|
Name |
Accession |
Description |
Interval |
E-value |
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-357 |
0e+00 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 593.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 1 MATITYDRATRLFpgSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIA 80
Cdd:COG3839 1 MASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 81 MVFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMD 160
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 161 EPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGSPS 240
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 241 MNLFTVPVTDGGVQIGDQLVPVPRDVLTAAGSEVIFGIRPEHVEIADSG--GLKLEIDVVEELGSEAFVFGRttVNGrtE 318
Cdd:COG3839 239 MNLLPGTVEGGGVRLGGVRLPLPAALAAAAGGEVTLGIRPEHLRLADEGdgGLEATVEVVEPLGSETLVHVR--LGG--Q 314
|
330 340 350
....*....|....*....|....*....|....*....
gi 1423915573 319 NLVARVDWRNPPEKGQVVHVRVDEAHAHIFATDaAGERL 357
Cdd:COG3839 315 ELVARVPGDTRLRPGDTVRLAFDPERLHLFDAE-TGRRL 352
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-357 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 512.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 1 MATITYDRATRLFPGsDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIA 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 81 MVFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMD 160
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 161 EPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGSPS 240
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 241 MNLFTVPVTDGGVQI---GDQLVPVPRDVLTAAGSEVIFGIRPEHVEIADSG-GLKLEIDVVEELGSEAFVFGRttVNGr 316
Cdd:PRK11650 240 MNLLDGRVSADGAAFelaGGIALPLGGGYRQYAGRKLTLGIRPEHIALSSAEgGVPLTVDTVELLGADNLAHGR--WGG- 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1423915573 317 tENLVARVDWRNPPEKGQVVHVRVDEAHAHIFATDaAGERL 357
Cdd:PRK11650 317 -QPLVVRLPHQERPAAGSTLWLHLPANQLHLFDAD-TGRRI 355
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
17-349 |
7.08e-153 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 434.14 E-value: 7.08e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAE 96
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGMVFQDYALFPHLTVAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRT 176
Cdd:COG3842 97 NVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMRE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 177 QIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGspSMNLFTVPVT---DGGV 253
Cdd:COG3842 177 ELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIG--EANLLPGTVLgdeGGGV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 254 QIGDQLVPVPRDVLTAAGSEVIFGIRPEHVEIADS---GGLKLEIDVVEELGSEAFVFGRTtvnGRTENLVARVDWRN-- 328
Cdd:COG3842 255 RTGGRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEgpeNGLPGTVEDVVFLGSHVRYRVRL---GDGQELVVRVPNRAal 331
|
330 340
....*....|....*....|.
gi 1423915573 329 PPEKGQVVHVRVDEAHAHIFA 349
Cdd:COG3842 332 PLEPGDRVGLSWDPEDVVVLP 352
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-357 |
6.04e-141 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 404.41 E-value: 6.04e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 1 MATITYDRATRLFpgSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIA 80
Cdd:PRK11000 1 MASVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 81 MVFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMD 160
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 161 EPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGSPS 240
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 241 MNLFTVPVTD---GGVQI---GDQLVPVPRDVLTA-AGSEVIFGIRPEHVEIADSGGLKLE--IDVVEELGSEAFVFgrT 311
Cdd:PRK11000 239 MNFLPVKVTAtaiEQVQVelpNRQQVWLPVEGRGVqVGANMSLGIRPEHLLPSDIADVTLEgeVQVVEQLGNETQIH--I 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1423915573 312 TVNGRTENLVARVDWRNPPEKGQVVHVRVDEAHAHIFATDA-AGERL 357
Cdd:PRK11000 317 QIPAIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGtACRRL 363
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
17-216 |
6.45e-128 |
|
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: 365.42 E-value: 6.45e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAE 96
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQNYALYPHMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRT 176
Cdd:cd03301 92 NIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1423915573 177 QIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQ 216
Cdd:cd03301 172 ELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
16-348 |
1.26e-110 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 326.33 E-value: 1.26e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDV-THAEPKDRDIAMVFQNYALYPHMTV 94
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQHYALFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQT 174
Cdd:COG1118 93 AENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 175 RTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGSPsmNLFTVPVTDGGVQ 254
Cdd:COG1118 173 RRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCV--NVLRGRVIGGQLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 255 IGDQLVPVPRDVltaAGSEVIFGIRPEHVEIAD----SGGLKLEIDVVEELGSEAFVFGRTTvNGRTENLVARV---DWR 327
Cdd:COG1118 251 ADGLTLPVAEPL---PDGPAVAGVRPHDIEVSRepegENTFPATVARVSELGPEVRVELKLE-DGEGQPLEAEVtkeAWA 326
|
330 340
....*....|....*....|..
