|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-369 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 556.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAM 80
Cdd:COG3839 1 MASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 161 PLSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVA 240
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRL-GTTTIYVTHDQVEAMTLADRIAVMNDGR-------IQQVGTPEELYDRPANLFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 241 GFIGSPRMNFLPGRIA--SFDAQGVVVALDhthenvhvpvDGAALQVSQAVTLGVRPEHLEFVDSssshDDAILSRAVSL 318
Cdd:COG3839 232 GFIGSPPMNLLPGTVEggGVRLGGVRLPLP----------AALAAAAGGEVTLGIRPEHLRLADE----GDGGLEATVEV 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1431886808 319 VEQLGEHSYVHLDqPGGAALIAKAPGDTRLAPGDRANLRVPRHATHLFTED 369
Cdd:COG3839 298 VEPLGSETLVHVR-LGGQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAE 347
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-376 |
0e+00 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 531.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAM 80
Cdd:PRK11000 1 MASVTLRNVTKAYGD-VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 161 PLSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVA 240
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRL-GRTMIYVTHDQVEAMTLADKIVVLDAGR-------VAQVGKPLELYHYPANRFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 241 GFIGSPRMNFLPGRIASFDAQGVVVALDhTHENVHVPVDGAALQVSQAVTLGVRPEHLefvdSSSSHDDAILSRAVSLVE 320
Cdd:PRK11000 232 GFIGSPKMNFLPVKVTATAIEQVQVELP-NRQQVWLPVEGRGVQVGANMSLGIRPEHL----LPSDIADVTLEGEVQVVE 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 321 QLGEHSYVHLDQPGG-AALIAKAPGDTRLAPGDRANLRVPRHATHLFTEDGFAAPSL 376
Cdd:PRK11000 307 QLGNETQIHIQIPAIrQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGTACRRL 363
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-370 |
2.32e-175 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 492.05 E-value: 2.32e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAM 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 161 PLSNLDATLRGQTRIEIARLHKQFAKASvVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVA 240
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTS-LYVTHDQVEAMTLADRVVVMNGGV-------AEQIGTPVEVYEKPASTFVA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 241 GFIGSPRMNFLPGRIasfDAQGVVVALDhthENVHVPVDGA-ALQVSQAVTLGVRPEHLEFVDsssshDDAILSRAVSLV 319
Cdd:PRK11650 233 SFIGSPAMNLLDGRV---SADGAAFELA---GGIALPLGGGyRQYAGRKLTLGIRPEHIALSS-----AEGGVPLTVDTV 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1431886808 320 EQLGEHSYVHLDQpGGAALIAKAPGDTRLAPGDRANLRVPRHATHLFTEDG 370
Cdd:PRK11650 302 ELLGADNLAHGRW-GGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADT 351
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-368 |
3.20e-153 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 435.68 E-value: 3.20e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAM 80
Cdd:COG3842 3 MPALELENVSKRYGD-VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 161 PLSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVA 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQREL-GITFIYVTHDQEEALALADRIAVMNDGR-------IEQVGTPEEIYERPATRFVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 241 GFIGspRMNFLPGRIASfDAQGVVVALDHThenVHVPVDgAALQVSQAVTLGVRPEHLEFVDSSsshDDAILSRAVSLVE 320
Cdd:COG3842 234 DFIG--EANLLPGTVLG-DEGGGVRTGGRT---LEVPAD-AGLAAGGPVTVAIRPEDIRLSPEG---PENGLPGTVEDVV 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1431886808 321 QLGEHSYVHLDQPGGAALIAKAPGDTR--LAPGDRANLRVPRHATHLFTE 368
Cdd:COG3842 304 FLGSHVRYRVRLGDGQELVVRVPNRAAlpLEPGDRVGLSWDPEDVVVLPA 353
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-225 |
2.66e-122 |
|
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: 351.94 E-value: 2.66e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVFQ 83
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 164 NLDATLRGQTRIEIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIG 225
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRL-GTTTIYVTHDQVEAMTMADRIAVMNDGQ-------IQQIG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-308 |
3.40e-113 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 334.99 E-value: 3.40e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYgDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVFQ 83
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 164 NLDATLRGQTRIEIARLHKQFAkASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVAGFI 243
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRKLG-ITFVFVTHDQEEALTMSDRIVVMRDGR-------IEQDGTPREIYEEPKNLFVARFI 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 244 GSprMNFLPGR-IASFDAQGVVVALDHTHENVHVPVDgaaLQVSQAVTLGVRPE--HLEFVDSSSSHD 308
Cdd:PRK09452 246 GE--INIFDATvIERLDEQRVRANVEGRECNIYVNFA---VEPGQKLHVLLRPEdlRVEEINDDEHAE 308
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-244 |
7.69e-110 |
|
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: 321.11 E-value: 7.69e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGaPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVFQ 83
Cdd:cd03300 1 IELENVSKFYGGF-VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 164 NLDATLRGQTRIEIARLHKQFAkASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVAGFI 243
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELG-ITFVFVTHDQEEALTMSDRIAVMNKGK-------IQQIGTPEEIYEEPANRFVADFI 231
|
.
gi 1431886808 244 G 244
Cdd:cd03300 232 G 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-365 |
5.99e-107 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 317.86 E-value: 5.99e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN-DVPAAQRGVAMV 81
Cdd:COG1118 2 SIEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEP 161
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 162 LSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVAG 241
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDEL-GGTTVFVTHDQEEALELADRVVVMNQGR-------IEQVGTPDEVYDRPATPFVAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 242 FIGSprMNFLPGRIASfdaqGVVVAldhthENVHVPVDGAALQvsQAVTLGVRPEHLEFVDssSSHDDAILSRAVSLVEQ 321
Cdd:COG1118 233 FLGC--VNVLRGRVIG----GQLEA-----DGLTLPVAEPLPD--GPAVAGVRPHDIEVSR--EPEGENTFPATVARVSE 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1431886808 322 LGEHS--YVHLDQPGGAALIAKAPGDT----RLAPGDRANLRVPRHATHL 365
Cdd:COG1118 298 LGPEVrvELKLEDGEGQPLEAEVTKEAwaelGLAPGDPVYLRPRPARVFL 347
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-225 |
2.72e-103 |
|
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: 303.67 E-value: 2.72e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVFQ 83
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 164 NLDATLRGQTRIEIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIG 225
Cdd:cd03259 160 ALDAKLREELREELKELQREL-GITTIYVTHDQEEALALADRIAVMNEGR-------IVQVG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-366 |
4.77e-95 |
|
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: 287.70 E-value: 4.77e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDGApVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAM 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFT-ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 161 PLSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVA 240
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRL-GVTTIMVTHDQEEALSMADRIVVMNHGV-------IEQVGTPQEIYRHPATPFVA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 241 GFIGspRMNFLPGRIASfDAQGVVVALDHThenvhvpVDGAALQVSQAVTLGVRPEHLEFvdSSSSHDDAILSRAVSLVE 320
Cdd:TIGR03265 233 DFVG--EVNWLPGTRGG-GSRARVGGLTLA-------CAPGLAQPGASVRLAVRPEDIRV--SPAGNAANLLLARVEDME 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 321 QLGEHSYVHLDQPG--GAALIAKAPGDTR----LAPGDRANLRVPRHATHLF 366
Cdd:TIGR03265 301 FLGAFYRLRLRLEGlpGQALVADVSASEVerlgIRAGQPIWIELPAERLRAF 352
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-366 |
1.02e-92 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 281.89 E-value: 1.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 2 ASISLRGVQKAYGDGAPVI---RDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMND-----VPA 73
Cdd:NF040933 1 VTVRVENVTKIFKKGKKEVvalDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 74 AQRGVAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQP 153
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 154 GVFLFDEPLSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDQIEAMTLADKI-VLLHagkdteryGSIAQIGAPLELYH 232
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQREL-KITTIIVSHDPADIFSLADRAgVINN--------GKFQQVGKPEEIYD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 233 RPRSRFVAGFIGSprMNFLPGRIASfdaQGVVVAldhthENVHVPVDGAALQVSQAVtLGVRPEHLEFVDS--SSSHDDA 310
Cdd:NF040933 232 NPANIFVARLIGD--INLLEGKVEE---EGLVDG-----NDLKIPLPNPKLEAGEVI-IGIRPEDIDISESdmRLPPGFV 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 311 ILSRA-VSLVEQLGEHSYVHLDQPGGAALIAKAPGDTRLAPGDRANLRVPRHATHLF 366
Cdd:NF040933 301 EVGKGrVKVSSYAGGVFRVVVSPIDDDSIEIIVNSDRPIEEGEEVNLYVRPDKIKIF 357
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-343 |
8.73e-91 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 276.99 E-value: 8.73e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 6 LRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVFQSY 85
Cdd:PRK11432 9 LKNITKRFGS-NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 86 ALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNL 165
Cdd:PRK11432 88 ALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 166 DATLRGQTRIEIARLHKQFAKASvVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVAGFIGS 245
Cdd:PRK11432 168 DANLRRSMREKIRELQQQFNITS-LYVTHDQSEAFAVSDTVIVMNKGK-------IMQIGSPQELYRQPASRFMASFMGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 246 PrmNFLPGRIasfdAQGVVVALDHthenvHVPV-DGAALQVSQ-AVTLGVRPE------------------------HLE 299
Cdd:PRK11432 240 A--NIFPATL----SGDYVDIYGY-----RLPRpAAFAFNLPDgECTVGVRPEaitlseqgeesqrctikhvaymgpQYE 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1431886808 300 FVDSSSSHDDAILSRAVSLVEQLGEHSYVHLdQPGGAALIAKAP 343
Cdd:PRK11432 309 VTVDWHGQELLLQVNATQLQPDLGEHYYLEI-HPYGMFLLADAA 351
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-245 |
4.59e-88 |
|
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: 266.13 E-value: 4.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVF 82
Cdd:cd03296 2 SIEVRNVSKRFGD-FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 QSYALFPHMTVFENMAFGLKLAK----TPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLF 158
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPrserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 159 DEPLSNLDATLRGQTRIEIARLHKQFAKASvVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRF 238
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTT-VFVTHDQEEALEVADRVVVMNKGR-------IEQVGTPDEVYDHPASPF 232
|
....*..
gi 1431886808 239 VAGFIGS 245
Cdd:cd03296 233 VYSFLGE 239
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-340 |
4.32e-87 |
|
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: 266.67 E-value: 4.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 36 LGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKV 115
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 116 REAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFAkASVVYVTHD 195
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG-ITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 196 QIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVAGFIGSprMNFLPGRIASFDAQGVVVALDHTHE--- 272
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGK-------IAQIGTPEEIYEEPANLFVARFIGE--INVFEATVIERKSEQVVLAGVEGRRcdi 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 273 NVHVPVDGAalqvsQAVTLGVRPEHLEFVD-SSSSHDDAILSrAVSLVEQLGEHSYVHLD-QPGGAALIA 340
Cdd:TIGR01187 232 YTDVPVEKD-----QPLHVVLRPEKIVIEEeDEANSSNAIIG-HVIDITYLGMTLEVHVRlETGQKVLVS 295
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-239 |
5.06e-81 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 248.47 E-value: 5.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDGA---PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEvmnDVPAAQRG 77
Cdd:COG1116 5 APALELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK---PVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 VAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFL 157
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 158 FDEPLSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLhagkdTERYGSIAQ---IGAPlelyhRP 234
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQET-GKTVLFVTHDVDEAVFLADRVVVL-----SARPGRIVEeidVDLP-----RP 230
|
....*
gi 1431886808 235 RSRFV 239
Cdd:COG1116 231 RDREL 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-244 |
5.86e-78 |
|
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: 239.93 E-value: 5.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGapVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVFQ 83
Cdd:cd03299 1 LKVENLSKDWKEF--KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 164 NLDATLRGQTRIEIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVAGFI 243
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEF-GVTVLHVTHDFEEAWALADKVAIMLNGK-------LIQVGKPEEVFKKPKNEFVAEFL 230
|
.
gi 1431886808 244 G 244
Cdd:cd03299 231 G 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-211 |
6.61e-77 |
|
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: 236.60 E-value: 6.61e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGA---PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAqrgVAM 80
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1431886808 161 PLSNLDATLRGQTRIEIARLHKQfAKASVVYVTHDQIEAMTLADKIVLLHA 211
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRE-TGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-351 |
1.67e-74 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 235.89 E-value: 1.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYgDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVFQ 83
Cdd:PRK11607 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 164 NLDATLRGQTRIEIARLHKQFAkASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVAGFI 243
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVG-VTCVMVTHDQEEAMTMAGRIAIMNRGK-------FVQIGEPEEIYEHPTTRYSAEFI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 244 GSprMNFLPGRIASFDAQGVVV---ALDH---THENVHVpVDGAALQVSqavtlgVRPEHLEFVDSSSSHDDAILSRAVS 317
Cdd:PRK11607 251 GS--VNVFEGVLKERQEDGLVIdspGLVHplkVDADASV-VDNVPVHVA------LRPEKIMLCEEPPADGCNFAVGEVI 321
|
330 340 350
....*....|....*....|....*....|....
gi 1431886808 318 LVEQLGEHSYVHLDQPGGAALIAKAPGDTRLAPG 351
Cdd:PRK11607 322 HIAYLGDLSIYHVRLKSGQMISAQLQNAHRYRKG 355
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-247 |
3.24e-74 |
|
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: 230.65 E-value: 3.24e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ--RGVAMV 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLE--ALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 160 EPLSNLDATLRGQTRIEIARLHKQFAKaSVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFV 239
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGK-TIVFVTHDIDEAFRLADRIAIMKNGE-------IVQVGTPDEILRSPANDFV 232
|
....*...
gi 1431886808 240 AGFIGSPR 247
Cdd:cd03295 233 AEFVGADR 240
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
4-298 |
9.52e-71 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 226.03 E-value: 9.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGL--EDLTDGDLFIGGEVMNDVPAAQRGVAMV 81
Cdd:TIGR03258 6 IRIDHLRVAYG-ANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFvkAAGLTGRIAIADRDLTHAPPHKRGLALL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEP 161
Cdd:TIGR03258 85 FQNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 162 LSNLDATLRGQTRIEIARLHKQFAKASVVYVTHDQIEAMTLADKIVLLhagkdteRYGSIAQIGAPLELYHRPRSRFVAG 241
Cdd:TIGR03258 165 LSALDANIRANMREEIAALHEELPELTILCVTHDQDDALTLADKAGIM-------KDGRLAAHGEPQALYDAPADGFAAE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 242 FIGspRMNFLPGRIASFDAQGVVVALDHTHENVHVPVDGAALQVSQavTLGVRPEHL 298
Cdd:TIGR03258 238 FLG--AANILPAIALGITEAPGLVDVSCGGAVIFAFGDGRHDGRDK--LACIRPEHL 290
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-255 |
3.89e-70 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 223.81 E-value: 3.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDGApVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVF 82
Cdd:PRK10851 2 SIEIANIKKSFGRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 QSYALFPHMTVFENMAFGLKL---AKTP-KDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLF 158
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVlprRERPnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 159 DEPLSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLhagkdteRYGSIAQIGAPLELYHRPRSRF 238
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEEL-KFTSVFVTHDQEEAMEVADRVVVM-------SQGNIEQAGTPDQVWREPATRF 232
|
250
....*....|....*..
gi 1431886808 239 VAGFIGSprMNFLPGRI 255
Cdd:PRK10851 233 VLEFMGE--VNRLQGTI 247
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-353 |
2.33e-67 |
|
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: 216.89 E-value: 2.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 22 DVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMND------VPAAQRGVAMVFQSYALFPHMTVFE 95
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 96 NMAFGLKLAKTPKDEIDrkVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRI 175
Cdd:COG4148 97 NLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 176 EIARLHKQFAkASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVAGfiGSPRMNFLPGRI 255
Cdd:COG4148 175 YLERLRDELD-IPILYVSHSLDEVARLADHVVLLEQGR-------VVASGPLAEVLSRPDLLPLAG--GEEAGSVLEATV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 256 ASFDAQGVVVALDHTHENVHVPvdGAALQVSQAVTLGVRPEH----LEFVDSSSshddaIL----SRAVSLVEQLGEHSY 327
Cdd:COG4148 245 AAHDPDYGLTRLALGGGRLWVP--RLDLPPGTRVRVRIRARDvslaLEPPEGSS-----ILnilpGRVVEIEPADGGQVL 317
|
330 340 350
....*....|....*....|....*....|
gi 1431886808 328 VHLDqPGGAALIA----KAPGDTRLAPGDR 353
Cdd:COG4148 318 VRLD-LGGQTLLAritrRSADELGLAPGQT 346
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-213 |
2.17e-64 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 204.89 E-value: 2.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MAS-ISLRGVQKAYGDGA---PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQR 76
Cdd:COG1136 1 MSPlLELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 77 G------VAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIV 150
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1431886808 151 RQPGVFLFDEPLSNLDAtlrgQTRIEIARLHKQFAK---ASVVYVTHDQiEAMTLADKIVLLHAGK 213
Cdd:COG1136 161 NRPKLILADEPTGNLDS----KTGEEVLELLRELNRelgTTIVMVTHDP-ELAARADRVIRLRDGR 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-213 |
1.35e-63 |
|
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: 200.88 E-value: 1.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMND----VPAAQRGVA 79
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFPHMTVFENMAFGlklaktpkdeidrkvreaarilqleallerrpkaLSGGQRQRVAIGRAIVRQPGVFLFD 159
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 160 EPLSNLDATLRGQTRIEIARLHKQFAKAsVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGIT-VVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
20-263 |
6.37e-62 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 203.16 E-value: 6.37e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ------RGVAMVFQSYALFPHMTV 93
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevrrKKIGMVFQQFALFPHMTI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 94 FENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQT 173
Cdd:TIGR01186 89 LQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 174 RIEIARLHKQFAKaSVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVAGFIGSPRMnflpg 253
Cdd:TIGR01186 169 QDELKKLQATLQK-TIVFITHDLDEAIRIGDRIVIMKAGE-------IVQVGTPDEILRNPANEYVEEFIGKVDL----- 235
|
250
....*....|
gi 1431886808 254 rIASFDAQGV 263
Cdd:TIGR01186 236 -SQVFDAERI 244
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-213 |
1.67e-61 |
|
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: 196.94 E-value: 1.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGA---PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG--- 77
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 ---VAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPG 154
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 155 VFLFDEPLSNLDAtlrgQTRIEIARLHKQFAK---ASVVYVTHDQiEAMTLADKIVLLHAGK 213
Cdd:cd03255 161 IILADEPTGNLDS----ETGKEVMELLRELNKeagTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-243 |
2.06e-61 |
|
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: 198.64 E-value: 2.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ------RGVAMVFQSYALFPHMTV 93
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 94 FENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQT 173
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 174 RIEIARLHKQFAKaSVVYVTHDQIEAMTLADKIVLLhagKDteryGSIAQIGAPLELYHRPRSRFVAGFI 243
Cdd:cd03294 200 QDELLRLQAELQK-TIVFITHDLDEALRLGDRIAIM---KD----GRLVQVGTPEEILTNPANDYVREFF 261
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-235 |
4.39e-61 |
|
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: 196.40 E-value: 4.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ--RGVAMV 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQS--YALFpHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFD 159
Cdd:COG1122 81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 160 EPLSNLDatLRGQTRIE--IARLHKQfaKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPR 235
Cdd:COG1122 160 EPTAGLD--PRGRRELLelLKRLNKE--GKTVIIVTHDLDLVAELADRVIVLDDGR-------IVADGTPREVFSDYE 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-213 |
2.25e-60 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 194.50 E-value: 2.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFcVFL-GPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN-----DVPAAQRG 77
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEF-VFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 VAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFL 157
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 158 FDEPLSNLDAtlrgQTRIEIARLHKQFAKA--SVVYVTHDQ--IEAMtlADKIVLLHAGK 213
Cdd:COG2884 161 ADEPTGNLDP----ETSWEIMELLEEINRRgtTVLIATHDLelVDRM--PKRVLELEDGR 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-213 |
2.77e-60 |
|
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: 193.67 E-value: 2.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 22 DVDLEIGEnEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMND------VPAAQRGVAMVFQSYALFPHMTVFE 95
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 96 NMAFGLKLAKTPKDEIdrKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRI 175
Cdd:cd03297 95 NLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1431886808 176 EIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03297 173 ELKQIKKNL-NIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-236 |
6.02e-59 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 191.36 E-value: 6.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN----DVPAAQRGVA 79
Cdd:COG1126 2 IEIENLHKSFGD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFPHMTVFENMAFGL-KLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLF 158
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 159 DEPLSNLDATLRGqtriEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRS 236
Cdd:COG1126 161 DEPTSALDPELVG----EVLDVMRDLAKEgmTMVVVTHEMGFAREVADRVVFMDGGR-------IVEEGPPEEFFENPQH 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-213 |
5.80e-58 |
|
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: 187.67 E-value: 5.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 5 SLRGVQKAYGDGA-PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG--VAMV 81
Cdd:cd03225 1 ELKNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQsyalFP-HM----TVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVF 156
Cdd:cd03225 81 FQ----NPdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 157 LFDEPLSNLDATLRGQTRIEIARLHKQfaKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE--GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-244 |
2.26e-57 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 186.88 E-value: 2.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgapVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVFQ 83
Cdd:COG3840 2 LRLDDLTYRYGD---FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYALFPHMTVFENMAFG----LKLAKTPKdeidRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFD 159
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGlrpgLKLTAEQR----AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 160 EPLSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFV 239
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRER-GLTVLMVTHDPEDAARIADRVLLVADGR-------IAADGPTAALLDGEPPPAL 226
|
....*
gi 1431886808 240 AGFIG 244
Cdd:COG3840 227 AAYLG 231
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-243 |
6.87e-56 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 188.00 E-value: 6.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ------RGVAMVFQSYALFPHMTV 93
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 94 FENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQT 173
Cdd:COG4175 123 LENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREM 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 174 RIEIARLHKQFAKaSVVYVTHDQIEAMTLADKIVLLhagKDteryGSIAQIGAPLELYHRPRSRFVAGFI 243
Cdd:COG4175 203 QDELLELQAKLKK-TIVFITHDLDEALRLGDRIAIM---KD----GRIVQIGTPEEILTNPANDYVADFV 264
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-213 |
8.01e-56 |
|
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: 183.26 E-value: 8.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ-----RGV 78
Cdd:COG1127 6 IEVRNLTKSFGD-RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSYALFPHMTVFENMAFGLK-LAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFL 157
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 158 FDEPLSNLDAtlRGQTRIE--IARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:COG1127 165 YDEPTAGLDP--ITSAVIDelIRELRDEL-GLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-213 |
4.69e-55 |
|
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: 180.42 E-value: 4.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN----DVPAAQRGVA 79
Cdd:cd03262 1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFPHMTVFENMAFGL-KLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLF 158
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 159 DEPLSNLDATLRGqtriEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03262 160 DEPTSALDPELVG----EVLDVMKDLAEEgmTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-224 |
2.65e-54 |
|
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: 178.91 E-value: 2.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGApVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDL-----TDGDLFIGGEVMN----DVPAA 74
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYdldvDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 75 QRGVAMVFQSYALFPhMTVFENMAFGLKLA-KTPKDEIDRKVREAARILQLEALLERRPKA--LSGGQRQRVAIGRAIVR 151
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHgIKLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 152 QPGVFLFDEPLSNLD--ATLrgqtRIE--IARLHKQFAkasVVYVTHDQIEAMTLADKIVLLHAGKDTErYGSIAQI 224
Cdd:cd03260 159 EPEVLLLDEPTSALDpiSTA----KIEelIAELKKEYT---IVIVTHNMQQAARVADRTAFLLNGRLVE-FGPTEQI 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-218 |
8.55e-54 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 178.52 E-value: 8.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDGA---PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDvPAAQRG 77
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 VamVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFL 157
Cdd:COG4525 80 V--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 158 FDEPLSNLDATLRGQTRIEIARLHKQFAKaSVVYVTHDQIEAMTLADKIVLL--HAGKDTERY 218
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGK-GVFLITHSVEEALFLATRLVVMspGPGRIVERL 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-233 |
1.36e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 177.18 E-value: 1.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGaPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGE-VMNDVPAAQRGVAMVF 82
Cdd:COG1131 1 IEVRGLTKRYGDK-TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdVARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 QSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPL 162
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431886808 163 SNLDATLRGQTRIEIARLHKQfaKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHR 233
Cdd:COG1131 160 SGLDPEARRELWELLRELAAE--GKTVLLSTHYLEEAERLCDRVAIIDKGR-------IVADGTPDELKAR 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-287 |
3.00e-53 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 180.31 E-value: 3.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 22 DVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMND------VPAAQRGVAMVFQSYALFPHMTVFE 95
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 96 NMAFGLKLAKTPkdeiDRKVREAA--RILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQT 173
Cdd:TIGR02142 95 NLRYGMKRARPS----ERRISFERviELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 174 RIEIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYhrprsrfvagfiGSPRMNFLPG 253
Cdd:TIGR02142 171 LPYLERLHAEF-GIPILYVSHSLQEVLRLADRVVVLEDGR-------VAAAGPIAEVW------------ASPDLPWLAR 230
|
250 260 270
....*....|....*....|....*....|....
