLAQ-------QWLDILGIdKRTADAPFHSLSWGQ- 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 143 QRVAL-ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEA 200
Cdd:PRK10938 407 QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-196 |
6.26e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 65.08 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 23 LDIP-SGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHirfhgtdvsrlHARERKVGFVFQHY---ALFRHMTVFDNIAFG 98
Cdd:cd03236 20 LPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-----------FDDPPDWDEILDEFrgsELQNYFTKLLEGDVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 99 LTVLPRRDRPTAAAIKTKVTQLLEMV-------------QLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
Cdd:cd03236 89 VIVKPQYVDLIPKAVKGKVGELLKKKdergkldelvdqlELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190
....*....|....*....|....*....|.
gi 17865703 166 ALDAQVRKELRRWLRQLHEELKFTSVfVTHD 196
Cdd:cd03236 169 YLDIKQRLNAARLIRELAEDDNYVLV-VEHD 198
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-214 |
6.33e-12 |
|
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: 62.78 E-value: 6.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 27 SGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFVFqhyalfrhmtvfdniafgltvlprrd 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 107 rptaaaiktkvtqllemvqlahlaDRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELR-----RWLRQ 181
Cdd:smart00382 55 ------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLL 110
|
170 180 190
....*....|....*....|....*....|....*...
gi 17865703 182 LHEELKFTSVFVTHDQE-----EATEVADRVVVMSQGN 214
Cdd:smart00382 111 LKSEKNLTVILTTNDEKdlgpaLLRRRFDRRIVLLLIL 148
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-221 |
8.58e-12 |
|
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: 66.89 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSR--LHARERKVGFVFQhyalfrhmtvfDN 94
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKigLHDLRFKITIIPQ-----------DP 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGLTVLPRRDrPTAAAIKTKVTQLLEmvqLAHLADRFPAQ--------------LSGGQKQRVALARALAVEPQILLL 160
Cdd:TIGR00957 1370 VLFSGSLRMNLD-PFSQYSDEEVWWALE---LAHLKTFVSALpdkldhecaeggenLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 161 DEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEATEVAdRVVVMSQGNIEQADAP 221
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTIRTQFEDC--TVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAP 1503
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-215 |
9.61e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.53 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 2 SIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSgkttllriiAGLEHQSSGHIRfhGTDVSRLHARERKvgFVFQ 81
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA---------A**RGALPAHV*--GPDAGRRPWRF*T--WCAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 82 HYALFRHMTVFDNIAFG----------LTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARAL 151
Cdd:NF000106 80 RRALRRTIG*HRPVR*GrresfsgrenLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865703 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-215 |
1.43e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.89 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGleHQS----SGHIRFHGTDVSRLHARER-KVG 77
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERaHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 78 --FVFQhYALfrHMTVFDNIAFGLTVLPRRDR----PTAAAIK--TKVTQLLEMVQL-AHLADRFPAQ-LSGGQKQRVAL 147
Cdd:CHL00131 86 ifLAFQ-YPI--EIPGVSNADFLRLAYNSKRKfqglPELDPLEflEIINEKLKLVGMdPSFLSRNVNEgFSGGEKKRNEI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVA-DRVVVMSQGNI 215
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLLDYIKpDYVHVMQNGKI 230
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-195 |
1.66e-11 |
|
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: 65.54 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGhirfhgtdvSRLHARERKVGFVFQHyALFRHMTVFDNIA 96
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG---------RLTKPAKGKLFYVPQR-PYMTLGTLRDQII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 97 FGLTVLPRRDRPTAAAiktKVTQLLEMVQLAHLADR---FPA------QLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
Cdd:TIGR00954 537 YPDSSEDMKRRGLSDK---DLEQILDNVQLTHILEReggWSAvqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180
....*....|....*....|....*...