gi 1423915573 328 N-PPEKGQVVHVRVDeaHAHIF 348
Cdd:COG1118 327 ElGLAPGDPVYLRPR--PARVF 346
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
17-218 |
1.95e-110 |
|
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: 321.01 E-value: 1.95e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAE 96
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQDYALFPHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRT 176
Cdd:cd03259 92 NIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELRE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1423915573 177 QIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCA 218
Cdd:cd03259 172 ELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
17-237 |
1.06e-109 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 319.95 E-value: 1.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAE 96
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQNYALFPHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRT 176
Cdd:cd03300 92 NIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 177 QIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMG 237
Cdd:cd03300 172 ELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
17-260 |
4.70e-106 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 315.73 E-value: 4.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAE 96
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQSYALFPHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRT 176
Cdd:PRK09452 106 NVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 177 QIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGspSMNLFTVPVTDggvQIG 256
Cdd:PRK09452 186 ELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIG--EINIFDATVIE---RLD 260
|
....
gi 1423915573 257 DQLV 260
Cdd:PRK09452 261 EQRV 264
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
20-349 |
9.70e-103 |
|
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: 306.58 E-value: 9.70e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAENMG 99
Cdd:TIGR03265 19 ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVFQSYALFPNLTVADNIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 100 FALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIA 179
Cdd:TIGR03265 99 YGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 180 QLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGspSMNLFTVPVTDGG-VQIGDQ 258
Cdd:TIGR03265 179 QLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVG--EVNWLPGTRGGGSrARVGGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 259 LVPVPRDVLTAAGSEVIFgIRPEHVEIADSG----GLKLEIDVVEELGSeafvFGRTTV---NGRTENLVARVDW----R 327
Cdd:TIGR03265 257 TLACAPGLAQPGASVRLA-VRPEDIRVSPAGnaanLLLARVEDMEFLGA----FYRLRLrleGLPGQALVADVSAseveR 331
|
330 340
....*....|....*....|..
gi 1423915573 328 NPPEKGQVVHVRVDEAHAHIFA 349
Cdd:TIGR03265 332 LGIRAGQPIWIELPAERLRAFA 353
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
2-348 |
1.13e-102 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 306.54 E-value: 1.13e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 2 ATITYDRATRLFPGSD--VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHA-----EP 74
Cdd:NF040933 1 VTVRVENVTKIFKKGKkeVVALDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASPgkiivPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 75 KDRDIAMVFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQP 154
Cdd:NF040933 81 EDRNIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 155 QVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAG 234
Cdd:NF040933 161 QVLLLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 235 FMGspSMNLFTVPVTDGGVQIGDQLVpVPRDVLTAAGSEVIFGIRPEHVEIADSGGLKLEIDV------VEELGSEAFVF 308
Cdd:NF040933 241 LIG--DINLLEGKVEEEGLVDGNDLK-IPLPNPKLEAGEVIIGIRPEDIDISESDMRLPPGFVevgkgrVKVSSYAGGVF 317
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1423915573 309 GRTTVNGRTENLVARVDWRNPPEKGQVVHVRVDEAHAHIF 348
Cdd:NF040933 318 RVVVSPIDDDSIEIIVNSDRPIEEGEEVNLYVRPDKIKIF 357
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
21-289 |
2.36e-102 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 305.49 E-value: 2.36e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAENMGF 100
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHMSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 101 ALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQ 180
Cdd:PRK11432 102 GLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 181 LQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGSPsmNLFTVPVTDGGVQIGDQLV 260
Cdd:PRK11432 182 LQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIFPATLSGDYVDIYGYRL 259
|
250 260 270
....*....|....*....|....*....|
gi 1423915573 261 PVPRDVLTA-AGSEVIFGIRPEHVEIADSG 289
Cdd:PRK11432 260 PRPAAFAFNlPDGECTVGVRPEAITLSEQG 289
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-285 |
3.00e-94 |
|
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: 284.00 E-value: 3.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 36 LVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAENMGFALKLAGTDKAEIRKR 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 116 VGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHD 195
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 196 QVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGSPSMNLFTVPVTDGGVQIGDQLVPVPRDVLTAAGSE-- 273
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIERKSEQVVLAGVEGRRCDIYTDVPVEkd 240
|
250
....*....|....