gi 1431886808 254 RIASFDAQGVVVALDHTHENVHVPVDGAALQVSQ 287
Cdd:TIGR02142 231 EDQGSLIEGVVAEHDQHYGLTALRLGGGHLWVPE 264
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-213 |
4.24e-52 |
|
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: 173.46 E-value: 4.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEvmnDVPAAQ-------- 75
Cdd:cd03261 1 IELRGLTKSFGG-RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE---DISGLSeaelyrlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 76 RGVAMVFQSYALFPHMTVFENMAFGLK-LAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPG 154
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 155 VFLFDEPLSNLDATLRGQTRIEIARLHKQFAKASVVyVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIM-VTHDLDTAFAIADRIAVLYDGK 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-213 |
7.21e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.92 E-value: 7.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYgDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ--RGVAMV 81
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFPhMTVFENMAFGLKLAKTPKDEidRKVREAARILQL-EALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:COG4619 80 PQEPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 161 PLSNLDATLRGqtRIE--IARLHKQfAKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:COG4619 157 PTSALDPENTR--RVEelLREYLAE-EGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-278 |
7.32e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 176.04 E-value: 7.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAY-GDGAPVI--RDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP-----AAQ 75
Cdd:COG1135 2 IELENLSKTFpTKGGPVTalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSerelrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 76 RGVAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGV 155
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 156 FLFDEPLSNLDAtlrgQTRIEI----ARLHKQFaKASVVYVTHDqieaM----TLADKIVLLHAGKdterygsIAQIGAP 227
Cdd:COG1135 162 LLCDEATSALDP----ETTRSIldllKDINREL-GLTIVLITHE----MdvvrRICDRVAVLENGR-------IVEQGPV 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 228 LELYHRPRSRFVAGFIGSPRMNFLPG----RIASFDAQGVVVALDHTHENVHVPV 278
Cdd:COG1135 226 LDVFANPQSELTRRFLPTVLNDELPEellaRLREAAGGGRLVRLTFVGESADEPL 280
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-217 |
1.20e-50 |
|
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: 169.98 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGA---PVIRDVDLEIGENE-FCVfLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGE-VMNDVPAAQRG- 77
Cdd:COG1124 2 LEVRNLSVSYGQGGrrvPVLKDVSLEVAPGEsFGL-VGESGSGKSTLLRALAGLERPWSGEVTFDGRpVTRRRRKAFRRr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 VAMVFQSY--ALFPHMTVFENMAFGLKLAKtpKDEIDRKVREAARILQL-EALLERRPKALSGGQRQRVAIGRAIVRQPG 154
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 155 VFLFDEPLSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDqIEAMT-LADKIVLLHAGKDTER 217
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREER-GLTYLFVSHD-LAVVAhLCDRVAVMQNGRIVEE 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-235 |
3.54e-50 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 168.53 E-value: 3.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDG---APVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP-----AAQ 75
Cdd:cd03258 2 IELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 76 RGVAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGV 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 156 FLFDEPLSNLDAtlrgQTRIEIARLHKQFAKA---SVVYVTHdQIEAM-TLADKIVLLHAGKdterygsIAQIGAPLELY 231
Cdd:cd03258 162 LLCDEATSALDP----ETTQSILALLRDINRElglTIVLITH-EMEVVkRICDRVAVMEKGE-------VVEEGTVEEVF 229
|
....
gi 1431886808 232 HRPR 235
Cdd:cd03258 230 ANPQ 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-230 |
5.09e-50 |
|
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: 168.68 E-value: 5.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG--VAMV 81
Cdd:COG1120 2 LEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELArrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFPHMTVFENMAFG----LKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFL 157
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1431886808 158 FDEPLSNLDatLRGQtrIEIARLHKQFAKA---SVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLEL 230
Cdd:COG1120 161 LDEPTSHLD--LAHQ--LEVLELLRRLARErgrTVVMVLHDLNLAARYADRLVLLKDGR-------IVAQGPPEEV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-233 |
1.21e-49 |
|
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: 174.71 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAP----VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ---- 75
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 76 -RGVAMVFQ--SYALFPHMTVFENMAFGLKLAKT-PKDEIDRKVREAARILQL-EALLERRPKALSGGQRQRVAIGRAIV 150
Cdd:COG1123 341 rRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 151 RQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFAKaSVVYVTHDqIEAM-TLADKIVLLHAGKDTERyGSIAQI-GAPL 228
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGL-TYLFISHD-LAVVrYIADRVAVMYDGRIVED-GPTEEVfANPQ 497
|
....*
gi 1431886808 229 ELYHR 233
Cdd:COG1123 498 HPYTR 502
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-243 |
2.21e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 166.42 E-value: 2.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGV----A 79
Cdd:PRK09493 2 IEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFPHMTVFENMAFG-LKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLF 158
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 159 DEPLSNLDATLRGqtriEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRS 236
Cdd:PRK09493 161 DEPTSALDPELRH----EVLKVMQDLAEEgmTMVIVTHEIGFAEKVASRLIFIDKGR-------IAEDGDPQVLIKNPPS 229
|
....*..
gi 1431886808 237 RFVAGFI 243
Cdd:PRK09493 230 QRLQEFL 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-224 |
5.73e-49 |
|
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: 165.42 E-value: 5.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGaPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGE-VMNDVPAAQRGVAMVF 82
Cdd:COG4555 2 IEVENLSKKYGKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 QSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPL 162
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 163 SNLDATLRGQTRIEIARLHKQfaKASVVYVTHDQIEAMTLADKIVLLHAGKdTERYGSIAQI 224
Cdd:COG4555 161 NGLDVMARRLLREILRALKKE--GKTVLFSSHIMQEVEALCDRVVILHKGK-VVAQGSLDEL 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-213 |
8.08e-49 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 165.23 E-value: 8.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN-----DVPAAQRGV 78
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTalrgrALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSYALFPHMTVFENMAFGLkLAKT----------PKDEIDRkVREAARILQLEALLERRPKALSGGQRQRVAIGRA 148
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGR-LGRTstwrsllglfPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 149 IVRQPGVFLFDEPLSNLD--------ATLRgqtriEIARLHkqfaKASVVYVTHdQIE-AMTLADKIVLLHAGK 213
Cdd:COG3638 161 LVQEPKLILADEPVASLDpktarqvmDLLR-----RIARED----GITVVVNLH-QVDlARRYADRIIGLRDGR 224
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-213 |
1.12e-47 |
|
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: 161.26 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFcVFL-GPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN-----DVPAAQRG 77
Cdd:TIGR02673 2 IEFHNVSKAYPGGVAALHDVSLHIRKGEF-LFLtGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNrlrgrQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 VAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFL 157
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 158 FDEPLSNLDATLRGQtrieIARLHKQFAK--ASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:TIGR02673 161 ADEPTGNLDPDLSER----ILDLLKRLNKrgTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-213 |
2.65e-47 |
|
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: 160.75 E-value: 2.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGA---PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG--- 77
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 --VAMVFQSY--ALFPHMTVFENMAFGLKLAK--TPKDEIDRKVREAARILQL-EALLERRPKALSGGQRQRVAIGRAIV 150
Cdd:cd03257 82 keIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 151 RQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDqIEAM-TLADKIVLLHAGK 213
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEEL-GLTLLFITHD-LGVVaKIADRVAVMYAGK 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-293 |
7.56e-47 |
|
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: 167.00 E-value: 7.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGA-PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLT---DGDLFIGGEVMNDVPAAQRG-- 77
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 VAMVFQS--YALFPhMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGV 155
Cdd:COG1123 85 IGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 156 FLFDEPLSNLDATLRGQTRIEIARLHKQFAKAsVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPR 235
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTT-VLLITHDLGVVAEIADRVVVMDDGR-------IVEDGPPEEILAAPQ 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431886808 236 SRFVAGFIGSPRMNFLPGRIAS---FDAQGVVVALDHTHENVHVPVDGAALQVSQAVTLGV 293
Cdd:COG1123 236 ALAAVPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGL 296
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-237 |
2.00e-46 |
|
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: 158.40 E-value: 2.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDvPAAQRGVamVFQSYALFPHMTVFENMAF 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 100 GLK--LAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEI 177
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431886808 178 ARLHKQfAKASVVYVTHDQIEAMTLADKIVLLHAGKDterygsiAQIGAPLEL-YHRPRSR 237
Cdd:TIGR01184 158 MQIWEE-HRVTVLMVTHDVDEALLLSDRVVMLTNGPA-------ANIGQILEVpFPRPRDR 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-230 |
3.30e-45 |
|
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: 165.39 E-value: 3.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAY-GDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ--RGVA 79
Cdd:COG2274 473 DIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFpHMTVFENMAFGlklAKTPKDEidrKVREAARILQLEALLERRPK-----------ALSGGQRQRVAIGRA 148
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLG---DPDATDE---EIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 149 IVRQPGVFLFDEPLSNLDAtlRGQTRIeIARLHKQFAKASVVYVTHDqIEAMTLADKIVLLHAGKdterygsIAQIGAPL 228
Cdd:COG2274 626 LLRNPRILILDEATSALDA--ETEAII-LENLRRLLKGRTVIIIAHR-LSTIRLADRIIVLDKGR-------IVEDGTHE 694
|
..
gi 1431886808 229 EL 230
Cdd:COG2274 695 EL 696
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-224 |
1.10e-44 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 154.81 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 2 ASISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTD-----GDLFIGGEVMN----DVP 72
Cdd:COG1117 10 PKIEVRNLNVYYGD-KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPgarveGEILLDGEDIYdpdvDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 73 AAQRGVAMVFQSYALFPhMTVFENMAFGLKLA-KTPKDEIDRKVREAariLQLEAL-------LERRPKALSGGQRQRVA 144
Cdd:COG1117 89 ELRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHgIKSKSELDEIVEES---LRKAALwdevkdrLKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 145 IGRAIVRQPGVFLFDEPLSNLD--ATLrgqtRIE--IARLHKQFakaSVVYVTHDQIEAMTLADKIVLLHAGKDTErYGS 220
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDpiSTA----KIEelILELKKDY---TIVIVTHNMQQAARVSDYTAFFYLGELVE-FGP 236
|
....
gi 1431886808 221 IAQI 224
Cdd:COG1117 237 TEQI 240
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-213 |
1.72e-44 |
|
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: 153.88 E-value: 1.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP-----AAQRGV 78
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSYALFPHMTVFENMAFGlKLAKTPK--------DEIDR-KVREAARILQLEALLERRPKALSGGQRQRVAIGRAI 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSG-RLGRRSTwrslfglfPKEEKqRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 150 VRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFAKAsVVYVTHdQIE-AMTLADKIVLLHAGK 213
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGIT-VIVSLH-QVDlAREYADRIVGLKDGR 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-248 |
3.91e-44 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 153.29 E-value: 3.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGApVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDvpaAQRGVAMVFQ 83
Cdd:PRK11247 13 LLLNAVSKRYGERT-VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE---AREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYALFPHMTVFENMAFGLKlaktpkdeidRKVREAArilqLEAL----LERR----PKALSGGQRQRVAIGRAIVRQPGV 155
Cdd:PRK11247 89 DARLLPWKKVIDNVGLGLK----------GQWRDAA----LQALaavgLADRanewPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 156 FLFDEPLSNLDATlrgqTRIE----IARLHKQFAkASVVYVTHDQIEAMTLADKIVLLHAGkdterygsiaQIGAPLEL- 230
Cdd:PRK11247 155 LLLDEPLGALDAL----TRIEmqdlIESLWQQHG-FTVLLVTHDVSEAVAMADRVLLIEEG----------KIGLDLTVd 219
|
250
....*....|....*...
gi 1431886808 231 YHRPRSRfvagfiGSPRM 248
Cdd:PRK11247 220 LPRPRRR------GSARL 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-230 |
6.15e-44 |
|
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: 151.50 E-value: 6.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGA-PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGG-EVMNDVPAAQRGVAMV 81
Cdd:cd03263 1 LQIRNLTKTYKKGTkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGySIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEP 161
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 162 LSNLDATLRgqtRIEIARLHKQFAKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLEL 230
Cdd:cd03263 161 TSGLDPASR---RAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGK-------LRCIGSPQEL 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
15-212 |
7.41e-44 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 152.55 E-value: 7.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDvPAAQRGVamVFQSYALFPHMTVF 94
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGV--VFQNEGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 95 ENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTR 174
Cdd:PRK11248 89 DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1431886808 175 IEIARLHKQFAKaSVVYVTHDQIEAMTLADKIVLLHAG 212
Cdd:PRK11248 169 TLLLKLWQETGK-QVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-213 |
1.28e-43 |
|
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: 150.72 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 22 DVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVFQSYALFPHMTVFENMAFGL 101
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 102 --KLAKTPKDEidRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEIAR 179
Cdd:cd03298 96 spGLKLTAEDR--QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....
gi 1431886808 180 LHKQfAKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03298 174 LHAE-TKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-233 |
1.58e-43 |
|
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: 152.20 E-value: 1.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGA-PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGG-EVMND--VPAAQRGVA 79
Cdd:TIGR04520 1 IEVENVSFSYPESEkPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEenLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSyalfPH-----MTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPG 154
Cdd:TIGR04520 81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 155 VFLFDEPLSNLDAtlRGQTRI--EIARLHKQFAKaSVVYVTHDqIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYH 232
Cdd:TIGR04520 157 IIILDEATSMLDP--KGRKEVleTIRKLNKEEGI-TVISITHD-MEEAVLADRVIVMNKGK-------IVAEGTPREIFS 225
|
.
gi 1431886808 233 R 233
Cdd:TIGR04520 226 Q 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-213 |
1.66e-43 |
|
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: 149.08 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGaPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG-VAMVF 82
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 QSYALFPHMTVFENMafglklaktpkdeidrkvreaarilqleallerrpkALSGGQRQRVAIGRAIVRQPGVFLFDEPL 162
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 163 SNLDAtlrgQTRIEIARLHKQFAK--ASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03230 124 SGLDP----ESRREFWELLRELKKegKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-195 |
4.80e-43 |
|
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: 149.10 E-value: 4.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMND-----VPAAQRGV 78
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLF 158
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1431886808 159 DEPLSNLDATlrgqTRIEIARLHKQFAKA--SVVYVTHD 195
Cdd:cd03292 161 DEPTGNLDPD----TTWEIMNLLKKINKAgtTVVVATHA 195
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-227 |
3.99e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 147.47 E-value: 3.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN--------DVPAA 74
Cdd:COG4161 2 SIQLKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkpsekAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 75 QRGVAMVFQSYALFPHMTVFENM-AFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQP 153
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1431886808 154 GVFLFDEPLSNLDATLRGQtrieIARLHKQFAKASV--VYVTHDQIEAMTLADKIVLLHAGKDTErYGSIAQIGAP 227
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQ----VVEIIRELSQTGItqVIVTHEVEFARKVASQVVYMEKGRIIE-QGDASHFTQP 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-209 |
4.29e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.54 E-value: 4.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEvmnDVPAAQRGVAM 80
Cdd:COG1121 4 MPAIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYAL---FPhMTVFENMAFGL----KLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQP 153
Cdd:COG1121 80 VPQRAEVdwdFP-ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 154 GVFLFDEPLSNLDAtlrgQTRIEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLL 209
Cdd:COG1121 159 DLLLLDEPFAGVDA----ATEEALYELLRELRREgkTILVVTHDLGAVREYFDRVLLL 212
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-213 |
1.69e-41 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 145.50 E-value: 1.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 24 DLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVFQSYALFPHMTVFENMAFG--- 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 101 -LKLAKTPKdeidRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGqtriEIAR 179
Cdd:PRK10771 99 gLKLNAAQR----EKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ----EMLT 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1431886808 180 LHKQFA---KASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:PRK10771 171 LVSQVCqerQLTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-163 |
2.50e-41 |
|
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: 142.40 E-value: 2.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN--DVPAAQRGVAMVFQSYALFPHMTVFENM 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTddERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 98 AFGLKLAKTPKDEIDRKVREAARILQLEALLERR----PKALSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-195 |
4.20e-41 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 143.78 E-value: 4.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDL---TDGDLFIGGEVMNDVPAAQRGVA 79
Cdd:COG4136 1 MLSLENLTITLG-GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFPHMTVFENMAFGLKlAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFD 159
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1431886808 160 EPLSNLDATLRGQTRiEIARLHKQFAKASVVYVTHD 195
Cdd:COG4136 159 EPFSKLDAALRAQFR-EFVFEQIRQRGIPALLVTHD 193
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-213 |
5.90e-41 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 142.14 E-value: 5.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDG-APVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAA--QRGVAM 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFpHMTVFENMafglklaktpkdeidrkvreaarilqleallerrpkaLSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 161 PLSNLDAtlrgQTRIEI-ARLHKQFAKASVVYVTHDqIEAMTLADKIVLLHAGK 213
Cdd:cd03228 123 ATSALDP----ETEALIlEALRALAKGKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-230 |
1.67e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 150.70 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ--RGVAM 80
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFpHMTVFENMAFGlklaktpKDEIDR-KVREAARILQLEALLERRPK-----------ALSGGQRQRVAIGRA 148
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYG-------RPDATDeEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 149 IVRQPGVFLFDEPLSNLDAtlrgQTRIEIAR-LHKQFAKASVVYVTHdQIEAMTLADKIVLLHAGKdterygsIAQIGAP 227
Cdd:COG1132 491 LLKDPPILILDEATSALDT----ETEALIQEaLERLMKGRTTIVIAH-RLSTIRNADRILVLDDGR-------IVEQGTH 558
|
...
gi 1431886808 228 LEL 230
Cdd:COG1132 559 EEL 561
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-216 |
1.78e-40 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 143.23 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN--------DVPAA 74
Cdd:PRK11124 2 SIQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsktpsdkAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 75 QRGVAMVFQSYALFPHMTVFENMAFG-LKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQP 153
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 154 GVFLFDEPLSNLDATLRGQtrieIARLHKQFAKASV--VYVTHDQIEAMTLADKIVLLHAGKDTE 216
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQ----IVSIIRELAETGItqVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-213 |
2.15e-40 |
|
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: 141.85 E-value: 2.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 2 ASISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG-VAM 80
Cdd:COG4133 1 MMLEAENLSCRRGE-RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMAFGLKLAKTPKDEIDrkVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 161 PLSNLDAtlRGQTRI-EIARLHKQfAKASVVYVTHDQIEAmtLADKIVLLHAGK 213
Cdd:COG4133 158 PFTALDA--AGVALLaELIAAHLA-RGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-213 |
7.53e-40 |
|
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: 138.92 E-value: 7.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 5 SLRGVQKAYGDGaPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP--AAQRGVAMVF 82
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPleELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 QsyalfphmtvfenmafglklaktpkdeidrkvreaarilqleallerrpkaLSGGQRQRVAIGRAIVRQPGVFLFDEPL 162
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1431886808 163 SNLDATLRGQTRIEIARLHKQfaKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd00267 109 SGLDPASRERLLELLRELAEE--GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-213 |
1.20e-39 |
|
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: 140.38 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 24 DLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVFQSYALFPHMTVFENMAFGLKL 103
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 104 AKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQ 183
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|
gi 1431886808 184 fAKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:TIGR01277 178 -RQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-233 |
1.41e-39 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 147.98 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAA--QRGVAM 80
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFpHMTVFENMAFGLKLAKtpkdeiDRKVREAARILQLEALLERRPK-----------ALSGGQRQRVAIGRAI 149
Cdd:COG4988 416 VPQNPYLF-AGTIRENLRLGRPDAS------DEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARAL 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 150 VRQPGVFLFDEPLSNLDAtlrgQTRIEI-ARLHKQFAKASVVYVTHDqIEAMTLADKIVLLHAGKdterygsIAQIGAPL 228
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDA----ETEAEIlQALRRLAKGRTVILITHR-LALLAQADRILVLDDGR-------IVEQGTHE 556
|
....*
gi 1431886808 229 ELYHR 233
Cdd:COG4988 557 ELLAK 561
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-213 |
1.51e-39 |
|
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: 140.65 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPA---AQRGVAM 80
Cdd:cd03219 1 LEVRGLTKRFG-GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENM----------AFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIV 150
Cdd:cd03219 80 TFQIPRLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 151 RQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQfaKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRER--GITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-242 |
3.47e-39 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 144.02 E-value: 3.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ------RGVAMVFQSYALFPHMTV 93
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 94 FENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQT 173
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 174 RIEIARLHKQFAKaSVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFVAGF 242
Cdd:PRK10070 204 QDELVKLQAKHQR-TIVFISHDLDEAMRIGDRIAIMQNGE-------VVQVGTPDEILNNPANDYVRTF 264
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-244 |
3.94e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 139.98 E-value: 3.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDGApVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLT-----DGDLFIGGEVM--NDVPA 73
Cdd:PRK14267 2 KFAIETVNLRVYYGSNH-VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 74 --AQRGVAMVFQSYALFPHMTVFENMAFGLKLAK--TPKDEIDRKVR----EAARILQLEALLERRPKALSGGQRQRVAI 145
Cdd:PRK14267 81 ieVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEwalkKAALWDEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 146 GRAIVRQPGVFLFDEPLSNLDATlrGQTRIE--IARLHKQFakaSVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQ 223
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPV--GTAKIEelLFELKKEY---TIVLVTHSPAQAARVSDYVAFLYLGK-------LIE 228
|
250 260
....*....|....*....|....*
gi 1431886808 224 IGAPLELYHRPR----SRFVAGFIG 244
Cdd:PRK14267 229 VGPTRKVFENPEheltEKYVTGALG 253
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-245 |
1.22e-38 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 138.78 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVM--------NDVPAAQ 75
Cdd:COG4598 9 LEVRDLHKSFGD-LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 76 RGV-------AMVFQSYALFPHMTVFENMAFG-LKLAKTPKDEidrkVREAARILqLE--ALLERR---PKALSGGQRQR 142
Cdd:COG4598 88 RQLqrirtrlGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAE----AIERAEAL-LAkvGLADKRdayPAHLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 143 VAIGRAIVRQPGVFLFDEPLSNLDATLRGqtriEIARLHKQFAK--ASVVYVTHDQIEAMTLADKIVLLHAGKdterygs 220
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPELVG----EVLKVMRDLAEegRTMLVVTHEMGFARDVSSHVVFLHQGR------- 231
|
250 260
....*....|....*....|....*
gi 1431886808 221 IAQIGAPLELYHRPRSRFVAGFIGS 245
Cdd:COG4598 232 IEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-241 |
2.37e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 138.12 E-value: 2.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDL-----TDGDLFIGGEVM--NDVPA 73
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ-VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIfkMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 74 AQRGVAMVFQSYALFPHMTVFENMAFGLKLAK--TPKDEIDRKVREAARILQLEALLERRPKA----LSGGQRQRVAIGR 147
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 148 AIVRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFAkasVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAP 227
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMT---IVLVTHFPQQAARISDYVAFLYKGQ-------IVEWGPT 229
|
250
....*....|....*...
gi 1431886808 228 LELYHRPR----SRFVAG 241
Cdd:PRK14247 230 REVFTNPRheltEKYVTG 247
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-213 |
3.49e-38 |
|
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: 137.43 E-value: 3.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFI-GGEVMN----DVPAAQRGV 78
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLeGTDITKlrgkKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSYALFPHMTVFENMAFGlKLAKTP---------KDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAI 149
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHG-RLGYKPtwrsllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 150 VRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFAKASVVYVtHDQIEAMTLADKIVLLHAGK 213
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINL-HQVDLAKKYADRIVGLKAGE 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-213 |
3.57e-38 |
|
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: 136.79 E-value: 3.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGA---PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN----DVPAAQR 76
Cdd:COG4181 9 IELRGLTKTVGTGAgelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldeDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 77 G--VAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEidrkvREAARILQ---LEALLERRPKALSGGQRQRVAIGRAIVR 151
Cdd:COG4181 89 ArhVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR-----ARARALLErvgLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1431886808 152 QPGVFLFDEPLSNLDATlRGQTRIE-IARLHKQfAKASVVYVTHDQieamTLA---DKIVLLHAGK 213
Cdd:COG4181 164 EPAILFADEPTGNLDAA-TGEQIIDlLFELNRE-RGTTLVLVTHDP----ALAarcDRVLRLRAGR 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-244 |
5.35e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 137.19 E-value: 5.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYgDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGG-EVMNDVP-AAQRG- 77
Cdd:PRK11264 1 MSAIEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDiTIDTARSlSQQKGl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 -------VAMVFQSYALFPHMTVFENMAFG-LKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAI 149
Cdd:PRK11264 80 irqlrqhVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 150 VRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQfaKASVVYVTHDQIEAMTLADKIVLLHAGKDTERYGSIAQIGAPLE 229
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE--KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
250
....*....|....*.