gi 17865703 168 DAQVRKELRRWLRqlheELKFTSVFVTH 195
Cdd:TIGR00954 614 SVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-215 |
1.88e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEH-QSSGHIRFHGTDVSRLHARE------------RKvgfvf 80
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQaiaqgiamvpedRK----- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 qHYALFRHMTVFDNIAfgLTVLPRRDRPT----AAAIKTKVTQLLEM-VQLAHLADRFpAQLSGGQKQRVALARALAVEP 155
Cdd:PRK13549 349 -RDGIVPVMGVGKNIT--LAALDRFTGGSriddAAELKTILESIQRLkVKTASPELAI-ARLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 156 QILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-209 |
2.16e-11 |
|
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: 61.82 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 24 DIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFhgtdvsrlharerkvgfvfqhyalfrhmtvfdniafgltvlp 103
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW------------------------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 104 rrDRPTAAAIKTKVtqllemvqlahladrfpaQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLH 183
Cdd:cd03222 59 --DGITPVYKPQYI------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*.
gi 17865703 184 EELKFTSVFVTHDQEEATEVADRVVV 209
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-243 |
4.16e-11 |
|
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: 64.55 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEhQSSGHIRFHGT--DVSRLHARERKVGF 78
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVswNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 79 VFQHYALFRHmTVFDNIafgltvlprrdRPTAAAIKTKVTQLLEMVQLAHLADRFPAQL-----------SGGQKQRVAL 147
Cdd:TIGR01271 1297 IPQKVFIFSG-TFRKNL-----------DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCL 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElkfTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWRE 227
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN---CTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
250
....*....|....*.
gi 17865703 228 paTRFVLEFMGEVNRL 243
Cdd:TIGR01271 1442 --TSLFKQAMSAADRL 1455
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-215 |
4.87e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.12 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ--SSGHIRFHGTDVSRLHARERKVGFVF 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLELSPEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 81 QHYALFRHMTVFDNIAFGLTVL---------PRRDRPTAAAIKTKVTQLLEMVQlAHLADRFPAQLSGGQKQRVALARAL 151
Cdd:PRK09580 82 MAFQYPVEIPGVSNQFFLQTALnavrsyrgqEPLDRFDFQDLMEEKIALLKMPE-DLLTRSVNVGFSGGEKKRNDILQMA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17865703 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEATEVA-DRVVVMSQGNI 215
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVLYQGRI 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-196 |
1.31e-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: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 22 SLDIP-SGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIrfhgtdvsrlharERKVGF--VFQHYA---LFRHmtvFDNI 95
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDY-------------DEEPSWdeVLKRFRgteLQDY---FKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 96 AFG-LTV---------LPRrdrptaaAIKTKVTQLLEMVQ-------------LAHLADRFPAQLSGGQKQRVALARALA 152
Cdd:COG1245 156 ANGeIKVahkpqyvdlIPK-------VFKGTVRELLEKVDergkldelaeklgLENILDRDISELSGGELQRVAIAAALL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17865703 153 VEPQILLLDEPFGALDaqVRKELR--RWLRQLHEELKftSVFVT-HD 196
Cdd:COG1245 229 RDADFYFFDEPSSYLD--IYQRLNvaRLIRELAEEGK--YVLVVeHD 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-182 |
2.24e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.43 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 8 IKKsfGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAglEHQSSGHIRfHGTDVSRLHAR----ERKVGFVFQHY 83
Cdd:TIGR00956 771 IKK--EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVIT-GGDRLVNGRPLdssfQRSIGYVQQQD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 84 ALFRHMTVFDNIAFGltvlPRRDRPTAAAIKTK------VTQLLEMVQLAHLADRFPAQ-LSGGQKQRVALARALAVEPQ 156
Cdd:TIGR00956 846 LHLPTSTVRESLRFS----AYLRQPKSVSKSEKmeyveeVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPK 921
|
170 180
....*....|....*....|....*..
