|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-364 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 618.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLDHIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAM 80
Cdd:COG3839 1 MASLELENVSKSYGG-VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 161 PLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGSPAM 240
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 241 NFFTGTLKDNYFHIENIRFKVPEGQlqklqkKGYNQKTLILGIRPEDIHDEPivlqsSPDSTVEINIEVAELLGAETMIH 320
Cdd:COG3839 240 NLLPGTVEGGGVRLGGVRLPLPAAL------AAAAGGEVTLGIRPEHLRLAD-----EGDGGLEATVEVVEPLGSETLVH 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446752175 321 GKLENQSFVARINARSELKAGDKLSVAFSLTKAHFFDSDTEVRI 364
Cdd:COG3839 309 VRLGGQELVARVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-364 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 547.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAM 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 161 PLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGSPAM 240
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 241 NFFTGTLKDnyfhiENIRFKVPEGQLQKL--QKKGYNQKTLILGIRPEDIHDepivlqSSPDSTVEINIEVAELLGAETM 318
Cdd:PRK11650 241 NLLDGRVSA-----DGAAFELAGGIALPLggGYRQYAGRKLTLGIRPEHIAL------SSAEGGVPLTVDTVELLGADNL 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446752175 319 IHGKLENQSFVARINARSELKAGDKLSVAFSLTKAHFFDSDTEVRI 364
Cdd:PRK11650 310 AHGRWGGQPLVVRLPHQERPAAGSTLWLHLPANQLHLFDADTGRRI 355
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-359 |
2.66e-154 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 438.69 E-value: 2.66e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLDHIFKLYDNktTAVS-DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIA 79
Cdd:PRK11000 1 MASVTLRNVTKAYGD--VVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 160 EPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGSPA 239
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 240 MNFFTGTLKDnyFHIENIRFKVPEGQLQKLQKKGYNQKT---LILGIRPEdiHdepIVLQSSPDSTVEINIEVAELLGAE 316
Cdd:PRK11000 239 MNFLPVKVTA--TAIEQVQVELPNRQQVWLPVEGRGVQVganMSLGIRPE--H---LLPSDIADVTLEGEVQVVEQLGNE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446752175 317 TMIHGKLE--NQSFVARINARSELKAGDKLSVAFSLTKAHFFDSD 359
Cdd:PRK11000 312 TQIHIQIPaiRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFRED 356
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-358 |
3.33e-152 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 432.60 E-value: 3.33e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLDHIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAM 80
Cdd:COG3842 3 MPALELENVSKRYGD-VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 161 PLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGSpaM 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGE--A 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 241 NFFTGTL---KDNYFHIENIRFKVPEGQLQKLQKKGYnqktliLGIRPEDIHdepiVLQSSPDSTVEINIEVAELLGAET 317
Cdd:COG3842 240 NLLPGTVlgdEGGGVRTGGRTLEVPADAGLAAGGPVT------VAIRPEDIR----LSPEGPENGLPGTVEDVVFLGSHV 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446752175 318 MIHGKLEN-QSFVARI--NARSELKAGDKLSVAFSLTKAHFFDS 358
Cdd:COG3842 310 RYRVRLGDgQELVVRVpnRAALPLEPGDRVGLSWDPEDVVVLPA 353
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-217 |
7.44e-145 |
|
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: 408.57 E-value: 7.44e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQ 83
Cdd:cd03301 1 VELENVTKRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446752175 164 NLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVG 217
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-356 |
1.43e-115 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 339.43 E-value: 1.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 3 ELVLDHIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGK-LMNDVAPKDRDIAMV 81
Cdd:COG1118 2 SIEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdLFTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 82 FQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 162 LSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGspAMN 241
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 242 FFTGTLKDNYFHIENIRFKVPEGQLQKLQKkgynqktliLGIRPEDIHdepIVLQSSPDSTVEINIEVAELLGAETMIHG 321
Cdd:COG1118 239 VLRGRVIGGQLEADGLTLPVAEPLPDGPAV---------AGVRPHDIE---VSREPEGENTFPATVARVSELGPEVRVEL 306
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446752175 322 KLENQS---FVARIN----ARSELKAGDKlsVAFSLTKAHFF 356
Cdd:COG1118 307 KLEDGEgqpLEAEVTkeawAELGLAPGDP--VYLRPRPARVF 346
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-308 |
1.19e-113 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 335.38 E-value: 1.19e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQNY 85
Cdd:PRK09452 17 LRGISKSFDGKE-VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 86 ALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:PRK09452 96 ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 166 DAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGSpaMNFFTG 245
Cdd:PRK09452 176 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE--INIFDA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 246 T----LKDNYF------HIENIRFKVPEGQLQKLQkkgynqktLILgiRPEDIHDEPIVLQSSPD-------------ST 302
Cdd:PRK09452 254 TvierLDEQRVranvegRECNIYVNFAVEPGQKLH--------VLL--RPEDLRVEEINDDEHAEgligyvrernykgMT 323
|
....*.
gi 446752175 303 VEINIE 308
Cdd:PRK09452 324 LDSVVE 329
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-236 |
4.36e-113 |
|
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: 328.81 E-value: 4.36e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQ 83
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 164 NLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIG 236
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-217 |
7.11e-113 |
|
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: 327.55 E-value: 7.11e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDnKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQ 83
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446752175 164 NLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVG 217
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-356 |
2.28e-110 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 326.22 E-value: 2.28e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLDHIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAM 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFGA-FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 161 PLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGSpaM 240
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE--V 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 241 NFFTGTLkdnyfhIENIRFKVPEGQLQKLQKKGYNQKTLILGIRPEDIHDEPIVLQsspDSTVEINIEVAELLGAETMIH 320
Cdd:TIGR03265 239 NWLPGTR------GGGSRARVGGLTLACAPGLAQPGASVRLAVRPEDIRVSPAGNA---ANLLLARVEDMEFLGAFYRLR 309
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446752175 321 GKLEN---QSFVARINA----RSELKAGDKLSVAFSLTKAHFF 356
Cdd:TIGR03265 310 LRLEGlpgQALVADVSAseveRLGIRAGQPIWIELPAERLRAF 352
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
6-356 |
2.38e-105 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 313.86 E-value: 2.38e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMND-----VAPKDRDIAM 80
Cdd:NF040933 8 VTKIFKKGKKEVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPPEDRNIGM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:NF040933 88 VFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQVLLLDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 161 PLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGSpaM 240
Cdd:NF040933 168 PFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLIGD--I 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 241 NFFTGTLK-DNYFHIENIRFKVPEGQLQKlqkkgynqKTLILGIRPEDIHDEPIVLQSSPD--STVEINIEVAELLGAET 317
Cdd:NF040933 246 NLLEGKVEeEGLVDGNDLKIPLPNPKLEA--------GEVIIGIRPEDIDISESDMRLPPGfvEVGKGRVKVSSYAGGVF 317
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446752175 318 MIHGK-LENQSFVARINARSELKAGDKLSVAFSLTKAHFF 356
Cdd:NF040933 318 RVVVSpIDDDSIEIIVNSDRPIEEGEEVNLYVRPDKIKIF 357
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-288 |
1.17e-98 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 296.63 E-value: 1.17e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYdNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQ 83
Cdd:PRK11432 7 VVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 164 NLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGSPamNFF 243
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIF 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446752175 244 TGTLKDNYFHIENIRFKVPEGqlqklQKKGYNQKTLILGIRPEDI 288
Cdd:PRK11432 244 PATLSGDYVDIYGYRLPRPAA-----FAFNLPDGECTVGVRPEAI 283
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-288 |
6.99e-93 |
|
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: 280.92 E-value: 6.99e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 36 VGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRV 115
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 116 TEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQ 195
Cdd:TIGR01187 82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 196 TEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGSpaMNFFTGTLKDN----------YFHIENIRFKVPEGQ 265
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE--INVFEATVIERkseqvvlagvEGRRCDIYTDVPVEK 239
|
250 260
....*....|....*....|...
gi 446752175 266 LQKLQkkgynqktliLGIRPEDI 288
Cdd:TIGR01187 240 DQPLH----------VVLRPEKI 252
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-237 |
8.26e-91 |
|
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: 272.29 E-value: 8.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 3 ELVLDHIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVF 82
Cdd:cd03296 2 SIEVRNVSKRFGD-FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 83 QNYALYPHMSVYDNMAFGLKLRK----LPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPrserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 159 DEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGS 237
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
3.80e-89 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 268.88 E-value: 3.80e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLDHIFKLY---DNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKDRD 77
Cdd:COG1116 5 APALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK---PVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 78 IAMVFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446752175 158 MDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-356 |
4.04e-87 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 266.94 E-value: 4.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKlyDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQ 83
Cdd:NF040840 2 IRIENLSK--DWKEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:NF040840 80 NYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 164 NLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGspAMNFF 243
Cdd:NF040840 160 ALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG--FENII 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 244 TGTLKD----NYFHIENIRFKVPEgqlqklQKKGynqkTLILGIRPEDihdepIVLQSSPDSTVEIN-----IEVAELLG 314
Cdd:NF040840 238 EGVAEKggegTILDTGNIKIELPE------EKKG----KVRIGIRPED-----ITISTEKVKTSARNefkgkVEEIEDLG 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446752175 315 AETMIHGKLENQsFVARINARS----ELKAGDKLSVAFSLTKAHFF 356
Cdd:NF040840 303 PLVKLTLDVGII-LVAFITRSSfldlEINEGKEVYASFKASAVHVF 347
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-208 |
2.15e-84 |
|
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: 255.09 E-value: 2.15e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNK---TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKDRDIAM 80
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE---PVTGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446752175 161 PLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVM 208
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
17-236 |
9.73e-84 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 254.34 E-value: 9.73e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 17 TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQNYALYPHMSVYDN 96
Cdd:TIGR00968 13 FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYALFKHLTVRDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 97 MAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSE 176
Cdd:TIGR00968 93 IAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKELRSW 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 177 ISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIG 236
Cdd:TIGR00968 173 LRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
11-249 |
1.42e-82 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 256.30 E-value: 1.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 11 KLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQNYALYPH 90
Cdd:PRK11607 27 KSFDGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 171 VSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGSpaMNFFTGTLKD 249
Cdd:PRK11607 186 DRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVFEGVLKE 262
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-237 |
3.97e-82 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 252.70 E-value: 3.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKD-----RDIAM 80
Cdd:COG1125 4 FENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGE---DIRDLDpvelrRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGL--EDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:COG1125 81 VIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 159 DEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGS 237
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-236 |
5.44e-80 |
|
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: 244.55 E-value: 5.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 20 VSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQNYALYPHMSVYDNMAF 99
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 100 GLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISK 179
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 180 LHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIG 236
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-254 |
1.29e-77 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 242.68 E-value: 1.29e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQNY 85
Cdd:PRK10851 5 IANIKKSFGR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 86 ALYPHMSVYDNMAFGLKL---RKLP-KDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:PRK10851 84 ALFRHMTVFDNIAFGLTVlprRERPnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 162 LSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGSpaMN 241
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE--VN 241
|
250
....*....|...
gi 446752175 242 FFTGTLKDNYFHI 254
Cdd:PRK10851 242 RLQGTIRGGQFHV 254
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-238 |
8.54e-76 |
|
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: 234.12 E-value: 8.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMV 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 82 FQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLED--YLKRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 160 EPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGSP 238
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-235 |
2.31e-72 |
|
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: 226.37 E-value: 2.31e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 17 TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD------RDIAMVFQNYALYPH 90
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 171 VSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFI 235
Cdd:cd03294 197 REMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-211 |
3.76e-72 |
|
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: 222.45 E-value: 3.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYdNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMND----VAPKDRDIA 79
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQNYALYPHMSVYDNMAFGlklrklpkdeinhrvteaakilgledylkrkpkaLSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446752175 160 EPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
17-236 |
2.41e-71 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 227.04 E-value: 2.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 17 TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAP------KDRDIAMVFQNYALYPH 90
Cdd:TIGR01186 6 KKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:TIGR01186 86 MTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 171 VSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIG 236
Cdd:TIGR01186 166 DSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-217 |
5.98e-68 |
|
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: 212.93 E-value: 5.98e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQ---DKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMND------VAPKDRDIAMVFQNYALYPHMS 92
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 93 VYDNMAFGLKLRKLPKDEInhRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVS 172
Cdd:cd03297 92 VRENLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446752175 173 MRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVG 217
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-213 |
2.54e-65 |
|
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: 206.57 E-value: 2.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRD------IA 79
Cdd:cd03255 6 LSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafrrrhIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:cd03255 86 FVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446752175 160 EPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMtMASRLVVMKDGII 213
Cdd:cd03255 166 EPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-235 |
4.78e-65 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 211.12 E-value: 4.78e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 17 TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD------RDIAMVFQNYALYPH 90
Cdd:COG4175 40 TVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:COG4175 120 RTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIR 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 171 VSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFI 235
Cdd:COG4175 200 REMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFV 264
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-227 |
6.46e-65 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 205.64 E-value: 6.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNyalyP- 89
Cdd:COG1122 10 YPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQN----Pd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 90 ----HMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:COG1122 86 dqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446752175 166 DAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:COG1122 166 DPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-213 |
1.50e-64 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 204.51 E-value: 1.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELV-LDHIFKLY---DNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR 76
Cdd:COG1136 1 MSPLLeLRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 77 D------IAMVFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIV 150
Cdd:COG1136 81 ArlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 151 RDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQtEAMTMASRLVVMKDGII 213
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-226 |
3.08e-63 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 201.52 E-value: 3.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTavsDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQ 83
Cdd:COG3840 2 LRLDDLTYRYGDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHMSVYDNMAFGLKLR-KLPKDEINhRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGLRPGlKLTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446752175 163 SNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:COG3840 158 SALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-349 |
4.87e-63 |
|
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: 204.95 E-value: 4.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMND------VAPKDRDIAMVFQNYALYPHMSVYD 95
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 96 NMAFGLKLRKLPKDEInhRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLrvsmRS 175
Cdd:COG4148 97 NLLYGRKRAPRAERRI--SFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR----KA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 176 EI----SKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGfiGSPAMNFFTGTLK--D 249
Cdd:COG4148 171 EIlpylERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAGSVLEATVAahD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 250 NYFHIenIRFKVPEGQLQKLQKKGYNQKTLILGIRPEDIhdePIVLQSSPDSTVeINI------EVAELLGAETMIHGKL 323
Cdd:COG4148 249 PDYGL--TRLALGGGRLWVPRLDLPPGTRVRVRIRARDV---SLALEPPEGSSI-LNIlpgrvvEIEPADGGQVLVRLDL 322
|
330 340 350
....*....|....*....|....*....|....*
gi 446752175 324 ENQSFVARINARS----ELKAGDKL-----SVAFS 349
Cdd:COG4148 323 GGQTLLARITRRSadelGLAPGQTVyaqikSVALL 357
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-231 |
1.01e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 197.59 E-value: 1.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRD-IAMVF 82
Cdd:COG1131 1 IEVRGLTKRYGDKT-ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 83 QNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 163 SNLDAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP-ENVFV 231
Cdd:COG1131 160 SGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLlEDVFL 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-208 |
2.11e-60 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 195.08 E-value: 2.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLDHIFKLYDNK---TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKDRD 77
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 78 IAMVFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG4525 78 RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446752175 158 MDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVM 208
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-217 |
1.16e-58 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 189.49 E-value: 1.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-----RDIAM 80
Cdd:COG2884 4 FENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG2884 84 VFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 161 PLSNLDAKlrvsMRSEISKLHRRLN---TTTIYVTHDQTEAMTMASRLVVMKDGIIQQVG 217
Cdd:COG2884 164 PTGNLDPE----TSWEIMELLEEINrrgTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-211 |
1.21e-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: 188.83 E-value: 1.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNyal 87
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVFQN--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 88 yP-HM----SVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd03225 84 -PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446752175 163 SNLDAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
1.47e-57 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 195.12 E-value: 1.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYD----NKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD---- 75
Cdd:COG1123 261 LEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 76 -RDIAMVFQN--YALYPHMSVYDNMAFGLKLRK-LPKDEINHRVTEAAKILGL-EDYLKRKPKALSGGQRQRVALGRAIV 150
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 151 RDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-226 |
1.72e-57 |
|
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: 187.11 E-value: 1.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRD-----I 78
Cdd:COG1127 6 IEVRNLTKSFGDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 79 AMVFQNYALYPHMSVYDNMAFGLK-LRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446752175 158 MDEPLSNLDAklrVSMRS---EISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:COG1127 165 YDEPTAGLDP---ITSAVideLIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-228 |
7.81e-57 |
|
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: 185.39 E-value: 7.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQ 83
Cdd:COG1124 7 LSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRVQMVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NY--ALYPHMSVYDNMAFGLKLRKLPkdEINHRVTEAAKILGL-EDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG1124 87 DPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446752175 161 PLSNLDaklrVSMRSEI----SKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPEN 228
Cdd:COG1124 165 PTSALD----VSVQAEIlnllKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-226 |
6.50e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 180.64 E-value: 6.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-----RDI 78
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 79 AMVFQNYALYPHMSVYDNMAFG-------LK--LRKLPKDEInHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAI 149
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGrlgrtstWRslLGLFPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 150 VRDAKVFLMDEPLSNLDAKL-RVSMRSeISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIqqvgtpkeVYDTP 226
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV--------VFDGP 230
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-228 |
6.48e-53 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 175.18 E-value: 6.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDvAPKD-----RDI 78
Cdd:COG1126 2 IEIENLHKSFGD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDinklrRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 79 AMVFQNYALYPHMSVYDNMAFGL-KLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446752175 158 MDEPLSNLDAKlrvsMRSEISKLHRRL---NTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPEN 228
Cdd:COG1126 160 FDEPTSALDPE----LVGEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-229 |
8.28e-53 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 175.23 E-value: 8.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMV 81
Cdd:COG1120 2 LEAENLSVGYGGRP-VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 82 FQNYALYPHMSVYDNMAFG----LKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446752175 158 MDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYdTPENV 229
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL-TPELL 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-211 |
1.07e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.46 E-value: 1.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTaVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMV 81
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 82 FQNYALYPhMSVYDNMAFGLKLRKLPKDEinHRVTEAAKILGL-EDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG4619 80 PQEPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446752175 161 PLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-227 |
4.50e-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: 172.69 E-value: 4.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTTaVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-----RDIAM 80
Cdd:cd03261 3 LRGLTKSFGGRTV-LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLK-LRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:cd03261 82 LFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 160 EPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:cd03261 162 EPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-227 |
8.25e-52 |
|
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: 179.71 E-value: 8.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDIS---NGSFYIDGKLMNDVAPKDR--DIAMVFQN 84
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgrRIGMVFQD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 85 --YALYPhMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:COG1123 92 pmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 163 SNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:COG1123 171 TALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-227 |
2.81e-51 |
|
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: 170.84 E-value: 2.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDN---KTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-----RD 77
Cdd:cd03258 4 LKNVSKVFGDtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkarRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 78 IAMVFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 158 MDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-217 |
4.86e-51 |
|
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: 169.99 E-value: 4.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR-----DIAM 80
Cdd:cd03257 7 LSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirrkEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNY--ALYPHMSVYDNMAFGLKLRKLP--KDEINHRVTEAAKILGL-EDYLKRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:cd03257 87 VFQDPmsSLNPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446752175 156 FLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVG 217
Cdd:cd03257 167 LIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-217 |
6.29e-51 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 169.27 E-value: 6.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 23 FNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQNYALYPHMSVYDNMAFG-- 100
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGlh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 101 --LKLRKLPKDeinhRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEIS 178
Cdd:TIGR01277 97 pgLKLNAEQQE----KVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 446752175 179 KLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVG 217
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-224 |
1.00e-50 |
|
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: 169.67 E-value: 1.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-----RDI 78
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 79 AMVFQNYALYPHMSVYDNMAFGL---------KLRKLPKDEINhRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAI 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrstwrsLFGLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 150 VRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYD 224
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-212 |
2.01e-50 |
|
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: 167.81 E-value: 2.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELvlDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD----- 75
Cdd:TIGR02673 1 MIEF--HNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 76 RDIAMVFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:TIGR02673 79 RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 156 FLMDEPLSNLDAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGI 212
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
16-228 |
5.20e-50 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 167.58 E-value: 5.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 16 KTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDI----AMVFQNYALYPHM 91
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 92 SVYDNMAFG-LKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLr 170
Cdd:PRK09493 93 TALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446752175 171 vsmRSEISKLHRRLNT---TTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPEN 228
Cdd:PRK09493 172 ---RHEVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-223 |
8.05e-50 |
|
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: 167.99 E-value: 8.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLY-DNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGklMNDVAPKD-----RDIA 79
Cdd:TIGR04520 3 VENVSFSYpESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENlweirKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQNyalyPH-----MSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:TIGR04520 81 MVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 155 VFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAmTMASRLVVMKDGIIQQVGTPKEVY 223
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
6-213 |
1.06e-49 |
|
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: 166.13 E-value: 1.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDnktTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQNY 85
Cdd:cd03298 3 LDKIRFSYG---EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 86 ALYPHMSVYDNMAFGL--KLRKLPKDEinHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03298 80 NLFAHLTVEQNVGLGLspGLKLTAEDR--QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446752175 164 NLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
10-222 |
1.59e-49 |
|
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: 165.82 E-value: 1.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDI-----SNGSFYIDGKLMNDVAPKD----RDIAM 80
Cdd:cd03260 6 LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelrRRVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPhMSVYDNMAFGLKLR-KLPKDEINHRVTEAAKILGLEDYLKRKPKA--LSGGQRQRVALGRAIVRDAKVFL 157
Cdd:cd03260 86 VFQKPNPFP-GSIYDNVAYGLRLHgIKLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 158 MDEPLSNLDAKLRVSMRSEISKLHRRlnTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-338 |
1.82e-49 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 169.91 E-value: 1.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVA------PKDRDIAMVFQNYALYPHMSVYD 95
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflpPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 96 NMAFGLKLRKLPKDEIN-HRVTEaakILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMR 174
Cdd:TIGR02142 95 NLRYGMKRARPSERRISfERVIE---LLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 175 SEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGgfiGSPAMNFFTGTLKDNYFHI 254
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA---REDQGSLIEGVVAEHDQHY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 255 ENIRFKVPEGQLQKLQKKGYNQKTLILGIRPEDIhdepIVLQSSPDSTVEINIEVAELLGAETMIHGKL------ENQSF 328
Cdd:TIGR02142 249 GLTALRLGGGHLWVPENLGPTGARLRLRVPARDV----SLALQKPEATSIRNILPARVVEIEDSDIGRVgvvlesGGKTL 324
|
330
....*....|..