gi 1423915573 274 --VIFGIRPEHVEI 285
Cdd:TIGR01187 241 qpLHVVLRPEKIVI 254
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-238 |
4.83e-88 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 267.34 E-value: 4.83e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGsDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAM 81
Cdd:COG1125 2 IEFENVTKRYPD-GTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 82 VFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADM--LDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLM 159
Cdd:COG1125 81 VIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELvgLDPEEYRDRYPHELSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 160 DEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGS 238
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-238 |
5.93e-87 |
|
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: 262.28 E-value: 5.93e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAE 96
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKL----AGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRV 172
Cdd:cd03296 94 NVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1423915573 173 QTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGS 238
Cdd:cd03296 174 ELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
14-212 |
1.13e-83 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 254.63 E-value: 1.13e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 14 PGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVThaePKDRDIAMVFQNYALYPHMT 93
Cdd:COG1116 20 GGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT---GPGPDRGVVFQEPALLPWLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQ 173
Cdd:COG1116 97 VLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRER 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1423915573 174 TRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:COG1116 177 LQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
17-237 |
2.24e-83 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 253.18 E-value: 2.24e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAE 96
Cdd:TIGR00968 12 SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYALFKHLTVRD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRT 176
Cdd:TIGR00968 92 NIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKELRS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 177 QIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMG 237
Cdd:TIGR00968 172 WLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-237 |
5.58e-81 |
|
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: 246.86 E-value: 5.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAENMGF 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 101 ALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQ 180
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 181 LQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMG 237
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-211 |
1.25e-80 |
|
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: 245.46 E-value: 1.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGSD--VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVThaePKDRDIAM 81
Cdd:cd03293 1 LEVRNVSKTYGGGGgaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT---GPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 82 VFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1423915573 162 PLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKG 211
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
23-303 |
1.29e-80 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 249.99 E-value: 1.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 23 QLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAENMGFAL 102
Cdd:NF040840 18 DISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAFGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 103 KLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQ 182
Cdd:NF040840 98 KLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 183 RRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGSPsmNLFTVPVTDGG----VQIGDQ 258
Cdd:NF040840 178 REFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFE--NIIEGVAEKGGegtiLDTGNI 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 259 LVPVPRDVLtaagSEVIFGIRPEHVEIADSG-------GLKLEIDVVEELGS 303
Cdd:NF040840 256 KIELPEEKK----GKVRIGIRPEDITISTEKvktsarnEFKGKVEEIEDLGP 303
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-239 |
1.55e-79 |
|
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: 243.36 E-value: 1.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGSDvPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAM 81
Cdd:cd03295 1 IEFENVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 82 VFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDL--GAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLM 159
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 160 DEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGSP 239
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-287 |
2.15e-76 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 240.12 E-value: 2.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 10 TRLFPGSdvPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALY 89
Cdd:PRK11607 26 TKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAK 169
Cdd:PRK11607 104 PHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 170 LRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGspSMNLFTVPVT 249
Cdd:PRK11607 184 LRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG--SVNVFEGVLK 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1423915573 250 ----DGGVQIGDQLV---PVPRDVLTAAGSEVIFGIRPEHVEIAD 287
Cdd:PRK11607 262 erqeDGLVIDSPGLVhplKVDADASVVDNVPVHVALRPEKIMLCE 306
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-235 |
3.32e-73 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 228.30 E-value: 3.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 18 VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD------RDIAMVFQNYALYPH 91