gi 17865703 157 ILL-LDEPFGALDAQVRKELRRWLRQL 182
Cdd:TIGR00956 922 LLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-215 |
3.30e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARER-KVGFvfqhyALF----RHMTVF 92
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAiNHGF-----ALVteerRSTGIY 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 93 DNIAFGLTVLprrdrptAAAIKTKVTQ--LLEMVQLAH--------LADRFPAQ------LSGGQKQRVALARALAVEPQ 156
Cdd:PRK10982 339 AYLDIGFNSL-------ISNIRNYKNKvgLLDNSRMKSdtqwvidsMRVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPE 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTsVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PRK10982 412 ILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGI-IIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-208 |
3.60e-10 |
|
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: 59.16 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 35 GPSGSGKTTLLR-IIAGL--EHQSSGHIRFHGTDVSRLHARERKVGFVFQH-----YALFRHMTVFDNIAFgltvlprrd 106
Cdd:cd03240 29 GQNGAGKTTIIEaLKYALtgELPPNSKGGAHDPKLIREGEVRAQVKLAFENangkkYTITRSLAILENVIF--------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 107 rptaaaiktkVTQ------LLEMvqlahladrfPAQLSGGQKQ------RVALARALAVEPQILLLDEPFGALDA-QVRK 173
Cdd:cd03240 100 ----------CHQgesnwpLLDM----------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEE 159
|
170 180 190
....*....|....*....|....*....|....*
gi 17865703 174 ELRRWLRQLHEELKFTSVFVTHDqEEATEVADRVV 208
Cdd:cd03240 160 SLAEIIEERKSQKNFQLIVITHD-EELVDAADHIY 193
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-224 |
6.94e-10 |
|
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: 59.15 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRL--HARERKVGFVFQHYALFRhmtvfDN 94
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplHTLRSRLSIILQDPILFS-----GS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGLTvlprrdrPTAAAIKTKVTQLLEMVQLAHLADRFPAQL-----------SGGQKQRVALARALAVEPQILLLDEP 163
Cdd:cd03288 111 IRFNLD-------PECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEA 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17865703 164 FGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEATEvADRVVVMSQGNIEQADAPDRV 224
Cdd:cd03288 184 TASIDMATENILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENL 241
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-224 |
1.40e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 58.29 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGtdvsrlharerKVGFVFQHYALFRHMTVFDNIAF 97
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIAISAGLSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 98 GLTVLPRRDRptaaAIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEpfgALDAQVRKELRR 177
Cdd:PRK13546 109 KMLCMGFKRK----EIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTFAQK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17865703 178 WLRQLHE--ELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRV 224
Cdd:PRK13546 182 CLDKIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-196 |
1.54e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 22 SLDIPS-GQMVALLGPSGSGKTTLLRIIAGL------EHQSSGHI-----RFHGTDV----SRLHARERKVGFVFQHYAL 85
Cdd:PRK13409 92 GLPIPKeGKVTGILGPNGIGKTTAVKILSGElipnlgDYEEEPSWdevlkRFRGTELqnyfKKLYNGEIKVVHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 86 frhmtvfdniafgltvLPRrdrptaaAIKTKVTQLLEMV-------------QLAHLADRFPAQLSGGQKQRVALARALA 152
Cdd:PRK13409 172 ----------------IPK-------VFKGKVRELLKKVdergkldevverlGLENILDRDISELSGGELQRVAIAAALL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17865703 153 VEPQILLLDEPFGALDaqVRKELR--RWLRQLHEElkfTSVFVT-HD 196
Cdd:PRK13409 229 RDADFYFFDEPTSYLD--IRQRLNvaRLIRELAEG---KYVLVVeHD 270
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-213 |
2.53e-09 |
|
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: 55.79 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRiiAGLEHQssghirfhgtdvsrlhARERKVGFVfqhYALFRHMTVFDN--- 94
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYAS----------------GKARLISFL---PKFSRNKLIFIDqlq 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 --IAFGLTVLPRrDRPTAAaiktkvtqllemvqlahladrfpaqLSGGQKQRVALARALAVEPQ--ILLLDEPFGALDAQ 170
Cdd:cd03238 70 flIDVGLGYLTL-GQKLST-------------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17865703 171 VRKELRRWLRQLhEELKFTSVFVTHDqEEATEVADRVVVMSQG 213
Cdd:cd03238 124 DINQLLEVIKGL-IDLGNTVILIEHN-LDVLSSADWIIDFGPG 164
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-219 |
2.96e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.64 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 7 RIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFhgtdvsrlhARERKVGFVFQHYALF 86