gi 446752175 329 VARIN--ARSEL 338
Cdd:TIGR02142 325 WARITrwARDEL 336
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-224 |
7.70e-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: 164.65 E-value: 7.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGK-LMNDVAPKDRDIAMVF 82
Cdd:COG4555 2 IEVENLSKKYGKVP-ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 83 QNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446752175 163 SNLDAKLRVSMRSEIsKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYD 224
Cdd:COG4555 161 NGLDVMARRLLREIL-RALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
4-210 |
8.47e-49 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 164.91 E-value: 8.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNK---TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPkdrDIAM 80
Cdd:NF040729 2 LKIQNISKTFINNkkeNEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGP---DRGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:NF040729 79 VFQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446752175 161 PLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKD 210
Cdd:NF040729 159 PLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSR 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-233 |
1.23e-48 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 163.98 E-value: 1.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTAvsdFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQ 83
Cdd:PRK10771 2 LKLTDITWLYHHLPMR---FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHMSVYDNMAFG----LKLrklpKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGlnpgLKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446752175 160 EPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIqqvgtpkeVYDTPENVFVGG 233
Cdd:PRK10771 155 EPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI--------AWDGPTDELLSG 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-287 |
1.24e-48 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 168.67 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 17 TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD------RDIAMVFQNYALYPH 90
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:PRK10070 121 MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 171 VSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVggfigspaMNFFTGTLKDN 250
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV--------RTFFRGVDISQ 272
|
250 260 270
....*....|....*....|....*....|....*..
gi 446752175 251 YFHIENIRFKVPEGQLQKlqKKGYNQKTLILGIRPED 287
Cdd:PRK10070 273 VFSAKDIARRTPNGLIRK--TPGFGPRSALKLLQDED 307
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-324 |
3.65e-48 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 166.02 E-value: 3.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNK---TTAVSDFNLHIQDKEfiVF--VGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD----- 75
Cdd:COG1135 4 LENLSKTFPTKggpVTALDDVSLTIEKGE--IFgiIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 76 RDIAMVFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 156 FLMDEPLSNLDAK-----LRVsmrseISKLHRRLNTTTIYVTHDqteaM----TMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:COG1135 162 LLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGRIVEQGPVLDVFANP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 227 ENVFVGGFIGSPamnfftgtlkdnyfhienIRFKVPEGQLQKLQKKGYNQKTLILGIRpEDIHDEPIVLQSSPDSTVEIN 306
Cdd:COG1135 233 QSELTRRFLPTV------------------LNDELPEELLARLREAAGGGRLVRLTFV-GESADEPLLSELARRFGVDVN 293
|
330
....*....|....*...
gi 446752175 307 IevaellgaetmIHGKLE 324
Cdd:COG1135 294 I-----------LSGGIE 300
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-281 |
6.13e-48 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 163.39 E-value: 6.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 17 TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-----RDIAMVFQnyalYPHM 91
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrKKVGLVFQ----FPEH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 92 -----SVYDNMAFGLKLRKLPKDEINHRVTEAAKILGL-EDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:TIGR04521 94 qlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 166 DAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPEnvfvggfigspamnfftg 245
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD------------------ 235
|
250 260 270
....*....|....*....|....*....|....*...
gi 446752175 246 tlkdnyfHIENIRFKVPEGQ--LQKLQKKGYNQKTLIL 281
Cdd:TIGR04521 236 -------ELEKIGLDVPEITelARKLKEKGLPVPKDPL 266
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-211 |
1.54e-47 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 161.79 E-value: 1.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKDRDIAMVFQ 83
Cdd:PRK11248 2 LQISHLYADYGGKP-ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGPGAERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446752175 164 NLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-213 |
1.98e-47 |
|
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: 160.00 E-value: 1.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPK----DRDIAMV 81
Cdd:cd03262 3 IKNLHKSFGDFH-VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 82 FQNYALYPHMSVYDNMAFGL-KLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03262 82 FQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 161 PLSNLDAKlrvsMRSEISKLHRRL---NTTTIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:cd03262 162 PTSALDPE----LVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-221 |
1.50e-46 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 158.05 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKT-TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGK--LMNDVAPKdRDIAM 80
Cdd:cd03263 1 LQIRNLTKTYKKGTkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsiRTDRKAAR-QSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446752175 161 PLSNLDAKLRVSMRSEISKLhrRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKE 221
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-222 |
4.39e-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: 157.24 E-value: 4.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPkdrDIAMVFQNYALYPHMSVYDNMAFGL 101
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 102 K--LRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISK 179
Cdd:TIGR01184 80 DrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446752175 180 LHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-222 |
7.41e-46 |
|
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: 166.55 E-value: 7.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 3 ELVLDHI-FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIA 79
Cdd:COG2274 473 DIELENVsFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQNYALYpHMSVYDNMAFGlklRKLPKDEinhRVTEAAKILGLEDYLKRKPK-----------ALSGGQRQRVALGRA 148
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLG---DPDATDE---EIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 149 IVRDAKVFLMDEPLSNLDAklrvsmRSE---ISKLHRRL-NTTTIYVTHDqTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:COG2274 626 LLRNPRILILDEATSALDA------ETEaiiLENLRRLLkGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-195 |
1.19e-45 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 155.08 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-----RD-IA 79
Cdd:TIGR03608 1 LKNISKKFGDKV-ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrREkLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 446752175 160 EPLSNLDAKlrvsMRSEISKLHRRLN---TTTIYVTHDQ 195
Cdd:TIGR03608 160 EPTGSLDPK----NRDEVLDLLLELNdegKTIIIVTHDP 194
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-213 |
1.38e-45 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 156.76 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTaVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISngsfyiDGKLMNDVAPKDR---DIAM 80
Cdd:PRK11247 13 LLLNAVSKRYGERTV-LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPS------AGELLAGTAPLAEareDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKLPKDEinhrvtEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446752175 161 PLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-257 |
6.76e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 153.28 E-value: 6.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 17 TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDI----AMVFQ--NYALYPH 90
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 mSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGL--EDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 169 LRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVY---DTPENVfvggFIGSPAMNFFTG 245
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFkevETLESI----GLAVPQVTYLVR 254
|
250
....*....|...
gi 446752175 246 TLKDNYFHI-ENI 257
Cdd:PRK13637 255 KLRKKGFNIpDDI 267
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-228 |
9.85e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.40 E-value: 9.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKDRDIAMVFQNYALYPH-- 90
Cdd:COG1121 16 YGGRP-VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRIGYVPQRAEVDWDfp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDNMAFGL----KLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:COG1121 92 ITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446752175 167 AKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQvGTPKEVYdTPEN 228
Cdd:COG1121 172 AATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVL-TPEN 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-221 |
2.02e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 158.40 E-value: 2.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 3 ELVLDHI-FKlYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIA 79
Cdd:COG1132 339 EIEFENVsFS-YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQNYALYpHMSVYDNMAFGlklRKLPKDEinhRVTEAAKILGLEDYLKRKPK-----------ALSGGQRQRVALGRA 148
Cdd:COG1132 418 VVPQDTFLF-SGTIRENIRYG---RPDATDE---EVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 149 IVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRrlNTTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGTPKE 221
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAH-RLSTIRNADRILVLDDGRIVEQGTHEE 560
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-213 |
2.93e-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: 149.48 E-value: 2.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 9 IFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMND-----VAPKDRDIAMVFQ 83
Cdd:cd03292 6 VTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraIPYLRRKIGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03292 86 DFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446752175 164 NLDAklrvSMRSEISKLHRRLN---TTTIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:cd03292 166 NLDP----DTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-226 |
4.56e-43 |
|
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: 151.74 E-value: 4.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLED---ISNGSFYIDGKLMNDVAPKD------RDIAM 80
Cdd:COG0444 11 FPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElrkirgREIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQN-Y-ALYPHMSVYDNMAFGLKL-RKLPKDEINHRVTEAAKILGL---EDYLKRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:COG0444 91 IFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPK 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 155 VFLMDEPLSNLDaklrVSMRSEI----SKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:COG0444 171 LLIADEPTTALD----VTIQAQIlnllKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENP 242
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-194 |
4.95e-43 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 148.40 E-value: 4.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHiFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGL--EDIS-NGSFYIDGKLMNDVAPKDRDIAM 80
Cdd:COG4136 2 LSLEN-LTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSaSGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKlRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190
....*....|....*....|....*....|....
gi 446752175 161 PLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHD 194
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-213 |
8.81e-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: 146.77 E-value: 8.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR-DIAMVF 82
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 83 QNYALYPHMSVYDNMafglklrklpkdeinhrvteaakilgledylkrkpkALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446752175 163 SNLDAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:cd03230 124 SGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
1.16e-42 |
|
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: 156.07 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 2 AELVLDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIA 79
Cdd:COG4988 335 PSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQNYALyPHMSVYDNMAFGlklRKLPKDEinhRVTEAAKILGLEDYLKRKPK-----------ALSGGQRQRVALGRA 148
Cdd:COG4988 415 WVPQNPYL-FAGTIRENLRLG---RPDASDE---ELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 149 IVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRrlNTTTIYVTHDqTEAMTMASRLVVMKDGIIQQVGTPKE 221
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-223 |
3.30e-41 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 145.93 E-value: 3.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLD--HIFKLY-DNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-- 75
Cdd:PRK13635 1 MKEEIIRveHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 76 RDIAMVFQNyalyPH-----MSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIV 150
Cdd:PRK13635 81 RQVGMVFQN----PDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 151 RDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTmASRLVVMKDGIIQQVGTPKEVY 223
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-256 |
6.30e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 145.26 E-value: 6.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTT-AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLM--NDVAPKDRDIAMVFQNya 86
Cdd:PRK13650 12 FKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteENVWDIRHKIGMVFQN-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 87 lyPH-----MSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:PRK13650 90 --PDnqfvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 162 LSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEaMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGfIGSPAMN 241
Cdd:PRK13650 168 TSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRGNDLLQLG-LDIPFTT 245
|
250
....*....|....*
gi 446752175 242 FFTGTLKDNYFHIEN 256
Cdd:PRK13650 246 SLVQSLRQNGYDLPE 260
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-224 |
6.85e-41 |
|
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: 143.98 E-value: 6.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-----RDI 78
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 79 AMVFQNYALYPHMSVYDNM---AFGLK------LRKLPKDEInHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAI 149
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgRLGYKptwrslLGRFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 150 VRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYD 224
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-163 |
1.16e-40 |
|
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: 140.48 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 20 VSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYPHMSVYDNM 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 98 AFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRK----PKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
2.07e-40 |
|
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: 140.21 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTAV-SDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAM 80
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYpHMSVYDNMafglklrklpkdeinhrvteaakilgledylkrkpkaLSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446752175 161 PLSNLDAKLRVSMRSEISKLHRrlNTTTIYVTHDqTEAMTMASRLVVMKDG 211
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-217 |
3.25e-40 |
|
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: 140.26 E-value: 3.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 15 NKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQnyalyphms 92
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKElaRKIAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 93 vydnmafglklrklpkdeinhrvteAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVS 172
Cdd:cd03214 81 -------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446752175 173 MRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVG 217
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
10-222 |
6.05e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 139.74 E-value: 6.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNyal 87
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGIIFQN--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 88 yPH-----MSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:PRK13632 92 -PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDEST 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 163 SNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAmTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:PRK13632 171 SMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-198 |
1.97e-38 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 136.45 E-value: 1.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGK-LMNDVAPKDRDIAMVF 82
Cdd:COG4133 3 LEAENLSCRRGERL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 83 QNYALYPHMSVYDNMAFGLKLRKLPKDEInhRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 446752175 163 SNLDAKlrvsMRSEISKL---HRRLNTTTIYVTHDQTEA 198
Cdd:COG4133 160 TALDAA----GVALLAELiaaHLARGGAVLLTTHQPLEL 194
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-215 |
2.31e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 137.45 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYdNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGK---LMNDVAPKD-----RD 77
Cdd:COG4161 5 LKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdFSQKPSEKAirllrQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 78 IAMVFQNYALYPHMSVYDNM-AFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:COG4161 84 VGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 157 LMDEPLSNLDAKLrvsmRSEISKLHRRLNTTTI---YVTHDQTEAMTMASRLVVMKDG-IIQQ 215
Cdd:COG4161 164 LFDEPTAALDPEI----TAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVVYMEKGrIIEQ 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-217 |
6.14e-38 |
|
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: 135.57 E-value: 6.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTT---AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDG-KLMNDVAPKDRDIA 79
Cdd:cd03266 2 ITADALTKRFRDVKKtvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 160 EPLSNLDAKLRVSMRSEISKLhRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVG 217
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-237 |
6.39e-38 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 138.78 E-value: 6.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 9 IFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-----RDIAMVFQ 83
Cdd:PRK11153 10 VFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK11153 90 HFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446752175 164 NLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGS 237
Cdd:PRK11153 170 ALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQS 243
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-211 |
7.19e-38 |
|
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: 133.14 E-value: 7.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 15 NKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQnyalyphms 92
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 93 vydnmafglklrklpkdeinhrvteaakilgledylkrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVS 172
Cdd:cd00267 81 ------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180 190
....*....|....*....|....*....|....*....
gi 446752175 173 MRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:cd00267 119 LLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-213 |
1.12e-37 |
|
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: 134.58 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKDRDIAMVFQNYAL---YP 89
Cdd:cd03235 9 YGGHP-VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRRSIdrdFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 90 hMSVYDNMAFGL-----KLRKLPKDEInHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSN 164
Cdd:cd03235 85 -ISVRDVVLMGLyghkgLFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446752175 165 LDAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:cd03235 163 VDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-218 |
1.40e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 135.14 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGK---LMNDVAPKD-----RD 77
Cdd:PRK11124 5 LNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdFSKTPSDKAirelrRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 78 IAMVFQNYALYPHMSVYDNMAFG-LKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK11124 84 VGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446752175 157 LMDEPLSNLDAKLRVSMRSEISKLhRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGT 218
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-226 |
2.88e-37 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 136.79 E-value: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-----RDIAMVFQN-YA-LYPHM 91
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYAsLNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 92 SVYDNMAFGLKL-RKLPKDEINHRVTEAAKILGL-EDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDakl 169
Cdd:COG4608 113 TVGDIIAEPLRIhGLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD--- 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446752175 170 rVSMRSEI----SKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:COG4608 190 -VSIQAQVlnllEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-217 |
1.51e-36 |
|
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: 131.55 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTtAVSDFNLHIQDKeFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDG-KLMNDVAPKDRDIAMVF 82
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 83 QNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 163 SNLDAKLRVSMRSEISKLHRrlNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVG 217
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
18-222 |
5.18e-36 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 131.31 E-value: 5.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 18 TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR---DIAMVFQNYALYPHMSVY 94
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlGIARTFQNPRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 95 DNMAFGLKLR----------KLPK-----DEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:COG0411 98 ENVLVAAHARlgrgllaallRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 160 EPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:COG0411 178 EPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-222 |
7.86e-36 |
|
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: 130.25 E-value: 7.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 18 TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR---DIAMVFQNYALYPHMSVY 94
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 95 DNMAFGLKLRKLP----------KDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSN 164
Cdd:cd03219 94 ENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 165 LDAKLRVSMRSEISKLhRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:cd03219 174 LNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-227 |
9.39e-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: 136.82 E-value: 9.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 2 AELVLDHI-FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDI 78
Cdd:COG4987 332 PSLELEDVsFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 79 AMVFQNYALYpHMSVYDNMAFGlklRKLPKDEinhRVTEAAKILGLEDYLKRKPK-----------ALSGGQRQRVALGR 147
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLRLA---RPDATDE---ELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 148 AIVRDAKVFLMDEPLSNLDAKLRVSMRSEISK-LHRRlntTTIYVTHDQTeAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEaLAGR---TVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
.
gi 446752175 227 E 227
Cdd:COG4987 561 G 561
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
1.80e-35 |
|
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: 129.03 E-value: 1.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDG-KLMNDVAPKDRDIAMVF 82
Cdd:cd03265 1 IEVENLVKKYGD-FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhDVVREPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 83 QNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 163 SNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKE 221
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
14-211 |
2.59e-35 |
|
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: 128.62 E-value: 2.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 14 DNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR------DIAMVFQNYAL 87
Cdd:TIGR02211 15 KLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkKLGFIYQFHHL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 88 YPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:TIGR02211 95 LPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446752175 168 KLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMaSRLVVMKDG 211
Cdd:TIGR02211 175 NNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDG 217
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
7-237 |
8.88e-35 |
|
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: 128.02 E-value: 8.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 7 DHIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLM-------NDVAPKD---- 75
Cdd:TIGR03005 4 SDVTKRFGI-LTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLyhmpgrnGPLVPADekhl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 76 ----RDIAMVFQNYALYPHMSVYDNMAFGLKLRK-LPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIV 150
Cdd:TIGR03005 83 rqmrNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLgMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 151 RDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVF 230
Cdd:TIGR03005 163 MRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEER 242
|
....*..