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 MTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLR 171
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 172 VQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGF 235
Cdd:cd03294 197 REMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-299 |
2.09e-72 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 228.81 E-value: 2.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 3 TITYDRATRLFPGSDVpaVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMV 82
Cdd:PRK10851 2 SIEIANIKKSFGRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 83 FQNYALYPHMTVAENMGFALKL----AGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFL 158
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 159 MDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGs 238
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG- 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 239 pSMNLFTVPVTDGGVQIGDQLVPVPRDVLTAAGSEVIFgiRPEHVEIADSGGL--KLEIDVVE 299
Cdd:PRK10851 239 -EVNRLQGTIRGGQFHVGAHRWPLGYTPAYQGPVDLFL--RPWEVDISRRTSLdsPLPVQVLE 298
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
18-235 |
3.04e-72 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 229.60 E-value: 3.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 18 VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD------RDIAMVFQNYALYPH 91
Cdd:COG4175 40 TVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrKKMSMVFQHFALLPH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 MTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLR 171
Cdd:COG4175 120 RTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIR 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 172 VQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGF 235
Cdd:COG4175 200 REMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADF 263
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
15-214 |
2.26e-68 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 214.14 E-value: 2.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 15 GSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRD------IAMVFQNYAL 88
Cdd:COG1136 18 EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlrrrhIGFVFQFFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 89 YPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDA 168
Cdd:COG1136 98 LPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1423915573 169 KLRVQTRTQIAQLQRRLGTTTVYVTHDQvEAMTMGDRVAVLKGGVL 214
Cdd:COG1136 178 KTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
17-212 |
1.46e-67 |
|
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: 210.51 E-value: 1.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAE----PKDRDIAMVFQNYALYPHM 92
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIGMVFQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVAENMGFalklagtdkaeirkrvgeaadmldlgayldrkpkALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRV 172
Cdd:cd03229 92 TVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1423915573 173 QTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:cd03229 138 EVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-214 |
1.27e-64 |
|
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: 204.26 E-value: 1.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 18 VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRD------IAMVFQNYALYPH 91
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafrrrhIGFVFQSFNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 MTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLR 171
Cdd:cd03255 97 LTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETG 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1423915573 172 VQTRTQIAQLQRRLGTTTVYVTHDQVEAMtMGDRVAVLKGGVL 214
Cdd:cd03255 177 KEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
17-226 |
1.60e-64 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 204.53 E-value: 1.60e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRD-IAMVFQNYALYPHMTVA 95
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQEPALYPDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 96 ENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTR 175
Cdd:COG1131 92 ENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELW 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 176 TQIAQLQRRlGTTTVYVTH--DQVEAMTmgDRVAVLKGGVLQQCASPRELYRR 226
Cdd:COG1131 172 ELLRELAAE-GKTVLLSTHylEEAERLC--DRVAIIDKGRIVADGTPDELKAR 221
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
20-237 |
1.89e-64 |
|
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: 208.94 E-value: 1.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEP------KDRDIAMVFQNYALYPHMT 93
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQ 173
Cdd:TIGR01186 88 ILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 174 TRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMG 237
Cdd:TIGR01186 168 MQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-215 |
6.82e-63 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 199.89 E-value: 6.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGsDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-----RD 78
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 79 IAMVFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFL 158
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 159 MDEPLSNLDAklrvQTRTQIAQL-QR--RLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQ 215
Cdd:COG2884 161 ADEPTGNLDP----ETSWEIMELlEEinRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-216 |
1.17e-62 |
|
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: 199.06 E-value: 1.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 30 DGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGG------RDVTHAEPKDRDIAMVFQNYALYPHMTVAENMGFALK 103
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 104 laGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQR 183
Cdd:cd03297 102 --RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|...