Cdd:PRK10636 317 KVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIKLGYFAQHQLEF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 87 --------RHMTvfdNIAFGLTVLPRRDRPTAAAIK-TKVTQLLEmvqlahladRFpaqlSGGQKQRVALARALAVEPQI 157
Cdd:PRK10636 388 lradesplQHLA---RLAPQELEQKLRDYLGGFGFQgDKVTEETR---------RF----SGGEKARLVLALIVWQRPNL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 158 LLLDEPFGALDAQVRKELRRWLRQLHEELkftsVFVTHDQEEATEVADRVVVMSQGNIEQAD 219
Cdd:PRK10636 452 LLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVEPFD 509
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-232 |
3.16e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSR--LHARERKVGFVFQHYALFRHMTVFDn 94
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFSGTVRFN- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 iafgltVLPRRDRPTAaaiktkvtQLLEMVQLAHLAD---RFPAQL-----------SGGQKQRVALARALAVEPQILLL 160
Cdd:PLN03232 1330 ------IDPFSEHNDA--------DLWEALERAHIKDvidRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 161 DEPFGALDAQVRKELRRWLRqlhEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPDRVWREPATRF 232
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIR---EEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
10-196 |
3.88e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 55.79 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 10 KSFGRTQVLndislDIPSGqMVALLGPSGSGKTTLLRIIA-GLEHQSSGHIRFHgTDVSRLHARERKVGFVFQH----YA 84
Cdd:COG0419 11 RSYRDTETI-----DFDDG-LNLIVGPNGAGKSTILEAIRyALYGKARSRSKLR-SDLINVGSEEASVELEFEHggkrYR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 85 LFRH---------------MTVFDNIaFGLTVLPRRDRPTAAAIKTKVTQLLEMVQLAHLADRF---------PAQLSGG 140
Cdd:COG0419 84 IERRqgefaefleakpserKEALKRL-LGLEIYEELKERLKELEEALESALEELAELQKLKQEIlaqlsgldpIETLSGG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 141 QKQRVALARALAvepqiLLLDepFGALDAQVRKELRRWLRQLHeelkftsvFVTHD 196
Cdd:COG0419 163 ERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-195 |
7.21e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRF---HGTDVSRLHARERKVGFVFQHYALFRHmTVF 92
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndsHNLKDINLKWWRSKIGVVSQDPLLFSN-SIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 93 DNIAFGLTVLP---------------------RRDRPTAAAI--------KTKVTQLLEMVQ-----------------L 126
Cdd:PTZ00265 478 NNIKYSLYSLKdlealsnyynedgndsqenknKRNSCRAKCAgdlndmsnTTDSNELIEMRKnyqtikdsevvdvskkvL 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 127 AH-----LADRF-------PAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVT 194
Cdd:PTZ00265 558 IHdfvsaLPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
|
.
gi 17865703 195 H 195
Cdd:PTZ00265 638 H 638
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-198 |
7.77e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFhGTDVsrlharerKVGFVFQHYA-LFRHMTVFDN 94
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL--------EVAYFDQHRAeLDPEKTVMDN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGltvlprrdrptaaaiKTKVtqlleMVQ------LAHLAD--------RFPAQ-LSGGQKQRVALARALAVEPQILL 159
Cdd:PRK11147 404 LAEG---------------KQEV-----MVNgrprhvLGYLQDflfhpkraMTPVKaLSGGERNRLLLARLFLKPSNLLI 463
|
170 180 190
....*....|....*....|....*....|....*....
gi 17865703 160 LDEPFGALDAQVRkELrrwLRQLHEELKFTSVFVTHDQE 198
Cdd:PRK11147 464 LDEPTNDLDVETL-EL---LEELLDSYQGTVLLVSHDRQ 498
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-196 |
2.60e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 3 IEIARIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHirfhgtdVSrLHARERkVGFVFQH 82
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGN-------VS-LDPNER-LGKLRQD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 83 YALFRHMTVFDNIAFGLT----VLPRRDRPTAaaiktkvtqLLEM-----VQLAHLADRFpAQLSG-------------- 139
Cdd:PRK15064 73 QFAFEEFTVLDTVIMGHTelweVKQERDRIYA---------LPEMseedgMKVADLEVKF-AEMDGytaearagelllgv 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17865703 140 ----------------GQKQRVALARALAVEPQILLLDEPFGALDAQVrkelRRWLRQLHEELKFTSVFVTHD 196
Cdd:PRK15064 143 gipeeqhyglmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISHD 211
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-195 |
4.05e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTdvsrlharerkVGFVFQHYALFRHMTVFDNIAF 97
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIAISSGLNGQLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 98 -GLTVLPRRDRptaaaIKTKVTQLLEMVQLAHLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELR 176
Cdd:PRK13545 109 kGLMMGLTKEK-----IKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170
....*....|....*....