gi 446752175 231 VGGFIGS 237
Cdd:TIGR03005 243 TREFLSK 249
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
10-222 |
1.42e-34 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 134.61 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYAL 87
Cdd:TIGR03375 471 FAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 88 YpHMSVYDNMAFGlklRKLPKDEinhRVTEAAKILGLEDYLKRKPK-----------ALSGGQRQRVALGRAIVRDAKVF 156
Cdd:TIGR03375 551 F-YGTLRDNIALG---APYADDE---EILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPIL 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446752175 157 LMDEPLSNLDaklrvsMRSEiSKLHRRLN-----TTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:TIGR03375 624 LLDEPTSAMD------NRSE-ERFKDRLKrwlagKTLVLVTH-RTSLLDLVDRIIVMDNGRIVADGPKDQV 686
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-228 |
1.89e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 127.27 E-value: 1.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDIS-----NGSFYIDGK--LMNDVAPKD--RDIAM 80
Cdd:PRK14267 10 LRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRniYSPDVDPIEvrREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKL--PKDEINHRVTEAAKILGL----EDYLKRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK14267 90 VFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 155 VFLMDEPLSNLDAklrVSMRsEISKLHRRLNT--TTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPEN 228
Cdd:PRK14267 170 ILLMDEPTANIDP---VGTA-KIEELLFELKKeyTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-213 |
2.69e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 127.12 E-value: 2.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYD----NKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVA--PKD-- 75
Cdd:COG1101 2 LELKNLSKTFNpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK---DVTklPEYkr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 76 -RDIAMVFQNYAL--YPHMSVYDNMA--------FGLKLRkLPKDEINHRVTEAAKI-LGLEDYLKRKPKALSGGQRQRV 143
Cdd:COG1101 79 aKYIGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRG-LTKKRRELFRELLATLgLGLENRLDTKVGLLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 144 ALGRAIVRDAKVFLMDEPLSNLDAKlrvsmRSEI-----SKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPK-----TAALvleltEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-213 |
3.11e-34 |
|
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: 125.78 E-value: 3.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDN-KTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYp 89
Cdd:cd03245 12 YPNqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQDVTLF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 90 HMSVYDNMAFGlklRKLPKDEinhRVTEAAKILGLEDYLKRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:cd03245 91 YGTLRDNITLG---APLADDE---RILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 159 DEPLSNLDaklrvsMRSE---ISKLHRRL-NTTTIYVTHdQTEAMTMASRLVVMKDGII 213
Cdd:cd03245 165 DEPTSAMD------MNSEerlKERLRQLLgDKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-215 |
5.80e-34 |
|
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: 125.24 E-value: 5.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTAVS---DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKDRD--- 77
Cdd:COG4181 9 IELRGLTKTVGTGAGELTilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDEDara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 78 ------IAMVFQNYALYPHMSVYDNMAFGLKLRKLPKDEinhrvTEAAKIL---GLEDYLKRKPKALSGGQRQRVALGRA 148
Cdd:COG4181 86 rlrarhVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR-----ARARALLervGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 149 IVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAmTMASRLVVMKDGIIQQ 215
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-222 |
1.06e-33 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 124.65 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYPH 90
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 mSVYDNMAFGlklRKLPKDEinhRVTEAAKILGLEDYLKRKPKA-----------LSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:cd03254 92 -TIMENIRLG---RPNATDE---EVIEAAKEAGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 160 EPLSNLDAKLRVSMRSEISKLhrRLNTTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKL--MKGRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-221 |
2.40e-33 |
|
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: 123.80 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYPhMSVYDNMAF 99
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 100 GLKLRKLPKDEinhrvtEAAKILGLEDYLKRKPKA-----------LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:cd03249 100 GKPDATDEEVE------EAAKKANIHDFIMSLPDGydtlvgergsqLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 169 lrvsmrSEI---SKLHR-RLNTTTIYVTHDQTeAMTMASRLVVMKDGIIQQVGTPKE 221
Cdd:cd03249 174 ------SEKlvqEALDRaMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-166 |
2.76e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.38 E-value: 2.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTL----RMIaglEDISN----GSFYIDGKlmnDVAPKDRD---- 77
Cdd:COG1117 17 LNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMN---DLIPGarveGEILLDGE---DIYDPDVDvvel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 78 ---IAMVFQNYALYPhMSVYDNMAFGLKLR-KLPKDEINHRVTEAAKILGL----EDYLKRKPKALSGGQRQRVALGRAI 149
Cdd:COG1117 91 rrrVGMVFQKPNPFP-KSIYDNVAYGLRLHgIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARAL 169
|
170
....*....|....*..
gi 446752175 150 VRDAKVFLMDEPLSNLD 166
Cdd:COG1117 170 AVEPEVLLMDEPTSALD 186
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-229 |
5.42e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 123.27 E-value: 5.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTTaVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQ 83
Cdd:COG4604 4 IKNVSKRYGGKVV-LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHMSVYDNMAFGL----KLRKLPKDEinHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:COG4604 83 ENHINSRLTVRELVAFGRfpysKGRLTAEDR--EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 160 EPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTP---------KEVYDTPENV 229
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPeeiitpevlSDIYDTDIEV 239
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-223 |
1.05e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 123.27 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 14 DNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDG---KLMNDVAPKDRDIAMVFQNyalyPH 90
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKAGMVFQN----PD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MS-----VYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:PRK13633 96 NQivatiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 166 DAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTmASRLVVMKDGIIQQVGTPKEVY 223
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-213 |
2.17e-32 |
|
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: 120.40 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 11 KLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVFQNYALYPH 90
Cdd:cd03268 8 KTYGKKR-VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDNMAFGLKLRKLPKDEINhrvtEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:cd03268 87 LTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446752175 171 VSMRSEISKLhRRLNTTTIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:cd03268 163 KELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-215 |
3.51e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 120.69 E-value: 3.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 17 TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAP------KDRDIAMVFQNYALYPH 90
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelRNQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446752175 171 VSMRSEISKLHRRLNTTTIYVTHDQTEAMTMaSRLVVMKDGIIQQ 215
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-213 |
4.99e-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: 119.28 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKDR--DIAMVFQ 83
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERrkSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 N--YALYPHmSVYDNMAFGLKlrklPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:cd03226 79 DvdYQLFTD-SVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 162 LSNLDAKlrvSMRSeISKLHRRLN---TTTIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:cd03226 154 TSGLDYK---NMER-VGELIRELAaqgKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
17-211 |
6.09e-32 |
|
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: 119.31 E-value: 6.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 17 TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMnDVAPKDRdIAMVFQNYALYPHMSVYDN 96
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARNR-IGYLPEERGLYPKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 97 MAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSE 176
Cdd:cd03269 91 LVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDV 170
|
170 180 190
....*....|....*....|....*....|....*
gi 446752175 177 ISKLhRRLNTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:cd03269 171 IREL-ARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
16-222 |
2.36e-31 |
|
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: 118.31 E-value: 2.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 16 KTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR---DIAMVFQNYALYPHMS 92
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 93 VYDNMAFGLKLRKlpKDEINHRVteaAKILG----LEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:cd03224 92 VEENLLLGAYARR--RAKRKARL---ERVYElfprLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 169 lrvsMRSEISKLHRRLN---TTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:cd03224 167 ----IVEEIFEAIRELRdegVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-226 |
2.60e-31 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 121.13 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 37 GPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMND------VAPKDRDIAMVFQNYALYPHMSVYDNMAFGLKlrKLPKDE 110
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA--KSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 111 INHRVteaaKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIY 190
Cdd:PRK11144 109 FDKIV----ALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 446752175 191 VTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:PRK11144 185 VSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-224 |
4.39e-31 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 117.72 E-value: 4.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTAV-SDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAM 80
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYpHMSVYDNMAFGLKlrklpkDEINHRVTEAAKILGLEDYLKRKPKA-----------LSGGQRQRVALGRAI 149
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGRP------GATREEVEEAARAANAHEFIMELPEGydtvigergvkLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 150 VRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRrlNTTTIYVTHDQTeAMTMASRLVVMKDGIIQQVGTPKEVYD 224
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-229 |
4.58e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.03 E-value: 4.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMN----DVAPKDRDIAMVFQN---- 84
Cdd:PRK13639 11 YPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkkSLLEVRKTVGIVFQNpddq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 85 -YAlyPhmSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK13639 91 lFA--P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 164 NLDAKlrvsMRSEISKLHRRLN---TTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENV 229
Cdd:PRK13639 167 GLDPM----GASQIMKLLYDLNkegITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
3-227 |
5.05e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 118.97 E-value: 5.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 3 ELVLDHIFKLYDNKT----TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYI------DGKLMNDVA 72
Cdd:PRK13634 2 DITFQKVEHRYQYKTpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 73 PKDRDIAMVFQnyalYP-HM----SVYDNMAFGLKLRKLPKDEINHRVTEAAKILGL-EDYLKRKPKALSGGQRQRVALG 146
Cdd:PRK13634 82 PLRKKVGIVFQ----FPeHQlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 147 RAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
.
gi 446752175 227 E 227
Cdd:PRK13634 238 D 238
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-224 |
5.58e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.70 E-value: 5.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHI-FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAM 80
Cdd:PRK13648 8 IVFKNVsFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQN--YALYPHMSVYDnMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PRK13648 88 VFQNpdNQFVGSIVKYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 159 DEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTmASRLVVMKDGIIQQVGTPKEVYD 224
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-227 |
1.14e-30 |
|
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: 122.10 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDiSNGSFYIDGKLMNDVAPKD-----RDIAMVFQN-YA-LYPHM 91
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 92 SVYDNMAFGLKL--RKLPKDEINHRVTEAAKILGL-EDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDak 168
Cdd:COG4172 380 TVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-- 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446752175 169 lrVSMRSEI----SKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDG-IIQQvGTPKEVYDTPE 227
Cdd:COG4172 458 --VSVQAQIldllRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGkVVEQ-GPTEQVFDAPQ 518
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-221 |
1.34e-30 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 123.14 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 3 ELVLDHI-FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMN--DVAPKDRDIA 79
Cdd:TIGR03797 451 AIEVDRVtFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAglDVQAVRRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQNYALYPHmSVYDNMAFGlklRKLPKDEinhrVTEAAKILGLEDYLKRKP-----------KALSGGQRQRVALGRA 148
Cdd:TIGR03797 531 VVLQNGRLMSG-SIFENIAGG---APLTLDE----AWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARA 602
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 149 IVRDAKVFLMDEPLSNLDAKlrvsMRSEISKLHRRLNTTTIYVTHDQTEAMTmASRLVVMKDGIIQQVGTPKE 221
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDNR----TQAIVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
7-227 |
1.49e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.59 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 7 DHI-FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGL---EDISNGSFYIDG-----KLMNDVAPKdrd 77
Cdd:PRK13640 9 KHVsFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGitltaKTVWDIREK--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 78 IAMVFQNY-ALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446752175 157 LMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAmTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
25-226 |
1.92e-30 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 116.82 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 25 LHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLM-------NDVAPKDRD--------IAMVFQNYALYP 89
Cdd:COG4598 29 LTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdGELVPADRRqlqrirtrLGMVFQSFNLWS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 90 HMSVYDNMAFG-LKLRKLPKDEInhrVTEAAKIL---GLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:COG4598 109 HMTVLENVIEApVHVLGRPKAEA---IERAEALLakvGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSAL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 166 DAK-----LRVsMRSeISKLHRrlntTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:COG4598 186 DPElvgevLKV-MRD-LAEEGR----TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNP 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-218 |
2.21e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.89 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKD-RD----- 77
Cdd:COG1129 5 LEMRGISKSFGG-VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE---PVRFRSpRDaqaag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 78 IAMVFQNYALYPHMSVYDNMAFGLKLRKLP---KDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 155 VFLMDEPLSNLDAKlrvsmrsEISKLH---RRL---NTTTIYVTHDQTEAMTMASRLVVMKDGiiQQVGT 218
Cdd:COG1129 161 VLILDEPTASLTER-------EVERLFriiRRLkaqGVAIIYISHRLDEVFEIADRVTVLRDG--RLVGT 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-226 |
2.52e-30 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 118.27 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR-----DIAMVFQN--YALYPHM 91
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 92 SVYDNMAFGLKLR--KLPKDEINHRVTEAAKILGL-EDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:PRK15079 116 TIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 169 LRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
16-227 |
3.82e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 115.88 E-value: 3.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 16 KTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYPHMSV 93
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 94 YDNMAFG----LKL--RKLPKDEinHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDa 167
Cdd:PRK11231 94 RELVAYGrspwLSLwgRLSAEDN--ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 168 klrVSMRSEISKLHRRLNT---TTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYdTPE 227
Cdd:PRK11231 171 ---INHQVELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM-TPG 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-222 |
4.01e-30 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 120.68 E-value: 4.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYI----DGKLMNDVAPKDRD-----IAMVFQNYALYP 89
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRGrakryIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 90 HMSVYDNM--AFGLKLrklPKDEINHRVTEAAKILGLED-----YLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:TIGR03269 379 HRTVLDNLteAIGLEL---PDELARMKAVITLKMVGFDEekaeeILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 163 SNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:TIGR03269 456 GTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-228 |
5.53e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 115.40 E-value: 5.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 24 NLHIQDKEFIVFVGPSGCGKSTTLRMIAGL-----EDISNGSFYIDGK--LMNDVAPKDRDIAMVFQNYALYPHMSVYDN 96
Cdd:PRK14247 23 NLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQdiFKMDVIELRRRVQMVFQIPNPIPNLSIFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 97 MAFGLKLRKLPKD--EINHRVTEAAKILGLEDYLKRKPKA----LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:PRK14247 103 VALGLKLNRLVKSkkELQERVRWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 171 VSMRSEISKLHRRLntTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPEN 228
Cdd:PRK14247 183 AKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-215 |
7.10e-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: 115.29 E-value: 7.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 18 TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-----RDIAMVFQNY--ALYPH 90
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQDSpsAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDNMAFGLK-LRKLPKDEINHRVTEAAKILGLE-DYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:TIGR02769 105 MTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446752175 169 LRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDG-IIQQ 215
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGqIVEE 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-221 |
7.33e-30 |
|
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: 114.63 E-value: 7.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMV 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 82 FQNYALYpHMSVYDNMAFGlklRKLPKDEinhRVTEAAKILGLEDYLKRKPKA-----------LSGGQRQRVALGRAIV 150
Cdd:cd03253 81 PQDTVLF-NDTIGYNIRYG---RPDATDE---EVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 151 RDAKVFLMDEPLSNLDaklrVSMRSEISKLHRRL--NTTTIYVTHDQTEAMTmASRLVVMKDGIIQQVGTPKE 221
Cdd:cd03253 154 KNPPILLLDEATSALD----THTEREIQAALRDVskGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-211 |
9.84e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 113.82 E-value: 9.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDG----KLMNDVAP-KDRDIAM 80
Cdd:PRK10908 4 FEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditRLKNREVPfLRRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK10908 84 IFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446752175 161 PLSNLDAKLRVSMRSEISKLHrRLNTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-208 |
1.05e-29 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 119.31 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYPH 90
Cdd:TIGR02857 331 YPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWVPQHPFLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 mSVYDNMAFGLKlrklpkDEINHRVTEAAKILGLEDYLKRKPKA-----------LSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:TIGR02857 411 -TIAENIRLARP------DASDAEIREALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAFLRDAPLLLLD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446752175 160 EPLSNLDAKLRVSMRSEISKLHRrlNTTTIYVTHDqTEAMTMASRLVVM 208
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-213 |
1.31e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 114.78 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 18 TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-----RDIAMVFQNY--ALYPH 90
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSisAVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDNMAFGLK-LRKLPKDEINHRVTEAAKILGLED-YLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:PRK10419 106 KTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446752175 169 LRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:PRK10419 186 LQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
24-227 |
1.68e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 114.08 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 24 NLHIQDKEFIVFVGPSGCGKSTTLRMIAGLED-----ISNGSFYID-----GKLMNDVAPKDRDIAMVFQNYALYPHMSV 93
Cdd:PRK11264 23 DLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtIRVGDITIDtarslSQQKGLIRQLRQHVGFVFQNFNLFPHRTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 94 YDNMAFG-LKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVS 172
Cdd:PRK11264 103 LENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 173 MRSEISKLHRRLNTTTIyVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:PRK11264 183 VLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
19-228 |
2.12e-29 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 113.23 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLED----ISNGSFYIDGKLMNDVAPKDRDIAMVFQN--YALYPHMS 92
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPpgltQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 93 VYDNMAFGLKLRKLPKDEINHRVTEAAKILGLED---YLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL 169
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 170 RVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPEN 228
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-227 |
3.28e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 113.54 E-value: 3.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTTAvSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYPH 90
Cdd:PRK10253 17 YGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDNMAFG------LKLRKLPKDEinHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSN 164
Cdd:PRK10253 96 ITVQELVARGryphqpLFTRWRKEDE--EAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 165 LDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYdTPE 227
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV-TAE 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-225 |
3.96e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.05 E-value: 3.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNdvaPKDRD-IAmvf 82
Cdd:COG4152 2 LELKGLTKRFGDKT-AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRrIG--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 83 qnY-----ALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG4152 75 --YlpeerGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446752175 158 MDEPLSNLD---AKLrvsMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDT 225
Cdd:COG4152 153 LDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-232 |
4.11e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.54 E-value: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVA--PKDRDI-AMVF 82
Cdd:PRK13644 4 LENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSklQGIRKLvGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 83 QN-YALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:PRK13644 84 QNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446752175 162 LSNLDAKLRVSMRSEISKLHRRlNTTTIYVTHDqTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVG 232
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-229 |
6.93e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 113.26 E-value: 6.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 24 NLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMN--DVAPKDRDIAMVFQNY-ALYPHMSVYDNMAFG 100
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaeNVWNLRRKIGMVFQNPdNQFVGATVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 101 LKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKL 180
Cdd:PRK13642 107 MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446752175 181 HRRLNTTTIYVTHDQTEAMTmASRLVVMKDGIIQQVGTPKEVYDTPENV 229
Cdd:PRK13642 187 KEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDM 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-228 |
1.02e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 112.06 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 12 LYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMN--------DVAPKDRDIAMVFQ 83
Cdd:PRK14246 18 LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqiDAIKLRKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHMSVYDNMAFGLKLRKLP-KDEINHRVTEAAKILGL----EDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PRK14246 98 QPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 159 DEPLSNLDAKLRVSMRSEISKLHRRLntTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPEN 228
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-204 |
2.91e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 111.03 E-value: 2.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 12 LYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGsFYIDGKLM--------NDVAPKD--RDIAMV 81
Cdd:PRK14243 18 VYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTfhgknlyaPDVDPVEvrRRIGMV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 82 FQNYALYPHmSVYDNMAFGLKLR--KLPKDEINHR-VTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PRK14243 97 FQKPNPFPK-SIYDNIAYGARINgyKGDMDELVERsLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446752175 159 DEPLSNLDAKLRVSMRSEISKLHRRLntTTIYVTHDqteaMTMASR 204
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQY--TIIIVTHN----MQQAAR 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
13-219 |
5.21e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.60 E-value: 5.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNyalyPH 90
Cdd:PRK13647 14 YKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGLVFQD----PD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 -----MSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:PRK13647 90 dqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446752175 166 DAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTP 219
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-199 |