gi 1423915573 184 RLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQ 216
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-229 |
1.79e-61 |
|
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: 197.33 E-value: 1.79e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 3 TITYDRATRlfpgsDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIA 80
Cdd:COG1124 8 SVSYGQGGR-----RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 81 MVFQNY--ALYPHMTVAENMGFALKLAGTDkaEIRKRVGEAADMLDLG-AYLDRKPKALSGGQRQRVAMGRAIVRQPQVF 157
Cdd:COG1124 83 MVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPELL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 158 LMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPAN 229
Cdd:COG1124 161 LLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-227 |
2.72e-61 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 204.75 E-value: 2.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 11 RLFPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-----RDIAMVFQN 85
Cdd:COG1123 271 PVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelrRRVQMVFQD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 86 --YALYPHMTVAENMGFALKLAGT-DKAEIRKRVGEAADMLDLGA-YLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:COG1123 351 pySSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILDE 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 162 PLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHD--QVEAMTmgDRVAVLKGGVLQQCASPRELYRRP 227
Cdd:COG1123 431 PTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlaVVRYIA--DRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-237 |
3.59e-61 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 196.13 E-value: 3.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 25 DLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAENMGFA--- 101
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQENNLFPHLTVAQNIGLGlrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 102 -LKLAGTDKAeirkRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQ 180
Cdd:COG3840 99 gLKLTAEQRA----QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 181 LQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMG 237
Cdd:COG3840 175 LCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
22-223 |
1.91e-60 |
|
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: 194.43 E-value: 1.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 22 DQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRD-----IAMVFQNYALYPHMTVAE 96
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrrIGMLFQGGALFDSLTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAGT-DKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTR 175
Cdd:COG1127 102 NVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVID 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1423915573 176 TQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:COG1127 182 ELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-227 |
2.36e-60 |
|
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: 193.70 E-value: 2.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNyalyP---- 90
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLVFQN----Pddql 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 -HMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAK 169
Cdd:COG1122 89 fAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 170 LRVQTRTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRP 227
Cdd:COG1122 169 GRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
13-212 |
4.98e-60 |
|
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: 192.30 E-value: 4.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNyalyP 90
Cdd:cd03225 9 YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrRKVGLVFQN----P 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 -HM----TVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:cd03225 85 dDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1423915573 166 LDAKLRVQTRTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:cd03225 165 LDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-286 |
3.03e-58 |
|
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: 192.62 E-value: 3.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 23 QLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAE------PKDRDIAMVFQNYALYPHMTVAE 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSArgiflpPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAGtdKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDaklrVQTRT 176
Cdd:COG4148 97 NLLYGRKRAP--RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD----LARKA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 177 QI----AQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPAnvFVAGFMGSPSMNLFTVPVT--- 249
Cdd:COG4148 171 EIlpylERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD--LLPLAGGEEAGSVLEATVAahd 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1423915573 250 -DGG---VQIGDQLVPVPRdVLTAAGSEVIFGIRPEHVEIA 286
Cdd:COG4148 249 pDYGltrLALGGGRLWVPR-LDLPPGTRVRVRIRARDVSLA 288
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-212 |
1.15e-57 |
|
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: 186.94 E-value: 1.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 3 TITYDRatrlfPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDR----- 77
Cdd:cd03257 8 SVSFPT-----GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 78 DIAMVFQNY--ALYPHMTVAENMGFALKLAG--TDKAEIRKRVGEAADMLDLGA-YLDRKPKALSGGQRQRVAMGRAIVR 152
Cdd:cd03257 83 EIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 153 QPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-229 |
5.49e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 188.75 E-value: 5.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 14 PGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-----RDIAMVFQNYAL 88
Cdd:COG1135 14 KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraarRKIGMIFQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 89 YPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDA 168