gi 1431886808 230 lyhrPRSR-FVAGFIG 244
Cdd:PRK11264 238 ----PRTRqFLEKFLL 249
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-209 |
1.70e-37 |
|
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: 134.28 E-value: 1.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 6 LRGVQKAYGDGApVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG------VA 79
Cdd:TIGR03608 1 LKNISKKFGDKV-ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASkfrrekLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFD 159
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 160 EPLSNLDAtlrgQTRIEIARLHKQFAKA--SVVYVTHDQiEAMTLADKIVLL 209
Cdd:TIGR03608 160 EPTGSLDP----KNRDEVLDLLLELNDEgkTIIIVTHDP-EVAKQADRVIEL 206
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-166 |
8.95e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 136.08 E-value: 8.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVI---RDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVM-----NDVPAAQ 75
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalseKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 76 RGVAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGV 155
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170
....*....|.
gi 1431886808 156 FLFDEPLSNLD 166
Cdd:PRK11153 162 LLCDEATSALD 172
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-230 |
1.00e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 134.35 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 2 ASISLRGVQKAYGDG-APVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMND--VPAAQRGV 78
Cdd:PRK13632 6 VMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSY-ALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFL 157
Cdd:PRK13632 86 GIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 158 FDEPLSNLDAtlRGQTRIE--IARLHKQfAKASVVYVTHDQIEAmTLADKIVLLHAGKdterygsIAQIGAPLEL 230
Cdd:PRK13632 166 FDESTSMLDP--KGKREIKkiMVDLRKT-RKKTLISITHDMDEA-ILADKVIVFSEGK-------LIAQGKPKEI 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-234 |
2.59e-36 |
|
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: 139.13 E-value: 2.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 2 ASISLRGVQKAY-GDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ--RGV 78
Cdd:COG4987 332 PSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSYALFpHMTVFENmafgLKLAKtpKDEIDRKVREAARILQLEALLERRPK-----------ALSGGQRQRVAIGR 147
Cdd:COG4987 412 AVVPQRPHLF-DTTLREN----LRLAR--PDATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 148 AIVRQPGVFLFDEPLSNLDAtlrgQTRIEI-ARLHKQFAKASVVYVTHDQiEAMTLADKIVLLHAGKdterygsIAQIGA 226
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDA----ATEQALlADLLEALAGRTVLLITHRL-AGLERMDRILVLEDGR-------IVEQGT 552
|
....*...
gi 1431886808 227 PLELYHRP 234
Cdd:COG4987 553 HEELLAQN 560
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-213 |
2.73e-36 |
|
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: 131.72 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVI---RDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGG-EVMNDVPAAQRGVA 79
Cdd:cd03266 2 ITADALTKRFRDVKKTVqavDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFD 159
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 160 EPLSNLDATLRgQTRIEIARLHKQFAKAsVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03266 162 EPTTGLDVMAT-RALREFIRQLRALGKC-ILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-213 |
3.11e-36 |
|
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: 130.25 E-value: 3.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 5 SLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG--VAMVF 82
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELArkIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 QsyalfphmtvfenmafglklaktpkdeidrkvreAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPL 162
Cdd:cd03214 80 Q----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 163 SNLDatLRGQTRI--EIARLHKQFAKAsVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03214 126 SHLD--IAHQIELleLLRRLARERGKT-VVMVLHDLNLAARYADRVILLKDGR 175
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
3-231 |
6.83e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 132.48 E-value: 6.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDGAP----VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAA---- 74
Cdd:PRK13637 2 SIKIENLTHIYMEGTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 75 QRGVAMVFQ--SYALFPHmTVFENMAFGLKLAKTPKDEIDRKVREAARILQL--EALLERRPKALSGGQRQRVAIGRAIV 150
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 151 RQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLEL 230
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEY-NMTIILVSHSMEDVAKLADRIIVMNKGK-------CELQGTPREV 232
|
.
gi 1431886808 231 Y 231
Cdd:PRK13637 233 F 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-213 |
2.74e-35 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 132.31 E-value: 2.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 22 DVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMND------VPAAQRGVAMVFQSYALFPHMTVFE 95
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 96 NMAFGLKlaKTPKDEIDRKVReaarILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRI 175
Cdd:PRK11144 96 NLRYGMA--KSMVAQFDKIVA----LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1431886808 176 EIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:PRK11144 170 YLERLAREI-NIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-230 |
6.74e-35 |
|
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: 128.50 E-value: 6.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDV--PAAQRGVAMV 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVtlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFpHMTVFENMAFGlKLAKTpkdeiDRKVREAARILQLEALLERRPKA-----------LSGGQRQRVAIGRAIV 150
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYG-RPDAT-----DEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 151 RQPGVFLFDEPLSNLDATlrgqTRIEI-ARLHKQFAKASVVYVTHDQIEAMTlADKIVLLHAGKdterygsIAQIGAPLE 229
Cdd:cd03253 154 KNPPILLLDEATSALDTH----TEREIqAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGR-------IVERGTHEE 221
|
.
gi 1431886808 230 L 230
Cdd:cd03253 222 L 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-209 |
1.38e-34 |
|
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: 126.88 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEvmnDVPAAQRGVAMVFQSYAL---FPhM 91
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRRSIdrdFP-I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 92 TVFENMAFGL----KLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDA 167
Cdd:cd03235 86 SVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1431886808 168 tlrgQTRIEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLL 209
Cdd:cd03235 166 ----KTQEDIYELLRELRREgmTILVVTHDLGLVLEYFDRVLLL 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-235 |
1.50e-34 |
|
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: 129.79 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGA---PVIRDVDLEIGENE-FCVfLGPSGCGKSTLLRMIAGLED---LTDGDLFIGGEVMNDVPAAQ- 75
Cdd:COG0444 2 LEVRNLKVYFPTRRgvvKAVDGVSFDVRRGEtLGL-VGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 76 -----RGVAMVFQ-SY-ALFPHMTVFENMAFGLKL-AKTPKDEIDRKVREAARILQL---EALLERRPKALSGGQRQRVA 144
Cdd:COG0444 81 rkirgREIQMIFQdPMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 145 IGRAIVRQPGVFLFDEPLSNLDATLRGQtrI--EIARLHKQFaKASVVYVTHD-----QIeamtlADKIVLLHAGKdter 217
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQ--IlnLLKDLQREL-GLAILFITHDlgvvaEI-----ADRVAVMYAGR---- 228
|
250
....*....|....*...
gi 1431886808 218 ygsIAQIGAPLELYHRPR 235
Cdd:COG0444 229 ---IVEEGPVEELFENPR 243
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-244 |
5.61e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 126.82 E-value: 5.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 13 YGDGAPViRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDL-----TDGDLFIGGEVMN----DVPAAQRGVAMVFQ 83
Cdd:PRK14243 20 YGSFLAV-KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYapdvDPVEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYALFPHmTVFENMAFGLKLA--KTPKDE-IDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGARINgyKGDMDElVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 161 PLSNLD--ATLrgqtRIE--IARLHKQFakaSVVYVTHDQIEAMTLADKIVLLHAGKDTE--RYGSIAQIGAPLELYHRP 234
Cdd:PRK14243 178 PCSALDpiSTL----RIEelMHELKEQY---TIIIVTHNMQQAARVSDMTAFFNVELTEGggRYGYLVEFDRTEKIFNSP 250
|
250
....*....|....
gi 1431886808 235 RSR----FVAGFIG 244
Cdd:PRK14243 251 QQQatrdYVSGRFG 264
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-213 |
5.89e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 131.29 E-value: 5.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEV---MNDVPAAQRGVAM 80
Cdd:COG1129 5 LEMRGISKSFG-GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPvrfRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMAFGLKLAKTPKdeIDRK--VREAARILQ---LEALLERRPKALSGGQRQRVAIGRAIVRQPGV 155
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRGGL--IDWRamRRRARELLArlgLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 156 FLFDEPLSNLDATlrgqtriEIARLHKQFAK-----ASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:COG1129 162 LILDEPTASLTER-------EVERLFRIIRRlkaqgVAIIYISHRLDEVFEIADRVTVLRDGR 217
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-206 |
6.46e-34 |
|
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: 125.16 E-value: 6.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGA---PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG--- 77
Cdd:TIGR02211 2 LKCENLGKRYQEGKldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 ---VAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPG 154
Cdd:TIGR02211 82 nkkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 155 VFLFDEPLSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDqieaMTLADKI 206
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNREL-NTSFLVVTHD----LELAKKL 208
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-245 |
5.79e-33 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 123.79 E-value: 5.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMND--------VPAAQ 75
Cdd:TIGR03005 1 VRFSDVTKRFGI-LTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHmpgrngplVPADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 76 RGVA-------MVFQSYALFPHMTVFENMAFGLKLAK-TPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGR 147
Cdd:TIGR03005 80 KHLRqmrnkigMVFQSFNLFPHKTVLDNVTEAPVLVLgMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 148 AIVRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQfAKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAP 227
Cdd:TIGR03005 160 ALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASE-HDLTMLLVTHEMGFAREFADRVCFFDKGR-------IVEQGKP 231
|
250
....*....|....*...
gi 1431886808 228 LELYHRPRSRFVAGFIGS 245
Cdd:TIGR03005 232 DEIFRQPKEERTREFLSK 249
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-161 |
8.52e-33 |
|
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: 122.16 E-value: 8.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPA---AQRGVAM 80
Cdd:cd03224 1 LEVENLNAGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPherARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENmafgLKLAKTPKDEIDRKvREAARILQ----LEALLERRPKALSGGQRQRVAIGRAIVRQPGVF 156
Cdd:cd03224 80 VPEGRRIFPELTVEEN----LLLGAYARRRAKRK-ARLERVYElfprLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
....*
gi 1431886808 157 LFDEP 161
Cdd:cd03224 155 LLDEP 159
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-213 |
9.52e-33 |
|
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: 121.94 E-value: 9.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGaPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGVAMVFQ 83
Cdd:cd03268 1 LKTNDLTKTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYALFPHMTVFENMAFGLKLAKTPKDEIDrkvrEAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1431886808 164 NLDATLRGQTRIEIARLHKQfaKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQ--GITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-213 |
1.21e-32 |
|
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: 121.60 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 13 YGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGevmNDVPAAQR--GVAMVFQS--YALF 88
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERrkSIGYVMQDvdYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 89 PHmTVFENMAFGLKLAktpkDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDat 168
Cdd:cd03226 86 TD-SVREELLLGLKEL----DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD-- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1431886808 169 lRGQTRiEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03226 159 -YKNME-RVGELIRELAAQgkAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-231 |
1.39e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.59 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAY-GDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMND--VPAAQRGVAM 80
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSY-ALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFD 159
Cdd:PRK13635 86 VFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 160 EPLSNLDATLRgQTRIEIARLHKQFAKASVVYVTHDQIEAMTlADKIVLLHAGKdterygsIAQIGAPLELY 231
Cdd:PRK13635 166 EATSMLDPRGR-REVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGE-------ILEEGTPEEIF 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-230 |
1.99e-32 |
|
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: 121.32 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPViRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGG-EVMNDVPAAQRGVAMVF 82
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhDVVREPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 QSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPL 162
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 163 SNLDATLRGQTRIEIARLHKQFAkASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLEL 230
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFG-MTILLTTHYMEEAEQLCDRVAIIDHGR-------IIAEGTPEEL 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-195 |
1.66e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 119.15 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 11 KAYGDG---APVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG------VAMV 81
Cdd:PRK11629 13 KRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqkLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEP 161
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....
gi 1431886808 162 LSNLDATLRGQTRIEIARLHKQFAKASVVyVTHD 195
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLV-VTHD 205
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-209 |
2.22e-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: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAA--QRGVAM 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHmTVFENMAFGLKLAktPKDEIDRKVREA-------ARILQLEALLERRPKALSGGQRQRVAIGRAIVRQP 153
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDA--SDAEIREALERAgldefvaALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1431886808 154 GVFLFDEPLSNLDATLRGQTRIEIARLhkqFAKASVVYVTHDqIEAMTLADKIVLL 209
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRAL---AQGRTVLLVTHR-LALAALADRIVVL 529
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-230 |
3.81e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 118.65 E-value: 3.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ--RGVAMV 81
Cdd:COG4604 2 IEIKNVSKRYGG-KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFPHMTVFENMAFG--------LklakTPKDEidRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQP 153
Cdd:COG4604 81 RQENHINSRLTVRELVAFGrfpyskgrL----TAEDR--EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 154 GVFLFDEPLSNLD--------ATLRgqtrieiaRLHKQFAKaSVVYVTHDQIEAMTLADKIVllhAGKDteryGSIAQIG 225
Cdd:COG4604 155 DYVLLDEPLNNLDmkhsvqmmKLLR--------RLADELGK-TVVIVLHDINFASCYADHIV---AMKD----GRVVAQG 218
|
....*
gi 1431886808 226 APLEL 230
Cdd:COG4604 219 TPEEI 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-213 |
5.66e-31 |
|
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: 117.29 E-value: 5.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGApVIRDVDLEIGENEFcVFLGPSGCGKSTLLRMIAGLEDLTDGDLFI-GGEVMNDVPAAQRGVAMVF 82
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 QSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPL 162
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 163 SNLDAtlrgQTRIEIARLHKQFAKASVVYV-TH--DQIEAMtlADKIVLLHAGK 213
Cdd:cd03264 159 AGLDP----EERIRFRNLLSELGEDRIVILsTHivEDVESL--CNQVAVLNKGK 206
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
6.57e-31 |
|
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: 115.60 E-value: 6.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVM---NDVPAAQRGVAM 80
Cdd:cd03216 1 LELRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVsfaSPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQsyalfphmtvfenmafglklaktpkdeidrkvreaarilqleallerrpkaLSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 161 PLSNLDATLRGQTRIEIARLHKQfaKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ--GVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-216 |
1.15e-30 |
|
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: 117.98 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDG--------APVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP--- 72
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 73 --AAQRGVAMVFQ-SYALF-PHMTVFENMAFGLK-LAKTPKDEIDRKVREAARILQLEA-LLERRPKALSGGQRQRVAIG 146
Cdd:TIGR02769 83 rrAFRRDVQLVFQdSPSAVnPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 147 RAIVRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFAKAsVVYVTHDQIEAMTLADKIVLLHAGKDTE 216
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTA-YLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-213 |
1.15e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 122.44 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgapVI--RDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVM-----NDvpAAQR 76
Cdd:COG3845 6 LELRGITKRFGG---VVanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirspRD--AIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 77 GVAMVFQSYALFPHMTVFENMAFGL---KLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQP 153
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 154 GVFLFDEPLSNLdatlrgqTRIEIARLH---KQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:COG3845 161 RILILDEPTAVL-------TPQEADELFeilRRLAAEgkSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-230 |
1.71e-30 |
|
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: 116.56 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ--RGVAMV 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFPHmTVFENMAFGLKLAKtpkdeiDRKVREAARILQLEALLERRPKA-----------LSGGQRQRVAIGRAIV 150
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRPNAT------DEEVIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 151 RQPGVFLFDEPLSNLD------------ATLRGQTRIEIA-RLhkqfakASVVYvthdqieamtlADKIVLLHAGKdter 217
Cdd:cd03254 156 RDPKILILDEATSNIDtetekliqealeKLMKGRTSIIIAhRL------STIKN-----------ADKILVLDDGK---- 214
|
250
....*....|...
gi 1431886808 218 ygsIAQIGAPLEL 230
Cdd:cd03254 215 ---IIEEGTHDEL 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-161 |
1.96e-30 |
|
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: 116.23 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPA---AQRG 77
Cdd:COG0410 1 MPMLEVENLHAGYGG-IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhriARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 VAMVFQSYALFPHMTVFENMAFGLKLAKtPKDEIDRKVreaARILQL-EALLERRPK---ALSGGQRQRVAIGRAIVRQP 153
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADL---ERVYELfPRLKERRRQragTLSGGEQQMLAIGRALMSRP 155
|
....*...
gi 1431886808 154 GVFLFDEP 161
Cdd:COG0410 156 KLLLLDEP 163
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-234 |
2.01e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 117.81 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIR----DVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN------DVPA 73
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 74 AQRGVAMVFQsyalFPHMTVFE-----NMAFGLKLAKTPKDEIDRKVREAARILQL-EALLERRPKALSGGQRQRVAIGR 147
Cdd:PRK13634 83 LRKKVGIVFQ----FPEHQLFEetvekDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 148 AIVRQPGVFLFDEPLSNLDAtlRGqtRIEI----ARLHKQfAKASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQ 223
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDP--KG--RKEMmemfYKLHKE-KGLTTVLVTHSMEDAARYADQIVVMHKGT-------VFL 226
|
250
....*....|.
gi 1431886808 224 IGAPLELYHRP 234
Cdd:PRK13634 227 QGTPREIFADP 237
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-195 |
3.64e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 115.36 E-value: 3.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN-----DVPAAQRGV 78
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLF 158
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1431886808 159 DEPLSNLDATLRGqtriEIARLHKQFAK--ASVVYVTHD 195
Cdd:PRK10908 162 DEPTGNLDDALSE----GILRLFEEFNRvgVTVLMATHD 196
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-236 |
6.02e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.84 E-value: 6.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 9 VQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDV--PAAQRGVA------- 79
Cdd:PRK10619 11 LHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdKDGQLKVAdknqlrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 ------MVFQSYALFPHMTVFENMAFG----LKLAKTPKDEidRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAI 149
Cdd:PRK10619 90 lrtrltMVFQHFNLWSHMTVLENVMEApiqvLGLSKQEARE--RAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 150 VRQPGVFLFDEPLSNLDATLRGqtriEIARLHKQFAK--ASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAP 227
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVG----EVLRIMQQLAEegKTMVVVTHEMGFARHVSSHVIFLHQGK-------IEEEGAP 236
|
....*....
gi 1431886808 228 LELYHRPRS 236
Cdd:PRK10619 237 EQLFGNPQS 245
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-235 |
6.46e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 117.53 E-value: 6.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 22 DVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ-----RGVAMVFQ-SYA-LFPHMTVF 94
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQdPYAsLNPRMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 95 ENMAFGLKLAK-TPKDEIDRKVREAARILQLEA-LLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQ 172
Cdd:COG4608 116 DIIAEPLRIHGlASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQ 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 173 TRIEIARLHKQFaKASVVYVTHD-----QIeamtlADKIVLLHAGKdterygsIAQIGAPLELYHRPR 235
Cdd:COG4608 196 VLNLLEDLQDEL-GLTYLFISHDlsvvrHI-----SDRVAVMYLGK-------IVEIAPRDELYARPL 250
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-213 |
1.07e-29 |
|
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: 113.84 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAY-GDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAA--QRGVA 79
Cdd:cd03245 2 RIEFRNVSFSYpNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFpHMTVFENMAFGLKLAKtpkdeiDRKVREAARILQLEALLERRPK-----------ALSGGQRQRVAIGRA 148
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 149 IVRQPGVFLFDEPLSNLDatLRGQTRIeIARLHKQFAKASVVYVTHdQIEAMTLADKIVLLHAGK 213
Cdd:cd03245 155 LLNDPPILLLDEPTSAMD--MNSEERL-KERLRQLLGDKTLIIITH-RPSLLDLVDRIIVMDSGR 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-233 |
1.24e-29 |
|
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: 114.80 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDG-DLFIGGEvmndvpaaQRGVAMVF 82
Cdd:COG1119 4 LELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE--------RRGGEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 Q--------SYALF----PHMTVFENMAFGLK----LAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIG 146
Cdd:COG1119 75 ElrkriglvSPALQlrfpRDETVLDVVLSGFFdsigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 147 RAIVRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFAKAsVVYVTH---DQIEAMTladKIVLLHAGKDTERyGSIAQ 223
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPT-LVLVTHhveEIPPGIT---HVLLLKDGRVVAA-GPKEE 229
|
250 260
....*....|....*....|
gi 1431886808 224 I----------GAPLELYHR 233
Cdd:COG1119 230 VltsenlseafGLPVEVERR 249
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-213 |
2.59e-29 |
|
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: 112.76 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNdvPAAQRGVAMVFQ 83
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 164 NLDATLRGQTRIEIARLhkQFAKASVVYVTH--DQIEAMtlADKIVLLHAGK 213
Cdd:cd03269 158 GLDPVNVELLKDVIREL--ARAGKTVILSTHqmELVEEL--CDRVLLLNKGR 205
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
3-213 |
3.30e-29 |
|
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: 119.20 E-value: 3.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAY-GDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAA--QRGVA 79
Cdd:TIGR03375 463 EIEFRNVSFAYpGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAdlRRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFpHMTVFENMAFGLKLAKtpkdeiDRKVREAARILQLEALLERRPK-----------ALSGGQRQRVAIGRA 148
Cdd:TIGR03375 543 YVPQDPRLF-YGTLRDNIALGAPYAD------DEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 149 IVRQPGVFLFDEPLSNLDATLRGQTrieIARLHKQFAKASVVYVTHdQIEAMTLADKIVLLHAGK 213
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDNRSEERF---KDRLKRWLAGKTLVLVTH-RTSLLDLVDRIIVMDNGR 676
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-216 |
3.45e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 112.89 E-value: 3.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP--AAQRGVAMVFQSYALFPHmT 92
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeIYRQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 93 VFENMAFGLKLAKTPKDEiDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQ 172
Cdd:PRK10247 97 VYDNLIFPWQIRNQQPDP-AIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1431886808 173 TRIEIARLHKQfAKASVVYVTHDQIEaMTLADKIVLL--HAGKDTE 216
Cdd:PRK10247 176 VNEIIHRYVRE-QNIAVLWVTHDKDE-INHADKVITLqpHAGEMQE 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-213 |
3.51e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 111.15 E-value: 3.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGA-PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG--VAM 80
Cdd:cd03246 1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHmTVFENMafglklaktpkdeidrkvreaarilqleallerrpkaLSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:cd03246 81 LPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 161 PLSNLDATlrGQTRIEIARLHKQFAKASVVYVTHdQIEAMTLADKIVLLHAGK 213
Cdd:cd03246 123 PNSHLDVE--GERALNQAIAALKAAGATRIVIAH-RPETLASADRILVLEDGR 172
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-237 |
3.52e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 113.98 E-value: 3.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 13 YGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLtDGDLFIGGEV----------MNDVPAAQRGVAMVF 82
Cdd:PRK14258 16 YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRVeffnqniyerRVNLNRLRRQVSMVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 QSYALFPhMTVFENMAFGLKLAK-TPKDEIDRKVREAARILQL----EALLERRPKALSGGQRQRVAIGRAIVRQPGVFL 157
Cdd:PRK14258 95 PKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 158 FDEPLSNLD--ATLRGQTRIEIARLHKQFakaSVVYVTHDQIEAMTLADKIVLLHAGKDteRYGSIAQIGAPLELYHRP- 234
Cdd:PRK14258 174 MDEPCFGLDpiASMKVESLIQSLRLRSEL---TMVIVSHNLHQVSRLSDFTAFFKGNEN--RIGQLVEFGLTKKIFNSPh 248
|
....*
gi 1431886808 235 --RSR 237
Cdd:PRK14258 249 dsRTR 253
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-216 |
4.78e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 113.63 E-value: 4.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDGA--------PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN--- 69
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGlsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAkln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 70 --DVPAAQRGVAMVFQSY--ALFPHMTVFENMAFGLK-LAKTPKDEIDRKVREAARILQL-EALLERRPKALSGGQRQRV 143
Cdd:PRK10419 81 raQRKAFRRDIQMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 144 AIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFAKAsVVYVTHDQIEAMTLADKIVLLHAGKDTE 216
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTA-CLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-213 |
1.46e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 112.39 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMND---VPAAQRGVAM 80
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfskLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQS-YALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFD 159
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 160 EPLSNLDATlRGQTRIE-IARLHKQfaKASVVYVTHDqIEAMTLADKIVLLHAGK 213
Cdd:PRK13644 162 EVTSMLDPD-SGIAVLErIKKLHEK--GKTIVYITHN-LEELHDADRIIVMDRGK 212
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-217 |
1.94e-28 |
|
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: 111.17 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAY-GDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ--RGVAM 80
Cdd:cd03251 1 VEFKNVTFRYpGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFpHMTVFENMAFGLKlaktpkDEIDRKVREAARILQLEALLERRPKA-----------LSGGQRQRVAIGRAI 149
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGRP------GATREEVEEAARAANAHEFIMELPEGydtvigergvkLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 150 VRQPGVFLFDEPLSNLDATLRGQTRIEIARLhkqfAKASVVYVTHDQIEAMTLADKIVLLHAGKDTER 217
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERL----MKNRTTFVIAHRLSTIENADRIVVLEDGKIVER 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-213 |
2.62e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 111.33 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAP----VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG-- 77
Cdd:COG1101 2 LELKNLSKTFNPGTVnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 VAMVFQSYAL--FPHMTVFENMA--------FGLKLAKTpKDEIDRkVREAARILQLEalLERRPKA----LSGGQRQRV 143
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLT-KKRREL-FRELLATLGLG--LENRLDTkvglLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 144 AIGRAIVRQPGVFLFDEPLSNLDAtlrgQTRIEIARLHKQFAKA---SVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDP----KTAALVLELTEKIVEEnnlTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-166 |
5.96e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 109.73 E-value: 5.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPA---AQRG 77
Cdd:COG1137 1 MMTLEAENLVKSYG-KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhkrARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 VAMVFQSYALFPHMTVFEN-MAFgLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVF 156
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNiLAV-LELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170
....*....|
gi 1431886808 157 LFDEPLSNLD 166
Cdd:COG1137 159 LLDEPFAGVD 168
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-243 |
1.33e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 109.37 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 13 YGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN--------DVPAAQRGVAMVFQS 84
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqiDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 85 YALFPHMTVFENMAFGLKL-AKTPKDEIDRKVREAARILQLEALLERR----PKALSGGQRQRVAIGRAIVRQPGVFLFD 159
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKShGIKEKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 160 EPLSNLDATLRGQTRIEIARLHKQFAkasVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSRFV 239
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIA---IVIVSHNPQQVARVADYVAFLYNGE-------LVEWGSSNEIFTSPKNELT 248
|
....