7.81e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 107.70 E-value: 7.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 18 TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFyidgklmnDVAPKDRdIAMVFQNYAL---YPhMSVY 94
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV--------RRAGGAR-VAYVPQRSEVpdsLP-LTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 95 DNMAFGL-----KLRKLPKDEiNHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL 169
Cdd:NF040873 76 DLVAMGRwarrgLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|
gi 446752175 170 RVSMRSEISKLHRRlNTTTIYVTHDQTEAM 199
Cdd:NF040873 155 RERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-227 |
9.26e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 110.48 E-value: 9.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 3 ELVLDHIFKLYDNKT----TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDG-------KLMNDV 71
Cdd:PRK13645 6 DIILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 72 APKDRDIAMVFQ--NYALYPHmSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGL-EDYLKRKPKALSGGQRQRVALGRA 148
Cdd:PRK13645 86 KRLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 149 IVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-228 |
1.02e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 109.09 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 12 LYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDIS-----NGSFYIDGKlmNDVAPKD------RDIAM 80
Cdd:PRK14239 13 VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGH--NIYSPRTdtvdlrKEIGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPhMSVYDNMAFGLKLR----KLPKDEINHRVTEAAKILG-LEDYLKRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:PRK14239 91 VFQQPNPFP-MSIYENVVYGLRLKgikdKQVLDEAVEKSLKGASIWDeVKDRLHDSALGLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446752175 156 FLMDEPLSNLDAklrVSMRS-EISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPEN 228
Cdd:PRK14239 170 ILLDEPTSALDP---ISAGKiEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
31-248 |
1.19e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 109.29 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 31 EFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDI---------------AMVFQNYALYPHMSVYD 95
Cdd:PRK10619 32 DVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkvadknqlrllrtrlTMVFQHFNLWSHMTVLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 96 N-MAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRK-PKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLrvsm 173
Cdd:PRK10619 112 NvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPEL---- 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 174 RSEISKLHRRL---NTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPEnvfvggfigSPAM-NFFTGTLK 248
Cdd:PRK10619 188 VGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ---------SPRLqQFLKGSLK 257
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-222 |
6.48e-27 |
|
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: 111.67 E-value: 6.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 16 KTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYPHmSV 93
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIGYLPQDVELFPG-TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 94 YDNMAfglKLRKLPKDEinhRVTEAAKILGLEDYLKRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:TIGR01842 409 AENIA---RFGENADPE---KIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 163 SNLDAKLRVSMRSEISKLHRRlNTTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-226 |
1.01e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 108.13 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVsdfnlhiqdkefivfVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKD--------RDIAMV 81
Cdd:PRK11308 36 FTLERGKTLAV---------------VGESGCGKSTLARLLTMIETPTGGELYYQGQ---DLLKADpeaqkllrQKIQIV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 82 FQN-YA-LYPHMSVYDNMAFGLKLR-KLPKDEINHRVTEAAKILGL--EDYlKRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK11308 98 FQNpYGsLNPRKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLrpEHY-DRYPHMFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446752175 157 LMDEPLSNLDaklrVSMRSEI----SKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:PRK11308 177 VADEPVSALD----VSVQAQVlnlmMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-211 |
1.51e-26 |
|
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: 103.84 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-RD-IAMVFQNYAL 87
Cdd:cd03246 8 FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElGDhVGYLPQDDEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 88 YPHmSVYDNMafglklrklpkdeinhrvteaakilgledylkrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:cd03246 88 FSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446752175 168 KLRVSMRSEISKLhRRLNTTTIYVTHdQTEAMTMASRLVVMKDG 211
Cdd:cd03246 130 EGERALNQAIAAL-KAAGATRIVIAH-RPETLASADRILVLEDG 171
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-222 |
2.49e-26 |
|
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: 109.84 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 16 KTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGklmNDVAPKDRDiamvfqnyALYPHM---- 91
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG---ADLSQWDRE--------ELGRHIgylp 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 92 --------SVYDNMA-FGLklrklPKDEinhRVTEAAKILGLEDYLKRKPK-----------ALSGGQRQRVALGRAIVR 151
Cdd:COG4618 413 qdvelfdgTIAENIArFGD-----ADPE---KVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446752175 152 DAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRlNTTTIYVTHDQTeAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-215 |
2.53e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 104.86 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 25 LHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGK---LMND---VAPKDRDIAMVFQNYALYPHMSVYDNMA 98
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhQMDEearAKLRAKHVGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 99 FGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEIS 178
Cdd:PRK10584 111 LPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 446752175 179 KLHRRLNTTTIYVTHDQTEAMTMASRLvVMKDGIIQQ 215
Cdd:PRK10584 191 SLNREHGTTLILVTHDLQLAARCDRRL-RLVNGQLQE 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
15-229 |
2.54e-26 |
|
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: 105.55 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 15 NKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGleDI---SNGSFYIDGKLMNDVAPKD--RDIAMV---FQNYa 86
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG--DLpptYGNDVRLFGERRGGEDVWElrKRIGLVspaLQLR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 87 LYPHMSVYDnM----AFG-LKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:COG1119 91 FPRDETVLD-VvlsgFFDsIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 162 LSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYdTPENV 229
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL-TSENL 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-227 |
2.85e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.09 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMnDVAPKD-----RDI 78
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGlmklrESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 79 AMVFQ--NYALYPhMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEdYLKRKPK-ALSGGQRQRVALGRAIVRDAKV 155
Cdd:PRK13636 85 GMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIE-HLKDKPThCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446752175 156 FLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-226 |
4.77e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 105.12 E-value: 4.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISnGSFYIDGKL----------MNDVAPKDRDIA 79
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVeffnqniyerRVNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQNYALYPhMSVYDNMAFGLKLRKL-PKDEINHRVTEAAKILGLEDYLKRKPKA----LSGGQRQRVALGRAIVRDAK 154
Cdd:PRK14258 92 MVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 155 VFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDG---IIQQV--GTPKEVYDTP 226
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNenrIGQLVefGLTKKIFNSP 247
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-227 |
9.39e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.50 E-value: 9.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQN---YAL 87
Cdd:PRK13652 13 YSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLVFQNpddQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 88 YPhmSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:PRK13652 93 SP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 168 KLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-218 |
3.73e-25 |
|
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: 99.81 E-value: 3.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD---RDIAM 80
Cdd:cd03216 1 LELRGITKRFGG-VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQnyalyphmsvydnmafglklrklpkdeinhrvteaakilgledylkrkpkaLSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 161 PLSNLDAKLRVSMRSEISKLhRRLNTTTIYVTHDQTEAMTMASRLVVMKDGiiQQVGT 218
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDG--RVVGT 163
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
16-227 |
4.47e-25 |
|
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: 101.60 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 16 KTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR---DIAMVFQNYALYPHMS 92
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 93 VYDNMAFGLKLRKlPKDEINHRVteaAKILG----LEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP---LSNL 165
Cdd:COG0410 95 VEENLLLGAYARR-DRAEVRADL---ERVYElfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPslgLAPL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 166 daklrvsMRSEISKLHRRLN---TTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:COG0410 171 -------IVEEIFEIIRRLNregVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-197 |
4.79e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.33 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHI-FKLydNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAM 80
Cdd:PRK10247 8 LQLQNVgYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHmSVYDNMAFGLKLRKLPKDEiNHRVTEAAKiLGLEDYLKRKP-KALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPWQIRNQQPDP-AIFLDDLER-FALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 446752175 160 EPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTE 197
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-224 |
5.52e-25 |
|
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: 105.95 E-value: 5.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYPHmSVYDN 96
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVALVSQDVVLFND-TIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 97 MAFGlKLRKLPKDEInHRVTEAAKilgLEDYLKRKPKA-----------LSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:TIGR02203 426 IAYG-RTEQADRAEI-ERALAAAY---AQDFVDKLPLGldtpigengvlLSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 166 DAKLRVSMRSEISKLHRrlNTTTIYVTHDQTeAMTMASRLVVMKDGIIQQVGTPKEVYD 224
Cdd:TIGR02203 501 DNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-224 |
1.92e-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: 99.87 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHI-FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPK--DRDIAM 80
Cdd:cd03252 1 ITFEHVrFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYpHMSVYDNMAFGLKLRKLpkdeinHRVTEAAKILGLEDYLKRKPK-----------ALSGGQRQRVALGRAI 149
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALADPGMSM------ERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 150 VRDAKVFLMDEPLSNLDAKlrvSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYD 224
Cdd:cd03252 154 IHNPRILIFDEATSALDYE---SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
20-222 |
1.97e-24 |
|
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: 104.82 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 20 VSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKD-----RDIAMVFQNYALYPHmSVY 94
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGV---DLAIADpawlrRQMGVVLQENVLFSR-SIR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 95 DNMAFGlklRKLPKDEinhRVTEAAKILGLEDYLKRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:TIGR01846 549 DNIALC---NPGAPFE---HVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDEATS 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 164 NLDAKLRVSMRSEISKLHRrlNTTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:TIGR01846 623 ALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEEL 678
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-227 |
3.00e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 99.33 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLDHIFKLYdNKTTAVSDFNLHIQDKEfIV-FVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmndvapkdrDI- 78
Cdd:COG1137 1 MMTLEAENLVKSY-GKRTVVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE----------DIt 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 79 ------------------AMVFQNyalyphMSVYDN-MAFgLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQ 139
Cdd:COG1137 69 hlpmhkrarlgigylpqeASIFRK------LTVEDNiLAV-LELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 140 RQRVALGRAIVRDAKVFLMDEPLSNLDAkLRVsmrSEISKLHRRLNTTTIYV--T-HDQTEAMTMASRLVVMKDGIIQQV 216
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDP-IAV---ADIQKIIRHLKERGIGVliTdHNVRETLGICDRAYIISEGKVLAE 217
|
250
....*....|.
gi 446752175 217 GTPKEVYDTPE 227
Cdd:COG1137 218 GTPEEILNNPL 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-194 |
3.07e-24 |
|
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: 103.59 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMV 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 82 FQNyalyPHM---SVYDNMAFGlklRKLPKDEinhRVTEAAKILGLEDYLKRKP-----------KALSGGQRQRVALGR 147
Cdd:TIGR02868 415 AQD----AHLfdtTVRENLRLA---RPDATDE---ELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446752175 148 AIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLntTTIYVTHD 194
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-227 |
5.64e-24 |
|
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: 102.84 E-value: 5.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTT----LRMIAGLEDISNGSFYIDGKLMNDVAPKD------RDIA 79
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQN--YALYPHMSVYDNMAFGLKL-RKLPKDEINHRVTEAAKILGL---EDYLKRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:COG4172 96 MIFQEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 154 KVFLMDEPLSNLDaklrVSMRSEI----SKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:COG4172 176 DLLIADEPTTALD----VTVQAQIldllKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-211 |
7.78e-24 |
|
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: 97.24 E-value: 7.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 16 KTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLED--ISNGSFYIDGKLMNDVAPKDRdIAMVFQNYALYPHMSV 93
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 94 YDNMAFGLKLRKLpkdeinhrvteaakilgledylkrkpkalSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAklrvSM 173
Cdd:cd03213 100 RETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDS----SS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446752175 174 RSEISKLHRRL---NTTTIYVTHD-QTEAMTMASRLVVMKDG 211
Cdd:cd03213 147 ALQVMSLLRRLadtGRTIICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-227 |
8.88e-24 |
|
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: 98.00 E-value: 8.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYdNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR---DIAM 80
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 161 PLSNLDAKlrvsMRSEISKLHRRLNTTTIYV---THDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:cd03218 160 PFAGVDPI----AVQDIQKIIKILKDRGIGVlitDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-227 |
1.16e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 98.68 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 21 SDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGklmnDVAPK---------DRDIAMVFQNYALYPHM 91
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG----ENIPAmsrsrlytvRKRMSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 92 SVYDNMAFGLKLR-KLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:PRK11831 100 NVFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 171 VSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:PRK11831 180 GVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-222 |
1.24e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 101.64 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKD-RD----- 77
Cdd:COG3845 6 LELRGITKRFGG-VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRSpRDaialg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 78 IAMVFQNYALYPHMSVYDNMAFGL---KLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLeptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446752175 155 VFLMDEPLSNLD----AKLRVSMRseisKLhRRLNTTTIYVTHDQTEAMTMASRLVVMKDGiiQQVGT--PKEV 222
Cdd:COG3845 162 ILILDEPTAVLTpqeaDELFEILR----RL-AAEGKSIIFITHKLREVMAIADRVTVLRRG--KVVGTvdTAET 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-223 |
1.33e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 98.70 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDG-KLMND-----VAPKDRDIAMVFQnyalYPHMS 92
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKtkdkyIRPVRKRIGMVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 93 VYDN-----MAFGLKLRKLPKDEINHRVTEAAKILGLE-DYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:PRK13646 98 LFEDtvereIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 167 AKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVY 223
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-211 |
1.89e-23 |
|
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: 96.38 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 21 SDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmndvapkdrdIAMVFQNyALYPHMSVYDNMAFG 100
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAYVSQE-PWIQNGTIRENILFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 101 LKLRKlpkdEINHRVTEAAkilGLEDYLKRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAkl 169
Cdd:cd03250 90 KPFDE----ERYEKVIKAC---ALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA-- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446752175 170 RVS---MRSEISKlHRRLNTTTIYVTHdQTEAMTMASRLVVMKDG 211
Cdd:cd03250 161 HVGrhiFENCILG-LLLNNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-218 |
2.49e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.07 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 24 NLHIQDKEFIVFVGPSGCGKSTTLRMIAGLedIS-NGSFYIDGKLMNDVAPKD--RDIAMVFQNYALyPHMSVYDNMAFG 100
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGF--LPyQGSLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 101 lklRKLPKDEINHRVTEAAKILgleDYLKRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAkl 169
Cdd:PRK11174 447 ---NPDASDEQLQQALENAWVS---EFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA-- 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 170 rvsmRSE---ISKLHR-RLNTTTIYVTH--DQTEAMtmaSRLVVMKDGIIQQVGT 218
Cdd:PRK11174 519 ----HSEqlvMQALNAaSRRQTTLMVTHqlEDLAQW---DQIWVMQDGQIVQQGD 566
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-234 |
6.17e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 100.18 E-value: 6.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 2 AELVLDHIFKLY---DNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKDRD- 77
Cdd:PRK10535 3 ALLELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ---DVATLDADa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 78 --------IAMVFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAI 149
Cdd:PRK10535 80 laqlrrehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 150 VRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAmTMASRLVVMKDGII--------QQVGTPKE 221
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVA-AQAERVIEIRDGEIvrnppaqeKVNVAGGT 237
|
250
....*....|....*..
gi 446752175 222 VYDTPE----NVFVGGF 234
Cdd:PRK10535 238 EPVVNTasgwRQFVSGF 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-228 |
7.60e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.93 E-value: 7.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVA-----PKDRDIAMVFQN-YA-LYPHM 91
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgklqALRRDIQFIFQDpYAsLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 92 SVYDNMAFGLKLRKL-PKDEINHRVTEAAKILGLE-DYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL 169
Cdd:PRK10261 419 TVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 170 RVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPEN 228
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQH 557
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 |
1.71e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.03 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 2 AELVLDHIFKLYDNKTTaVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRD-IAM 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKLV-VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 161 PLSNLDAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDT 225
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-224 |
1.85e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.76 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 11 KLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGK---LMndvapkdrDIAMVFQnyal 87
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsaLL--------ELGAGFH---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 88 yPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:COG1134 101 -PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 168 KLRvsmrseiSKLHRRLN------TTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYD 224
Cdd:COG1134 180 AFQ-------KKCLARIRelresgRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-249 |
3.98e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.78 E-value: 3.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 35 FVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMN--------DVAPKDRDIAMVFQNYALYPhMSVYDNMAFGLKLRKL 106
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGgrsifnyrDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 107 -PKDEI----NHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLH 181
Cdd:PRK14271 131 vPRKEFrgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 182 RRLntTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVFVGGFIGSpamnfFTGTLKD 249
Cdd:PRK14271 211 DRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAG-----LSGDVKD 271
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-217 |
5.05e-22 |
|
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: 92.98 E-value: 5.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 18 TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmndVAPkdrdiaMVFQNYALYPHMSVYDNM 97
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR----VSS------LLGLGGGFNPELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 98 AFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEI 177
Cdd:cd03220 106 YLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446752175 178 SKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVG 217
Cdd:cd03220 186 RELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-214 |
7.48e-22 |
|
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: 92.78 E-value: 7.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-RDIAMVF-Q 83
Cdd:cd03267 23 LKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlRRIGVVFgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03267 103 KTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446752175 164 NLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQ 214
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-223 |
8.02e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 93.66 E-value: 8.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMN------DVAPKDRDIAMVFQnyalYPHMS 92
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 93 VYD-----NMAFGLKLRKLPKDEINHRVTEAAKILGL-EDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:PRK13649 98 LFEetvlkDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 167 AKLRVSMRSEISKLHrRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVY 223
Cdd:PRK13649 178 PKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-194 |
9.45e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.29 E-value: 9.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 21 SDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIdgklmndvaPKDRDIAMVFQNYALYPHMSVYDNMAFG 100
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEPPLDDDLTVLDTVLDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 101 LK-LRKLPK--DEINHRV--------------------------TEAAKIL-GL---EDYLKRKPKALSGGQRQRVALGR 147
Cdd:COG0488 86 DAeLRALEAelEELEAKLaepdedlerlaelqeefealggweaeARAEEILsGLgfpEEDLDRPVSELSGGWRRRVALAR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446752175 148 AIVRDAKVFLMDEPLSNLDAklrvsmrsE-ISKLHRRLNT---TTIYVTHD 194
Cdd:COG0488 166 ALLSEPDLLLLDEPTNHLDL--------EsIEWLEEFLKNypgTVLVVSHD 208
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
20-226 |
9.88e-22 |
|
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: 96.55 E-value: 9.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 20 VSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVaPKDR---DIAMVFQNYALYpHMSVYDN 96
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVAMVDQDIFLF-EGTVRDN 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 97 MAfgLKLRKLPKDEInhrvTEAAKILGLEDYLKRKPKA-----------LSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:TIGR03796 573 LT--LWDPTIPDADL----VRACKDAAIHDVITSRPGGydaelaegganLSGGQRQRLEIARALVRNPSILILDEATSAL 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446752175 166 DAKLRVSMRSEIsklhRRLNTTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:TIGR03796 647 DPETEKIIDDNL----RRRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-224 |
1.10e-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: 96.73 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 3 ELVLDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVapkDRDIAMVF 82
Cdd:TIGR01193 473 DIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 83 QNY-ALYPHM---SVYDNMAFGLKlRKLPKDEINhRVTEAAKI--------LGLEDYLKRKPKALSGGQRQRVALGRAIV 150
Cdd:TIGR01193 550 INYlPQEPYIfsgSILENLLLGAK-ENVSQDEIW-AACEIAEIkddienmpLGYQTELSEEGSSISGGQKQRIALARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446752175 151 RDAKVFLMDEPLSNLDAklrVSMRSEISKLHRRLNTTTIYVTHDQTEAmTMASRLVVMKDGIIQQVGTPKEVYD 224
Cdd:TIGR01193 628 TDSKVLILDESTSNLDT---ITEKKIVNNLLNLQDKTIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLD 697
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-228 |
1.14e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.31 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 18 TAVSDFNLHIQDKEFIVFVGPSGCGKSTT----LRMIAglediSNGSFYIDGKLMNDVAPKD-----RDIAMVFQ--NYA 86
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 87 LYPHMSVYDNMAFGLKL--RKLPKDEINHRVTEAAKILGLE-DYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 164 NLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPEN 228
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQ 519
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-207 |
1.69e-21 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 92.09 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 27 IQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGklmNDVAPKDRDIAMVFQnyalyphMSVYDnmafglKLRKL 106
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL---DTVSYKPQYIKADYE-------GTVRD------LLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 107 PKDEINHR--VTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRL 184
Cdd:cd03237 86 TKDFYTHPyfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
170 180
....*....|....*....|...