gi 17865703 177 RWLRQLHEELKfTSVFVTH 195
Cdd:PRK13545 184 DKMNEFKEQGK-TIFFISH 201
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-222 |
4.80e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.13 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARE-RKV-GFVFQHYALFRHMTVFDN 94
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlRKVlGIIPQAPVLFSGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 95 IAFGltvlprrdrptaaaiKTKVTQLLEMVQLAHLAD---RFPAQL-----------SGGQKQRVALARALAVEPQILLL 160
Cdd:PLN03130 1334 DPFN---------------EHNDADLWESLERAHLKDvirRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVL 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 161 DEPFGAL----DAQVRKELRrwlrqlhEELKFTSVFVTHDQEEATEVADRVVVMSQGNIEQADAPD 222
Cdd:PLN03130 1399 DEATAAVdvrtDALIQKTIR-------EEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPE 1457
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-215 |
6.69e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 31 VALLGPSGSGKTTLLRIIAGLEHQSSGHIrFHGTDVsrlharerKVGFVFQHYAlfrhmtvfDNIAFGLTVLPRRDRPTA 110
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKV--------RMAVFSQHHV--------DGLDLSSNPLLYMMRCFP 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 111 AAIKTKVTQLLEMVQLA-HLADRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkft 189
Cdd:PLN03073 601 GVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGV--- 677
|
170 180
....*....|....*....|....*.
gi 17865703 190 sVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PLN03073 678 -LMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-180 |
7.51e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.47 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQS--SGHIRFHGTDvSRLHARERKVGFVFQHYALFRHMTV 91
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP-KKQETFARISGYCEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 92 FDNIAFglTVLPRRDRPTAAAIKTK-VTQLLEMVQLAHLADR---FPA--QLSGGQKQRVALARALAVEPQILLLDEPFG 165
Cdd:PLN03140 971 RESLIY--SAFLRLPKEVSKEEKMMfVDEVMELVELDNLKDAivgLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170
....*....|....*
gi 17865703 166 ALDAQVRKELRRWLR 180
Cdd:PLN03140 1049 GLDARAAAIVMRTVR 1063
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
19-210 |
1.05e-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: 48.12 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 19 NDISLdiPSGQMVALLGPSGSGKTTLLRIIAglehqssghirfhgtdvsrlharerkvgfvfqhYALFRHMTVfdniafg 98
Cdd:cd03227 14 NDVTF--GEGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSA------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 99 ltvLPRRDRPTAAAIKTKVTqlLEMVQLAHladrfpaQLSGGQKQRVALARALA----VEPQILLLDEPFGALDAQVRKE 174
Cdd:cd03227 52 ---TRRRSGVKAGCIVAAVS--AELIFTRL-------QLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQA 119
|
170 180 190
....*....|....*....|....*....|....*.