gi 1431886808 240 AGFI 243
Cdd:PRK14246 249 EKYV 252
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-161 |
1.91e-27 |
|
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: 108.38 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 5 SLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQR---GVAMV 81
Cdd:TIGR03410 2 EVSNLNVYYG-QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFPHMTVFENMAFGLKLAKTPKDEIDrkvreaARILQ----LEALLERRPKALSGGQRQRVAIGRAIVRQPGVFL 157
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIP------DEIYElfpvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
....
gi 1431886808 158 FDEP 161
Cdd:TIGR03410 155 LDEP 158
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-209 |
7.73e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.39 E-value: 7.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEvmndvpaaqRGVAMVFQSYAL---FPhM 91
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------ARVAYVPQRSEVpdsLP-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 92 TVFENMAFGL----KLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDA 167
Cdd:NF040873 73 TVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1431886808 168 TLRGQTRIEIARLHKQfaKASVVYVTHDqIEAMTLADKIVLL 209
Cdd:NF040873 153 ESRERIIALLAEEHAR--GATVVVVTHD-LELVRRADPCVLL 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-213 |
1.07e-26 |
|
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: 106.09 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPA---AQRGVAM 80
Cdd:cd03218 1 LRAENLSKRYG-KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhkrARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 161 PLSNLDATlrgqTRIEIARLHKQFAKASV-VYVT-HDQIEAMTLADKIVLLHAGK 213
Cdd:cd03218 160 PFAGVDPI----AVQDIQKIIKILKDRGIgVLITdHNVRETLSITDRAYIIYEGK 210
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-213 |
1.58e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 106.35 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 16 GAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP----AAQRGVamVFQSYAL-FPh 90
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSpwelARRRAV--LPQHSSLaFP- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 91 MTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAI------VRQPGVFLF-DEPLS 163
Cdd:COG4559 90 FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPRWLFlDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 164 NLDatLRGQtrIEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:COG4559 170 ALD--LAHQ--HAVLRLARQLARRggGVVAVLHDLNLAAQYADRILLLHQGR 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-233 |
1.59e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.12 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVM--NDVPAAQRGVAMVFQSY-ALFPHMTVF 94
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteENVWDIRHKIGMVFQNPdNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 95 ENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRgQTR 174
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGR-LEL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 175 IEIARLHKQFAKASVVYVTHDqIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHR 233
Cdd:PRK13650 180 IKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQ-------VESTSTPRELFSR 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
13-213 |
2.82e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 106.36 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 13 YGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNdvPAAQR----GVAMVFQSY--A 86
Cdd:PRK13647 14 YKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN--AENEKwvrsKVGLVFQDPddQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 87 LFPhMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLD 166
Cdd:PRK13647 92 VFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1431886808 167 AtlRGQ-TRIEI-ARLHKQfaKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:PRK13647 171 P--RGQeTLMEIlDRLHNQ--GKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-213 |
3.67e-26 |
|
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: 103.78 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAG-LEDLTD-GDLFIGGE-VMNDVPAAQrgVAMVFQSYALFPHMTVF 94
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVsGEVLINGRpLDKRSFRKI--IGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 95 ENMAFGLKLaktpkdeidrkvreaarilqleallerrpKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATlrgqTR 174
Cdd:cd03213 101 ETLMFAAKL-----------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS----SA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1431886808 175 IEIARLHKQFAKA--SVVYVTHD-QIEAMTLADKIVLLHAGK 213
Cdd:cd03213 148 LQVMSLLRRLADTgrTIICSIHQpSSEIFELFDKLLLLSQGR 189
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-235 |
4.39e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 107.10 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 22 DVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGD-LFIGGEV--MNDVP--AAQRGVAMVFQS--YALFPHMTVF 94
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEvAWLGKDLlgMKDDEwrAVRSDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 95 ENMAFGLKL--AKTPKDEIDRKVREA-ARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRG 171
Cdd:PRK15079 119 EIIAEPLRTyhPKLSRQEVKDRVKAMmLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 172 QtrieIARLHKQFAKA---SVVYVTHDQIEAMTLADKIVLLHAGKDTErygsiaqIGAPLELYHRPR 235
Cdd:PRK15079 199 Q----VVNLLQQLQREmglSLIFIAHDLAVVKHISDRVLVMYLGHAVE-------LGTYDEVYHNPL 254
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-231 |
4.44e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.54 E-value: 4.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN----DVPAAQRGVA 79
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkkSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSY--ALFPHmTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFL 157
Cdd:PRK13639 82 IVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1431886808 158 FDEPLSNLDAtlrgQTRIEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELY 231
Cdd:PRK13639 161 LDEPTSGLDP----MGASQIMKLLYDLNKEgiTIIISTHDVDLVPVYADKVYVMSDGK-------IIKEGTPKEVF 225
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-234 |
4.63e-26 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 110.05 E-value: 4.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYG-DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN--DVPAAQRGVA 79
Cdd:TIGR03797 451 AIEVDRVTFRYRpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFPHmTVFENMAFGLKLakTPKDeidrkVREAARILQLEALLERRP-----------KALSGGQRQRVAIGRA 148
Cdd:TIGR03797 531 VVLQNGRLMSG-SIFENIAGGAPL--TLDE-----AWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARA 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 149 IVRQPGVFLFDEPLSNLD-----------ATLRGqTRIEIA-RLhkqfakaSVVyvthdqieamTLADKIVLLHAGKdte 216
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDnrtqaivseslERLKV-TRIVIAhRL-------STI----------RNADRIYVLDAGR--- 661
|
250
....*....|....*...
gi 1431886808 217 rygsIAQIGAPLELYHRP 234
Cdd:TIGR03797 662 ----VVQQGTYDELMARE 675
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-224 |
6.16e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.86 E-value: 6.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLtDGDLFIGGEVM----------NDVPAAQRGVAMVFQSYALFP 89
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDL-NPEVTITGSIVynghniysprTDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 90 hMTVFENMAFGLKLA----KTPKDE-IDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSN 164
Cdd:PRK14239 100 -MSIYENVVYGLRLKgikdKQVLDEaVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 165 LDATLRGQTRIEIARLHKQFakaSVVYVTHDQIEAMTLADKIVLLHAGKDTErYGSIAQI 224
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDY---TMLLVTRSMQQASRISDRTGFFLDGDLIE-YNDTKQM 234
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-213 |
1.03e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.08 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 2 ASISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ--RGVA 79
Cdd:PRK13548 1 AMLEARNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYAL-FPhMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVR------Q 152
Cdd:PRK13548 80 VLPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 153 PGVFLFDEPLSNLDatLRGQtrIEIARLHKQFAK---ASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:PRK13548 159 PRWLLLDEPTSALD--LAHQ--HHVLRLARQLAHergLAVIVVLHDLNLAARYADRIVLLHQGR 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3-213 |
4.70e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.90 E-value: 4.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDGAP----VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN------DVP 72
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 73 AAQRGVAMVFQsyalFPHMTVFE-----NMAFGLKLAKTPKDEIDRKVREAARILQL-EALLERRPKALSGGQRQRVAIG 146
Cdd:PRK13649 82 QIRKKVGLVFQ----FPESQLFEetvlkDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 147 RAIVRQPGVFLFDEPLSNLDAtlrgQTRIEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDP----KGRKELMTLFKKLHQSgmTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-232 |
1.09e-24 |
|
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: 101.08 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGD--GAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMND--VPAAQRGVA 79
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlnLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFPhMTVFENMAFGLKlaktpkDEIDRKVREAAR-------ILQL----EALLERRPKALSGGQRQRVAIGRA 148
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYGKP------DATDEEVEEAAKkanihdfIMSLpdgyDTLVGERGSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 149 IVRQPGVFLFDEPLSNLDA--------TL----RGQTRIEIA-RLHkqfakasvvyvthdqieamTL--ADKIVLLHAGK 213
Cdd:cd03249 154 LLRNPKILLLDEATSALDAeseklvqeALdramKGRTTIVIAhRLS-------------------TIrnADLIAVLQNGQ 214
|
250
....*....|....*....
gi 1431886808 214 DTERyGSIAQIGAPLELYH 232
Cdd:cd03249 215 VVEQ-GTHDELMAQKGVYA 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-230 |
1.16e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 105.27 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 7 RGVQKAygdgapvIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLF--IGGEV--MNDVPAAQRGVA--- 79
Cdd:TIGR03269 294 RGVVKA-------VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEWvdMTKPGPDGRGRAkry 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 --MVFQSYALFPHMTVFENM--AFGLKLAktpkDEIDRkvREAARILQL--------EALLERRPKALSGGQRQRVAIGR 147
Cdd:TIGR03269 367 igILHQEYDLYPHRTVLDNLteAIGLELP----DELAR--MKAVITLKMvgfdeekaEEILDKYPDELSEGERHRVALAQ 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 148 AIVRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFAKASVVyVTHDQIEAMTLADKIVLLhagkdteRYGSIAQIGAP 227
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFII-VSHDMDFVLDVCDRAALM-------RDGKIVKIGDP 512
|
...
gi 1431886808 228 LEL 230
Cdd:TIGR03269 513 EEI 515
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-224 |
1.86e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.72 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ------- 75
Cdd:COG4152 1 MLELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 76 RGvamvfqsyaLFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGV 155
Cdd:COG4152 80 RG---------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431886808 156 FLFDEPLSNLDATLRGQTRIEIARLHKQfaKASVVYVTH--DQIEAmtLADKIVLLHAGKdTERYGSIAQI 224
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAK--GTTVIFSSHqmELVEE--LCDRIVIINKGR-KVLSGSVDEI 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-231 |
3.54e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.85 E-value: 3.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAP----VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGG-------EVMNDVP 72
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 73 AAQRGVAMVFQ--SYALFPHmTVFENMAFGLKLAKTPKDEIDRKVREAARILQL-EALLERRPKALSGGQRQRVAIGRAI 149
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 150 VRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFAKaSVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLE 229
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKK-RIIMVTHNMDQVLRIADEVIVMHEGK-------VISIGSPFE 237
|
..
gi 1431886808 230 LY 231
Cdd:PRK13645 238 IF 239
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-213 |
4.93e-24 |
|
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: 98.31 E-value: 4.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGevmndvpaaqrGVAMVFQSYALFPhMTVF 94
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQEPWIQN-GTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 95 ENMAFGLKLaktpkDEidRKVREAARILQLEALLERRPK-----------ALSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:cd03250 84 ENILFGKPF-----DE--ERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 164 NLDA--------------TLRGQTRIeiarlhkqfakasvvYVTHdQIEAMTLADKIVLLHAGK 213
Cdd:cd03250 157 AVDAhvgrhifencilglLLNNKTRI---------------LVTH-QLQLLPHADQIVVLDNGR 204
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-204 |
5.32e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 99.84 E-value: 5.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEvmnDVPAAQRG------ 77
Cdd:PRK11831 8 VDMRGVSFTRGN-RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE---NIPAMSRSrlytvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 --VAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRkvreAARILQLEALLER-----RPKALSGGQRQRVAIGRAIV 150
Cdd:PRK11831 84 krMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLH----STVMMKLEAVGLRgaaklMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 151 RQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFAKASVVyVTHDQIEAMTLAD 204
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVV-VSHDVPEVLSIAD 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-229 |
5.37e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.32 E-value: 5.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ--RGVAM 80
Cdd:PRK11231 2 TLRTENLTVGYGT-KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMAFG----LKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVF 156
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 157 LFDEPLSNLDatLRGQtrIEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGKdterygSIAQiGAPLE 229
Cdd:PRK11231 161 LLDEPTTYLD--INHQ--VELMRLMRELNTQgkTVVTVLHDLNQASRYCDHLVVLANGH------VMAQ-GTPEE 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-213 |
6.35e-24 |
|
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: 98.50 E-value: 6.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 19 VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLED---LTDGDLFIGGEVMNdvPAA-QRGVAMVFQSYALFPHMTVF 94
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRK--PDQfQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 95 ENMAFG--LKLAKTPKDEIDRKVREAARILQL--EALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATlr 170
Cdd:cd03234 100 ETLTYTaiLRLPRKSSDAIRKKRVEDVLLRDLalTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF-- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1431886808 171 gqTRIEIARLHKQFAKA-SVVYVTHDQ--IEAMTLADKIVLLHAGK 213
Cdd:cd03234 178 --TALNLVSTLSQLARRnRIVILTIHQprSDLFRLFDRILLLSSGE 221
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-217 |
6.82e-24 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 103.36 E-value: 6.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 2 ASISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAA--QRGVA 79
Cdd:COG5265 356 GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFpHMTVFENMAFGlklaktpKDEIDR-KVREAARILQLEALLERRPKA-----------LSGGQRQRVAIGR 147
Cdd:COG5265 436 IVPQDTVLF-NDTIAYNIAYG-------RPDASEeEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 148 AIVRQPGVFLFDEPLSNLD--------ATL----RGQTRIEIA-RLhkqfakaSVvyVTHdqieamtlADKIVLLHAGKD 214
Cdd:COG5265 508 TLLKNPPILIFDEATSALDsrteraiqAALrevaRGRTTLVIAhRL-------ST--IVD--------ADEILVLEAGRI 570
|
...
gi 1431886808 215 TER 217
Cdd:COG5265 571 VER 573
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
23-231 |
6.93e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.78 E-value: 6.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 23 VDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN--DVPAAQRGVAMVFQSY-ALFPHMTVFENMAF 99
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNPdNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 100 GLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEIAR 179
Cdd:PRK13642 106 GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 180 LHKQFaKASVVYVTHDQIEAMTlADKIVLLHAGKdterygsIAQIGAPLELY 231
Cdd:PRK13642 186 IKEKY-QLTVLSITHDLDEAAS-SDRILVMKAGE-------IIKEAAPSELF 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-216 |
7.92e-24 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 98.71 E-value: 7.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAY-GDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAA--QRGVAM 80
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFpHMTVFENMAfglkLAKTPKDEidRKVREAAR-------ILQL----EALLERRPKALSGGQRQRVAIGRAI 149
Cdd:cd03252 81 VLQENVLF-NRSIRDNIA----LADPGMSM--ERVIEAAKlagahdfISELpegyDTIVGEQGAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 150 VRQPGVFLFDEPLSNLDATlrgQTRIEIARLHKQFAKASVVYVTHdQIEAMTLADKIVLLHAGKDTE 216
Cdd:cd03252 154 IHNPRILIFDEATSALDYE---SEHAIMRNMHDICAGRTVIIIAH-RLSTVKNADRIIVMEKGRIVE 216
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-213 |
1.79e-23 |
|
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: 101.75 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 2 ASISLRGVQKAY-GDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG--V 78
Cdd:COG4618 329 GRLSVENLTVVPpGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSYALFPHmTVFENMA-FGlklaktpkDEIDRKVREAAR-------ILQL----EALLERRPKALSGGQRQRVAIG 146
Cdd:COG4618 409 GYLPQDVELFDG-TIAENIArFG--------DADPEKVVAAAKlagvhemILRLpdgyDTRIGEGGARLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431886808 147 RAIVRQPGVFLFDEPLSNLDAT----LRGQtrieIARLHKQfaKASVVYVTHDQiEAMTLADKIVLLHAGK 213
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEgeaaLAAA----IRALKAR--GATVVVITHRP-SLLAAVDKLLVLRDGR 543
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-236 |
2.02e-23 |
|
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: 101.68 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 22 DVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDlTDGDLFIGGEVMNDVPAAQ-----RGVAMVFQS-YA-LFPHMTVF 94
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRMTVG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 95 ENMAFGLKLAKTP--KDEIDRKVREAARILQL-EALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRG 171
Cdd:COG4172 383 QIIAEGLRVHGPGlsAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQA 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 172 QTrIEI-ARLHKQFaKASVVYVTHDQ--IEAMtlADKIVLLHAGKDTERygsiaqiGAPLELYHRPRS 236
Cdd:COG4172 463 QI-LDLlRDLQREH-GLAYLFISHDLavVRAL--AHRVMVMKDGKVVEQ-------GPTEQVFDAPQH 519
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-231 |
2.08e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.28 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAY-GDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN--DVPAAQRGVAM 80
Cdd:PRK13648 8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQS-YALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFD 159
Cdd:PRK13648 88 VFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 160 EPLSNLDATLRgQTRIEIARLHKQFAKASVVYVTHDQIEAMTlADKIVLLHAGKdterygsIAQIGAPLELY 231
Cdd:PRK13648 168 EATSMLDPDAR-QNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGT-------VYKEGTPTEIF 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-213 |
3.02e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 6 LRGVQKAYGdGAPVIRDVDLEIGENEfCV-FLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVmndvpaaqRgVAMVFQS 84
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGD-RIgLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL--------R-IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 85 YALFPHMTVFENMAFGL---------------KLAKTPKD-----------------EIDRKVREAARILQL-EALLERR 131
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDaelraleaeleeleaKLAEPDEDlerlaelqeefealggwEAEARAEEILSGLGFpEEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 132 PKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDatlrgqtrIE-IARLH---KQFAKAsVVYVTHDQ--IEAMtlADK 205
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--------LEsIEWLEeflKNYPGT-VLVVSHDRyfLDRV--ATR 218
|
....*...
gi 1431886808 206 IVLLHAGK 213
Cdd:COG0488 219 ILELDRGK 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-213 |
3.62e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.85 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGG---EVMNDVPAAQRGVAMVFQSyalfPH---- 90
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PDnqiv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 91 -MTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATL 169
Cdd:PRK13633 100 aTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1431886808 170 RGQTRIEIARLHKQFAkASVVYVTHDQIEAMTlADKIVLLHAGK 213
Cdd:PRK13633 180 RREVVNTIKELNKKYG-ITIILITHYMEEAVE-ADRIIVMDSGK 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-195 |
5.75e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.00 E-value: 5.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 23 VDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG------VAMVFQSYALFPHMTVFEN 96
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 97 mafgLKLAKTPKDEIDRKVREAARILQLEALLERR----PKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDAtlrgQ 172
Cdd:PRK10584 109 ----VELPALLRGESSRQSRNGAKALLEQLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR----Q 180
|
170 180
....*....|....*....|....*..
gi 1431886808 173 TRIEIA----RLHKQFAkASVVYVTHD 195
Cdd:PRK10584 181 TGDKIAdllfSLNREHG-TTLILVTHD 206
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
17-212 |
7.92e-23 |
|
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: 100.11 E-value: 7.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 17 APVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG--VAMVFQSYALFPHmTVF 94
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIGYLPQDVELFPG-TVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 95 ENMA-FGlklaktpKDEIDRKVREAARILQLEALLERRPK-----------ALSGGQRQRVAIGRAIVRQPGVFLFDEPL 162
Cdd:TIGR01842 410 ENIArFG-------ENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1431886808 163 SNLDATlrGQTRIEIARLHKQFAKASVVYVTHdQIEAMTLADKIVLLHAG 212
Cdd:TIGR01842 483 SNLDEE--GEQALANAIKALKARGITVVVITH-RPSLLGCVDKILVLQDG 529
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-213 |
4.14e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.91 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN----DVPAAQRGVA 79
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQS--YALFPhMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFL 157
Cdd:PRK13636 86 MVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 158 FDEPLSNLDAtlRGQTriEIARLHKQFAKA---SVVYVTHDqIEAMTL-ADKIVLLHAGK 213
Cdd:PRK13636 165 LDEPTAGLDP--MGVS--EIMKLLVEMQKElglTIIIATHD-IDIVPLyCDNVFVMKEGR 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
37-235 |
4.86e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.42 E-value: 4.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 37 GPSGCGKSTLLRMIAGLEDLTDGDLFIGGE-VMNDVPAAQ----RGVAMVFQS-YA-LFPHMTVFENMAFGLKLaKTPKD 109
Cdd:PRK11308 48 GESGCGKSTLARLLTMIETPTGGELYYQGQdLLKADPEAQkllrQKIQIVFQNpYGsLNPRKKVGQILEEPLLI-NTSLS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 110 EIDRKvreaARILQLEALL-------ERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEIARLHK 182
Cdd:PRK11308 127 AAERR----EKALAMMAKVglrpehyDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 183 QFaKASVVYVTHDQIEAMTLADKIVLLHAGKDTERyGSIAQIgaplelYHRPR 235
Cdd:PRK11308 203 EL-GLSYVFISHDLSVVEHIADEVMVMYLGRCVEK-GTKEQI------FNNPR 247
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-273 |
1.09e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.71 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN--DVPAAQRGV 78
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkeNIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSY--ALFPhMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVF 156
Cdd:PRK13652 81 GLVFQNPddQIFS-PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 157 LFDEPLSNLDATLRGQTRIEIARLHKQFAkASVVYVTHDQIEAMTLADKIVLLHAGKDTErYGSIAQIGAPLELYHRPRS 236
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYG-MTVIFSTHQLDLVPEMADYIYVMDKGRIVA-YGTVEEIFLQPDLLARVHL 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 1431886808 237 rfvagfigspRMNFLPGRIASFDAQGVVVALDHTHEN 273
Cdd:PRK13652 238 ----------DLPSLPKLIRSLQAQGIAIDMAYTYQE 264
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-242 |
1.09e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.72 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 2 ASISLRGVQKAYGDG---APVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGG----EVMNDVPAA 74
Cdd:PRK10535 3 ALLELKDIRRSYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvaTLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 75 QR--GVAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQ 152
Cdd:PRK10535 83 LRreHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 153 PGVFLFDEPLSNLDAtlrgQTRIEIARLHKQFAKA--SVVYVTHD-QIEAMtlADKIVLLHAGK---DTERYGSIAQIGA 226
Cdd:PRK10535 163 GQVILADEPTGALDS----HSGEEVMAILHQLRDRghTVIIVTHDpQVAAQ--AERVIEIRDGEivrNPPAQEKVNVAGG 236
|
250
....*....|....*...
gi 1431886808 227 PLELYHRPRS--RFVAGF 242
Cdd:PRK10535 237 TEPVVNTASGwrQFVSGF 254
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-232 |
1.12e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.64 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAP----VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN------DVPA 73
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 74 AQRGVAMVFQsyalFPHMTVFE-----NMAFGLKLAKTPKDEIDRKVREAARILQL-EALLERRPKALSGGQRQRVAIGR 147
Cdd:PRK13643 82 VRKKVGVVFQ----FPESQLFEetvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 148 AIVRQPGVFLFDEPLSNLDAtlrgQTRIEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIG 225
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDP----KARIEMMQLFESIHQSgqTVVLVTHLMDDVADYADYVYLLEKGH-------IISCG 226
|
....*..