gi 446752175 185 NTTTIYVTHDQTEAMTMASRLVV 207
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLIV 188
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-228 |
2.42e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.76 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 15 NKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYAL-YPhM 91
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLsFP-F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 92 SVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVR------DAKVFLMDEPLSNL 165
Cdd:PRK13548 92 TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 166 DakLR---VSMRseiskLHRRL----NTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYdTPEN 228
Cdd:PRK13548 172 D--LAhqhHVLR-----LARQLaherGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL-TPET 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-226 |
2.49e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.14 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 17 TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKD-----RDIAMVFQNYAL---- 87
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGD---DVEALSaraasRRVASVPQDTSLsfef 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 88 ----------YPHMSVYDNMafglklrklpkDEINHRVTEAA-KILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK09536 93 dvrqvvemgrTPHRSRFDTW-----------TETDRAAVERAmERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 157 LMDEPLSNLDaklrVSMRSEISKLHRRL---NTTTIYVTHDqteaMTMASR----LVVMKDGIIQQVGTPKEVYDTP 226
Cdd:PRK09536 162 LLDEPTASLD----INHQVRTLELVRRLvddGKTAVAAIHD----LDLAARycdeLVLLADGRVRAAGPPADVLTAD 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-218 |
3.56e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.03 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYpH 90
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrRNIAVVFQDAGLF-N 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDNMAFGlklrklPKDEINHRVTEAAKILGLEDYLKRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:PRK13657 423 RSIEDNIRVG------RPDATDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 160 EPLSNLDAKLRVSMRSEISKLhrRLNTTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGT 218
Cdd:PRK13657 497 EATSALDVETEAKVKAALDEL--MKGRTTFIIAH-RLSTVRNADRILVFDNGRVVESGS 552
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
15-211 |
4.29e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 91.23 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 15 NKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGL--EDISNGS--------FYIDGKLMNDVAPKDRDIAMVFQN 84
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGShiellgrtVQREGRLARDIRKSRANTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 85 YALYPHMSVYDNMAFGlKLRKLP---------KDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:PRK09984 95 FNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 156 FLMDEPLSNLDAKlrvSMRSEISKLhRRLNTT---TIYVTHDQTE-AMTMASRLVVMKDG 211
Cdd:PRK09984 174 ILADEPIASLDPE---SARIVMDTL-RDINQNdgiTVVVTLHQVDyALRYCERIVALRQG 229
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
10-226 |
4.57e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.48 E-value: 4.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGL---EDISNGSFYIDGKLMNDVAPKD------RDIAM 80
Cdd:PRK09473 22 FSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKElnklraEQISM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQN--YALYPHMSVYDNMAFGLKLRK-LPKDEI---NHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK09473 102 IFQDpmTSLNPYMRVGEQLMEVLMLHKgMSKAEAfeeSVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446752175 155 VFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-222 |
4.63e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.46 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 18 TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDG----KLMNDVApkdRDIAMVF-QNYALYPHMS 92
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfKRRKEFA---RRIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 93 VYDNmaFGL--KLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD--AK 168
Cdd:COG4586 113 AIDS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDvvSK 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446752175 169 LRVsmRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDG----------IIQQVGTPKEV 222
Cdd:COG4586 191 EAI--REFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGriiydgsleeLKERFGPYKTI 252
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-223 |
6.24e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 91.33 E-value: 6.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 17 TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMN------DVAPKDRDIAMVFQnyalYPH 90
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQ----FPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYD-----NMAFGLKLRKLPKDEINHRVTEAAKILGL-EDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSN 164
Cdd:PRK13643 95 SQLFEetvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 165 LDAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVY 223
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
9-275 |
6.28e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 91.69 E-value: 6.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 9 IFKLYDNKT----TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGS---FYIDGKLMNDVAPKD------ 75
Cdd:PRK13651 8 IVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEKEkvlekl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 76 -----------------RDIAMVFQ--NYALYpHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGL-EDYLKRKPKAL 135
Cdd:PRK13651 88 viqktrfkkikkikeirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 136 SGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQ 215
Cdd:PRK13651 167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIK 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 216 VGTPKEVydtpenvfvggfigspamnfftgtLKDNYFHIEN-------IRFKvpegqlQKLQKKGYN 275
Cdd:PRK13651 246 DGDTYDI------------------------LSDNKFLIENnmeppklLNFV------NKLEKKGID 282
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-226 |
1.58e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.85 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMN--DVAPKDRDIAMVFQN--YALYPHMSVY 94
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 95 DNMAFGLKLR-KLPKDEINHRVTEAAKILGL-EDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDaklrVS 172
Cdd:PRK15112 108 QILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD----MS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 173 MRSEISKLHRRLNTTT----IYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:PRK15112 184 MRSQLINLMLELQEKQgisyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-222 |
1.90e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.18 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLDHIFKLYDNKTTaVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGK---LMNDVAPKDRD 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRV-VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisLLPLHARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 78 IAMVFQNYALYPHMSVYDNMAFGLKLRK-LPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 157 LMDEPLSNLDAKLRVSMRSEISKLhRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-213 |
3.15e-20 |
|
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: 87.10 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRD---IAMV---FQNYALYPHMS 92
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 93 VYDNMAFGLklrklpkdeinhrvteaakilgledylkrkpkALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDaklrVS 172
Cdd:cd03215 95 VAENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVD----VG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446752175 173 MRSEISKLHRRL---NTTTIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:cd03215 139 AKAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-229 |
3.27e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 88.63 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 16 KTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYPHMSV 93
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLAFPFTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 94 YDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIV-------RDAKVFLMDEPLSNLD 166
Cdd:COG4559 93 EEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 167 AK--LRVsMRseiskLHRRL---NTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYdTPENV 229
Cdd:COG4559 173 LAhqHAV-LR-----LARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL-TDELL 233
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
31-224 |
3.44e-20 |
|
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: 87.98 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 31 EFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKDRDIAMVFQNYAL---YPhMSVYDNMAFGLK----- 102
Cdd:TIGR03771 7 ELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGRTghigw 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 103 LRKLPKDEinHRVTEAA-KILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD---AKLRVSMRSEIS 178
Cdd:TIGR03771 83 LRRPCVAD--FAAVRDAlRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDmptQELLTELFIELA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446752175 179 KlhrrLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQvGTPKEVYD 224
Cdd:TIGR03771 161 G----AGTAILMTTHDLAQAMATCDRVVLLNGRVIAD-GTPQQLQD 201
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
10-183 |
5.02e-20 |
|
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: 87.71 E-value: 5.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLED---ISNGSFYIDGKLMNDVAPKDRdIAMVFQNYA 86
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKC-VAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 87 LYPHMSVYDNMAFGLKLR---KLPKDEINHRV-TEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:cd03234 92 LLPGLTVRETLTYTAILRlprKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180
....*....|....*....|.
gi 446752175 163 SNLDAKLRVSMRSEISKLHRR 183
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARR 192
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-166 |
5.95e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 91.34 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 18 TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKDRDIAM----VFQNYALYPHMSV 93
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---PVDAGDIATRRrvgyMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 94 YDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:NF033858 357 RQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-228 |
6.31e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.59 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 20 VSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDiSNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYPHMSVYDNM 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 98 AFGLKlRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVR-------DAKVFLMDEPLSNLDAKLR 170
Cdd:COG4138 91 ALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 171 VSMRSEISKLHrRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYdTPEN 228
Cdd:COG4138 170 AALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-TPEN 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-227 |
7.00e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.14 E-value: 7.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHiqdkEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMN----DVAPKDRDIAMVFQNyalyPHMSVY--- 94
Cdd:PRK13638 23 DFSLS----PVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrGLLALRQQVATVFQD----PEQQIFytd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 95 --DNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVS 172
Cdd:PRK13638 95 idSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 173 MRSEISKLHRRLNTTTIyVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:PRK13638 175 MIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-227 |
7.58e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.14 E-value: 7.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKT----TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGL----------EDISNGSFYIDGKLMN 69
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 70 DVAPKD--------RDIAMVFQ--NYALYPHmSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGL-EDYLKRKPKALSGG 138
Cdd:PRK13631 102 NPYSKKiknfkelrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 139 QRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMrSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGT 218
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
....*....
gi 446752175 219 PKEVYDTPE 227
Cdd:PRK13631 260 PYEIFTDQH 268
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-217 |
1.40e-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: 85.06 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHI-FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRD-IAMV 81
Cdd:cd03247 1 LSINNVsFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 82 FQNYALYpHMSVYDNmafglklrklpkdeinhrvteaakiLGledylkrkpKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:cd03247 81 NQRPYLF-DTTLRNN-------------------------LG---------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 162 LSNLDAKLRVSMRSEISKLHRrlNTTTIYVTHDQTeAMTMASRLVVMKDGIIQQVG 217
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-213 |
1.52e-19 |
|
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: 86.37 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPK--DRDIAMVFQNYALYPHmSVYDNMAF 99
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 100 GLKLRKLpkdeinHRVTEAAKILGLEDYLKRKPKA-----------LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:cd03248 111 GLQSCSF------ECVKEAAQKAHAHSFISELASGydtevgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446752175 169 LRVSMRSEISKLHRRlnTTTIYVTHdQTEAMTMASRLVVMKDGII 213
Cdd:cd03248 185 SEQQVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-226 |
3.55e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.01 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPK--DRDIAMVFQNYALYPHmSVYDNMAF 99
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 100 GLklRKLPKDEInhrvTEAAKILGLEDYLKRKPKA-----------LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:TIGR00958 578 GL--TDTPDEEI----MAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 169 LRVSMRSEISKLHRrlntTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:TIGR00958 652 CEQLLQESRSRASR----TVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-236 |
3.83e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 37 GPSGCGKSTTLRMIAGLEDISNGSFYIDGKLM---NDVAPKDRDIAMVFQNYALYPHMSVYDNmafgLKLRKLP------ 107
Cdd:PRK11288 37 GENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGVAIIYQELHLVPEMTVAEN----LYLGQLPhkggiv 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 108 -KDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKlrvsmrsEISKLHR---R 183
Cdd:PRK11288 113 nRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR-------EIEQLFRvirE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 184 L---NTTTIYVTHDQTEAMTMASRLVVMKDGiiQQVGTPKEVYDTPENVFVGGFIG 236
Cdd:PRK11288 186 LraeGRVILYVSHRMEEIFALCDAITVFKDG--RYVATFDDMAQVDRDQLVQAMVG 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-219 |
6.39e-19 |
|
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: 88.92 E-value: 6.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGK-LMNDVAPKDRDIAMVFQNYALYPHMSVYDNM 97
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 98 AFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEI 177
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446752175 178 skLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTP 219
Cdd:TIGR01257 1105 --LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-209 |
6.49e-19 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 84.13 E-value: 6.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlMNDVAPKDRDIAMVFQ 83
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK-TATRGDRSRFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHMSVYDNMAF-----GLKLRKLPKDeinhrvteAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PRK13543 90 LPGLKADLSTLENLHFlcglhGRRAKQMPGS--------ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446752175 159 DEPLSNLDAKlRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMK 209
Cdd:PRK13543 162 DEPYANLDLE-GITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-263 |
7.29e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.65 E-value: 7.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 16 KTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMN----DVAPKD--RDIAMVFQnyalYP 89
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKlrKKVSLVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 90 HMSVYDN-----MAFGLKLRKLPKDEINHRVTEAAKILGL-EDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK13641 95 EAQLFENtvlkdVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 164 NLDAKLRVSMrSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVfVGGFIGSPAMNFF 243
Cdd:PRK13641 175 GLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWL-KKHYLDEPATSRF 252
|
250 260
....*....|....*....|
gi 446752175 244 TGTLKDNYFHIENIRFKVPE 263
Cdd:PRK13641 253 ASKLEKGGFKFSEMPLTIDE 272
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-221 |
7.56e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.77 E-value: 7.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 3 ELVLDHIFKLYDNKTT-AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIA 79
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQNYALYpHMSVYDNMAFGLKlRKLPKDEINhrvtEAAKILGLEDYLKRKPKA-----------LSGGQRQRVALGRA 148
Cdd:PRK11176 421 LVSQNVHLF-NDTIANNIAYART-EQYSREQIE----EAARMAYAMDFINKMDNGldtvigengvlLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 149 IVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRrlNTTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGTPKE 221
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEKADEILVVEDGEIVERGTHAE 564
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-219 |
1.22e-18 |
|
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: 83.70 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 14 DNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTT----LRMIagleDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYAL 87
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 88 YPHmSVYDNMAFglkLRKLPKDEINhrvtEAAKILGLEDYLKRKPKAL-----------SGGQRQRVALGRAIVRDAKVF 156
Cdd:cd03244 90 FSG-TIRSNLDP---FGEYSDEELW----QALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 157 LMDEPLSNLD----AKLRVSMRSEISklhrrlNTTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGTP 219
Cdd:cd03244 162 VLDEATASVDpetdALIQKTIREAFK------DCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-193 |
1.30e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 21 SDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmndvAPKDRDIAMVF-----QNyALYPHMSVYD 95
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG-----DIDDPDVAEAChylghRN-AMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 96 NMAFGLKLRklpkDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKlRVSMRS 175
Cdd:PRK13539 93 NLEFWAAFL----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFA 167
|
170
....*....|....*...
gi 446752175 176 EISKLHRRLNTTTIYVTH 193
Cdd:PRK13539 168 ELIRAHLAQGGIVIAATH 185
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
8-222 |
1.48e-18 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 86.87 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 8 HIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNY 85
Cdd:TIGR01192 339 HITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESlrKSIATVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 86 ALYpHMSVYDNMAFGlklRKLPKDEinhRVTEAAKILGLEDYLKRKPKA-----------LSGGQRQRVALGRAIVRDAK 154
Cdd:TIGR01192 419 GLF-NRSIRENIRLG---REGATDE---EVYEAAKAAAAHDFILKRSNGydtlvgergnrLSGGERQRLAIARAILKNAP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 155 VFLMDEPLSNLDAKLRVSMRSEISKLhrRLNTTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:TIGR01192 492 ILVLDEATSALDVETEARVKNAIDAL--RKNRTTFIIAH-RLSTVRNADLVLFLDQGRLIEKGSFQEL 556
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-211 |
5.39e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 5.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYdNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR---DIAMVF 82
Cdd:PRK09700 8 MAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIGIIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 83 QNYALYPHMSVYDNMAFG-LKLRK------LPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKV 155
Cdd:PRK09700 87 QELSVIDELTVLENLYIGrHLTKKvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446752175 156 FLMDEPLSNLDAKlrvsmrsEISKLH------RRLNTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:PRK09700 167 IIMDEPTSSLTNK-------EVDYLFlimnqlRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-218 |
6.62e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 84.87 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 2 AELVLDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIA 79
Cdd:COG5265 356 GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQNYALYpHMSVYDNMAFGlklrklpKDEINHR-VTEAAKILGLEDYLKRKPKA-----------LSGGQRQRVALGR 147
Cdd:COG5265 436 IVPQDTVLF-NDTIAYNIAYG-------RPDASEEeVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIAR 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 148 AIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRrlNTTTIYVTH------DqteamtmASRLVVMKDGIIQQVGT 218
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHrlstivD-------ADEILVLEAGRIVERGT 575
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
17-161 |
9.51e-18 |
|
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: 81.42 E-value: 9.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 17 TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR---DIAMVFQNYALYPHMSV 93
Cdd:TIGR03410 13 SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVPQGREIFPRLTV 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 94 YDNMAFGLKLRKLPKDEINHRVTEAAKILglEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:TIGR03410 93 EENLLTGLAALPRRSRKIPDEIYELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-193 |
2.06e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.32 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 20 VSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLedisngSFYIDGKLmndVAPKDRDIAMVFQN-Y--------AL-YP 89
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL------WPYGSGRI---ARPAGARVLFLPQRpYlplgtlreALlYP 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 90 HMSvydnmafglklRKLPKDEInhrvTEAAKILGLEDYLKR------KPKALSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:COG4178 450 ATA-----------EAFSDAEL----REALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190
....*....|....*....|....*....|.
gi 446752175 164 NLDAKLRVSMrseISKLHRRL-NTTTIYVTH 193
Cdd:COG4178 515 ALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-228 |
3.08e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.36 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 23 FNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISnGSFYIDGKLMNDVAPKD----RD---------IAM-VFQNYALY 88
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMpVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 89 PHMSVydnmafglklrklPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVR-------DAKVFLMDEP 161
Cdd:PRK03695 94 QPDKT-------------RTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 162 LSNLDAKLRVSMRSEISKLHrRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYdTPEN 228
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL-TPEN 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
10-228 |
3.29e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.98 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKL------------------MNDV 71
Cdd:PRK10261 22 FMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLlrrrsrqvielseqsaaqMRHV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 72 apKDRDIAMVFQN--YALYPHMSVYDNMAFGLKLRK-LPKDEI---NHRVTEAAKILGLEDYLKRKPKALSGGQRQRVAL 145
Cdd:PRK10261 102 --RGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQgASREEAmveAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 146 GRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDT 225
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
...
gi 446752175 226 PEN 228
Cdd:PRK10261 260 PQH 262
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-214 |
4.73e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLmnDVA--PKDRDiamv 81
Cdd:COG0488 316 LELEGLSKSYGDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV--KIGyfDQHQE---- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 82 fqnyALYPHMSVYDNMAFGLKlrklpkdeiNHRVTEAAKILGL----EDYLKRKPKALSGGQRQRVALGRAIVRDAKVFL 157
Cdd:COG0488 389 ----ELDPDKTVLDELRDGAP---------GGTEQEVRGYLGRflfsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 158 MDEPLSNLDaklrVSMRSEISKLhrrLNT---TTIYVTHDQTEAMTMASRLVVMKDGIIQ 214
Cdd:COG0488 456 LDEPTNHLD----IETLEALEEA---LDDfpgTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
36-230 |
4.88e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.83 E-value: 4.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 36 VGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYPHMSVYDNMAFGlklrKLP------ 107
Cdd:PRK10575 43 IGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYLPQQLPAAEGMTVRELVAIG----RYPwhgalg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 108 --KDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLN 185
Cdd:PRK10575 119 rfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERG 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446752175 186 TTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVY--DTPENVF 230
Cdd:PRK10575 199 LTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMrgETLEQIY 245
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-227 |
6.53e-17 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 79.49 E-value: 6.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 11 KLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDgklMNDVAPKD--------------R 76
Cdd:TIGR02323 11 KSYGGGK-GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYI---MRSGAELElyqlseaerrrlmrT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 77 DIAMVFQNYALYPHMSVYDN-------MAFGL----KLRKLPKDEINHRVTEAAKIlglEDylkrKPKALSGGQRQRVAL 145
Cdd:TIGR02323 87 EWGFVHQNPRDGLRMRVSAGanigerlMAIGArhygNIRATAQDWLEEVEIDPTRI---DD----LPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 146 GRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDT 225
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDD 239
|
..