gi 17865703 175 LRRWLRqLHEELKFTSVFVTHDqEEATEVADRVVVM 210
Cdd:cd03227 120 LAEAIL-EHLVKGAQVIVITHL-PELAELADKLIHI 153
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-210 |
1.18e-06 |
|
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: 48.80 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 1 MSIEIARIKK--SFGRTQVLNDISLDIPSgqMVALLGPSGSGKTTLLRIIA-GLEHQSSGHIRFHGTDVSRLHA-RERKV 76
Cdd:cd03279 1 MKPLKLELKNfgPFREEQVIDFTGLDNNG--LFLICGPTGAGKSTILDAITyALYGKTPRYGRQENLRSVFAPGeDTAEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 77 GFVFQ----HYALFR--HMTV--FDNIAFgltvLP--RRDRPTAAAIKTkvtqllemvqlahladrfpaqLSGGQKQRVA 146
Cdd:cd03279 79 SFTFQlggkKYRVERsrGLDYdqFTRIVL----LPqgEFDRFLARPVST---------------------LSGGETFLAS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865703 147 LARALAVEPQI----------LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVfVTHDQEEATEVADRVVVM 210
Cdd:cd03279 134 LSLALALSEVLqnrggarleaLFIDEGFGTLDPEALEAVATALELIRTENRMVGV-ISHVEELKERIPQRLEVI 206
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
14-213 |
1.30e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.79 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTL----------LRIIAGLehqSSGHIRFHGT----DVSRLH------ARE 73
Cdd:cd03270 7 REHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESL---SAYARQFLGQmdkpDVDSIEglspaiAID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 74 RK---------VGFVFQHYALFRhmtvfdniafgltVLPRRdrptaAAIKTKVTQLLEmVQLAHLA-DRFPAQLSGGQKQ 143
Cdd:cd03270 84 QKttsrnprstVGTVTEIYDYLR-------------LLFAR-----VGIRERLGFLVD-VGLGYLTlSRSAPTLSGGEAQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 144 RVALARALAVEPQ--ILLLDEPFGALDAQVRKELRRWLRQLhEELKFTSVFVTHDqEEATEVADRVVVMSQG 213
Cdd:cd03270 145 RIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD-EDTIRAADHVIDIGPG 214
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-168 |
1.34e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 11 SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAglEHQSSG--------HIRFH-------------GTDVSRL 69
Cdd:PLN03073 186 SVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDGipkncqilHVEQEvvgddttalqcvlNTDIERT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 70 HARERKVGFVFQHyalfrhMTVFDNIAFGLTVLPRRDRPTAAAIKTKVTQL---LEMVQ-----------LAHLA----- 130
Cdd:PLN03073 264 QLLEEEAQLVAQQ------RELEFETETGKGKGANKDGVDKDAVSQRLEEIykrLELIDaytaearaasiLAGLSftpem 337
|
170 180 190
....*....|....*....|....*....|....*....
gi 17865703 131 -DRFPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
Cdd:PLN03073 338 qVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-215 |
1.60e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.23 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 14 RTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQS---SGHIRFHGTDVSRLHAReRKVGFVFQHYALFRH 88
Cdd:PLN03140 175 KTKltILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPR-KTSAYISQNDVHVGV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 89 MTVFDNIAFG------------LTVLPRRDRPT-------------AAAIKTKVTQL----------LEMVQLAHLADRF 133
Cdd:PLN03140 254 MTVKETLDFSarcqgvgtrydlLSELARREKDAgifpeaevdlfmkATAMEGVKSSLitdytlkilgLDICKDTIVGDEM 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 134 PAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLhEELKFTSVFVTHDQ--EEATEVADRVVVMS 211
Cdd:PLN03140 334 IRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQI-VHLTEATVLMSLLQpaPETFDLFDDIILLS 412
|
....
gi 17865703 212 QGNI 215
Cdd:PLN03140 413 EGQI 416
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2-215 |
2.89e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 2 SIEIARikksfGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGT-------------DVSR 68
Cdd:PRK10636 6 SLQIRR-----GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetpalPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 69 LHarerkvgFVFQHYALFRHMTVFDNIAFG-------LTVLPRRDRPTAAAIKTKVTQLLEMV-----QLAHLADRFpaq 136
Cdd:PRK10636 81 LE-------YVIDGDREYRQLEAQLHDANErndghaiATIHGKLDAIDAWTIRSRAASLLHGLgfsneQLERPVSDF--- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17865703 137 lSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkftsVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:PRK10636 151 -SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTL----ILISHDRDFLDPIVDKIIHIEQQSL 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-215 |
4.59e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLE--HQSSGHIRFHGT--DVSRLH-ARERKVGFVFQ---HYALFR 87
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKevDVSTVSdAIDAGLAYVTEdrkGYGLNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 88 HMTVFDNIAfgLTVLPR--------RDRPTAAA------IKTKVTQLLEMVqlahladrfpAQLSGGQKQRVALARALAV 153
Cdd:NF040905 354 IDDIKRNIT--LANLGKvsrrgvidENEEIKVAeeyrkkMNIKTPSVFQKV----------GNLSGGNQQKVVLSKWLFT 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17865703 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEATEVADRVVVMSQGNI 215
Cdd:NF040905 422 DPDVLILDEPTRGIDVGAKYEIYTIINELAAEGK-GVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
136-207 |
8.24e-05 |
|
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: 43.40 E-value: 8.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 136 QLSGGQKQRVALARALA---VEPQ-ILLLDEPFGALDAQVRKELRRWLRQLHEELKFtsvFVTHDQEEATEVADRV 207
Cdd:cd03272 158 QLSGGQKSLVALALIFAiqkCDPApFYLFDEIDAALDAQYRTAVANMIKELSDGAQF---ITTTFRPELLEVADKF 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
86-213 |
9.67e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 86 FRHMTVFDNIAF--GLTVLPRRD---RPTAAAIKTKVTQLLEmVQLAHLA-DRFPAQLSGGQKQRVALARALAVEPQ--I 157
Cdd:TIGR00630 433 VSELSIREAHEFfnQLTLTPEEKkiaEEVLKEIRERLGFLID-VGLDYLSlSRAAGTLSGGEAQRIRLATQIGSGLTgvL 511
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 17865703 158 LLLDEPFGALDAQVRKELRRWLRQLhEELKFTSVFVTHDqEEATEVADRVVVMSQG 213
Cdd:TIGR00630 512 YVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYVIDIGPG 565
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
18-45 |
1.06e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 1.06e-04
10 20
....*....|....*....|....*...