gi 1431886808 226 APLELYH 232
Cdd:PRK13643 227 TPSDVFQ 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-217 |
1.23e-21 |
|
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: 96.32 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAY-GDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAA--QRGVAM 80
Cdd:TIGR02203 331 VEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAslRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHmTVFENMAFGlklakTPKDEIDRKVREAARILQLEALLERRPKA-----------LSGGQRQRVAIGRAI 149
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG-----RTEQADRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 150 VRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQfaKASVVyVTHdQIEAMTLADKIVLLHAGKDTER 217
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQG--RTTLV-IAH-RLSTIEKADRIVVMDDGRIVER 548
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-230 |
1.32e-21 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 92.22 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 25 LEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEvmnDVPAAQRGVAMVFQSYAL---FP---HMTVFENMA 98
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFPisvAHTVMSGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 99 FGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLD---ATLRGQTRI 175
Cdd:TIGR03771 78 GHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDmptQELLTELFI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 176 EIARlhkqfAKASVVYVTHDQIEAMTLADKIVLLHagkdteryGSIAQIGAPLEL 230
Cdd:TIGR03771 158 ELAG-----AGTAILMTTHDLAQAMATCDRVVLLN--------GRVIADGTPQQL 199
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-195 |
1.74e-21 |
|
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: 95.89 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 2 ASISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP--AAQRGVA 79
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqdEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFpHMTVFENMAFGlklaktPKDEIDRKVREAARILQLEALLERRP-----------KALSGGQRQRVAIGRA 148
Cdd:TIGR02868 413 VCAQDAHLF-DTTVRENLRLA------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1431886808 149 IVRQPGVFLFDEPLSNLDATLRGQTrieIARLHKQFAKASVVYVTHD 195
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADEL---LEDLLAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-242 |
1.84e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.76 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 13 YGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN----DVPAAQRGVAMVFQSyalf 88
Cdd:PRK13638 11 YQD-EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQD---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 89 PHMTVF-----ENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:PRK13638 86 PEQQIFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 164 NLDATLRGQTRIEIARLHKQfaKASVVYVTHDQIEAMTLADKIVLLhagkdteRYGSIAQIGAPLELYHRPRSRFVAGF 242
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQ--GNHVIISSHDIDLIYEISDAVYVL-------RQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-232 |
2.04e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 95.96 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP--AAQRGVAM 80
Cdd:TIGR01193 473 DIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDrhTLRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHmTVFENMAFGLKlAKTPKDEIDRkvreAARILQLEALLERRPKA-----------LSGGQRQRVAIGRAI 149
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLGAK-ENVSQDEIWA----ACEIAEIKDDIENMPLGyqtelseegssISGGQKQRIALARAL 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 150 VRQPGVFLFDEPLSNLDATLrgQTRIeIARLHKQFAKaSVVYVTHdQIEAMTLADKIVLLHAGKDTERyGS----IAQIG 225
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTIT--EKKI-VNNLLNLQDK-TIIFVAH-RLSVAKQSDKIIVLDHGKIIEQ-GShdelLDRNG 700
|
....*..
gi 1431886808 226 APLELYH 232
Cdd:TIGR01193 701 FYASLIH 707
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-221 |
2.36e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGgevmndvpaaqRGVAMVF- 82
Cdd:COG0488 316 LELEGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG-----------ETVKIGYf 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 -QSYALF-PHMTVFENMafglklaktpkdeidRKVREAARILQLEALLER----------RPKALSGGQRQRVAIGRAIV 150
Cdd:COG0488 384 dQHQEELdPDKTVLDEL---------------RDGAPGGTEQEVRGYLGRflfsgddafkPVGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 151 RQPGVFLFDEPLSNLDAtlrgQTRIEIARLHKQFaKASVVYVTHDQ--IEamTLADKIVLLHAGKDTERYGSI 221
Cdd:COG0488 449 SPPNVLLLDEPTNHLDI----ETLEALEEALDDF-PGTVLLVSHDRyfLD--RVATRILEFEDGGVREYPGGY 514
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
23-212 |
4.13e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 91.61 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 23 VDLEIGENEFCVFLGPSGCGKSTLLRMIAGLedlTDGDLFIG-------------GEVMNDVPAAQRGVAMVFQSYALFP 89
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGshiellgrtvqreGRLARDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 90 HMTVFENMAFGlKLAKTP----------KDEIDRKVREAARIlQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFD 159
Cdd:PRK09984 100 RLSVLENVLIG-ALGSTPfwrtcfswftREQKQRALQALTRV-GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 160 EPLSNLDATlrgQTRIEIARLH--KQFAKASVVYVTHDQIEAMTLADKIVLLHAG 212
Cdd:PRK09984 178 EPIASLDPE---SARIVMDTLRdiNQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-194 |
4.85e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.87 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 2 ASISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLfiggevmnDVPAAQRgvaMV 81
Cdd:COG4178 361 GALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR---VL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 F---QSYalFPHMTVFENMAFglklAKTPKDEIDRKVREAARILQLEALLER------RPKALSGGQRQRVAIGRAIVRQ 152
Cdd:COG4178 430 FlpqRPY--LPLGTLREALLY----PATAEAFSDAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHK 503
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1431886808 153 PGVFLFDEPLSNLDATLRGQTrieIARLHKQFAKASVVYVTH 194
Cdd:COG4178 504 PDWLFLDEATSALDEENEAAL---YQLLREELPGTTVISVGH 542
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-213 |
5.37e-21 |
|
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: 90.85 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 5 SLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEV-MNDVPAAQRGVAMVF- 82
Cdd:cd03267 22 SLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpWKRRKKFLRRIGVVFg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 QSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPL 162
Cdd:cd03267 102 QKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 163 SNLDATLRGQTRIEIARLHKQFaKASVVYVTHD--QIEAmtLADKIVLLHAGK 213
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRER-GTTVLLTSHYmkDIEA--LARRVLVIDKGR 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-230 |
5.80e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.18 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 2 ASISLRGVQKAYGDGApVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGE-VMNDVPAAQRGVAM 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMA-----FGLKLAktpkdEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGV 155
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLvfgryFGLSAA-----AARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 156 FLFDEPLSNLDAtlrgQTRIEI-ARLHKQFAKA-SVVYVTHDQIEAMTLADKIVLLHAGKdterygSIAQiGAPLEL 230
Cdd:PRK13537 160 LVLDEPTTGLDP----QARHLMwERLRSLLARGkTILLTTHFMEEAERLCDRLCVIEEGR------KIAE-GAPHAL 225
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
3-231 |
7.45e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.38 E-value: 7.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDGAP----VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGG-EVMNDV------ 71
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTkdkyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 72 PAAQRgVAMVFQsyalFPHMTVFEN-----MAFGLKLAKTPKDEIdrKVREAARILQL---EALLERRPKALSGGQRQRV 143
Cdd:PRK13646 82 PVRKR-IGMVFQ----FPESQLFEDtvereIIFGPKNFKMNLDEV--KNYAHRLLMDLgfsRDVMSQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 144 AIGRAIVRQPGVFLFDEPLSNLDAtlrgQTRIEIARLHKQFA---KASVVYVTHDQIEAMTLADKIVLLhagkdteRYGS 220
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDP----QSKRQVMRLLKSLQtdeNKTIILVSHDMNEVARYADEVIVM-------KEGS 223
|
250
....*....|.
gi 1431886808 221 IAQIGAPLELY 231
Cdd:PRK13646 224 IVSQTSPKELF 234
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-234 |
1.14e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.01 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDG-APVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGL---EDLTDGDLFIGGEVMND--VPAAQRG 77
Cdd:PRK13640 6 VEFKHVSFTYPDSkKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAktVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 VAMVFQSY-ALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVF 156
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 157 LFDEPLSNLDATLRGQTrIEIARLHKQFAKASVVYVTHDqIEAMTLADKIVLLHAGKdterygSIAQiGAPLELYHRP 234
Cdd:PRK13640 166 ILDESTSMLDPAGKEQI-LKLIRKLKKKNNLTVISITHD-IDEANMADQVLVLDDGK------LLAQ-GSPVEIFSKV 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-213 |
1.23e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.66 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDGAPV----IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN------DVP 72
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 73 AAQRGVAMVFQsyalFPHMTVFEN-----MAFGLKLAKTPKDEIDRKVREAARILQL-EALLERRPKALSGGQRQRVAIG 146
Cdd:PRK13641 82 KLRKKVSLVFQ----FPEAQLFENtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 147 RAIVRQPGVFLFDEPLSNLDAtlrgQTRIEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDP----EGRKEMMQLFKDYQKAghTVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-233 |
1.84e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.97 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 2 ASISLRGVQKAYGDGA-PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ--RGV 78
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSYALFPHmTVFENmafgLKLAKtpKDEIDRKVREAARILQLEALLER------------RPkaLSGGQRQRVAIG 146
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDN----LLLAA--PNASDEALIEVLQQVGLEKLLEDdkglnawlgeggRQ--LSGGEQRRLGIA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 147 RAIVRQPGVFLFDEPLSNLDAtlrgQTRIEIARLHKQFAK-ASVVYVTHdQIEAMTLADKIVLLHAGKDTErYGS----I 221
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDA----ETERQILELLAEHAQnKTVLMITH-RLTGLEQFDRICVMDNGQIIE-QGThqelL 561
|
250
....*....|..
gi 1431886808 222 AQIGAPLELYHR 233
Cdd:PRK11160 562 AQQGRYYQLKQR 573
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-212 |
1.86e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.81 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEV---MNDVPAAQRGVAM 80
Cdd:PRK15439 12 LCARSISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcarLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMAFGlkLAKTPKDEidRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFG--LPKRQASM--QKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 161 PLSNLdatlrgqTRIEIARLHKQFAK-----ASVVYVTHDQIEAMTLADKIVLLHAG 212
Cdd:PRK15439 167 PTASL-------TPAETERLFSRIREllaqgVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
4-217 |
2.25e-20 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 93.08 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGD-GAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP--AAQRGVAM 80
Cdd:TIGR03796 478 VELRNITFGYSPlEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPreVLANSVAM 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFpHMTVFENMAfgLKLAKTPKDEIDRKVREAA-------RILQLEALLERRPKALSGGQRQRVAIGRAIVRQP 153
Cdd:TIGR03796 558 VDQDIFLF-EGTVRDNLT--LWDPTIPDADLVRACKDAAihdvitsRPGGYDAELAEGGANLSGGQRQRLEIARALVRNP 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 154 GVFLFDEPLSNLDATL----------RGQTRIEIA-RLhkqfakaSVVyvtHDqieamtlADKIVLLHAGKDTER 217
Cdd:TIGR03796 635 SILILDEATSALDPETekiiddnlrrRGCTCIIVAhRL-------STI---RD-------CDEIIVLERGKVVQR 692
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-230 |
2.42e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGE-VMNDVPAAQRGVA 79
Cdd:PRK13536 39 TVAIDLAGVSKSYGD-KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFPHMTVFENMA-----FGLKLAKTpkDEIDRKVREAARilqLEALLERRPKALSGGQRQRVAIGRAIVRQPG 154
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLvfgryFGMSTREI--EAVIPSLLEFAR---LESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 155 VFLFDEPLSNLDATLRgqtRIEIARLHKQFAKA-SVVYVTHDQIEAMTLADKIVLLHAGKdterygSIAQiGAPLEL 230
Cdd:PRK13536 193 LLILDEPTTGLDPHAR---HLIWERLRSLLARGkTILLTTHFMEEAERLCDRLCVLEAGR------KIAE-GRPHAL 259
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-246 |
2.48e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.46 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN--DVPAAQRGVAMVFQ--SYALFPHMTVFE 95
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQdpSTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 96 NMAFGLKLaKTPKDEIDRKVREAARILQLEALLERR---PKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQ 172
Cdd:PRK15112 109 ILDFPLRL-NTDLEPEQREKQIIETLRQVGLLPDHAsyyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 173 TRIEIARLHKQFAkASVVYVTHDQIEAMTLADKIVLLHAGKDTERyGSIAQI-GAPLelyHRPRSRFVAGFIGSP 246
Cdd:PRK15112 188 LINLMLELQEKQG-ISYIYVTQHLGMMKHISDQVLVMHQGEVVER-GSTADVlASPL---HELTKRLIAGHFGEA 257
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-213 |
4.41e-20 |
|
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: 87.97 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 19 VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVmndvpAAQRGVAMVFQsyalfPHMTVFENMA 98
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-----SSLLGLGGGFN-----PELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 99 FGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEIA 178
Cdd:cd03220 107 LNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLR 186
|
170 180 190
....*....|....*....|....*....|....*
gi 1431886808 179 RLHKQfaKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03220 187 ELLKQ--GKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-244 |
5.01e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.00 E-value: 5.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 16 GAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDG-----DLFIGGEVM---NDVPAAQRGVAMVFQSYAL 87
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 88 FPhMTVFENMAFGLKLAK-TPKDEIdRKVREAaRILQL---EALLER---RPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:PRK14271 113 FP-MSIMDNVLAGVRAHKlVPRKEF-RGVAQA-RLTEVglwDAVKDRlsdSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 161 PLSNLDATlrgqTRIEIARLHKQFA-KASVVYVTHDQIEAMTLADKIVLLHAGKDTERYGSIAQIGAPlelYHRPRSRFV 239
Cdd:PRK14271 190 PTSALDPT----TTEKIEEFIRSLAdRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP---KHAETARYV 262
|
....*
gi 1431886808 240 AGFIG 244
Cdd:PRK14271 263 AGLSG 267
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
15-213 |
6.13e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.82 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLED--LTDGDLFIGGEVMNDVPA---AQRGVAMVFQSYALFP 89
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPderARAGIFLAFQYPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 90 HMTVFEnmaFgLKLAKTPKDEID-------RKVREAARILQLEALLERRP--KALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:COG0396 91 GVSVSN---F-LRTALNARRGEElsareflKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 161 PLSNLDA-TLRGQTRIeIARLHKQfaKASVVYVTH-----DQIEamtlADKIVLLHAGK 213
Cdd:COG0396 167 TDSGLDIdALRIVAEG-VNKLRSP--DRGILIITHyqrilDYIK----PDFVHVLVDGR 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-237 |
1.63e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN--DVPAAQRGV 78
Cdd:PRK09536 1 MPMIDVSDLSVEFGD-TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSYAL--------------FPHMTVFENMafglklakTPKDeiDRKVREAARILQLEALLERRPKALSGGQRQRVA 144
Cdd:PRK09536 80 ASVPQDTSLsfefdvrqvvemgrTPHRSRFDTW--------TETD--RAAVERAMERTGVAQFADRPVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 145 IGRAIVRQPGVFLFDEPLSNLDATLRGQTrIEIARLHKQFAKAsVVYVTHDQIEAMTLADKIVLLHAgkdteryGSIAQI 224
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRT-LELVRRLVDDGKT-AVAAIHDLDLAARYCDELVLLAD-------GRVRAA 220
|
250
....*....|...
gi 1431886808 225 GAPLELYHRPRSR 237
Cdd:PRK09536 221 GPPADVLTADTLR 233
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-216 |
1.64e-19 |
|
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: 86.69 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 26 EIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAaqrgvamvfQSYALFPhMTVFEnmafgLKLAK 105
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQ---------YIKADYE-GTVRD-----LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 106 TPKDEIDRKVR-EAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDAtlrgQTRIEIARLHKQF 184
Cdd:cd03237 86 TKDFYTHPYFKtEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV----EQRLMASKVIRRF 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1431886808 185 A---KASVVYVTHDQIEAMTLADKIVLL--HAGKDTE 216
Cdd:cd03237 162 AennEKTAFVVEHDIIMIDYLADRLIVFegEPSVNGV 198
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-231 |
2.74e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.60 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 19 VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGL-----EDLTDGDLFIGGEVMNDVPAA-------------QRGVAM 80
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskyGTIQVGDIYIGDKKNNHELITnpyskkiknfkelRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQ--SYALFPHmTVFENMAFGLKLAKTPKDEIDRKVREAARILQL-EALLERRPKALSGGQRQRVAIGRAIVRQPGVFL 157
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 158 FDEPLSNLDAtlRGQTriEIARLHKQfAKAS---VVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELY 231
Cdd:PRK13631 200 FDEPTAGLDP--KGEH--EMMQLILD-AKANnktVFVITHTMEHVLEVADEVIVMDKGK-------ILKTGTPYEIF 264
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-224 |
3.60e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.81 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYgDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVM---NDVPAAQRG 77
Cdd:PRK11288 2 SPYLSFDGIGKTF-PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 VAMVFQSYALFPHMTVFENM-------AFGLklaktpkdeIDRK--VREAARilQLEALLER-----RPKALSGGQRQRV 143
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLylgqlphKGGI---------VNRRllNYEARE--QLEHLGVDidpdtPLKYLSIGQRQMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 144 AIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQfAKAsVVYVTHDQIEAMTLADKIVLLHAGKDTERYGSIAQ 223
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRV-ILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQ 227
|
.
gi 1431886808 224 I 224
Cdd:PRK11288 228 V 228
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
36-213 |
6.75e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.89 E-value: 6.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 36 LGPSGCGKSTLLRMIAGLEDlTDGDLFIGGEVMNDVPAAQ--RGVAMVFQSYALFPHMTVFENMAFGLKlAKTPKDEIDR 113
Cdd:COG4138 28 IGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYLALHQP-AGASSEAVEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 114 KVREAARILQLEALLERRPKALSGGQRQRVAIGrAIVRQ--PGV------FLFDEPLSNLDatlrgqtrieIA------R 179
Cdd:COG4138 106 LLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLA-AVLLQvwPTInpegqlLLLDEPMNSLD----------VAqqaaldR 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 1431886808 180 LHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:COG4138 175 LLRELCQQgiTVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
3-216 |
7.26e-19 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 88.26 E-value: 7.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYG-DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGE--VMNDVPAAQRGVA 79
Cdd:TIGR01846 455 AITFENIRFRYApDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVdlAIADPAWLRRQMG 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFPHmTVFENMAFGLKLAKtpkdeiDRKVREAARILQLEALLERRPK-----------ALSGGQRQRVAIGRA 148
Cdd:TIGR01846 535 VVLQENVLFSR-SIRDNIALCNPGAP------FEHVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARA 607
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 149 IVRQPGVFLFDEPLSNLDATlrgQTRIEIARLHKQFAKASVVYVTHdQIEAMTLADKIVLLHAGKDTE 216
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYE---SEALIMRNMREICRGRTVIIIAH-RLSTVRACDRIIVLEKGQIAE 671
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-216 |
9.88e-19 |
|
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: 82.75 E-value: 9.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGD-GAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRG-VAMV 81
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFpHMTVFENmafglklaktpkdeidrkvreaarilqlealLERRpkaLSGGQRQRVAIGRAIVRQPGVFLFDEP 161
Cdd:cd03247 81 NQRPYLF-DTTLRNN-------------------------------LGRR---FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1431886808 162 LSNLDATlrgqTRIEIARLHKQFAK-ASVVYVTHdQIEAMTLADKIVLLHAGKDTE 216
Cdd:cd03247 126 TVGLDPI----TERQLLSLIFEVLKdKTLIWITH-HLTGIEHMDKILFLENGKIIM 176
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-213 |
1.07e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.16 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ---RG 77
Cdd:PRK11614 3 KVMLSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 VAMVFQSYALFPHMTVFENMAFGLKLAKtpKDEIDRKVreaARILQL-EALLERRPK---ALSGGQRQRVAIGRAIVRQP 153
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFFAE--RDQFQERI---KWVYELfPRLHERRIQragTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 154 GVFLFDEPLSNLDATLRGQTRIEIARLHKQfaKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQ--GMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-213 |
1.66e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 87.31 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVM-----NDVPAAQ 75
Cdd:PRK11147 1 MSLISIHGAWLSFSD-APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvarlqQDPPRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 76 RGvamvfqsyalfphmTVFENMAFGLK-LAKTPK-----------DEIDRKVREAARI---------LQLE-------AL 127
Cdd:PRK11147 80 EG--------------TVYDFVAEGIEeQAEYLKryhdishlvetDPSEKNLNELAKLqeqldhhnlWQLEnrinevlAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 128 LERRPKA----LSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDAtlrgqTRIE-IARLHKQFaKASVVYVTHDQ--IEAM 200
Cdd:PRK11147 146 LGLDPDAalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI-----ETIEwLEGFLKTF-QGSIIFISHDRsfIRNM 219
|
250
....*....|...
gi 1431886808 201 tlADKIVLLHAGK 213
Cdd:PRK11147 220 --ATRIVDLDRGK 230
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-253 |
2.24e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.83 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKS----TLLRMI--AGLEDLTDGDLFI--GGEV--MNDVPAAQ----RG--VAMV 81
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRrrSRQVieLSEQSAAQmrhvRGadMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQS--YALFPHMTVFENMAFGLKLAKTPKDEidRKVREAARILQL------EALLERRPKALSGGQRQRVAIGRAIVRQP 153
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLHQGASRE--EAMVEAKRMLDQvripeaQTILSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 154 GVFLFDEPLSNLDATLRGQTRIEIARLHKQFAKAsVVYVTHDQIEAMTLADKIVLLHAGKDTERyGSIAQIgaplelYHR 233
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMG-VIFITHDMGVVAEIADRVLVMYQGEAVET-GSVEQI------FHA 259
|
250 260
....*....|....*....|.
gi 1431886808 234 PRSRFVAGFIGS-PRMNFLPG 253
Cdd:PRK10261 260 PQHPYTRALLAAvPQLGAMKG 280
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-166 |
2.65e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.40 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYgDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP---AAQRG 77
Cdd:PRK10895 1 MATLTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 78 VAMVFQSYALFPHMTVFENMAFGLKLAKTPKDEiDRKVR--EAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGV 155
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAE-QREDRanELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170
....*....|.
gi 1431886808 156 FLFDEPLSNLD 166
Cdd:PRK10895 159 ILLDEPFAGVD 169
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-213 |
2.87e-18 |
|
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: 86.99 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 16 GAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGG-EVMNDVPAAQRGVAMVFQSYALFPHMTVF 94
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkDIETNLDAVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 95 ENMAFGLKLAKTPKDEIDrkvreaariLQLEALLE-------RRPKA--LSGGQRQRVAIGRAIVRQPGVFLFDEPLSNL 165
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQ---------LEMEAMLEdtglhhkRNEEAqdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1431886808 166 DATLRgqtRIEIARLHKQFAKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:TIGR01257 1093 DPYSR---RSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-213 |
4.08e-18 |
|
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: 82.52 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAA--QRGVAMVFQSYALFPHmTVFE 95
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 96 NMAFGLKLAKtpkdeiDRKVREAARILQLEALLERRPKA-----------LSGGQRQRVAIGRAIVRQPGVFLFDEPLSN 164
Cdd:cd03248 107 NIAYGLQSCS------FECVKEAAQKAHAHSFISELASGydtevgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1431886808 165 LDAtlrgQTRIEIARLHKQFAKASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03248 181 LDA----ESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-213 |
4.13e-18 |
|
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: 80.19 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGaPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVmndvpaaqrgvamvfq 83
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYALFPHmtvfenmafglklaktpkdeidrkvreaarilqleallerrpkaLSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:cd03221 64 KIGYFEQ--------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 164 NLDAtlrgQTRIEIARLHKQFAKAsVVYVTHDQ--IEAmtLADKIVLLHAGK 213
Cdd:cd03221 100 HLDL----ESIEALEEALKEYPGT-VILVSHDRyfLDQ--VATKIIELEDGK 144
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-234 |
5.12e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.93 E-value: 5.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGevmndVPAAQ-------RGVAMVFQSYALFPH 90
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG-----VPLVQydhhylhRQVALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 91 mTVFENMAFGLKlaKTPKDEIDRKVREAAR---ILQLEALL--ERRPKA--LSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:TIGR00958 570 -SVRENIAYGLT--DTPDEEIMAAAKAANAhdfIMEFPNGYdtEVGEKGsqLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 164 NLDAtlrgqtriEIARLHKQ---FAKASVVYVTHdQIEAMTLADKIVLLhagkdteRYGSIAQIGAPLELYHRP 234
Cdd:TIGR00958 647 ALDA--------ECEQLLQEsrsRASRTVLLIAH-RLSTVERADQILVL-------KKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-213 |
7.54e-18 |
|
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: 80.55 E-value: 7.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 16 GAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGE-VMNDVP--AAQRGVAMV---FQSYALFP 89
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpVTRRSPrdAIRAGIAYVpedRKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 90 HMTVFENMAFGLklaktpkdeidrkvreaarilqleallerrpkALSGGQRQRVAIGRAIVRQPGVFLFDEPlsnldaTl 169
Cdd:cd03215 92 DLSVAENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEP------T- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1431886808 170 RG---QTRIEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:cd03215 133 RGvdvGAKAEIYRLIRELADAgkAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-213 |
8.21e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 83.21 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAP----VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDL--FIGGEVMNDVPAA--- 74
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 75 ---------------------QRGVAMVFQ--SYALFpHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQL-EALLER 130
Cdd:PRK13651 83 vleklviqktrfkkikkikeiRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 131 RPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDAtlrgQTRIEI----ARLHKQfaKASVVYVTHDQIEAMTLADKI 206
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDP----QGVKEIleifDNLNKQ--GKTIILVTHDLDNVLEWTKRT 235
|
....*..
gi 1431886808 207 VLLHAGK 213
Cdd:PRK13651 236 IFFKDGK 242
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-224 |
1.02e-17 |
|
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: 84.74 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGA---PVIRDVDLEIGENEFCVFLGPSGCGKS----TLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ- 75
Cdd:COG4172 7 LSVEDLSVAFGQGGgtvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 76 ---RG--VAMVFQ--SYALFPHMTVFENMAFGLKLaktpkdeiDRKVREAA---RILQL---------EALLERRPKALS 136
Cdd:COG4172 87 rriRGnrIAMIFQepMTSLNPLHTIGKQIAEVLRL--------HRGLSGAAaraRALELlervgipdpERRLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 137 GGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDqieaMTL----ADKIVLLHAG 212
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQREL-GMALLLITHD----LGVvrrfADRVAVMRQG 233
|
250
....*....|..