gi 446752175 226 PE 227
Cdd:TIGR02323 240 PQ 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-229 |
9.22e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 9.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEfIV-FVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAPKD-RD-----IAMVFQN---YALY 88
Cdd:COG1129 267 VVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPADSGEIRLDGK---PVRIRSpRDairagIAYVPEDrkgEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 89 PHMSVYDNMAFGLkLRKLPKDEINHRVTEAAKIlglEDYLKR---KP-------KALSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:COG1129 343 LDLSIRENITLAS-LDRLSRGGLLDRRRERALA---EEYIKRlriKTpspeqpvGNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446752175 159 DEPLSNLDaklrVSMRSEISKLHRRL---NTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVydTPENV 229
Cdd:COG1129 419 DEPTRGID----VGAKAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA--TEEAI 486
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-229 |
2.72e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.00 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 2 AELVLDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDvAPKDRDIAMV 81
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 82 FQNYAL---YP-------HMSVYDNMAFglkLRKlPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVR 151
Cdd:PRK15056 84 PQSEEVdwsFPvlvedvvMMGRYGHMGW---LRR-AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 152 DAKVFLMDEPLSNLDAKLRVSMRSEISKLhrRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGtPKEVYDTPENV 229
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLREL--RDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG-PTETTFTAENL 234
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-215 |
2.99e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.87 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD-RD-IAMVFQNYAL 87
Cdd:PRK11160 346 FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaISVVSQRVHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 88 YPHmSVYDNMafglklrKLPKDEIN-HRVTEAAKILGLEDYLKRKP----------KALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK11160 426 FSA-TLRDNL-------LLAAPNASdEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446752175 157 LMDEPLSNLDAKlrvsMRSEISKLHRRL--NTTTIYVTHDQTeAMTMASRLVVMKDG-IIQQ 215
Cdd:PRK11160 498 LLDEPTEGLDAE----TERQILELLAEHaqNKTVLMITHRLT-GLEQFDRICVMDNGqIIEQ 554
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-245 |
3.76e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 78.72 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 11 KLYDNKTTaVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR-DIAMVFQNYALYP 89
Cdd:PRK13536 49 KSYGDKAV-VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRIGVVPQFDNLDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 90 HMSVYDNMA-----FGLKLRKLpkDEINHRVTEAAKilgLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSN 164
Cdd:PRK13536 128 EFTVRENLLvfgryFGMSTREI--EAVIPSLLEFAR---LESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 165 LDAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTpenvfvggFIGSPAMNFFT 244
Cdd:PRK13536 203 LDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE--------HIGCQVIEIYG 273
|
.
gi 446752175 245 G 245
Cdd:PRK13536 274 G 274
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-168 |
3.91e-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: 75.86 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 15 NKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPK-DRDIAMVFQNYALYPHMSV 93
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 94 YDNMAFglkLRKLPKDEINHrVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:TIGR01189 91 LENLHF---WAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-194 |
5.29e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.08 E-value: 5.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLH-----IQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSfyIDGKLmnDVAPKDRDIAMVFqnyalypHMSVYDN 96
Cdd:PRK13409 352 DFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE--VDPEL--KISYKPQYIKPDY-------DGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 97 mafglkLRKLPKD-EINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDaklrVSMRS 175
Cdd:PRK13409 421 ------LRSITDDlGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VEQRL 490
|
170 180
....*....|....*....|...
gi 446752175 176 EISKLHRRL----NTTTIYVTHD 194
Cdd:PRK13409 491 AVAKAIRRIaeerEATALVVDHD 513
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-269 |
6.18e-16 |
|
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: 79.67 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTT-AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGK--LMNdvapkdrdIAM 80
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiLTN--------ISD 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 81 VFQNYALYPHMSVYDNMAFG-------LKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDA 153
Cdd:TIGR01257 2010 VHQNMGYCPQFDAIDDLLTGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 154 KVFLMDEPLSNLDAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVydtpENVFVGG 233
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL----KSKFGDG 2164
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446752175 234 FIGS---------------PAMNFFTGTLKDNY---FHIENIRFKVPEGQLQKL 269
Cdd:TIGR01257 2165 YIVTmkikspkddllpdlnPVEQFFQGNFPGSVqreRHYNMLQFQVSSSSLARI 2218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-226 |
6.63e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 77.47 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLDHIFKLYDNKTT---AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLED----ISNGSFYIDGKLMNDVAP 73
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 74 KDR------DIAMVFQN--YALYPHMSVYDNMAFGLKLRKL-PKDEINHRVTEAAKILGLEDYLKR---KPKALSGGQRQ 141
Cdd:PRK11022 81 KERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 142 RVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKE 221
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
....*
gi 446752175 222 VYDTP 226
Cdd:PRK11022 241 IFRAP 245
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-211 |
7.77e-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: 75.93 E-value: 7.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYI--DGKLMNDVAPKDRDIAMVFQNYALY-------- 88
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREILALRRRTIGYvsqflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 89 PHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKA-LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:COG4778 106 PRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPPAtFSGGEQQRVNIARGFIADPPLLLLDEPTASLDA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446752175 168 KLRVSMRSEISKLHRRlNTTTIYVTHDqTEAM-TMASRLVVMKDG 211
Cdd:COG4778 186 ANRAVVVELIEEAKAR-GTAIIGIFHD-EEVReAVADRVVDVTPF 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-213 |
1.44e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHiqDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAP---KDRDIAMVFQNYALYPHMSVYDNMA 98
Cdd:PRK15439 31 DFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLVPQEPLLFPNLSVKENIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 99 FGLKLRKLPKDeinhRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAklrvsmrSEIS 178
Cdd:PRK15439 109 FGLPKRQASMQ----KMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTP-------AETE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446752175 179 KLHRRLNTT------TIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:PRK15439 178 RLFSRIRELlaqgvgIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-226 |
1.90e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.12 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 20 VSDFNLHIQDKEFIVFVGPSGCGKSTTlrmIAGLEDI-------SNGSFYIDGKLMNDVAPKDRDIAMVFQN--YALYPH 90
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLT---CAAALGIlpagvrqTAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDNMAFGLKLRKLPKDeiNHRVTEAAKILGLED---YLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:PRK10418 96 HTMHTHARETCLALGKPAD--DATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 168 KLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-227 |
1.92e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.03 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLM-----NDVAPKDrdIAMVFQNYALYPHMSV 93
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpgHQIARMG--VVRTFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 94 YDNMAFG----LK------LRKLPKdeinHRVTEAAKI---------LGLEDYLKRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK11300 98 IENLLVAqhqqLKtglfsgLLKTPA----FRRAESEALdraatwlerVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 155 VFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
13-194 |
2.29e-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: 77.13 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTTAVSDFNLH-----IQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSfyIDGKLmnDVAPK------DRDiamv 81
Cdd:COG1245 344 YPDLTKSYGGFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE--VDEDL--KISYKpqyispDYD---- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 82 fqnyalyphMSVYDNmafglkLRKLPKDEINHRV--TEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMD 159
Cdd:COG1245 416 ---------GTVEEF------LRSANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190
....*....|....*....|....*....|....*....
gi 446752175 160 EPLSNLDaklrVSMRSEISKLHRRL----NTTTIYVTHD 194
Cdd:COG1245 481 EPSAHLD----VEQRLAVAKAIRRFaenrGKTAMVVDHD 515
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-233 |
4.17e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.76 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLDHIFKLYdNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDvAPKDR---- 76
Cdd:PRK11614 3 KVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD-WQTAKimre 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 77 DIAMVFQNYALYPHMSVYDNMAFGLKLRKlpKDEINHRVteaAKILGLEDYL--KRKPKA--LSGGQRQRVALGRAIVRD 152
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAE--RDQFQERI---KWVYELFPRLheRRIQRAgtMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 153 AKVFLMDEPLSNLDAKLRVSMRSEISKLhRRLNTTTIYVTHDQTEAMTMASRLVVMKDG--IIQQVGTPKEVYDTPENVF 230
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGhvVLEDTGDALLANEAVRSAY 234
|
...
gi 446752175 231 VGG 233
Cdd:PRK11614 235 LGG 237
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-221 |
4.86e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.24 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 26 HIQDKEFIVFVGPSGCGKSTTLRMIA-----GLEdiSNGSFYIDGKLMNdvAPKDRDI-AMVFQNYALYPHMSVYDNMAF 99
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAfrspkGVK--GSGSVLLNGMPID--AKEMRAIsAYVQQDDLFIPTLTVREHLMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 100 GLKLR---KLPKDEINHRVTEAAKILGLEDYLKRK------PKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAklr 170
Cdd:TIGR00955 123 QAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS--- 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 171 vSMRSEISKLHRRLNT--TTIYVTHDQ--TEAMTMASRLVVMKDGIIQQVGTPKE 221
Cdd:TIGR00955 200 -FMAYSVVQVLKGLAQkgKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-285 |
5.03e-15 |
|
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: 75.99 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGS-------------FYID-------- 64
Cdd:TIGR03269 3 VKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSgriiyhvalcekcGYVErpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 65 -GKLMNDVAPKDRD---------------IAMVFQ-NYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDY 127
Cdd:TIGR03269 82 cPVCGGTLEPEEVDfwnlsdklrrrirkrIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 128 LKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHdQTEAMT-MASRLV 206
Cdd:TIGR03269 162 ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH-WPEVIEdLSDKAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 207 VMKDGIIQQVGTPKEVYdtpeNVFVGGF----------IGSPAMNffTGTLKDNYFHIE--------NIRFKVPEGQLQK 268
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVV----AVFMEGVsevekeceveVGEPIIK--VRNVSKRYISVDrgvvkavdNVSLEVKEGEIFG 314
|
330 340
....*....|....*....|.
gi 446752175 269 L-QKKGYNQKTL---ILGIRP 285
Cdd:TIGR03269 315 IvGTSGAGKTTLskiIAGVLE 335
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-195 |
5.72e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.07 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 14 DNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDgklmndvapkdrdiamvFQNYALYPHMSV 93
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----------------VPDNQFGREASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 94 YDNMAfglklRKLPKDEinhrVTEAAKILGLED--YLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRV 171
Cdd:COG2401 103 IDAIG-----RKGDFKD----AVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180
....*....|....*....|....
gi 446752175 172 SMRSEISKLHRRLNTTTIYVTHDQ 195
Cdd:COG2401 174 RVARNLQKLARRAGITLVVATHHY 197
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-211 |
9.28e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 72.75 E-value: 9.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 20 VSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRD------IAMVFQNYALYpHMSV 93
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrysVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 94 YDNMAFGLKLRKlpkdEINHRVTEAAKI--------LGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:cd03290 96 EENITFGSPFNK----QRYKAVTDACSLqpdidllpFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446752175 166 DAKLRVS-MRSEISKLHRRLNTTTIYVTHdQTEAMTMASRLVVMKDG 211
Cdd:cd03290 172 DIHLSDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-168 |
1.07e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.14 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 21 SDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNdvapKDRDiamVFQNYALY--------PHMS 92
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYHQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 93 VYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRkpkALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVR---QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-226 |
1.22e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.04 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTtAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGS--FYIDGKLMNDVA----PKDR- 76
Cdd:PRK11701 7 LSVRGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhYRMRDGQLRDLYalseAERRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 77 ----DIAMVFQNYA--LYPHMSVYDN-----MAFGLK----LRK-----LPKDEInhrvtEAAKIlgleDYLkrkPKALS 136
Cdd:PRK11701 86 llrtEWGFVHQHPRdgLRMQVSAGGNigerlMAVGARhygdIRAtagdwLERVEI-----DAARI----DDL---PTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 137 GGQRQRVALGRAIVRDAKVFLMDEPLSNLD----AKLRVSMRSeiskLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGI 212
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRG----LVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
250
....*....|....
gi 446752175 213 IQQVGTPKEVYDTP 226
Cdd:PRK11701 230 VVESGLTDQVLDDP 243
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-166 |
2.13e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 18 TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLR-MIAGLEDISnGSFYIDGKLmnDVApkdrdiamVFQNY--ALYPHMSVY 94
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQADS-GRIHCGTKL--EVA--------YFDQHraELDPEKTVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 95 DNMAFGlklrklpKDE--INHRvteAAKILG-LEDYL---KR--KP-KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:PRK11147 402 DNLAEG-------KQEvmVNGR---PRHVLGyLQDFLfhpKRamTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
.
gi 446752175 166 D 166
Cdd:PRK11147 472 D 472
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
37-193 |
2.76e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.75 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 37 GPSGCGKSTTLRMIAGLEDISNGSFYIDGK-LMNDVAPKDRDIAMVFQNYALYPHMSVYDNMAFGLKLrklpkDEINHRV 115
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFERQsIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHF-----SPGAVGI 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 116 TEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKlHRRLNTTTIYVTH 193
Cdd:PRK13540 109 TELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
236-288 |
2.78e-14 |
|
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: 66.45 E-value: 2.78e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446752175 236 GSPAMNFFTGTLKDNYFHIENIRFKVPEGQLQKLQKKGYNQKTLILGIRPEDI 288
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLLVLGGGVTLPLPEGQVLALKLYVGKEVILGIRPEHI 53
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-226 |
5.55e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.21 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 14 DNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYPHm 91
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFSD- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 92 SVYDNMAFGlklrklPKDEINHRVTEAAKILGLEDYLKRKPKA-----------LSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK10789 404 TVANNIALG------RPDATQQEIEHVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 161 PLSNLDAklrvsmRSEISKLHR----RLNTTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:PRK10789 478 ALSAVDG------RTEHQILHNlrqwGEGRTVIISAH-RLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-260 |
5.85e-14 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 70.86 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 36 VGPSGCGKSTTLRMIAGlEDISN-GSF------------YIDGKLMN---DVAPKDRDIAMVFQNYALYPHmsvydnmAF 99
Cdd:cd03236 32 VGPNGIGKSTALKILAG-KLKPNlGKFddppdwdeildeFRGSELQNyftKLLEGDVKVIVKPQYVDLIPK-------AV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 100 GLKLRKL--PKDEiNHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMrsei 177
Cdd:cd03236 104 KGKVGELlkKKDE-RGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA---- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 178 SKLHRRLNTTTIY---VTHDqteamtmASRLVVMKDGIIQQVGTPKE--VYDTPENVFVGgfigspaMNFFTgtlkDNYF 252
Cdd:cd03236 179 ARLIRELAEDDNYvlvVEHD-------LAVLDYLSDYIHCLYGEPGAygVVTLPKSVREG-------INEFL----DGYL 240
|
....*...
gi 446752175 253 HIENIRFK 260
Cdd:cd03236 241 PTENMRFR 248
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
57-230 |
9.42e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.75 E-value: 9.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 57 SNGSFYIDGKLMNDVAPKD-RDIAMVFQNYALYPHMSVYDNMAFGlklrklPKDEINHRVTEAAKILGLEDYLKRKP--- 132
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPnky 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 133 --------KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHdQTEAMTMASR 204
Cdd:PTZ00265 1349 dtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
170 180 190
....*....|....*....|....*....|.
gi 446752175 205 LVVMKD-----GIIQQVGTPKEVYDTPENVF 230
Cdd:PTZ00265 1428 IVVFNNpdrtgSFVQAHGTHEELLSVQDGVY 1458
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-224 |
9.53e-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: 72.67 E-value: 9.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 24 NLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmndvapkdrdIAMVFQNyALYPHMSVYDNMAFGLKL 103
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------VAYVPQQ-AWIQNDSLRENILFGKAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 104 rklpKDEINHRVTEAAKIL--------GLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRS 175
Cdd:TIGR00957 726 ----NEKYYQQVLEACALLpdleilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446752175 176 EISKLHRRL-NTTTIYVTHDQTeAMTMASRLVVMKDGIIQQVGTPKEVYD 224
Cdd:TIGR00957 802 HVIGPEGVLkNKTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-216 |
1.95e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.35 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTtaVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD---RDIAMVFQNY---A 86
Cdd:PRK09700 274 RDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdnG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 87 LYPHMSVYDNMAFG--LKLRKL--------PKDEinHRVTEAA-KILGLE-DYLKRKPKALSGGQRQRVALGRAIVRDAK 154
Cdd:PRK09700 352 FFPNFSIAQNMAISrsLKDGGYkgamglfhEVDE--QRTAENQrELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 155 VFLMDEPLSNLDaklrVSMRSEISKLHRRL---NTTTIYVTHDQTEAMTMASRLVVMKDGIIQQV 216
Cdd:PRK09700 430 VIIFDEPTRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-227 |
2.08e-13 |
|
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: 71.01 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGL--EDISNGSFYIDGKLMndVAPKDRD---- 77
Cdd:TIGR02633 2 LEMKGIVKTFGG-VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPL--KASNIRDtera 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 78 -IAMVFQNYALYPHMSVYDNMAFG----LKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKA-LSGGQRQRVALGRAIVR 151
Cdd:TIGR02633 79 gIVIIHQELTLVPELSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 152 DAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDGiiQQVGT-PKEVYDTPE 227
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG--QHVATkDMSTMSEDD 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-213 |
7.57e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 7.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 21 SDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD---RDIAMVFQNY---ALYPHMSVY 94
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairAGIMLCPEDRkaeGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 95 DNMAFGLKLRKLPKDEINHRVTEAAKIlglEDYLKR----------KPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSN 164
Cdd:PRK11288 350 DNINISARRHHLRAGCLINNRWEAENA---DRFIRSlniktpsreqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446752175 165 LDaklrVSMRSEISKLHRRL---NTTTIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:PRK11288 427 ID----VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-193 |
9.87e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.67 E-value: 9.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYI-DGKLMNDVAPK--DRDIAMVFQNYALYPHmSVYDNMA 98
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKwwRSKIGVVSQDPLLFSN-SIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 99 FGL-KLRKL-------------PKDEINHRVTEAAKILG-------------------------------------LEDY 127
Cdd:PTZ00265 482 YSLySLKDLealsnyynedgndSQENKNKRNSCRAKCAGdlndmsnttdsneliemrknyqtikdsevvdvskkvlIHDF 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 128 LKRKP-----------KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTH 193
Cdd:PTZ00265 562 VSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-222 |
1.64e-12 |
|
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: 69.17 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 17 TTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmndvapkdrdIAMVFQNYALYPHmSVYDN 96
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 97 MAFGLKLrklpkDEinHRVTEAAKILGLEDYLKRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:TIGR01271 507 IIFGLSY-----DE--YRYTSVIKACQLEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 166 DaklrVSMRSEI--SKLHRRL-NTTTIYVThDQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:TIGR01271 580 D----VVTEKEIfeSCLCKLMsNKTRILVT-SKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-227 |
2.05e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLD--HIFKLYDNkTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDIS--NGSFYIDGKLMndVAPKDR 76
Cdd:PRK13549 1 MMEYLLEmkNITKTFGG-VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEEL--QASNIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 77 D-----IAMVFQNYALYPHMSVYDNMAFGLKLRK---LPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRA 148
Cdd:PRK13549 78 DteragIAIIHQELALVKELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 149 IVRDAKVFLMDEPLSNLDAKlRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGiiQQVGT-PKEVYDTPE 227
Cdd:PRK13549 158 LNKQARLLILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG--RHIGTrPAAGMTEDD 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-216 |
2.31e-12 |
|
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: 65.36 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDIS---NGSFYIDGKLMNDVAPK-DR 76
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKyPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 77 DIAMVFQNYALYPHMSVYDNMAFGLKLRklpkdeiNHRVTeaakilgledylkrkpKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:cd03233 84 EIIYVSEEDVHFPTLTVRETLDFALRCK-------GNEFV----------------RGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446752175 157 LMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIyVTHDQT--EAMTMASRLVVMKDGiiQQV 216
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTF-VSLYQAsdEIYDLFDKVLVLYEG--RQI 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
36-194 |
2.93e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.89 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 36 VGPSGCGKSTTLRMIAGlEDISN-GSFyidgklmnDVAPKDRDIAMVFQNYALYPHMS-VYDN---------------MA 98
Cdd:COG1245 105 LGPNGIGKSTALKILSG-ELKPNlGDY--------DEEPSWDEVLKRFRGTELQDYFKkLANGeikvahkpqyvdlipKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 99 FGLKLRKLPK--DEINhRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMrse 176
Cdd:COG1245 176 FKGTVRELLEkvDERG-KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNV--- 251
|
170 180
....*....|....*....|.