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLL 45
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
35-84 |
2.01e-04 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 41.72 E-value: 2.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 17865703 35 GPSGSGKTTLLRIIA---GLEHQSSGHIrFHGTdvsrlhARERKVGFV-FQHYA 84
Cdd:PRK04182 7 GPPGSGKTTVARLLAeklGLKHVSAGEI-FREL------AKERGMSLEeFNKYA 53
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
31-76 |
2.26e-04 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 40.93 E-value: 2.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 17865703 31 VALLGPSGSGKTTLLRIIA---GLEHQSSGHIRFHgtDVSRL---HARERKV 76
Cdd:cd02020 2 IAIDGPAGSGKSTVAKLLAkklGLPYLDTGGIRTE--EVGKLaseVAAIPEV 51
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
137-211 |
3.66e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 137 LSGGQKQ------RVALARALAVEPQILLLDEPFGALDAQVRKEL----RRWLRQLHEelkftSVFVTHDqEEATEVADR 206
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLvdimERYLRKIPQ-----VIIVSHD-EELKDAADY 862
|
....*
gi 17865703 207 VVVMS 211
Cdd:PRK03918 863 VIRVS 867
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
135-181 |
8.29e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.98 E-value: 8.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 135 AQLSGGQKQR---VALARALA----------VEPQILLLDEPFGALDAQVRKELRRWLRQ 181
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
18-44 |
9.45e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 9.45e-04
10 20
....*....|....*....|....*..
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTL 44
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
18-45 |
9.76e-04 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 40.29 E-value: 9.76e-04
10 20
....*....|....*....|....*...
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLL 45
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI 38
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
18-44 |
1.39e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 1.39e-03
10 20
....*....|....*....|....*..
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTL 44
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-221 |
1.43e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.92 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIRFHGTDVSRLHARERKVGFvfqhyalfrHMTVFDNIA 96
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF---------SMIPQDPVL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 97 FGLTVLPRRDrPTAAAIKTKVTQLLEMVQlahLADRFPAQLSG--------------GQKQRVALARALAVEPQ-ILLLD 161
Cdd:PTZ00243 1396 FDGTVRQNVD-PFLEASSAEVWAALELVG---LRERVASESEGidsrvleggsnysvGQRQLMCMARALLKKGSgFILMD 1471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17865703 162 EPFG----ALDAQVRKELRRWLRqlheelKFTSVFVTHDQEEATEVaDRVVVMSQGNIEQADAP 221
Cdd:PTZ00243 1472 EATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSP 1528
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-208 |
2.00e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 131 DRFPAQLSGGQKQRVALARALAVEPQ--ILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDqEEATEVADRVV 208
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHD-EQMISLADRII 548
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
18-45 |
2.40e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 2.40e-03
10 20
....*....|....*....|....*...
gi 17865703 18 LNDISLDIPSGQMVALLGPSGSGKTTLL 45
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| cyt_kin_arch |
TIGR02173 |
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ... |
30-59 |
2.54e-03 |
|
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017.