gi 1431886808 213 KDTERyGSIAQI 224
Cdd:COG4172 234 EIVEQ-GPTAEL 244
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-235 |
1.34e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.57 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 23 VDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPA---AQRGVAMVFQSYALFPHMTVFENM-- 97
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqiARMGVVRTFQHVRLFREMTVIENLlv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 98 --------AFGLKLAKTP------KDEIDRkvreAARILQLEALLE---RRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:PRK11300 104 aqhqqlktGLFSGLLKTPafrraeSEALDR----AATWLERVGLLEhanRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 161 PLsnldATLRGQTRIE----IARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAGKdterygSIAQiGAPLELYHRPR 235
Cdd:PRK11300 180 PA----AGLNPKETKEldelIAELRNEH-NVTVLLIEHDMKLVMGISDRIYVVNQGT------PLAN-GTPEEIRNNPD 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-274 |
1.55e-17 |
|
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: 84.08 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYgDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDL--TDGDL-----------------FIG 64
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpsKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 65 ------GEVMNDVPA------------AQRGVAMVFQ-SYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLE 125
Cdd:TIGR03269 80 epcpvcGGTLEPEEVdfwnlsdklrrrIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 126 ALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDAtlrgqtriEIARL-HKQFAKA------SVVYVTH--DQ 196
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDP--------QTAKLvHNALEEAvkasgiSMVLTSHwpEV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 197 IEamTLADKIVLLHAgkdteryGSIAQIGAPLELYhrprSRFVAGF----------IGSP--RMNFLPGRIASFDaQGVV 264
Cdd:TIGR03269 232 IE--DLSDKAIWLEN-------GEIKEEGTPDEVV----AVFMEGVsevekeceveVGEPiiKVRNVSKRYISVD-RGVV 297
|
330
....*....|
gi 1431886808 265 VALDHTHENV 274
Cdd:TIGR03269 298 KAVDNVSLEV 307
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-213 |
2.45e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.14 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 16 GAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVM--NDVPAA-QRGVAMV---FQSYALFP 89
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVriRSPRDAiRAGIAYVpedRKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 90 HMTVFENMAFGL--KLAKTPKdeIDRKvREAARILQL-EAL------LERRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:COG1129 344 DLSIRENITLASldRLSRGGL--LDRR-RERALAEEYiKRLriktpsPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 161 PlsnldaTlRG---QTRIEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:COG1129 421 P------T-RGidvGAKAEIYRLIRELAAEgkAVIVISSELPELLGLSDRILVMREGR 471
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-212 |
2.89e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.30 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP---AAQRGVAM 80
Cdd:PRK09700 6 ISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMAFGLKLAKT--PKDEID-RKVREAARILQLEALLERRPKA----LSGGQRQRVAIGRAIVRQP 153
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKvcGVNIIDwREMRVRAAMMLLRVGLKVDLDEkvanLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 154 GVFLFDEPLSNLDATLRGQTRIEIARLHKQfaKASVVYVTHDQIEAMTLADKIVLLHAG 212
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKE--GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-233 |
3.40e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 19 VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVmndvpAAQRGVAMVFQsyalfPHMTVFENMA 98
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV-----SALLELGAGFH-----PELTGRENIY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 99 FGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEIA 178
Cdd:COG1134 111 LNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIR 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 179 RLHKQfaKASVVYVTHD--QIEamTLADKIVLLHAGKDTErYGSIAQIgapLELYHR 233
Cdd:COG1134 191 ELRES--GRTVIFVSHSmgAVR--RLCDRAIWLEKGRLVM-DGDPEEV---IAAYEA 239
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-167 |
4.27e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 4.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 16 GAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDL-FIGGEVMNDVPAAQrgVAMVFQSYALFPHMTVF 94
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkLDGGDIDDPDVAEA--CHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 95 ENMAFGLKLAKTPkdeiDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDA 167
Cdd:PRK13539 92 ENLEFWAAFLGGE----ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-230 |
6.86e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.65 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 6 LRGVQKAYGDGA-PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ--RGVAMVF 82
Cdd:PRK10253 8 LRGEQLTLGYGKyTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 QSYALFPHMTVFENMAFGlKLAKTP-----KDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFL 157
Cdd:PRK10253 88 QNATTPGDITVQELVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1431886808 158 FDEPLSNLDATlrgqTRIEIARLHKQFAKA---SVVYVTHDQIEAMTLADKIVLLhagkdteRYGSIAQIGAPLEL 230
Cdd:PRK10253 167 LDEPTTWLDIS----HQIDLLELLSELNREkgyTLAAVLHDLNQACRYASHLIAL-------REGKIVAQGAPKEI 231
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-217 |
7.38e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.07 E-value: 7.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP--AAQRGVAM 80
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLShsVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHmTVFENMAFGlklaktpKDEIDRKVREAARILQLEALLERRPKA-----------LSGGQRQRVAIGRAI 149
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLG-------RDISEEQVWQALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLALARVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 150 VRQPGVFLFDEPLSNLDATlrgqTRIEIARLHKQFAKASVVYVTHDQIEAMTLADKIVLLHAGKDTER 217
Cdd:PRK10790 492 VQTPQILILDEATANIDSG----TEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQ 555
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-195 |
7.39e-17 |
|
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: 81.91 E-value: 7.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 5 SLRGVQKAYGDGAPVIRDVDL------EIGenefcvFLGPSGCGKSTLLRMIAGLedltDGDlfIGGEVMndvPAAQRGV 78
Cdd:TIGR03719 6 TMNRVSKVVPPKKEILKDISLsffpgaKIG------VLGLNGAGKSTLLRIMAGV----DKD--FNGEAR---PQPGIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSYALFPHMTVFENMAFGLKLAK--------------TPKDEIDRKVREAARiLQ----------LEALLERRPKA 134
Cdd:TIGR03719 71 GYLPQEPQLDPTKTVRENVEEGVAEIKdaldrfneisakyaEPDADFDKLAAEQAE-LQeiidaadawdLDSQLEIAMDA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 135 L------------SGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATlrgqtriEIARL--HKQFAKASVVYVTHD 195
Cdd:TIGR03719 150 LrcppwdadvtklSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-------SVAWLerHLQEYPGTVVAVTHD 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-213 |
1.10e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.71 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 22 DVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGD--LFiGGEV-MNDVpAAQRGVAMVFQSYALFPHMTVFENMA 98
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawLF-GQPVdAGDI-ATRRRVGYMSQAFSLYGELTVRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 99 FGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRG---QTRI 175
Cdd:NF033858 362 LHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDmfwRLLI 441
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1431886808 176 EIARlhkqfaKASV-VYV-THDQIEAMtLADKIVLLHAGK 213
Cdd:NF033858 442 ELSR------EDGVtIFIsTHFMNEAE-RCDRISLMHAGR 474
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-194 |
1.31e-16 |
|
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: 77.40 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDV-PAAQRGVAMVFQSYALFPHMTV 93
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 94 FENMAFglkLAKTPKDEiDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATlrGQT 173
Cdd:TIGR01189 91 LENLHF---WAAIHGGA-QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA--GVA 164
|
170 180
....*....|....*....|..
gi 1431886808 174 RI-EIARLHKQfAKASVVYVTH 194
Cdd:TIGR01189 165 LLaGLLRAHLA-RGGIVLLTTH 185
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-207 |
2.59e-16 |
|
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: 77.47 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFI--GGEVMNDVPAAQRGVAMV------FQSYAL-- 87
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREILALrrrtigYVSQFLrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 88 FPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQL-EALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLD 166
Cdd:COG4778 105 IPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1431886808 167 ATLRgQTRIEIARLHKQfAKASVVYVTHDqIEAM-TLADKIV 207
Cdd:COG4778 185 AANR-AVVVELIEEAKA-RGTAIIGIFHD-EEVReAVADRVV 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-213 |
3.05e-16 |
|
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: 76.41 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLED--LTDGDLFIGGEVMNDVPA---AQRGVAMVFQSYALFP 89
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPeerARLGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 90 hmtvfenmafGLKLAktpkdEIDRKVREaarilqleallerrpkALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDAT- 168
Cdd:cd03217 91 ----------GVKNA-----DFLRYVNE----------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDa 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1431886808 169 LRGQTRIeIARLHKQfaKASVVYVTH-----DQIEamtlADKIVLLHAGK 213
Cdd:cd03217 140 LRLVAEV-INKLREE--GKSVLIITHyqrllDYIK----PDRVHVLYDGR 182
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-232 |
5.19e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 79.37 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLfiggeVMNDVPAAQ------RG-VAMVFQSYALFPH 90
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI-----RFHDIPLTKlqldswRSrLAVVSQTPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 91 mTVFENMAFGLKLAKtpKDEIDRKVREAA---RILQL----EALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:PRK10789 404 -TVANNIALGRPDAT--QQEIEHVARLASvhdDILRLpqgyDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 164 NLDatlrGQTRIEIARLHKQFAKASVVYVTHDQIEAMTLADKIVLLHAGKDTERyGS----IAQIGAPLELYH 232
Cdd:PRK10789 481 AVD----GRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQR-GNhdqlAQQSGWYRDMYR 548
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-213 |
5.86e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.82 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLedL--TDGDLfiggEVMNDVPAAQR-----GVAMVF-QSYALFPHM 91
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI--LvpTSGEV----RVLGYVPFKRRkefarRIGVVFgQRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 92 TVFENmafgLKLAKT----PKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDA 167
Cdd:COG4586 112 PAIDS----FRLLKAiyriPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1431886808 168 TlrGQTRIE--IARLHKQFaKASVVYVTHD--QIEAmtLADKIVLLHAGK 213
Cdd:COG4586 188 V--SKEAIRefLKEYNRER-GTTILLTSHDmdDIEA--LCDRVIVIDHGR 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-213 |
7.91e-16 |
|
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: 75.38 E-value: 7.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLedlTDGDLFIGGEVM-NDVPAA------QRGVAMVFQSYAL 87
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIHyNGIPYKefaekyPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 88 FPHMTVFENMAFGLKLAKtpkDEIDRKVreaarilqleallerrpkalSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDA 167
Cdd:cd03233 95 FPTLTVRETLDFALRCKG---NEFVRGI--------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1431886808 168 TlrgqTRIEIARLHKQFAKA--SVVYVTHDQI--EAMTLADKIVLLHAGK 213
Cdd:cd03233 152 S----TALEILKCIRTMADVlkTTTFVSLYQAsdEIYDLFDKVLVLYEGR 197
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
24-249 |
1.10e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.07 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 24 DLEIGENEFCVflGPSGCGKSTLLRMIAGL---EDLTDGD-LFIGGEVMNdVPAAQ------RGVAMVFQS--YALFPHM 91
Cdd:PRK09473 38 SLRAGETLGIV--GESGSGKSQTAFALMGLlaaNGRIGGSaTFNGREILN-LPEKElnklraEQISMIFQDpmTSLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 92 TVFENMAFGLKLAK-TPKDEidrKVREAARILQLEALLERR------PKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSN 164
Cdd:PRK09473 115 RVGEQLMEVLMLHKgMSKAE---AFEESVRMLDAVKMPEARkrmkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 165 LDATLRGQTRIEIARLHKQFAKAsVVYVTHDQIEAMTLADKIVLLHAGKDTErYGSIAQIgaplelYHRPRSRFVAGFIG 244
Cdd:PRK09473 192 LDVTVQAQIMTLLNELKREFNTA-IIMITHDLGVVAGICDKVLVMYAGRTME-YGNARDV------FYQPSHPYSIGLLN 263
|
....*.
gi 1431886808 245 S-PRMN 249
Cdd:PRK09473 264 AvPRLD 269
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-167 |
2.91e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 77.31 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAA--QRGVAMV 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAslRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFpHMTVFENmafgLKLAKTpkDEIDRKVREAARILQLEALLERRPK-----------ALSGGQRQRVAIGRAIV 150
Cdd:PRK13657 415 FQDAGLF-NRSIEDN----IRVGRP--DATDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALL 487
|
170
....*....|....*..
gi 1431886808 151 RQPGVFLFDEPLSNLDA 167
Cdd:PRK13657 488 KDPPILILDEATSALDV 504
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
36-230 |
2.91e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 36 LGPSGCGKSTLLRMIAG--LEDLT-DGDLFIGGEVMnDVPAAQRGVAMVFQSYALFPHMTVFENMAFG--LKL-AKTPKD 109
Cdd:TIGR00955 57 MGSSGAGKTTLMNALAFrsPKGVKgSGSVLLNGMPI-DAKEMRAISAYVQQDDLFIPTLTVREHLMFQahLRMpRRVTKK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 110 EIDRKVREaarILQLEALL---------ERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTrieIARL 180
Cdd:TIGR00955 136 EKRERVDE---VLQALGLRkcantrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV---VQVL 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 181 HKQFAKASVVYVTHDQ--IEAMTLADKIVLLHAGKdterygsIAQIGAPLEL 230
Cdd:TIGR00955 210 KGLAQKGKTIICTIHQpsSELFELFDKIILMAEGR-------VAYLGSPDQA 254
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-213 |
3.29e-15 |
|
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: 76.79 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGL--EDLTDGDLFIGGE--VMNDVPAAQR-GV 78
Cdd:TIGR02633 2 LEMKGIVKTFG-GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSplKASNIRDTERaGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSYALFPHMTVFENMAFG----LKLAKTPKDEIDRKVREAARILQLEALLERRPKA-LSGGQRQRVAIGRAIVRQP 153
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 154 GVFLFDEPLSNLDATlRGQTRIEIARLHKQFAKAsVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:TIGR02633 161 RLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVA-CVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-213 |
3.95e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.51 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 19 VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFiggevmndvpaAQRGVAMVFQSyALFPHMTVFENMA 98
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 99 FglklaKTPKDEIDrkVREAARILQLEALLERRPKA-----------LSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDA 167
Cdd:PTZ00243 743 F-----FDEEDAAR--LADAVRVSQLEADLAQLGGGleteigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 168 -------------TLRGQTRieiarlhkqfakasvVYVTHdQIEAMTLADKIVLLHAGK 213
Cdd:PTZ00243 816 hvgervveecflgALAGKTR---------------VLATH-QVHVVPRADYVVALGDGR 858
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-224 |
4.73e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.42 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTdGDLFIGGEVMNDVPAAQ--RGVAMVFQSYALFpHMT 92
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrKHLSWVGQNPQLP-HGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 93 VFENMAFGLKLAKtpkDEIDRKVREAARILQLEALLER--------RPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSN 164
Cdd:PRK11174 439 LRDNVLLGNPDAS---DEQLQQALENAWVSEFLPLLPQgldtpigdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 165 LDAtlRGQTRIEIArLHKQFAKASVVYVTHdQIEAMTLADKIVLLHAGKDTERyGSIAQI 224
Cdd:PRK11174 516 LDA--HSEQLVMQA-LNAASRRQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQ-GDYAEL 570
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-195 |
5.94e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 76.36 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 26 EIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVmndvpaaqrgvamvfqSYAlfP-------HMTVFENma 98
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKI----------------SYK--PqyispdyDGTVEEF-- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 99 fglkLAKTPKDEIDRKV--REAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDAtlrgQTRIE 176
Cdd:COG1245 422 ----LRSANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV----EQRLA 493
|
170 180
....*....|....*....|..
gi 1431886808 177 IARLHKQFA---KASVVYVTHD 195
Cdd:COG1245 494 VAKAIRRFAenrGKTAMVVDHD 515
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-212 |
7.05e-15 |
|
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: 74.12 E-value: 7.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 16 GAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVmndvpaaqrgvAMVFQSYALFPHmTVFE 95
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRI-----------SFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 96 NMAFGLKLaktpkDEIdrKVREAARILQLEALLERRPK-----------ALSGGQRQRVAIGRAIVRQPGVFLFDEPLSN 164
Cdd:cd03291 117 NIIFGVSY-----DEY--RYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1431886808 165 LDatLRGQTRIEIARLHKQFAKASVVYVThDQIEAMTLADKIVLLHAG 212
Cdd:cd03291 190 LD--VFTEKEIFESCVCKLMANKTRILVT-SKMEHLKKADKILILHEG 234
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-204 |
7.28e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 72.68 E-value: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGE-VMNDVPAAQRGVAMVFQSYALFPHMTVFEN 96
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsIKKDLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 97 MAFGLKLAKTPKdEIDrkvrEAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLD--ATLRGQTR 174
Cdd:PRK13540 95 CLYDIHFSPGAV-GIT----ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDelSLLTIITK 169
|
170 180 190
....*....|....*....|....*....|
gi 1431886808 175 IEIARlhkqfAKASVVYVTHDQIEAMTLAD 204
Cdd:PRK13540 170 IQEHR-----AKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
35-213 |
8.28e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.43 E-value: 8.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 35 FLGPSGCGKSTLLRMIAGLEDlTDGDLFIGGEVMNDVPA---AQRGVAMVFQSYALFpHMTVFENMAFGLKlAKTPKDEI 111
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAaelARHRAYLSQQQTPPF-AMPVFQYLTLHQP-DKTRTEAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 112 DRKVREAARILQLEALLERRPKALSGGQRQRvaigraiVRQPGVFL--------------FDEPLSNLDATLRGQtrieI 177
Cdd:PRK03695 104 ASALNEVAEALGLDDKLGRSVNQLSGGEWQR-------VRLAAVVLqvwpdinpagqlllLDEPMNSLDVAQQAA----L 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1431886808 178 ARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:PRK03695 173 DRLLSELCQQgiAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-227 |
8.76e-15 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 72.91 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDG-APVIRDVDLEIGENEFCVFLGPSGCGKST----LLRMIagleDLTDGDLFIGGEVMNDVPAAQ-- 75
Cdd:cd03244 2 DIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 76 RGVAMVFQSYALFPHmTVFENMAFglkLAKTPKDEIDRKVREA-------ARILQLEALLERRPKALSGGQRQRVAIGRA 148
Cdd:cd03244 78 SRISIIPQDPVLFSG-TIRSNLDP---FGEYSDEELWQALERVglkefveSLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 149 IVRQPGVFLFDEPLSNLDatlrGQTRIEIAR-LHKQFAKASVVYVTHdQIEAMTLADKIVLLHAGKdterygsIAQIGAP 227
Cdd:cd03244 154 LLRKSKILVLDEATASVD----PETDALIQKtIREAFKDCTVLTIAH-RLDTIIDSDRILVLDKGR-------VVEFDSP 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-195 |
9.46e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.54 E-value: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 5 SLRGVQKAYGDGAPVIRDVDL------EIGenefcvFLGPSGCGKSTLLRMIAGLEdlTDgdlfIGGEVmndVPAAQRGV 78
Cdd:PRK11819 8 TMNRVSKVVPPKKQILKDISLsffpgaKIG------VLGLNGAGKSTLLRIMAGVD--KE----FEGEA---RPAPGIKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSYALFPHMTVFEN--MAFGLKLAK------------TPKDEIDRKVREAARiLQ----------LEALLE----- 129
Cdd:PRK11819 73 GYLPQEPQLDPEKTVRENveEGVAEVKAAldrfneiyaayaEPDADFDALAAEQGE-LQeiidaadawdLDSQLEiamda 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 130 -RRP------KALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATlrgqtriEIARL--HKQFAKASVVYVTHD 195
Cdd:PRK11819 152 lRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE-------SVAWLeqFLHDYPGTVVAVTHD 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-233 |
1.03e-14 |
|
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: 76.14 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVmndvpaaqrgvAMVFQSyALFPHMTVF 94
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV-----------AYVPQQ-AWIQNDSLR 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 95 ENMAFGLKLaktpKDEIDRKVREAARIL-QLEAL-------LERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLD 166
Cdd:TIGR00957 717 ENILFGKAL----NEKYYQQVLEACALLpDLEILpsgdrteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 167 ATLRGQTRIEIARLHKQFAKASVVYVTHDqIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHR 233
Cdd:TIGR00957 793 AHVGKHIFEHVIGPEGVLKNKTRILVTHG-ISYLPQVDVIIVMSGGK-------ISEMGSYQELLQR 851
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-212 |
1.18e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKaygdgaPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEdltdgdLFIGGEVMNDVPAAQRGvamvfq 83
Cdd:COG2401 36 VELRVVER------YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL------KGTPVAGCVDVPDNQFG------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 syalfPHMTVFENMAfglklaktPKDEIDRKVREAARI-LQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPL 162
Cdd:COG2401 98 -----REASLIDAIG--------RKGDFKDAVELLNAVgLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1431886808 163 SNLDATLRGQTRIEIARLHKQFAKASVVYVTHDQIEAMTLADKIVLLHAG 212
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVGYG 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-224 |
1.37e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.82 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVM---NDVPAAQRGVAMVFQSY---ALFPHMTV 93
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDAVKKGMAYITESRrdnGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 94 FENMAFG--LKLAK--------TPKDEidRKVREAAR-ILQLE-ALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEP 161
Cdd:PRK09700 359 AQNMAISrsLKDGGykgamglfHEVDE--QRTAENQReLLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431886808 162 LSNLDATlrgqTRIEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLhagkdteRYGSIAQI 224
Cdd:PRK09700 437 TRGIDVG----AKAEIYKVMRQLADDgkVILMVSSELPEIITVCDRIAVF-------CEGRLTQI 490
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-226 |
1.93e-14 |
|
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: 75.33 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 16 GAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVmndvpaaqrgvAMVFQSYALFPHmTVFE 95
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRI-----------SFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 96 NMAFGLKLaktpkDEIdrKVREAARILQLEALLERRPK-----------ALSGGQRQRVAIGRAIVRQPGVFLFDEPLSN 164
Cdd:TIGR01271 506 NIIFGLSY-----DEY--RYTSVIKACQLEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 165 LDATlrgqTRIEIAR--LHKQFAKASVVYVThDQIEAMTLADKIVLLHAGKdTERYGSIAQIGA 226
Cdd:TIGR01271 579 LDVV----TEKEIFEscLCKLMSNKTRILVT-SKLEHLKKADKILLLHEGV-CYFYGTFSELQA 636
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-194 |
1.97e-14 |
|
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: 70.65 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLfiggevmnDVPaAQRGVAMVFQ 83
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMP-EGEDLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 -SYalfphmtvfenMAFG-LKlaktpkdeidrkvreaarilqlEALLerRP--KALSGGQRQRVAIGRAIVRQPGVFLFD 159
Cdd:cd03223 72 rPY-----------LPLGtLR----------------------EQLI--YPwdDVLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190
....*....|....*....|....*....|....*..
gi 1431886808 160 EPLSNLDATLRgqtrieiARLHKQF--AKASVVYVTH 194
Cdd:cd03223 117 EATSALDEESE-------DRLYQLLkeLGITVISVGH 146
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-194 |
2.21e-14 |
|
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: 71.37 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFI-GGEVMNDVPAAQRGVAMVFQSYALFPHMTV 93
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 94 FENMAFglklakTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATlrgqt 173
Cdd:cd03231 91 LENLRF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA----- 159
|
170 180
....*....|....*....|....*.
gi 1431886808 174 riEIARLHKQFAK-----ASVVYVTH 194
Cdd:cd03231 160 --GVARFAEAMAGhcargGMVVLTTH 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
37-233 |
2.25e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.36 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 37 GPSGCGKST----LLRMIAgledlTDGDLFIGGEVMNDVPAAQ-----RGVAMVFQ--SYALFPHMTVFENMAFGLKL-- 103
Cdd:PRK15134 319 GESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpNSSLNPRLNVLQIIEEGLRVhq 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 104 AKTPKDEIDRKVREAARILQLEALLERR-PKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTrIEIARLHK 182
Cdd:PRK15134 394 PTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI-LALLKSLQ 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 183 QFAKASVVYVTHDQIEAMTLADKIVLLHAGKDTERyGSIAQI-GAPLELYHR 233
Cdd:PRK15134 473 QKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQ-GDCERVfAAPQQEYTR 523
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-212 |
3.22e-14 |
|
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: 71.21 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 12 AYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLF-----IGGEVMNDVPAAQRG-VAMVFQSY 85
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknESEPSFEATRSRNRYsVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 86 ALFpHMTVFENMAFGlklakTPKDEIDRKVREAARILQL---------EALLERRPKALSGGQRQRVAIGRAIVRQPGVF 156
Cdd:cd03290 89 WLL-NATVEENITFG-----SPFNKQRYKAVTDACSLQPdidllpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1431886808 157 LFDEPLSNLDATLRGQTRIEIARLHKQFAKASVVYVTHdQIEAMTLADKIVLLHAG 212
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-232 |
3.37e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 73.90 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAY-GDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMND--VPAAQRGVAM 80
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFpHMTVFENMAFGLKlAKTPKDEIDRkvreAARILQLEALLERRPKA-----------LSGGQRQRVAIGRAI 149
Cdd:PRK11176 422 VSQNVHLF-NDTIANNIAYART-EQYSREQIEE----AARMAYAMDFINKMDNGldtvigengvlLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 150 VRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQfaKASVVyVTH--DQIEAmtlADKIVLLHAGKDTERyGS----IAQ 223
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQKN--RTSLV-IAHrlSTIEK---ADEILVVEDGEIVER-GThaelLAQ 568
|
....*....