gi 446752175 177 iSKLHRRL---NTTTIYVTHD 194
Cdd:COG1245 252 -ARLIRELaeeGKYVLVVEHD 271
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-193 |
3.24e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.82 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 6 LDHIFKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPK--DRDIAMVFQ 83
Cdd:PRK10790 343 IDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHmSVYDNMAFGlklRKLPKDEINH-----RVTEAAKIL--GLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVF 156
Cdd:PRK10790 423 DPVVLAD-TFLANVTLG---RDISEEQVWQaletvQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190
....*....|....*....|....*....|....*..
gi 446752175 157 LMDEPLSNLDAKLRVSMRSEISKLhrRLNTTTIYVTH 193
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAH 533
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-196 |
3.55e-12 |
|
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: 64.10 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 20 VSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIdgklmndvaPKDRDIAMVFQNyalyPHMSVydnmaf 99
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR----PYLPL------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 100 GLkLRklpkDEINHrvteaakilgledylkrkP--KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRsei 177
Cdd:cd03223 78 GT-LR----EQLIY------------------PwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY--- 131
|
170
....*....|....*....
gi 446752175 178 SKLHRRLnTTTIYVTHDQT 196
Cdd:cd03223 132 QLLKELG-ITVISVGHRPS 149
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
31-167 |
3.69e-12 |
|
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: 64.82 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 31 EFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPK-DRDIAMVFQNYALYPHMSVYDNMAFglkLRKLPKD 109
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENLRF---WHADHSD 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 110 EinhRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:cd03231 104 E---QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-206 |
5.57e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.90 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 25 LHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMvfqnyalyphmSVYDNMAFGLK 102
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDppRNVEG-----------TVYDFVAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 103 ------------------------LRKLPK--DEINH--------RVTEAAKILGLEDylKRKPKALSGGQRQRVALGRA 148
Cdd:PRK11147 93 eqaeylkryhdishlvetdpseknLNELAKlqEQLDHhnlwqlenRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446752175 149 IVRDAKVFLMDEPLSNLDAklrvsmrSEISKLHRRLNT---TTIYVTHDQTEAMTMASRLV 206
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDI-------ETIEWLEGFLKTfqgSIIFISHDRSFIRNMATRIV 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-226 |
6.84e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.11 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYidgklmndvapKDRDIAMVFQNyALYPHMSVYDNMAFGl 101
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQ-AWIMNATVRGNILFF- 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 102 klrklpKDEINHRVTEAAKIL-----------GLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKL- 169
Cdd:PTZ00243 745 ------DEEDAARLADAVRVSqleadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVg 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 170 -RVSMRSEISKLHRRlntTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:PTZ00243 819 eRVVEECFLGALAGK---TRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-211 |
8.44e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTT----LRMIAglediSNGSFYIDG-------KLMNDVAPKDR-- 76
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTalsiLRLLP-----SPPVVYPSGdirfhgeSLLHASEQTLRgv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 77 ---DIAMVFQN--YALYPHMSVYDNMAFGLKL-----RKLPKDEIN---HRV--TEAAKILGleDYlkrkPKALSGGQRQ 141
Cdd:PRK15134 90 rgnKIAMIFQEpmVSLNPLHTLEKQLYEVLSLhrgmrREAARGEILnclDRVgiRQAAKRLT--DY----PHQLSGGERQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 142 RVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-221 |
9.33e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 9.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 21 SDFNLHIQDKEFIVFVGPSGCGKSTTLR-MIAGLEDISNGSFYIDGKlmndvapkdrdIAMVFQNYALYpHMSVYDNMAF 99
Cdd:PLN03130 634 SNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-----------VAYVPQVSWIF-NATVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 100 GLklrklPKDEinHRVTEAAKILGLEDYLKRKPKA-----------LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAk 168
Cdd:PLN03130 702 GS-----PFDP--ERYERAIDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA- 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446752175 169 lRVSMRSEISKLHRRL-NTTTIYVThDQTEAMTMASRLVVMKDGIIQQVGTPKE 221
Cdd:PLN03130 774 -HVGRQVFDKCIKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEE 825
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-218 |
1.39e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.68 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTaVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMiagledisngsfyidgkLMNDVAPKD-------- 75
Cdd:PRK15064 320 LEVENLTKGFDNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRT-----------------LVGELEPDSgtvkwsen 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 76 -------RDIAMVFQNyalypHMSVYDNMAfglKLRKLPKDEINHRVTeAAKILGLEDYLKRKPKALSGGQRQRVALGRA 148
Cdd:PRK15064 382 anigyyaQDHAYDFEN-----DLTLFDWMS---QWRQEGDDEQAVRGT-LGRLLFSQDDIKKSVKVLSGGEKGRMLFGKL 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446752175 149 IVRDAKVFLMDEPLSNLDaklrvsMRSeISKLHRRLNT---TTIYVTHDQTEAMTMASRLVVMK-DGIIQQVGT 218
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMD------MES-IESLNMALEKyegTLIFVSHDREFVSSLATRIIEITpDGVVDFSGT 519
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-226 |
1.45e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.93 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLED----ISNGSFYIDGKLMNDVAPKDR------DIAMVFQN--YA 86
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQEpsSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 87 LYPHMSVYDNMafglkLRKLPKDEI--------NHRVTEAAKIL---GL---EDYLKRKPKALSGGQRQRVALGRAIVRD 152
Cdd:COG4170 102 LDPSAKIGDQL-----IEAIPSWTFkgkwwqrfKWRKKRAIELLhrvGIkdhKDIMNSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 153 AKVFLMDEPLSNLDAklrvSMRSEISKLHRRLN----TTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTP 226
Cdd:COG4170 177 PRLLIADEPTNAMES----TTQAQIFRLLARLNqlqgTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-170 |
1.75e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 62.58 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKdrDIAMVFQNYALYPHMSVYDNMAFGL 101
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP--YCTYIGHNLGLKLEMTVFENLKFWS 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446752175 102 KLrklpkdeINHRVTEAAKI--LGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLR 170
Cdd:PRK13541 96 EI-------YNSAETLYAAIhyFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-231 |
2.17e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.15 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 16 KTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR---DIAMVFQ----NyaLY 88
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAvcpRIAYMPQglgkN--LY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 89 PHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDE------PL 162
Cdd:NF033858 91 PTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEpttgvdPL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 163 S-----NLDAKLRVSmRSEISKLhrrlnTTTIYvthdqteaMTMASR---LVVMKDGIIQQVGTPKEV-----YDTPENV 229
Cdd:NF033858 171 SrrqfwELIDRIRAE-RPGMSVL-----VATAY--------MEEAERfdwLVAMDAGRVLATGTPAELlartgADTLEAA 236
|
..
gi 446752175 230 FV 231
Cdd:NF033858 237 FI 238
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-195 |
2.19e-11 |
|
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: 60.93 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 4 LVLDHIFKLYDNKTTaVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLmndvapkdrdiamvfq 83
Cdd:cd03221 1 IELENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 84 NYALYPHmsvydnmafglklrklpkdeinhrvteaakilgledylkrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:cd03221 64 KIGYFEQ--------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190
....*....|....*....|....*....|..
gi 446752175 164 NLDAKLRVSMRSEISKLHRrlntTTIYVTHDQ 195
Cdd:cd03221 100 HLDLESIEALEEALKEYPG----TVILVSHDR 127
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-241 |
2.97e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.90 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 31 EFIVFVGPSGCGKSTTLRMIAGLediSNGSFYIDGKLMNDVAPKD---RDIAMVFQNYALYPHMSVYDNMAFGLKLRkLP 107
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGR---IQGNNFTGTILANNRKPTKqilKRTGFVTQDDILYPHLTVRETLVFCSLLR-LP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 108 KDEINHRVTEAAKILGLEDYLKRKP---------KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEIS 178
Cdd:PLN03211 171 KSLTKQEKILVAESVISELGLTKCEntiignsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLG 250
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446752175 179 KLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVfvgGFIGSPAMN 241
Cdd:PLN03211 251 SLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESV---GFSPSFPMN 310
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-227 |
3.07e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTT--AVSDFNLHIQDKEFIVFVGPSGCGKSTTLR-MIAGLEDISNGSFYIDGKLMndVAPKdrdIAMVFqnyalyp 89
Cdd:PLN03232 624 WDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVA--YVPQ---VSWIF------- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 90 HMSVYDNMAFGLKLRklpkdeiNHRVTEAAKILGLEDYLKRKPKA-----------LSGGQRQRVALGRAIVRDAKVFLM 158
Cdd:PLN03232 692 NATVRENILFGSDFE-------SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 159 DEPLSNLDAKLRVSMRSEISKlHRRLNTTTIYVThDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPE 227
Cdd:PLN03232 765 DDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-211 |
3.74e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPK---DRDIAMVFQNYALYPHMSVYD 95
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKealENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 96 NMAFGLKLRK---LPKDEInHRVTEAA-KILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRV 171
Cdd:PRK10982 93 NMWLGRYPTKgmfVDQDKM-YRDTKAIfDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446752175 172 SMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:PRK10982 172 HLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-194 |
5.10e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 36 VGPSGCGKSTTLRMIAGlEDISN-GSFyidgklmNDVAPKDRDIAM----VFQNY-----------ALYPHMSVYDNMAF 99
Cdd:PRK13409 105 LGPNGIGKTTAVKILSG-ELIPNlGDY-------EEEPSWDEVLKRfrgtELQNYfkklyngeikvVHKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 100 GLKLRKLPK--DEINhRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMrsei 177
Cdd:PRK13409 177 KGKVRELLKkvDERG-KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNV---- 251
|
170
....*....|....*....
gi 446752175 178 SKLHRRL--NTTTIYVTHD 194
Cdd:PRK13409 252 ARLIRELaeGKYVLVVEHD 270
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-244 |
6.84e-11 |
|
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: 62.18 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmndvapkdrdIAMVFQNYALYPHmSVYDNMAFGL 101
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG-TIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 102 KLrklpkDEinHRVTEAAKILGLEDYLKRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD-AKL 169
Cdd:cd03291 123 SY-----DE--YRYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDvFTE 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 170 RVSMRSEISKLhrRLNTTTIYVThDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDT-PEnvFVGGFIGSPAMNFFT 244
Cdd:cd03291 196 KEIFESCVCKL--MANKTRILVT-SKMEHLKKADKILILHEGSSYFYGTFSELQSLrPD--FSSKLMGYDTFDQFS 266
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-166 |
9.01e-11 |
|
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: 63.03 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 7 DHIFKLYDNKttavsdfnLHIQDKEFIV-------FVGPSGCGKSTTLRMIAGLEDISNGSFYIdGKLMndvapkdrDIA 79
Cdd:TIGR03719 326 ENLTKAFGDK--------LLIDDLSFKLppggivgVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQNY-ALYPHMSVYDNMAFGLKLRKLPKDEINHRVteaakilgledYLKR----------KPKALSGGQRQRVALGRA 148
Cdd:TIGR03719 389 YVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRA-----------YVGRfnfkgsdqqkKVGQLSGGERNRVHLAKT 457
|
170
....*....|....*...
gi 446752175 149 IVRDAKVFLMDEPLSNLD 166
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLD 475
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-207 |
1.44e-10 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 59.51 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 27 IQDKEFIVFVGPSGCGKSTTLRMIAGLEDisngsfyidgklmndvaPKDRDIAMvfqnyalyphmsvydnmafglklrkl 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLI-----------------PNGDNDEW-------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 107 pkdeinHRVTEAAKilglEDYLKrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNT 186
Cdd:cd03222 59 ------DGITPVYK----PQYID-----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKK 123
|
170 180
....*....|....*....|.
gi 446752175 187 TTIYVTHDQTEAMTMASRLVV 207
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHV 144
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-227 |
1.76e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 20 VSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMndvapkdrdIAMVFQNYALYPHM--SVYDNM 97
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR---------IGYVPQKLYLDTTLplTVNRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 98 AFGLKLRK---LPKDEinhRVtEAAKILgleDYLKRKpkaLSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMR 174
Cdd:PRK09544 91 RLRPGTKKediLPALK---RV-QAGHLI---DAPMQK---LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446752175 175 SEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQvGTPKEVYDTPE 227
Cdd:PRK09544 161 DLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCS-GTPEVVSLHPE 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-224 |
2.27e-10 |
|
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: 59.46 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLED--ISNGSFYIDGKLMNDVAPKDR---DIAMVFQNYALYPhmsvydn 96
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIP------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 97 mafGLKlrklpkdeinhrvteaakilgLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAklrVSMRS- 175
Cdd:cd03217 91 ---GVK---------------------NADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI---DALRLv 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446752175 176 --EISKLhRRLNTTTIYVTHDQTEAMTMASRLV-VMKDGIIQQVGtPKEVYD 224
Cdd:cd03217 144 aeVINKL-REEGKSVLIITHYQRLLDYIKPDRVhVLYDGRIVKSG-DKELAL 193
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-216 |
2.96e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 2 AELVLDHIFKLYDNKTTAV-SDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDIS----NGSFYIDGKLMNDVAPKDR 76
Cdd:TIGR00956 58 LTRGFRKLKKFRDTKTFDIlKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEIKKHYR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 77 -DIAMVFQNYALYPHMSVYDNMAFGLKLRK-------LPKDE-INHRVTEAAKILGLEDYLKRKP-----KALSGGQRQR 142
Cdd:TIGR00956 138 gDVVYNAETDVHFPHLTVGETLDFAARCKTpqnrpdgVSREEyAKHIADVYMATYGLSHTRNTKVgndfvRGVSGGERKR 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 143 VALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTT---TIYvtHDQTEAMTMASRLVVMKDGiiQQV 216
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTplvAIY--QCSQDAYELFDKVIVLYEG--YQI 290
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
13-215 |
3.68e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.14 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLmndVAPKDRD-----IAMVFQNYAL 87
Cdd:PRK10522 332 YQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP---VTAEQPEdyrklFSAVFTDFHL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 88 YPHM-----SVYDNMAFGLKLRKLpkdEINHRVT-EAAKILGLEdylkrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:PRK10522 409 FDQLlgpegKPANPALVEKWLERL---KMAHKLElEDGRISNLK---------LSKGQKKRLALLLALAEERDILLLDEW 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446752175 162 LSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQtEAMTMASRLVVMKDGIIQQ 215
Cdd:PRK10522 477 AADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLSE 529
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
27-219 |
4.02e-10 |
|
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: 58.96 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 27 IQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYphmsvydnmAFGLKLR 104
Cdd:cd03369 31 VKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLF---------SGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 105 KLPKDEINHR-VTEAAKIlgledylKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL----DAKLRVSMRSEISk 179
Cdd:cd03369 102 LDPFDEYSDEeIYGALRV-------SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIdyatDALIQKTIREEFT- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446752175 180 lhrrlNTTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGTP 219
Cdd:cd03369 174 -----NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-213 |
5.43e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 21 SDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDR-DIAMVF-----QNYALYPHMS-- 92
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 93 ------VYDNMAFGLKlrklPKDEiNHRVTEAAKILGLEDYLKRKP-KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:PRK15439 360 wnvcalTHNRRGFWIK----PARE-NAVLERYRRALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446752175 166 DaklrVSMRSEISKLHRRL---NTTTIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:PRK15439 435 D----VSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-222 |
1.28e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.27 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 14 DNKTTAVSDFNLHIQDKEfIVFV-GPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRDIAMVF------QNYA 86
Cdd:COG3845 268 DRGVPALKDVSLEVRAGE-ILGIaGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGRG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 87 LYPHMSVYDNMAFGlKLRKLP--------KDEINHRvteAAKILglEDYLKRKP------KALSGGQRQRVALGRAIVRD 152
Cdd:COG3845 347 LVPDMSVAENLILG-RYRRPPfsrggfldRKAIRAF---AEELI--EEFDVRTPgpdtpaRSLSGGNQQKVILARELSRD 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 153 AKVFLMDEPLSNLDAklrvsmrSEISKLHRRL------NTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:COG3845 421 PKLLIAAQPTRGLDV-------GAIEFIHQRLlelrdaGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-218 |
1.50e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 15 NKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLE--DISNGSFYIDGKLMNDVAPKDRD---IAMVFQNYALYP 89
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhlgIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 90 HMSVYD--NMAFGLKLRKLPKDEIN-----HRVTEAAKILGLED-YLKRK-PKALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:CHL00131 98 GVSNADflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPsFLSRNvNEGFSGGEKKRNEILQMALLDSELAILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 161 PLSNLDAKLRVSMRSEISKLhRRLNTTTIYVTHDQteamtmasRLV---------VMKDGIIQQVGT 218
Cdd:CHL00131 178 TDSGLDIDALKIIAEGINKL-MTSENSIILITHYQ--------RLLdyikpdyvhVMQNGKIIKTGD 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-213 |
2.50e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 23 FNLHiqDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD---RDIAMVFQNY---ALYPHMSVYDN 96
Cdd:PRK10762 273 FTLR--KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRkrdGLVLGMSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 97 MAFgLKLRKLPKD--EINHrvteAAKILGLEDYLK----RKPKA------LSGGQRQRVALGRAIVRDAKVFLMDEPLSN 164
Cdd:PRK10762 351 MSL-TALRYFSRAggSLKH----ADEQQAVSDFIRlfniKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446752175 165 LDaklrVSMRSEISKLHRRLNT---TTIYVTHDQTEAMTMASRLVVMKDGII 213
Cdd:PRK10762 426 VD----VGAKKEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-183 |
2.84e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 1 MAELVLDH-IFKLYDNKTTAVSDfnLHIQDKEFIVFVGPSGCGKSTTLRMIAG------------LEDISNGSFYIDGKL 67
Cdd:PRK10938 1 MSSLQISQgTFRLSDTKTLQLPS--LTLNAGDSWAFVGANGSGKSALARALAGelpllsgerqsqFSHITRLSFEQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 68 MNDVApKDRDIAMvfqnyaLYPhmsvyDNMAFGLKLRKLPKDEINH--RVTEAAKILGLEDYLKRKPKALSGGQRQRVAL 145
Cdd:PRK10938 79 VSDEW-QRNNTDM------LSP-----GEDDTGRTTAEIIQDEVKDpaRCEQLAQQFGITALLDRRFKYLSTGETRKTLL 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 446752175 146 GRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRR 183
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-229 |
5.96e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAG--LEDISNGSFYIDGKLMNDVAPKDR-DIAMVFQNYALYPHMSvydNMA 98
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDVTLNGEPLAAiDAPRLARLRAVLPQAA---QPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 99 FGLKLRKL----------PKDEINHR----VTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAI---------VRDAKV 155
Cdd:PRK13547 96 FAFSAREIvllgrypharRAGALTHRdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446752175 156 FLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYdTPENV 229
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL-TPAHI 248
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
33-166 |
7.76e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 7.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 33 IVFV-GPSGCGKSTTLRMIAGLEDISNGSFyidgKLMNDVapkdrDIAMVFQNY-ALYPHMSVYDNMAFGLKLRKLPKDE 110
Cdd:PRK11819 352 IVGIiGPNGAGKSTLFKMITGQEQPDSGTI----KIGETV-----KLAYVDQSRdALDPNKTVWEEISGGLDIIKVGNRE 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 111 INHRVteaakilgledYLKR----------KPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLD 166
Cdd:PRK11819 423 IPSRA-----------YVGRfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-205 |
9.79e-09 |
|
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: 53.53 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 30 KEFIVFVGPSGCGKSTTLRMIAGLEDISNGSF-YIDGKLMNDVAPKDRdiamvfqnyalyphmsvydnmafglklrklpk 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQL-------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 109 deinhrvteaakilgLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEIS-----KLHRR 183
Cdd:smart00382 50 ---------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSE 114
|
170 180
....*....|....*....|..