Pssm-ID: 274012 [Multi-domain] Cd Length: 171 Bit Score: 38.17 E-value: 2.54e-03
10 20 30
....*....|....*....|....*....|...
gi 17865703 30 MVALLGPSGSGKTTLLRIIA---GLEHQSSGHI 59
Cdd:TIGR02173 2 IITISGPPGSGKTTVAKILAeklSLKLISAGDI 34
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
14-44 |
2.57e-03 |
|
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: 40.00 E-value: 2.57e-03
10 20 30
....*....|....*....|....*....|.
gi 17865703 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTL 44
Cdd:TIGR00630 8 REHNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
27-60 |
2.64e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.53 E-value: 2.64e-03
10 20 30
....*....|....*....|....*....|....
gi 17865703 27 SGQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIR 60
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEIS 117
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
28-60 |
2.74e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.15 E-value: 2.74e-03
10 20 30
....*....|....*....|....*....|...
gi 17865703 28 GQMVALLGPSGSGKTTLLRIIAGLEHQSSGHIR 60
Cdd:PRK01889 195 GKTVALLGSSGVGKSTLVNALLGEEVQKTGAVR 227
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
136-208 |
2.99e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 2.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17865703 136 QLSGGQKQRVALARALA---VEPQ-ILLLDEPFGALDAQVRKELRRWLRQLHEELKFtsvFVTHDQEEATEVADRVV 208
Cdd:pfam02463 1077 LLSGGEKTLVALALIFAiqkYKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQF---IVISLREEMLEKADKLV 1150
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
14-44 |
4.57e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.90 E-value: 4.57e-03
10 20 30
....*....|....*....|....*....|.
gi 17865703 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTL 44
Cdd:PRK00349 12 REHNLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| DLIC |
pfam05783 |
Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein ... |
25-57 |
4.99e-03 |
|
Dynein light intermediate chain (DLIC); This family consists of several eukaryotic dynein light intermediate chain proteins. The light intermediate chains (LICs) of cytoplasmic dynein consist of multiple isoforms, which undergo post-translational modification to produce a large number of species. DLIC1 is known to be involved in assembly, organization, and function of centrosomes and mitotic spindles when bound to pericentrin. DLIC2 is a subunit of cytoplasmic dynein 2 that may play a role in maintaining Golgi organization by binding cytoplasmic dynein 2 to its Golgi-associated cargo.
Pssm-ID: 368612 Cd Length: 468 Bit Score: 38.67 E-value: 4.99e-03
10 20 30
....*....|....*....|....*....|...
gi 17865703 25 IPSGQMVALLGPSGSGKTTLLRIIAGLEHQSSG 57
Cdd:pfam05783 22 LPSGKNVLVLGEDGSGKTTLIAKLQGVEHPKKG 54
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
241-282 |
5.68e-03 |
|
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common architecture comprising two variable hydrophobic transmembrane domains (TMDs) that form the translocation pathway and two conserved hydrophilic ABC-ATPases that hydrolyze ATP. This is the C-terminal regulatory domain found at the ATPase subunit of CysA, a putative sulfate ABC transporter from Alicyclobacillus acidocaldarius. The regulatory domain of CysA is built up of an elongated beta-barrel composed of two beta-sandwiches that form a common hydrophobic core.
Pssm-ID: 465531 [Multi-domain] Cd Length: 43 Bit Score: 34.34 E-value: 5.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 17865703 241 NRLTGTVRGGQFHVGAHRWPLGYTPAYQG-PVDLFLRPWEVDI 282
Cdd:pfam17850 1 NLFHGRVEDGRVRIGGLALPLPELAGAEGsEVVAYVRPHDLEI 43
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
14-80 |
8.61e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 36.36 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17865703 14 RTQVLNDISLDIPSGqmVALLGPSGSGKTTLLRIIAGL------------------EHQSSGHIRFHGTDVSRLHARERK 75
Cdd:cd00009 7 IEALREALELPPPKN--LLLYGPPGTGKTTLARAIANElfrpgapflylnasdlleGLVVAELFGHFLVRLLFELAEKAK 84
|
....*
gi 17865703 76 VGFVF 80
Cdd:cd00009 85 PGVLF 89
|
|
| |