gi 1431886808 224 IGAPLELYH 232
Cdd:PRK11176 569 NGVYAQLHK 577
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
79-223 |
3.63e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 74.30 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 79 AMVFQSYALFpHMTVFENMAFGlklaktPKDEIDRKVREAARILQLEALLERRP-----------KALSGGQRQRVAIGR 147
Cdd:PTZ00265 1299 SIVSQEPMLF-NMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIAR 1371
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 148 AIVRQPGVFLFDEPLSNLDAT---LRGQTRIEIarlhKQFAKASVVYVTHdQIEAMTLADKIVLLHagkDTERYGSIAQ 223
Cdd:PTZ00265 1372 ALLREPKILLLDEATSSLDSNsekLIEKTIVDI----KDKADKTIITIAH-RIASIKRSDKIVVFN---NPDRTGSFVQ 1442
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
36-210 |
4.17e-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: 73.67 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 36 LGPSGCGKSTLLRMIAGLEDLTDGDLfiggevmnDVPAAQRGVAMVFQSYALFPHmtvFENMAFG-LKLAKTPK--DEID 112
Cdd:COG1245 105 LGPNGIGKSTALKILSGELKPNLGDY--------DEEPSWDEVLKRFRGTELQDY---FKKLANGeIKVAHKPQyvDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 113 R-----------------KVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDAtlrGQtRI 175
Cdd:COG1245 174 KvfkgtvrellekvdergKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI---YQ-RL 249
|
170 180 190
....*....|....*....|....*....|....*..
gi 1431886808 176 EIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLH 210
Cdd:COG1245 250 NVARLIRELAEEgkYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-213 |
5.29e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.04 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 6 LRGVQKAYGdGAPVIRDVDLEIGENEfCVFL-GPSGCGKSTLLRMIAGL--EDLTDGDLFIGGEVM---NDVPAAQRGVA 79
Cdd:PRK13549 8 MKNITKTFG-GVKALDNVSLKVRAGE-IVSLcGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELqasNIRDTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARIL---QLEALLERRPKALSGGQRQRVAIGRAIVRQPGVF 156
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLaqlKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 157 LFDEPLSNLDAtlrGQTRI--EIARLHKQFAKAsVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:PRK13549 166 ILDEPTASLTE---SETAVllDIIRDLKAHGIA-CIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-230 |
6.67e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.97 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 33 CVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN--DVPAAQRGVAMVFQSYALFPHMTVFENMAFGlklaKTP--- 107
Cdd:PRK10575 40 TGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVAYLPQQLPAAEGMTVRELVAIG----RYPwhg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 108 -----KDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEIARLHK 182
Cdd:PRK10575 116 algrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQ 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1431886808 183 QFAkASVVYVTHDQIEAMTLADKIVLLHAGKdterygSIAQiGAPLEL 230
Cdd:PRK10575 196 ERG-LTVIAVLHDINMAARYCDYLVALRGGE------MIAQ-GTPAEL 235
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-168 |
1.23e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.22 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 31 EFCVFLGPSGCGKSTLLRMIAGLedlTDGDLFIGGEVMND-VPAAQ--RGVAMVFQSYALFPHMTVFENMAFgLKLAKTP 107
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGR---IQGNNFTGTILANNrKPTKQilKRTGFVTQDDILYPHLTVRETLVF-CSLLRLP 170
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 108 KD-EIDRKVREAARILQLEALLERRP--------KALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDAT 168
Cdd:PLN03211 171 KSlTKQEKILVAESVISELGLTKCENtiignsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-210 |
1.39e-13 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 70.09 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 28 GENEFCVF-------------LGPSGCGKSTLLRMIAGlEDLTDGDLFIGGEVMNDVPAAQRGVAMvfQSYalfphmtvF 94
Cdd:cd03236 11 GPNSFKLHrlpvpregqvlglVGPNGIGKSTALKILAG-KLKPNLGKFDDPPDWDEILDEFRGSEL--QNY--------F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 95 ENMAFG-LKLAKTPK--DEIDRKVR-----------------EAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPG 154
Cdd:cd03236 80 TKLLEGdVKVIVKPQyvDLIPKAVKgkvgellkkkdergkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 155 VFLFDEPLSNLDAtlrGQtRIEIARLHKQFAK--ASVVYVTHDQIEAMTLADKIVLLH 210
Cdd:cd03236 160 FYFFDEPSSYLDI---KQ-RLNAARLIRELAEddNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-195 |
1.66e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.76 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 26 EIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVmndvpaaqrgvamvfqSYA---LFP--HMTVFENmafg 100
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKI----------------SYKpqyIKPdyDGTVEDL---- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 101 lkLAKTPKD--------EIdrkvreaARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDAtlrgQ 172
Cdd:PRK13409 421 --LRSITDDlgssyyksEI-------IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV----E 487
|
170 180
....*....|....*....|....*.
gi 1431886808 173 TRIEIARLHKQFA---KASVVYVTHD 195
Cdd:PRK13409 488 QRLAVAKAIRRIAeerEATALVVDHD 513
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-216 |
2.03e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.08 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKSTLLR-MIAGLEDLTDGDLFIGGEVmndvpaaqrgvAMVFQSYALFpHMTVFEN 96
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTV-----------AYVPQVSWIF-NATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 97 MAFGLKLAKtpkDEIDRKVREAARILQLEAL-------LERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDA-- 167
Cdd:PLN03130 699 ILFGSPFDP---ERYERAIDVTALQHDLDLLpggdlteIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhv 775
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 168 -----------TLRGQTRieiarlhkqfakasvVYVThDQIEAMTLADKIVLLHAGKDTE 216
Cdd:PLN03130 776 grqvfdkcikdELRGKTR---------------VLVT-NQLHFLSQVDRIILVHEGMIKE 819
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-213 |
2.40e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.21 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENE-FCVfLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQR---GVAMV---FQSYAL 87
Cdd:COG3845 269 RGVPALKDVSLEVRAGEiLGI-AGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYIpedRLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 88 FPHMTVFENMAFGL----KLAKTPKdeIDRK-VREAArilqlEALLER---RP-------KALSGGQRQRVAIGRAIVRQ 152
Cdd:COG3845 348 VPDMSVAENLILGRyrrpPFSRGGF--LDRKaIRAFA-----EELIEEfdvRTpgpdtpaRSLSGGNQQKVILARELSRD 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 153 PGVFLFDEPLSNLD--AtlrgqtrieIARLHKQFAK-----ASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:COG3845 421 PKLLIAAQPTRGLDvgA---------IEFIHQRLLElrdagAAVLLISEDLDEILALSDRIAVMYEGR 479
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-195 |
3.56e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.73 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMndvpaaqrgVAMVFQ 83
Cdd:TIGR03719 323 IEAENLTKAFGD-KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK---------LAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SY-ALFPHMTVFENMAFGLklaktpkDEI---DRKVREAARILQLE---ALLERRPKALSGGQRQRVAIGRaIVRQPG-V 155
Cdd:TIGR03719 393 SRdALDPNKTVWEEISGGL-------DIIklgKREIPSRAYVGRFNfkgSDQQKKVGQLSGGERNRVHLAK-TLKSGGnV 464
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1431886808 156 FLFDEPLSNLDA-TLRGqtrIEIARLhkQFAKASVVyVTHD 195
Cdd:TIGR03719 465 LLLDEPTNDLDVeTLRA---LEEALL--NFAGCAVV-ISHD 499
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
36-223 |
3.56e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.29 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 36 LGPSGCGKSTLLRMIAGLED---LTDGDLFIGGEVMNDvpAAQRGVAMVFQSYALFPHMTVFENMAFGLKL---AKTPKD 109
Cdd:TIGR00956 795 MGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDS--SFQRSIGYVQQQDLHLPTSTVRESLRFSAYLrqpKSVSKS 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 110 EIDRKVREAARILQLE----ALLERRPKALSGGQRQRVAIGRAIVRQPGVFLF-DEPLSNLDAtlrgQTRIEIARLHKQF 184
Cdd:TIGR00956 873 EKMEYVEEVIKLLEMEsyadAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDS----QTAWSICKLMRKL 948
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1431886808 185 AKA--SVVYVTHdQIEAMTLA--DKIVLLHAGKDTERYGSIAQ 223
Cdd:TIGR00956 949 ADHgqAILCTIH-QPSAILFEefDRLLLLQKGGQTVYFGDLGE 990
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-213 |
3.69e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.29 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 19 VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGledLTDG-DLFIGGEV------MNDVPAAQRG-VAMVFQSYALFPH 90
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS---NTDGfHIGVEGVItydgitPEEIKKHYRGdVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 91 MTVFENMAFGLKLaKTPK---DEIDRKVR---EAARILQLEALLERRP--------KALSGGQRQRVAIGRAIVRQPGVF 156
Cdd:TIGR00956 153 LTVGETLDFAARC-KTPQnrpDGVSREEYakhIADVYMATYGLSHTRNtkvgndfvRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431886808 157 LFDEPLSNLDATlrgqTRIEIARLHKQFAK--ASVVYVTHDQI--EAMTLADKIVLLHAGK 213
Cdd:TIGR00956 232 CWDNATRGLDSA----TALEFIRALKTSANilDTTPLVAIYQCsqDAYELFDKVIVLYEGY 288
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-235 |
4.10e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.65 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ-----RGVAMVFQS-YA-LFPHMT 92
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 93 VFENMAFGLKLAKTPKDEIDRKvrEAARILQLEALLE----RRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDAT 168
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKAAAA--RVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 169 LRGQTRIEIARLHKQFAKAsVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPR 235
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIA-YLFISHDMAVVERISHRVAVMYLGQ-------IVEIGPRRAVFENPQ 556
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-227 |
4.47e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 67.44 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYG-DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP--AAQRGVA 79
Cdd:cd03369 6 EIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPleDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 80 MVFQSYALFPHmTVFENMafglklakTPKDEI-DRKVREAARILqlEALLErrpkaLSGGQRQRVAIGRAIVRQPGVFLF 158
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNL--------DPFDEYsDEEIYGALRVS--EGGLN-----LSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 159 DEPLSNLDAtlrgQTRIEIAR-LHKQFAKASVVYVTHdQIEAMTLADKIVLLHAGKdterygsIAQIGAP 227
Cdd:cd03369 150 DEATASIDY----ATDALIQKtIREEFTNSTILTIAH-RLRTIIDYDKILVMDAGE-------VKEYDHP 207
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-209 |
7.78e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.84 E-value: 7.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 36 LGPSGCGKSTLLRMIAG--------LEDLTDGDlfiggEVMNdvpaAQRGVAMvfQSYalfphmtvFENMAFG-LKLAKT 106
Cdd:PRK13409 105 LGPNGIGKTTAVKILSGelipnlgdYEEEPSWD-----EVLK----RFRGTEL--QNY--------FKKLYNGeIKVVHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 107 PK--DEIDR----KVREA-------------ARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDA 167
Cdd:PRK13409 166 PQyvDLIPKvfkgKVRELlkkvdergkldevVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1431886808 168 tlrGQtRIEIARLHKQFAK-ASVVYVTHDQIEAMTLADKIVLL 209
Cdd:PRK13409 246 ---RQ-RLNVARLIRELAEgKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-224 |
1.16e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 68.01 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 23 VDLEIGENEFCVFLGPSGCGKSTLLRMIAGLED----LTDGDLFIGGEVMNDVPAAQR------GVAMVFQ--SYALFPH 90
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQepSSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 91 MTVFENMAFGLklaktPKDEIDRKV--REAARILQLEALLER------------RPKALSGGQRQRVAIGRAIVRQPGVF 156
Cdd:COG4170 106 AKIGDQLIEAI-----PSWTFKGKWwqRFKWRKKRAIELLHRvgikdhkdimnsYPHELTEGECQKVMIAMAIANQPRLL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 157 LFDEPLSNLDATlrgqTRIEIARL---HKQFAKASVVYVTHDqIEAMT-LADKIVLLHAGKDTERyGSIAQI 224
Cdd:COG4170 181 IADEPTNAMEST----TQAQIFRLlarLNQLQGTSILLISHD-LESISqWADTITVLYCGQTVES-GPTEQI 246
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-221 |
1.19e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.23 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEfCVFL-GPSGCGKSTLLRMIAGLEDLTDGDLFIGGE-VMNDVPAAQRG-VAM 80
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGE-LLFLiGGNGSGKSTLAMLLTGLYQPQSGEILLDGKpVTAEQPEDYRKlFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMAFGLKLAKT--PKDEIDRKVR-EAARILQLEallerrpkaLSGGQRQRVAIGRAIVRQPGVFL 157
Cdd:PRK10522 402 VFTDFHLFDQLLGPEGKPANPALVEKwlERLKMAHKLElEDGRISNLK---------LSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 158 FDEPLSNLDATLRGQTRIEIARLHKQFAKaSVVYVTHDQiEAMTLADKIVLLHAGKDTERYGSI 221
Cdd:PRK10522 473 LDEWAADQDPHFRREFYQVLLPLLQEMGK-TIFAISHDD-HYFIHADRLLEMRNGQLSELTGEE 534
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-233 |
1.46e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.96 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKS-TLLRMIAGLED----LTDGD-LFIGGEVMNDVPAAQRGV-----AMVFQS-- 84
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDiRFHGESLLHASEQTLRGVrgnkiAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 85 YALFPHMTVFENMAFGLKLAKTPKdeidrkvREAAR-----------ILQLEALLERRPKALSGGQRQRVAIGRAIVRQP 153
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLHRGMR-------REAARgeilncldrvgIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 154 GVFLFDEPLSNLDATLRGQTrIEIARLHKQFAKASVVYVTHDQIEAMTLADKIVLLHAGKDTERYGSIAQIGAPLELYHR 233
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQI-LQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-219 |
1.56e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 65.73 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 22 DVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEdlTDGDlfIGGEVMND----VPAAQRGVAMVFQSYALFPHMTVfenm 97
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGRK--TAGV--ITGEILINgrplDKNFQRSTGYVEQQDVHSPNLTV---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 98 afglklaktpkdeidrkvREAariLQLEALLerrpKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDAtlrgQTRIEI 177
Cdd:cd03232 97 ------------------REA---LRFSALL----RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS----QAAYNI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1431886808 178 ARLHKQFAKA--SVVYVTHdQIEAMTLA--DKIVLLHAGKDTERYG 219
Cdd:cd03232 148 VRFLKKLADSgqAILCTIH-QPSASIFEkfDRLLLLKRGGKTVYFG 192
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-166 |
3.44e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 64.89 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 37 GPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQRGvaMVFQSYALFPHMTVFENMAFGLKLAKTPKdeidrKVR 116
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCT--YIGHNLGLKLEMTVFENLKFWSEIYNSAE-----TLY 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1431886808 117 EAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLD 166
Cdd:PRK13541 106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-213 |
4.18e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.45 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 6 LRGVQKAYgDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGD-LFIGGEV--MNDVPAAQRGVAMVF 82
Cdd:PRK10982 1 MSNISKSF-PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSiLFQGKEIdfKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 QSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARIL-QLEALLERRPKA--LSGGQRQRVAIGRAIVRQPGVFLFD 159
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFdELDIDIDPRAKVatLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 160 EPLSNLdatlrgqTRIEIARLHKQFAK-----ASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:PRK10982 160 EPTSSL-------TEKEVNHLFTIIRKlkergCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
15-167 |
5.03e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNdvpaAQRGvamVFQSYALF------ 88
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYHQDLLYlghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 89 --PHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRpkaLSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLD 166
Cdd:PRK13538 85 ikTELTALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
.
gi 1431886808 167 A 167
Cdd:PRK13538 162 K 162
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-237 |
7.76e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.72 E-value: 7.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKStlLRMIAGLEDLTDGDLFIGGEVMND----VPAAQRG--VAMVFQS--YALFP 89
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDgkpvAPCALRGrkIATIMQNprSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 90 hmtvFENMA-----FGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSN 164
Cdd:PRK10418 95 ----LHTMHthareTCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 165 LDATLRGQTRIEIARLHKQFAkASVVYVTHDQIEAMTLADKIVLLHAGKdterygsIAQIGAPLELYHRPRSR 237
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRA-LGMLLVTHDMGVVARLADDVAVMSHGR-------IVEQGDVETLFNAPKHA 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-233 |
1.23e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKSTLLR-MIAGLEDLTDGDLFIGGEVMNdVPAaqrgVAMVFQSyalfphmTVFEN 96
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVAY-VPQ----VSWIFNA-------TVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 97 MAFGlklAKTPKDEIDRKVREAARILQLEALLER-------RPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDA-- 167
Cdd:PLN03232 699 ILFG---SDFESERYWRAIDVTALQHDLDLLPGRdlteigeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhv 775
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431886808 168 -----------TLRGQTRieiarlhkqfakasvVYVThDQIEAMTLADKIVLLHAGKDTERyGSIAQIGAPLELYHR 233
Cdd:PLN03232 776 ahqvfdscmkdELKGKTR---------------VLVT-NQLHFLPLMDRIILVSEGMIKEE-GTFAELSKSGSLFKK 835
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-235 |
1.68e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.76 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 1 MASISLRGVQKAYGDGAPVIRDVD---LEIGENEFCVFLGPSGCGKSTLLRMIAGLED----LTDGDLFIGGEVMNDVPA 73
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 74 AQR------GVAMVFQS--YALFPHMTVFENMAFGLKLAKTPkdeiDRKVREAARILQL--------EALLERRPKALSG 137
Cdd:PRK11022 81 KERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGG----NKKTRRQRAIDLLnqvgipdpASRLDVYPHQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 138 GQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTrIEIARLHKQFAKASVVYVTHDQIEAMTLADKIVLLHAGKdter 217
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQI-IELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQ---- 231
|
250
....*....|....*...
gi 1431886808 218 ygsIAQIGAPLELYHRPR 235
Cdd:PRK11022 232 ---VVETGKAHDIFRAPR 246
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-166 |
5.57e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.59 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 2 ASISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVpAAQRGVAMV 81
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-LQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYAL---FP-------HMTVFENMAFgLKLAKTPKDEIdrkVREA-ARILQLEaLLERRPKALSGGQRQRVAIGRAIV 150
Cdd:PRK15056 84 PQSEEVdwsFPvlvedvvMMGRYGHMGW-LRRAKKRDRQI---VTAAlARVDMVE-FRHRQIGELSGGQKKRVFLARAIA 158
|
170
....*....|....*.
gi 1431886808 151 RQPGVFLFDEPLSNLD 166
Cdd:PRK15056 159 QQGQVILLDEPFTGVD 174
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-252 |
1.55e-10 |
|
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: 63.11 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAY-GDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGE-VMNDVPAAQRGVAMV 81
Cdd:TIGR01257 1938 LRLNELTKVYsGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsILTNISDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEP 161
Cdd:TIGR01257 2018 PQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 162 LSNLDATLRG---QTRIEIARLHKqfakaSVVYVTHDQIEAMTLADKIVLLHAGKdTERYGSIAQIgaplelyhrpRSRF 238
Cdd:TIGR01257 2098 TTGMDPQARRmlwNTIVSIIREGR-----AVVLTSHSMEECEALCTRLAIMVKGA-FQCLGTIQHL----------KSKF 2161
|
250
....*....|....*....
gi 1431886808 239 VAGF-----IGSPRMNFLP 252
Cdd:TIGR01257 2162 GDGYivtmkIKSPKDDLLP 2180
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-216 |
3.28e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.94 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 5 SLRGVQKAYGDGAPvIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAG------------LEDLTDGDLFIGGEvmndvp 72
Cdd:PRK11701 8 SVRGLTKLYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSArlapdagevhyrMRDGQLRDLYALSE------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 73 aAQRGVAM------VFQSYA--LFPHMTVFEN-----MAFGLK----LAKTPKDEIDRKVREAARIlqleallERRPKAL 135
Cdd:PRK11701 81 -AERRRLLrtewgfVHQHPRdgLRMQVSAGGNigerlMAVGARhygdIRATAGDWLERVEIDAARI-------DDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 136 SGGQRQRVAIGRAIVRQPGVFLFDEPLSNLD----ATLRGQTRIEIARLHkqfakASVVYVTHDQIEAMTLADKIVLLHA 211
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGLVRELG-----LAVVIVTHDLAVARLLAHRLLVMKQ 227
|
....*
gi 1431886808 212 GKDTE 216
Cdd:PRK11701 228 GRVVE 232
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
11-196 |
5.21e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.27 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 11 KAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLE--DLTDGDLFIGGEVMNDVPA---AQRGVAMVFQSY 85
Cdd:CHL00131 14 HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPeerAHLGIFLAFQYP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 86 ALFPHMTV--FENMAFGLKLAKTPKDEID-----RKVREAARILQLEA-LLERR-PKALSGGQRQRVAIGRAIVRQPGVF 156
Cdd:CHL00131 94 IEIPGVSNadFLRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNvNEGFSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1431886808 157 LFDEPLSNLDA-TLRgqtriEIARLHKQFAKA--SVVYVTHDQ 196
Cdd:CHL00131 174 ILDETDSGLDIdALK-----IIAEGINKLMTSenSIILITHYQ 211
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-185 |
7.26e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGevmNDVPAAQRGVAMVFQSY--ALFPHMT 92
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGDRSRFMAYLGHlpGLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 93 VFENMAF-----GLKLAKTPKDeidrkvreAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDa 167
Cdd:PRK13543 99 TLENLHFlcglhGRRAKQMPGS--------ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD- 169
|
170 180
....*....|....*....|.
gi 1431886808 168 tLRGQT---RIEIARLHKQFA 185
Cdd:PRK13543 170 -LEGITlvnRMISAHLRGGGA 189
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-166 |
1.47e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 19 VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIG-GEVMNDVPAA--QRGVAMVFQSYALFPHmTVFE 95
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKwwRSKIGVVSQDPLLFSN-SIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 96 NMAFGLKLAK----------------------------------------TPKDEI-----------DRKVREAARIL-- 122
Cdd:PTZ00265 479 NIKYSLYSLKdlealsnyynedgndsqenknkrnscrakcagdlndmsntTDSNELiemrknyqtikDSEVVDVSKKVli 558
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1431886808 123 ---------QLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLD 166
Cdd:PTZ00265 559 hdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-195 |
2.00e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGApVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMndvpaaqrgVAMVFQ 83
Cdd:PRK11819 325 IEAENLSKSFGDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVK---------LAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SY-ALFPHMTVFENMAFGLKLAKTPKDEIdrkvreAARilqleALLER----------RPKALSGGQRQRVAIGRaIVRQ 152
Cdd:PRK11819 395 SRdALDPNKTVWEEISGGLDIIKVGNREI------PSR-----AYVGRfnfkggdqqkKVGVLSGGERNRLHLAK-TLKQ 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1431886808 153 PG-VFLFDEPLSNLDA-TLRGqtrIEIARLhkQFAKASVVyVTHD 195
Cdd:PRK11819 463 GGnVLLLDEPTNDLDVeTLRA---LEEALL--EFPGCAVV-ISHD 501
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
244-298 |
2.33e-09 |
|
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK transport protein.