gi 446752175 184 LNTTTIYVTHDQTEAMTMASRL 205
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRR 136
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-222 |
2.58e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.72 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALY---------PH 90
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrFKITIIPQDPVLFsgslrmnldPF 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDN---MAFGLK-----LRKLPkDEINHRVTEaakilGLEDylkrkpkaLSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:TIGR00957 1384 SQYSDEevwWALELAhlktfVSALP-DKLDHECAE-----GGEN--------LSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 163 SNLDAK----LRVSMRSE-----ISKLHRRLNTTTIYvthdqteamtmaSRLVVMKDGIIQQVGTPKEV 222
Cdd:TIGR00957 1450 AAVDLEtdnlIQSTIRTQfedctVLTIAHRLNTIMDY------------TRVIVLDKGEVAEFGAPSNL 1506
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
37-211 |
9.71e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 37 GPSGCGKSTTLRMIAGLediSNGSFYIDGKLMNDVAPKD----RDIAMVFQNYALYPHMSVYDNMAFGLKLR---KLPKD 109
Cdd:TIGR00956 796 GASGAGKTTLLNVLAER---VTTGVITGGDRLVNGRPLDssfqRSIGYVQQQDLHLPTSTVRESLRFSAYLRqpkSVSKS 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 110 EINHRVTEAAKILGLEDYlkrkPKALSG--------GQRQRVALGRAIVRDAKVFL-MDEPLSNLDAKLRVSmrseISKL 180
Cdd:TIGR00956 873 EKMEYVEEVIKLLEMESY----ADAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWS----ICKL 944
|
170 180 190
....*....|....*....|....*....|....*
gi 446752175 181 HRRLNTT--TIYVTHDQTEAMTMAS--RLVVMKDG 211
Cdd:TIGR00956 945 MRKLADHgqAILCTIHQPSAILFEEfdRLLLLQKG 979
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
36-211 |
1.08e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 36 VGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKDRD---IAMVFQNYALYPHMSVYDNMAFGLKLRKlPKDEIN 112
Cdd:PRK10762 36 VGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGIIHQELNLIPQLTIAENIFLGREFVN-RFGRID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 113 HRV--TEAAKI---LGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLhRRLNTT 187
Cdd:PRK10762 115 WKKmyAEADKLlarLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRG 193
|
170 180
....*....|....*....|....
gi 446752175 188 TIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:PRK10762 194 IVYISHRLKEIFEICDDVTVFRDG 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-194 |
1.49e-07 |
|
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: 53.02 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 33 IVFVGPSGCGKSTTLRMIAGLEDISNGSfyidgklmnDVAPKDRDIAMVFQNYALYPHMSVYDNMAFGL-----KLRKL- 106
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDKDFNGE---------ARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVaeikdALDRFn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 107 --------PKDEINHRVTEAAKilgLEDYLK------------------RKP------KALSGGQRQRVALGRAIVRDAK 154
Cdd:TIGR03719 105 eisakyaePDADFDKLAAEQAE---LQEIIDaadawdldsqleiamdalRCPpwdadvTKLSGGERRRVALCRLLLSKPD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446752175 155 VFLMDEPLSNLDAKlrvsmrsEISKLHRRLNT---TTIYVTHD 194
Cdd:TIGR03719 182 MLLLDEPTNHLDAE-------SVAWLERHLQEypgTVVAVTHD 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
13-230 |
2.84e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 51.06 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 13 YDNKTTAV-SDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIDGKlmnDVAP------KDRdIAMVFQNY 85
Cdd:cd03288 29 YENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI---DISKlplhtlRSR-LSIILQDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 86 ALYPhmsvyDNMAFGLKLRKLPKDEinhRVTEAAKILGLEDYLKRKPKAL-----------SGGQRQRVALGRAIVRDAK 154
Cdd:cd03288 105 ILFS-----GSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446752175 155 VFLMDEPLSNLD-AKLRVSMRSEISKLHRRlntTTIYVTHDQTEAMTmASRLVVMKDGIIQQvgtpkevYDTPENVF 230
Cdd:cd03288 177 ILIMDEATASIDmATENILQKVVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVE-------CDTPENLL 242
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
10-235 |
3.07e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.73 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 10 FKLYDNKTTAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLED----ISNGSFYIDGKLMNDVAPKDR------DIA 79
Cdd:PRK15093 13 FKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 80 MVFQ--NYALYPHMSVYDNMA---------------FGLKLRKlpKDEINHRVteaaKILGLEDYLKRKPKALSGGQRQR 142
Cdd:PRK15093 93 MIFQepQSCLDPSERVGRQLMqnipgwtykgrwwqrFGWRKRR--AIELLHRV----GIKDHKDAMRSFPYELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 143 VALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
250
....*....|...
gi 446752175 223 YDTPENVFVGGFI 235
Cdd:PRK15093 247 VTTPHHPYTQALI 259
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
57-214 |
4.89e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 57 SNGSFYIDGKLMNDVAPKD---RDIAMVFQN---YALYPHMSVYDNMAfglkLRKLPKDEINHRVTEAAKILGLEDYLKR 130
Cdd:PRK13549 316 WEGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVGKNIT----LAALDRFTGGSRIDDAAELKTILESIQR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 131 -KPKA---------LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDaklrVSMRSEISKLHRRL---NTTTIYVTHDQTE 197
Cdd:PRK13549 392 lKVKTaspelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGID----VGAKYEIYKLINQLvqqGVAIIVISSELPE 467
|
170
....*....|....*..
gi 446752175 198 AMTMASRLVVMKDGIIQ 214
Cdd:PRK13549 468 VLGLSDRVLVMHEGKLK 484
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-214 |
4.95e-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: 51.36 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 20 VSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGL-EDISNGSFYIDGKLMNDVAPKD---RDIAMVFQN---YALYPHMS 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 93 VYDNMAfglkLRKLPKDEINHRVTEAAKILGLEDYLKR-KPKA---------LSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:TIGR02633 356 VGKNIT----LSVLKSFCFKMRIDAAAELQIIGSAIQRlKVKTaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446752175 163 SNLDaklrVSMRSEISKLHRRL---NTTTIYVTHDQTEAMTMASRLVVMKDGIIQ 214
Cdd:TIGR02633 432 RGVD----VGAKYEIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
36-167 |
5.18e-07 |
|
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: 49.55 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 36 VGPSGCGKSTTLRMIAGLEDISngsfYIDGKLMNDVAPKD----RDIAMVFQNYALYPHMSVYDNMAFGLKLRklpkdei 111
Cdd:cd03232 39 MGESGAGKTTLLDVLAGRKTAG----VITGEILINGRPLDknfqRSTGYVEQQDVHSPNLTVREALRFSALLR------- 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 112 nhrvteaakilgledylkrkpkALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:cd03232 108 ----------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-160 |
1.65e-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: 49.80 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 23 FNLHIQDKEfIVF-VGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLmndVAPKDRD-----IAMVFQNYALYPHMSVYDN 96
Cdd:COG4615 351 IDLTIRRGE-LVFiVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREayrqlFSAVFSDFHLFDRLLGLDG 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446752175 97 MAFGLKLRKLPKD-EINHRVT-EAAKILGLedylkrkpkALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:COG4615 427 EADPARARELLERlELDHKVSvEDGRFSTT---------DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
36-230 |
7.49e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 36 VGPSGCGKSTTLRMIAGLEDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYPhmsvyDNMAFGLKlrklPKDEINH 113
Cdd:PLN03232 1268 VGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFS-----GTVRFNID----PFSEHND 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 114 R-VTEAAKILGLEDYLKRKPKAL-----------SGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLH 181
Cdd:PLN03232 1339 AdLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEF 1418
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446752175 182 RrlnTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVF 230
Cdd:PLN03232 1419 K---SCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
29-194 |
7.66e-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: 46.06 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 29 DKEFIVFVGPSGCGKSTTLRMIagledisNGSFYIDGKLMNDVAPKDRDIA----------MVFQN-----YALYPHMSV 93
Cdd:cd03240 21 FSPLTLIVGQNGAGKTTIIEAL-------KYALTGELPPNSKGGAHDPKLIregevraqvkLAFENangkkYTITRSLAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 94 YDNMAFglklrkLPKDEINhrvteaaKILGLEdylkrkPKALSGGQRQ------RVALGRAIVRDAKVFLMDEPLSNLDA 167
Cdd:cd03240 94 LENVIF------CHQGESN-------WPLLDM------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE 154
|
170 180
....*....|....*....|....*...
gi 446752175 168 -KLRVSMRSEISKLHRRLNTTTIYVTHD 194
Cdd:cd03240 155 eNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-193 |
7.83e-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: 47.82 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 20 VSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDISNGSFYIdgklmndvaPKDRDIAMVFQNyalyPHMS------- 92
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQR----PYMTlgtlrdq 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 93 -VYDNMAFGLKLRKLPKDEInhrvTEAAKILGLEDYLKRK---------PKALSGGQRQRVALGRAIVRDAKVFLMDEPL 162
Cdd:TIGR00954 535 iIYPDSSEDMKRRGLSDKDL----EQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|.
gi 446752175 163 SnldaKLRVSMRSEISKLHRRLNTTTIYVTH 193
Cdd:TIGR00954 611 S----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
36-211 |
9.86e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 36 VGPSGCGKSTTLRMIAG----------------------LEDISNGSFYIDGKLMND--VAPKDRD--IAMVFQNYALYp 89
Cdd:PRK10938 292 VGPNGAGKSTLLSLITGdhpqgysndltlfgrrrgsgetIWDIKKHIGYVSSSLHLDyrVSTSVRNviLSGFFDSIGIY- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 90 hMSVYDnmafglKLRKLpkdeinhrVTEAAKILGLEDYLKRKP-KALSGGQrQRVAL-GRAIVRDAKVFLMDEPLSNLDA 167
Cdd:PRK10938 371 -QAVSD------RQQKL--------AQQWLDILGIDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDP 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446752175 168 KLRVSMRSEISKLHRRLNTTTIYVTHDQTEA-MTMASRLVVMKDG 211
Cdd:PRK10938 435 LNRQLVRRFVDVLISEGETQLLFVSHHAEDApACITHRLEFVPDG 479
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
36-194 |
1.86e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 36 VGPSGCGKSTTLRMIAGLEDISNGsfyiDGKLMNDVApkdrdIAMVFQNYALYPHMSVYDN--MAFGLKLRKLPK-DEIN 112
Cdd:PRK11819 39 LGLNGAGKSTLLRIMAGVDKEFEG----EARPAPGIK-----VGYLPQEPQLDPEKTVRENveEGVAEVKAALDRfNEIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 113 HRVTE--------AAKILGLEDYLK------------------RKP------KALSGGQRQRVALGRAIVRDAKVFLMDE 160
Cdd:PRK11819 110 AAYAEpdadfdalAAEQGELQEIIDaadawdldsqleiamdalRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDE 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 446752175 161 PLSNLDAKlrvsmrsEISKLHRRLNT---TTIYVTHD 194
Cdd:PRK11819 190 PTNHLDAE-------SVAWLEQFLHDypgTVVAVTHD 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-230 |
2.13e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 27 IQDKEFIVFVGPSGCGKSTTL----RMIagleDISNGSFYIDGKLMNDVAPKD--RDIAMVFQNYALYPHmSVYDNM--- 97
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLltfmRMV----EVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQNVdpf 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 98 -------------AFGLKLRKLPKDE-INHRVTEaakilGLEDYlkrkpkalSGGQRQRVALGRAIV-RDAKVFLMDEPL 162
Cdd:PTZ00243 1408 leassaevwaaleLVGLRERVASESEgIDSRVLE-----GGSNY--------SVGQRQLMCMARALLkKGSGFILMDEAT 1474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446752175 163 SN----LDAKLRVSMRSEISklhrrlNTTTIYVTHdQTEAMTMASRLVVMKDGIIQQVGTPKEVYDTPENVF 230
Cdd:PTZ00243 1475 ANidpaLDRQIQATVMSAFS------AYTVITIAH-RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
281-356 |
3.29e-05 |
|
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: 41.45 E-value: 3.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 281 LGIRPEDIHdepIvlqSSPDSTVEINIEVAELLGAETMIHGKLENQSFVARI---NARSELKAGDKLSVAFSLTKAHFF 356
Cdd:pfam08402 1 LAIRPEKIR---L---AAAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRvpnAHARPPAPGDRVGLGWDPEDAHVL 73
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
241-289 |
3.67e-05 |
|
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common architecture comprising two variable hydrophobic transmembrane domains (TMDs) that form the translocation pathway and two conserved hydrophilic ABC-ATPases that hydrolyze ATP. This is the C-terminal regulatory domain found at the ATPase subunit of CysA, a putative sulfate ABC transporter from Alicyclobacillus acidocaldarius. The regulatory domain of CysA is built up of an elongated beta-barrel composed of two beta-sandwiches that form a common hydrophobic core.
Pssm-ID: 465531 [Multi-domain] Cd Length: 43 Bit Score: 40.51 E-value: 3.67e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446752175 241 NFFTGTLKDNYFHIENIRFKVPEGQlqklqkkGYNQKTLILGIRPEDIH 289
Cdd:pfam17850 1 NLFHGRVEDGRVRIGGLALPLPELA-------GAEGSEVVAYVRPHDLE 42
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
135-215 |
4.59e-05 |
|
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: 44.46 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 135 LSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAklrVSMRSEISKLHRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQ 214
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP---ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVR 215
|
.
gi 446752175 215 Q 215
Cdd:cd03289 216 Q 216
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
36-168 |
7.65e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 36 VGPSGCGKSTTLRMIAGLEdiSNGsfYIDGKLMNDVAPKDRDI-----AMVFQNYALYPHMSVYDNMAFGLKLRkLPKdE 110
Cdd:PLN03140 912 MGVSGAGKTTLMDVLAGRK--TGG--YIEGDIRISGFPKKQETfarisGYCEQNDIHSPQVTVRESLIYSAFLR-LPK-E 985
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 111 INH--------RVTEAAKILGLEDYLKRKP--KALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:PLN03140 986 VSKeekmmfvdEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
3-222 |
7.78e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.65 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 3 ELVLDHIFKLYDNKT-TAVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGleDISNGSFYIDgklmndvapKDRDIAMV 81
Cdd:PRK13546 22 ERMKDALIPKHKNKTfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGG--SLSPTVGKVD---------RNGEVSVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 82 FQNYALYPHMSVYDNMAFGLKLRKLPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEP 161
Cdd:PRK13546 91 AISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446752175 162 LSNLDAKLRVSMRSEISKLhRRLNTTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:PRK13546 171 LSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
106-222 |
8.08e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 106 LPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRlN 185
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-G 194
|
90 100 110
....*....|....*....|....*....|....*..
gi 446752175 186 TTTIYVTHDQTEAMTMASRLVVMKDGIIQQVGTPKEV 222
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
118-227 |
1.32e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 118 AAKIL-GLE---DYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRrlntTTIYVTH 193
Cdd:PLN03073 324 AASILaGLSftpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSH 399
|
90 100 110
....*....|....*....|....*....|....
gi 446752175 194 DQTEAMTMASRLVVMKDgiiQQVGTPKEVYDTPE 227
Cdd:PLN03073 400 AREFLNTVVTDILHLHG---QKLVTYKGDYDTFE 430
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
91-229 |
1.49e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 91 MSVYDNMAF--GLKL---RKLPKDEINHRVTEAAKIL---GLeDYL--KRKPKALSGGQRQRVALGRAI------Vrdak 154
Cdd:TIGR00630 436 LSIREAHEFfnQLTLtpeEKKIAEEVLKEIRERLGFLidvGL-DYLslSRAAGTLSGGEAQRIRLATQIgsgltgV---- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 155 VFLMDEPLSNLDAKLRVSMRSEISKLhRRLNTTTIYVTHDQtEAMTMASRLVVMKDG-------IIQQvGTPKEVYDTPE 227
Cdd:TIGR00630 511 LYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDE-DTIRAADYVIDIGPGagehggeVVAS-GTPEEILANPD 587
|
..
gi 446752175 228 NV 229
Cdd:TIGR00630 588 SL 589
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-232 |
1.49e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.88 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 23 FNLHIQDKEFIVfvGPSGCGKSTTLRMIAGLEDISNGSFYIDGklmndvapkdrdiamvfqnyalyphmsvYDNMAFGLK 102
Cdd:PLN03130 1260 FEISPSEKVGIV--GRTGAGKSSMLNALFRIVELERGRILIDG----------------------------CDISKFGLM 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 103 -LRKL--------------------PKDEINH-RVTEAAKILGLEDYLKRKPKAL-----------SGGQRQRVALGRAI 149
Cdd:PLN03130 1310 dLRKVlgiipqapvlfsgtvrfnldPFNEHNDaDLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 150 VRDAKVFLMDEPLSNL----DAKLRVSMRSEISK-----LHRRLNTttiyvthdqteaMTMASRLVVMKDGIIQQVGTPK 220
Cdd:PLN03130 1390 LRRSKILVLDEATAAVdvrtDALIQKTIREEFKSctmliIAHRLNT------------IIDCDRILVLDAGRVVEFDTPE 1457
|
250
....*....|..
gi 446752175 221 EVYDTPENVFVG 232
Cdd:PLN03130 1458 NLLSNEGSAFSK 1469
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
24-195 |
1.65e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.77 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 24 NLHIQDKEFIVFVGPSGCGKSTTLRMIAGLED--ISNGSFYIDGKLMNDVAPKDR---DIAMVFQNYALYPHMSvydNMA 98
Cdd:PRK09580 21 NLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageGIFMAFQYPVEIPGVS---NQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 99 FglkLRKLPKDEINHRVTEAAKILGLEDYLKRKPKAL---------------SGGQRQRVALGRAIVRDAKVFLMDEPLS 163
Cdd:PRK09580 98 F---LQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDS 174
|
170 180 190
....*....|....*....|....*....|..
gi 446752175 164 NLDAKLRVSMRSEISKLhRRLNTTTIYVTHDQ 195
Cdd:PRK09580 175 GLDIDALKIVADGVNSL-RDGKRSFIIVTHYQ 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-215 |
4.16e-03 |
|
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: 39.12 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 22 DFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGLEDiSNGSFYIDGKLMNDVAPKDRDIAmvfqnYALYPHMSVYDNMAFGL 101
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA-----FGVIPQKVFIFSGTFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 102 KLRKLPK--DEINHRVTEAakiLGLEDYLKRKPK-----------ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAK 168
Cdd:TIGR01271 1311 NLDPYEQwsDEEIWKVAEE---VGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV 1387
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446752175 169 LRVSMRSEISklHRRLNTTTIYVTHdQTEAMTMASRLVVMKDGIIQQ 215
Cdd:TIGR01271 1388 TLQIIRKTLK--QSFSNCTVILSEH-RVEALLECQQFLVIEGSSVKQ 1431
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-165 |
5.82e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446752175 19 AVSDFNLHIQDKEFIVFVGPSGCGKSTTLRMIAGL------EdisnGSFYIDGKLMN--DV-APKDRDIAMVFQNYALYP 89
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyE----GEILFDGEVCRfkDIrDSEALGIVIIHQELALIP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446752175 90 HMSVYDNMAFGLKLRK---LPKDEINHRVTEAAKILGLEDYLKRKPKALSGGQRQRVALGRAIVRDAKVFLMDEPLSNL 165
Cdd:NF040905 92 YLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
134-211 |
9.70e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 37.79 E-value: 9.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446752175 134 ALSGGQRQRVALGRAIVRDAKVFLMDEPLSNLDAKLRVSMRSEISKLHRRlNTTTIYVTHDQTEAMTMASRLVVMKDG 211
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| |