Pssm-ID: 465563 [Multi-domain] Cd Length: 53 Bit Score: 52.59 E-value: 2.33e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1431886808 244 GSPRMNFLPGRI----ASFDAQGVVVALDHTHenvhvpVDGAALQVSQAVTLGVRPEHL 298
Cdd:pfam17912 1 GSPPMNFLPATVvedgLLVLGGGVTLPLPEGQ------VLALKLYVGKEVILGIRPEHI 53
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-210 |
2.58e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 56.04 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 26 EIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDlfiggevmndvpaaqrgvamvfqsyalfphmtvfenmafglklak 105
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN--------------------------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 106 tpkDEIDRkVREAARILQLEallerrpkaLSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDAtlrgQTRIEIARLHKQF- 184
Cdd:cd03222 56 ---DEWDG-ITPVYKPQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDI----EQRLNAARAIRRLs 118
|
170 180
....*....|....*....|....*...
gi 1431886808 185 --AKASVVYVTHDQIEAMTLADKIVLLH 210
Cdd:cd03222 119 eeGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-183 |
3.10e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 24 DLEIGENEFCVFLGPSGCGKSTLLRMIAGleDLTdgdlFIGGEVMNDvpaaqrgvamvFQSyalfPHMTVFENMA----- 98
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAG--ELP----LLSGERQSQ-----------FSH----ITRLSFEQLQklvsd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 99 ----------------FGLKLAKTPKDEIDRKVR--EAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:PRK10938 82 ewqrnntdmlspgeddTGRTTAEIIQDEVKDPARceQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180
....*....|....*....|...
gi 1431886808 161 PLSNLDATLRGQTRIEIARLHKQ 183
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQS 184
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-238 |
5.50e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.25 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDGAP-VIRDVDLEIGENEFCVFLGPSGCGKSTLL----RMIagleDLTDGDLFIGGEvmnDVPA---- 73
Cdd:PTZ00243 1308 SLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGR---EIGAyglr 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 74 -AQRGVAMVFQSYALFPHmTVFENM-AFglkLAKTPKdeidrkvrEAARILQLEALLER--------RPKALSGG----- 138
Cdd:PTZ00243 1381 eLRRQFSMIPQDPVLFDG-TVRQNVdPF---LEASSA--------EVWAALELVGLRERvasesegiDSRVLEGGsnysv 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 139 -QRQRVAIGRAIV-RQPGVFLFDEPLSNLDATLRGQTRieiARLHKQFAKASVVYVTHdQIEAMTLADKIVLLHagkdte 216
Cdd:PTZ00243 1449 gQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQ---ATVMSAFSAYTVITIAH-RLHTVAQYDKIIVMD------ 1518
|
250 260
....*....|....*....|..
gi 1431886808 217 rYGSIAQIGAPLELYHRPRSRF 238
Cdd:PTZ00243 1519 -HGAVAEMGSPRELVMNRQSIF 1539
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-209 |
6.25e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.28 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGApVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLfiggevmndVPAAQRGVAMVFQ 83
Cdd:PRK09544 5 VSLENVSVSFGQRR-VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYALFPHMTVFENMAFGLKLAKTPKDeidrkVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:PRK09544 75 KLYLDTTLPLTVNRFLRLRPGTKKED-----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1431886808 164 NLDatLRGQTRIE--IARLHKQFAKAsVVYVTHDQIEAMTLADKIVLL 209
Cdd:PRK09544 150 GVD--VNGQVALYdlIDQLRRELDCA-VLMVSHDLHLVMAKTDEVLCL 194
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-259 |
7.98e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 56.73 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 23 VDLEIGENEFCVFLGPSGCGKSTLLRMIAGLedlTDGDLFIGGEVM--NDV------PAAQR-----GVAMVFQSyalfP 89
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADRMrfDDIdllrlsPRERRklvghNVSMIFQE----P 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 90 HMTVFENMAFGLKLAK-----TPK----DEIDRKVREAARILQL------EALLERRPKALSGGQRQRVAIGRAIVRQPG 154
Cdd:PRK15093 99 QSCLDPSERVGRQLMQnipgwTYKgrwwQRFGWRKRRAIELLHRvgikdhKDAMRSFPYELTEGECQKVMIAIALANQPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 155 VFLFDEPLSNLDATLRGQTRIEIARLHkQFAKASVVYVTHDQIEAMTLADKIVLLHAGKDTERYGSIAQIGAPLELYHRP 234
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLN-QNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQA 257
|
250 260 270
....*....|....*....|....*....|
gi 1431886808 235 RSRFVAGFiGSP-----RMNFLPGRIASFD 259
Cdd:PRK15093 258 LIRAIPDF-GSAmphksRLNTLPGAIPLLE 286
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-212 |
2.60e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.45 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGleDLTD----------GDLFIGGEVMNDVPA---AQRGVAMV 81
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGggaprgarvtGDVTLNGEPLAAIDAprlARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 82 FQSYALFPhMTVFENMAFGLKLAKTPKDEIDRKVRE-AARILQL---EALLERRPKALSGGQRQRVAIGRAI-------- 149
Cdd:PRK13547 90 QAAQPAFA-FSAREIVLLGRYPHARRAGALTHRDGEiAWQALALagaTALVGRDVTTLSGGELARVQFARVLaqlwpphd 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 150 -VRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQFaKASVVYVTHDQIEAMTLADKIVLLHAG 212
Cdd:PRK13547 169 aAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDW-NLGVLAIVHDPNLAARHADRIAMLADG 231
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
15-166 |
2.86e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.03 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLED--LTDGDL-FIGGEVMNDVPA--AQRGVAMVFQSYALFP 89
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVeFKGKDLLELSPEdrAGEGIFMAFQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 90 HMT--VFENMAFGLKLAKTPKDEIDR-----KVREAARILQLEA-LLERRPK-ALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:PRK09580 92 GVSnqFFLQTALNAVRSYRGQEPLDRfdfqdLMEEKIALLKMPEdLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDE 171
|
....*.
gi 1431886808 161 PLSNLD 166
Cdd:PRK09580 172 SDSGLD 177
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-213 |
9.43e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.85 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVpAAQRGVA--MVFQSY-----ALFPH 90
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR-SPQDGLAngIVYISEdrkrdGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 91 MTVFENMAF-GLKLAKTPKDEIDRKVREAA--RILQLEAL----LERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLS 163
Cdd:PRK10762 345 MSVKENMSLtALRYFSRAGGSLKHADEQQAvsDFIRLFNIktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 164 NLDAtlrGQTRiEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:PRK10762 425 GVDV---GAKK-EIYQLINQFKAEglSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-207 |
1.07e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 6 LRGVQKAYgDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGleDLTDgdlfIGGEVM---NdvpaAQRGVaMVF 82
Cdd:PRK15064 322 VENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG--ELEP----DSGTVKwseN----ANIGY-YAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 83 QSYALFPH-MTVFENMAfglkLAKTPKDEiDRKVREA-ARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:PRK15064 390 DHAYDFENdLTLFDWMS----QWRQEGDD-EQAVRGTlGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDE 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1431886808 161 PLSNLDatlrgQTRIEIARLHKQFAKASVVYVTHDQIEAMTLADKIV 207
Cdd:PRK15064 465 PTNHMD-----MESIESLNMALEKYEGTLIFVSHDREFVSSLATRII 506
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-161 |
1.52e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDvpAAQRgvAMVFQ 83
Cdd:NF033858 2 ARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD--ARHR--RAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYA---------LFPHMTVFENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPG 154
Cdd:NF033858 77 RIAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
....*..
gi 1431886808 155 VFLFDEP 161
Cdd:NF033858 157 LLILDEP 163
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
36-167 |
2.57e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.93 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 36 LGPSGCGKSTLLRMIAGLED--LTDGDLFIGGevmndVPAAQRGVAMVF----QSYALFPHMTVFENMAFG--LKLAK-T 106
Cdd:PLN03140 912 MGVSGAGKTTLMDVLAGRKTggYIEGDIRISG-----FPKKQETFARISgyceQNDIHSPQVTVRESLIYSafLRLPKeV 986
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1431886808 107 PKDEIDRKVREAARILQLEALLER---RP--KALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDA 167
Cdd:PLN03140 987 SKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-213 |
6.87e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMND---VPAAQRGVAMVFQ---SYALFPHM 91
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaNEAINHGFALVTEerrSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 92 TV-FENMAFGLKLAKTPKDEIDRKVREAARILQLEALLERRPK------ALSGGQRQRVAIGRAIVRQPGVFLFDEPLSN 164
Cdd:PRK10982 342 DIgFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGhrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1431886808 165 LDATlrgqTRIEIARLHKQFAK--ASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:PRK10982 422 IDVG----AKFEIYQLIAELAKkdKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-213 |
6.91e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.98 E-value: 6.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGL-EDLTDGDLFIGG---EVMNDVPAAQRGVAMVFQS---YALFPHMT 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGkpvDIRNPAQAIRAGIAMVPEDrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 93 VFENMAFGLKLAKTPKDEID-----RKVREAARILQLEALLERRPKA-LSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLD 166
Cdd:TIGR02633 356 VGKNITLSVLKSFCFKMRIDaaaelQIIGSAIQRLKVKTASPFLPIGrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1431886808 167 ATlrgqTRIEIARLHKQFAK--ASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:TIGR02633 436 VG----AKYEIYKLINQLAQegVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
291-366 |
6.97e-07 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 46.46 E-value: 6.97e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431886808 291 LGVRPEHLEFVDSSSShddaiLSRAVSLVEQLGEHSYVHLDQPGGAALIAKAP--GDTRLAPGDRANLRVPRHATHLF 366
Cdd:pfam08402 1 LAIRPEKIRLAAAANG-----LSGTVTDVEYLGDHTRYHVELAGGEELVVRVPnaHARPPAPGDRVGLGWDPEDAHVL 73
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-208 |
8.68e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.14 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 30 NEFCVFLGPSGCGKSTLLRMIAGLEDLTDGD-LFIGGEVMndvpaaqrgvamvfqsyalfphmtvfenmafglklaktpk 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDI---------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 109 deidrkvREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEIARLH----KQF 184
Cdd:smart00382 42 -------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllKSE 114
|
170 180
....*....|....*....|....
gi 1431886808 185 AKASVVYVTHDQIEAMTLADKIVL 208
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRRRF 138
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
15-257 |
9.66e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.85 E-value: 9.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDlTDGDLFIGGEVMNDVPAAQ--RGVAMVFQSYALFPHmT 92
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKwrKAFGVIPQKVFIFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 93 VFENmafgLKLAKTPKDEIDRKVREAARIL--------QLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSN 164
Cdd:cd03289 93 FRKN----LDPYGKWSDEEIWKVAEEVGLKsvieqfpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 165 LDAtlrgqTRIEIAR--LHKQFAKASVVYVTHdQIEAMTLADKIVLLHAGKdTERYGSIAQIgaplelyHRPRSRFVAGF 242
Cdd:cd03289 169 LDP-----ITYQVIRktLKQAFADCTVILSEH-RIEAMLECQRFLVIEENK-VRQYDSIQKL-------LNEKSHFKQAI 234
|
250
....*....|....*
gi 1431886808 243 IGSPRMNFLPGRIAS 257
Cdd:cd03289 235 SPSDRLKLFPRRNSS 249
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-170 |
1.33e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDgAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAG------LEDLTdgdLFiG-----GEVMNDVp 72
Cdd:PRK10938 261 IVLNNGVVSYND-RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgySNDLT---LF-GrrrgsGETIWDI- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 73 aaQRGVAMVFQSYalfpHM-----TVFENM-------AFGLKLAKTpkDEIDRKVREAARILQLEALLERRP-KALSGGQ 139
Cdd:PRK10938 335 --KKHIGYVSSSL----HLdyrvsTSVRNVilsgffdSIGIYQAVS--DRQQKLAQQWLDILGIDKRTADAPfHSLSWGQ 406
|
170 180 190
....*....|....*....|....*....|.
gi 1431886808 140 RQRVAIGRAIVRQPGVFLFDEPLSNLDATLR 170
Cdd:PRK10938 407 QRLALIVRALVKHPTLLILDEPLQGLDPLNR 437
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
3-160 |
1.33e-06 |
|
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: 50.18 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAY----GDGAPVIRDVDLEI--GEnefCVFL-GPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVmndVPAAQ 75
Cdd:COG4615 327 TLELRGVTYRYpgedGDEGFTLGPIDLTIrrGE---LVFIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 76 RGV-----AMVFQSYALFPHMtvfenmaFGLKLAKTPKD--------EIDRKVR-EAARILQLeallerrpkALSGGQRQ 141
Cdd:COG4615 401 REAyrqlfSAVFSDFHLFDRL-------LGLDGEADPARarellerlELDHKVSvEDGRFSTT---------DLSQGQRK 464
|
170
....*....|....*....
gi 1431886808 142 RVAIGRAIVRQPGVFLFDE 160
Cdd:COG4615 465 RLALLVALLEDRPILVFDE 483
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-224 |
1.68e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.04 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVmnDVPAAQRGvamvfqsyaLFPHMTVFENMAF 99
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV--SVIAISAG---------LSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 100 GLKLAKTPKDEIDRKVREAARILQLEALLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEIAR 179
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1431886808 180 LHKQfaKASVVYVTHDQIEAMTLADKIVLLHAGKDTErYGSIAQI 224
Cdd:PRK13546 189 FKEQ--NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD-YGELDDV 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-238 |
1.89e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 3 SISLRGVQKAYGDG-APVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGG-EV----MNDVpaaQR 76
Cdd:PLN03232 1234 SIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcDVakfgLTDL---RR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 77 GVAMVFQSYALFPHMTVFENMAFglklaktpKDEIDRKVREAARILQLEALLERRPKAL-----------SGGQRQRVAI 145
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFNIDPF--------SEHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 146 GRAIVRQPGVFLFDEPLSNLDatLRGQTRIEiARLHKQFAKASVVYVTHdQIEAMTLADKIVLLHAGKdterygsIAQIG 225
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVD--VRTDSLIQ-RTIREEFKSCTMLVIAH-RLNTIIDCDKILVLSSGQ-------VLEYD 1451
|
250
....*....|...
gi 1431886808 226 APLELYHRPRSRF 238
Cdd:PLN03232 1452 SPQELLSRDTSAF 1464
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-224 |
1.89e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.91 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 15 DGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDlTDGDLFIGGEVMNDVPAAQRGVAmvfqsYALFPHMTVF 94
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA-----FGVIPQKVFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 95 ENMAFGLKL---AKTPKDEIDRKVREAArilqLEALLERRPK-----------ALSGGQRQRVAIGRAIVRQPGVFLFDE 160
Cdd:TIGR01271 1304 FSGTFRKNLdpyEQWSDEEIWKVAEEVG----LKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSKAKILLLDE 1379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1431886808 161 PLSNLDAtlrgqTRIEIAR--LHKQFAKASVVYVTHdQIEAMtLADKIVLLHAGKDTERYGSIAQI 224
Cdd:TIGR01271 1380 PSAHLDP-----VTLQIIRktLKQSFSNCTVILSEH-RVEAL-LECQQFLVIEGSSVKQYDSIQKL 1438
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-166 |
2.18e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 4 ISLRGVQKAYGDGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVmndvpaaqrgvamvfq 83
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV---------------- 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 syalfpHMTVF-ENMAFGLKLAKTP--------KDEIDRKVREAARILQLEALLERRPK-ALSGGQRQRVAIGRAIVRQP 153
Cdd:PLN03073 573 ------RMAVFsQHHVDGLDLSSNPllymmrcfPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKP 646
|
170
....*....|...
gi 1431886808 154 GVFLFDEPLSNLD 166
Cdd:PLN03073 647 HILLLDEPSNHLD 659
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-207 |
2.79e-06 |
|
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: 47.60 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 34 VFLGPSGCGKSTLlrmIAGLEDLTDGDLF---IGGEVMNDVPAAQ--RG-VAMVFQS-----YALFPHMTVFENMAFglk 102
Cdd:cd03240 26 LIVGQNGAGKTTI---IEALKYALTGELPpnsKGGAHDPKLIREGevRAqVKLAFENangkkYTITRSLAILENVIF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 103 lakTPKDEIDrkvreaarilqleALLERRPKALSGGQRQ------RVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIE 176
Cdd:cd03240 100 ---CHQGESN-------------WPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAE 163
|
170 180 190
....*....|....*....|....*....|.
gi 1431886808 177 IARLHKQFAKASVVYVTHDQiEAMTLADKIV 207
Cdd:cd03240 164 IIEERKSQKNFQLIVITHDE-ELVDAADHIY 193
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-212 |
2.84e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 48.37 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 18 PVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVP--AAQRGVAMVFQSYALFPHmtvfe 95
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlhTLRSRLSIILQDPILFSG----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 96 NMAFGLKLAKTPKDEidrKVREAARILQLEALLERRPKAL-----------SGGQRQRVAIGRAIVRQPGVFLFDEPLSN 164
Cdd:cd03288 110 SIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATAS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1431886808 165 LDATLRG--QTRIEIArlhkqFAKASVVYVTHdQIEAMTLADKIVLLHAG 212
Cdd:cd03288 187 IDMATENilQKVVMTA-----FADRTVVTIAH-RVSTILDADLVLVLSRG 230
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-160 |
4.37e-06 |
|
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: 48.59 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 16 GAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIggevmndvPAAQRgvamvfqsyaLF-----PH 90
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK--------PAKGK----------LFyvpqrPY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 91 MTV--FENMAFglkLAKTPKDEIDRKVREAARI-----LQLEALLERR---------PKALSGGQRQRVAIGRAIVRQPG 154
Cdd:TIGR00954 526 MTLgtLRDQII---YPDSSEDMKRRGLSDKDLEqildnVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQ 602
|
....*.
gi 1431886808 155 VFLFDE 160
Cdd:TIGR00954 603 FAILDE 608
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
16-213 |
7.68e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.60 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 16 GAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMN-DVP--AAQRGVAMV---FQSYALFP 89
Cdd:PRK11288 265 GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPrdAIRAGIMLCpedRKAEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 90 HMTVFENMAFGLKLAKTPKDEI--DRKVREAARiLQLEALLERRPKA------LSGGQRQRVAIGRAIVRQPGVFLFDEP 161
Cdd:PRK11288 345 VHSVADNINISARRHHLRAGCLinNRWEAENAD-RFIRSLNIKTPSReqlimnLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 162 LSNLDATLRGqtriEIARLHKQFAKA--SVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:PRK11288 424 TRGIDVGAKH----EIYNVIYELAAQgvAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-220 |
9.93e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.39 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLrmiagledltdgdlfiggevmNDVPAAQRGVAMVFQSYALFPHMTVFenmaf 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV---------------------NEGLYASGKARLISFLPKFSRNKLIF----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 100 glklaktpkdeidrkvreaarILQLEAL---------LERRPKALSGGQRQRVAIGRAIVRQPG--VFLFDEPLSNLDAT 168
Cdd:cd03238 65 ---------------------IDQLQFLidvglgyltLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1431886808 169 LRGQTRIEIARLHKQfaKASVVYVTHDQiEAMTLADKIVLLhaGKDTERYGS 220
Cdd:cd03238 124 DINQLLEVIKGLIDL--GNTVILIEHNL-DVLSSADWIIDF--GPGSGKSGG 170
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
58-213 |
3.14e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.69 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 58 DGDLFIGG---EVMNDVPAAQRGVAMVFQS---YALFPHMTVFENM--------AFGLKL-----AKTPKDEIDR-KVRE 117
Cdd:PRK13549 317 EGEIFIDGkpvKIRNPQQAIAQGIAMVPEDrkrDGIVPVMGVGKNItlaaldrfTGGSRIddaaeLKTILESIQRlKVKT 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 118 AArilqlealLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATlrgqTRIEIARLHKQFAKA--SVVYVTHD 195
Cdd:PRK13549 397 AS--------PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVG----AKYEIYKLINQLVQQgvAIIVISSE 464
|
170
....*....|....*...
gi 1431886808 196 QIEAMTLADKIVLLHAGK 213
Cdd:PRK13549 465 LPEVLGLSDRVLVMHEGK 482
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-224 |
4.25e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.65 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 20 IRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEvmndvpaaqrgVAMVFQSYALFPHMTVFENMAF 99
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------AALIAISSGLNGQLTGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 100 -GLKLAKTPKD--EIDRKVREAARILQleaLLERRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIE 176
Cdd:PRK13545 109 kGLMMGLTKEKikEIIPEIIEFADIGK---FIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1431886808 177 IARLHKQfaKASVVYVTHDQIEAMTLADKIVLLHAGKDTErYGSIAQI 224
Cdd:PRK13545 186 MNEFKEQ--GKTIFFISHSLSQVKSFCTKALWLHYGQVKE-YGDIKEV 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-230 |
1.23e-04 |
|
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: 44.17 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 19 VIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGevmndVPAAQRGVAMVFQSYALFPHMTVFenMA 98
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG-----LNIAKIGLHDLRFKITIIPQDPVL--FS 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 99 FGLKLAKTPKDEI-DRKVREAARILQLEALLERRP-----------KALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLD 166
Cdd:TIGR00957 1374 GSLRMNLDPFSQYsDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431886808 167 atLRGQTRIEiARLHKQFAKASVVYVTHDQIEAMTLADKIVLlhagkdteRYGSIAQIGAPLEL 230
Cdd:TIGR00957 1454 --LETDNLIQ-STIRTQFEDCTVLTIAHRLNTIMDYTRVIVL--------DKGEVAEFGAPSNL 1506
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
84-236 |
1.73e-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: 43.85 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 84 SYALFPHMTVFENMAFGLKLAKTPK-----DEIDRKVREAARILQ---LEAL-LERRPKALSGGQRQRVA----IGRAIV 150
Cdd:TIGR00630 429 SIADVSELSIREAHEFFNQLTLTPEekkiaEEVLKEIRERLGFLIdvgLDYLsLSRAAGTLSGGEAQRIRlatqIGSGLT 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 151 rqpGV-FLFDEPL--------SNLDATLRgqtrieiaRLHKQfaKASVVYVTHDQiEAMTLADKIVLL--HAGkdtERYG 219
Cdd:TIGR00630 509 ---GVlYVLDEPSiglhqrdnRRLINTLK--------RLRDL--GNTLIVVEHDE-DTIRAADYVIDIgpGAG---EHGG 571
|
170
....*....|....*..
gi 1431886808 220 SIAQIGAPLELYHRPRS 236
Cdd:TIGR00630 572 EVVASGTPEEILANPDS 588
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-213 |
2.59e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.12 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 6 LRGVQKAYGDGAPVI----------RDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGLEDLTDGDLFIGGEVMNDVPAAQ 75
Cdd:PRK15439 255 LPGNRRQQAAGAPVLtvedltgegfRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 76 R-GVAMVF-----QSYALFPHMT--------VFENMAFGLKLAKtpkdeiDRKVREA-ARILQLEALLERRP-KALSGGQ 139
Cdd:PRK15439 335 RlARGLVYlpedrQSSGLYLDAPlawnvcalTHNRRGFWIKPAR------ENAVLERyRRALNIKFNHAEQAaRTLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1431886808 140 RQRVAIGRAIVRQPGVFLFDEPLSNLDATlrgqTRIEIARLHKQFAK--ASVVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:PRK15439 409 QQKVLIAKCLEASPQLLIVDEPTRGVDVS----ARNDIYQLIRSIAAqnVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
20-61 |
4.32e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.84 E-value: 4.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1431886808 20 IRDVDLEIGEneFCVFLGPSGCGKSTLLRMIAGLEDLTDGDL 61
Cdd:COG4637 13 LRDLELPLGP--LTVLIGANGSGKSNLLDALRFLSDAARGGL 52
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
112-213 |
5.10e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 112 DRKVReAARILQLEALLE---RRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLDATLRGQTRIEIARLHKQfaKAS 188
Cdd:NF000106 120 DARAR-ADELLERFSLTEaagRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD--GAT 196
|
90 100
....*....|....*....|....*
gi 1431886808 189 VVYVTHDQIEAMTLADKIVLLHAGK 213
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTVIDRGR 221
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
130-166 |
6.26e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 6.26e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1431886808 130 RRPKALSGGQRQRVAIGRAIVRQPGVFLFDEPLSNLD 166
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-182 |
7.00e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 6 LRGVQKAYGdGAPVIRDVDLEIGENEFCVFLGPSGCGKSTLLRMIAGL--EDLTDGDLFIGGEVMN--DVPAA-QRGVAM 80
Cdd:NF040905 4 MRGITKTFP-GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEVCRfkDIRDSeALGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 81 VFQSYALFPHMTVFENMAFGLKLAKtpKDEIDRK--VREAARILQLEALLErRPKALSG----GQRQRVAIGRAIVRQPG 154
Cdd:NF040905 83 IHQELALIPYLSIAENIFLGNERAK--RGVIDWNetNRRARELLAKVGLDE-SPDTLVTdigvGKQQLVEIAKALSKDVK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1431886808 155 VFLFDEP-----------LSNLDATLRGQ--TRIEIArlHK 182
Cdd:NF040905 160 LLILDEPtaalneedsaaLLDLLLELKAQgiTSIIIS--HK 198
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
33-60 |
6.26e-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: 37.76 E-value: 6.26e-03
10 20
....*....|....*....|....*...
gi 1431886808 33 CVFLGPSGCGKSTLLRMIAGLEDLTDGD 60
Cdd:cd01854 88 SVLVGQSGVGKSTLLNALLPELVLATGE 115
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
130-206 |
6.47e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.01 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431886808 130 RRPKALSGGQRQRVAIGR--AIVR-QPGVF-LFDEPLSNLDAtlrgQTRIEIARLHKQFAKASVVYVTHDQIEAMTLADK 205
Cdd:cd03272 154 QEMQQLSGGQKSLVALALifAIQKcDPAPFyLFDEIDAALDA----QYRTAVANMIKELSDGAQFITTTFRPELLEVADK 229
|
.
gi 1431886808 206 I 206
Cdd:cd03272 230 F 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-46 |
7.79e-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: 38.46 E-value: 7.79e-03
|
| |