Cdd:COG1135 94 LSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 169 klrvQTRTQIAQL----QRRLGTTTVYVTHDqveamtMG------DRVAVLKGGVLQQCASPRELYRRPAN 229
Cdd:COG1135 174 ----ETTRSILDLlkdiNRELGLTIVLITHE------MDvvrricDRVAVLENGRIVEQGPVLDVFANPQS 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-228 |
9.94e-56 |
|
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: 190.11 E-value: 9.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDG---GQILIGGRDVTHAEPKDR--DIAMVFQN-- 85
Cdd:COG1123 14 YPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRgrRIGMVFQDpm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 86 YALYPhMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:COG1123 94 TQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 166 LDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPA 228
Cdd:COG1123 173 LDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
3.02e-55 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 181.60 E-value: 3.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 1 MATITYDRATRLFPGS--DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPkDRd 78
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 79 iAMVFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFL 158
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 159 MDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-227 |
6.92e-55 |
|
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: 179.70 E-value: 6.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGS--DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD----- 76
Cdd:cd03258 2 IELKNVSKVFGDTggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 77 RDIAMVFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQV 156
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 157 FLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTH--DQVEAMTmgDRVAVLKGGVLQQCASPRELYRRP 227
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELGLTIVLITHemEVVKRIC--DRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
17-229 |
7.53e-55 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 179.80 E-value: 7.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVThAEPKD-----RDIAMVFQNYALYPH 91
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDinklrRKVGMVFQQFNLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 MTVAENMGFAL-KLAGTDKAEIRKRvgeAADMLD---LGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD 167
Cdd:COG1126 92 LTVLENVTLAPiKVKKMSKAEAEER---AMELLErvgLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 168 AK-----LRVqtrtqIAQLQRRlGTTTVYVTHDqveamtMG------DRVAVLKGGVLQQCASPRELYRRPAN 229
Cdd:COG1126 169 PElvgevLDV-----MRDLAKE-GMTMVVVTHE------MGfarevaDRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-212 |
7.68e-54 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 177.56 E-value: 7.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGsDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-----RD 78
Cdd:COG3638 3 LELRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 79 IAMVFQNYALYPHMTVAEN--------MGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAI 150
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 151 VRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHdQVE-AMTMGDRVAVLKGG 212
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDG 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
17-214 |
1.82e-53 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 176.59 E-value: 1.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDR-DIAMVFQNYALYPHMTVA 95
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrQIGVLPDERGLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 96 ENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTR 175
Cdd:COG4555 93 ENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLR 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1423915573 176 TQIAQLqRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:COG4555 173 EILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
22-223 |
2.24e-52 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 173.46 E-value: 2.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 22 DQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-----RDIAMVFQNYALYPHMTVAE 96
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGMLFQSGALFDSLTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAGT-DKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTR 175
Cdd:cd03261 97 NVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVID 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1423915573 176 TQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:cd03261 177 DLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-212 |
3.90e-52 |
|
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: 172.05 E-value: 3.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGsDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-----RD 78
Cdd:TIGR02673 2 IEFHNVSKAYPG-GVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 79 IAMVFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFL 158
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 159 MDEPLSNLDAklrvQTRTQIAQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:TIGR02673 161 ADEPTGNLDP----DLSERILDLLKRLnkrGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-228 |
2.49e-51 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 173.76 E-value: 2.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 18 VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-----RDIAMVFQN-YA-LYP 90
Cdd:COG4608 31 VKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMQMVFQDpYAsLNP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HMTVAENMGFALKLAG-TDKAEIRKRVGEAADMLDLGA-YLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDa 168
Cdd:COG4608 111 RMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD- 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1423915573 169 klrVQTRTQI----AQLQRRLGTTTVYVTHD--QVEAMTmgDRVAVLKGGVLQQCASPRELYRRPA 228
Cdd:COG4608 190 ---VSIQAQVlnllEDLQDELGLTYLFISHDlsVVRHIS--DRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
22-214 |
3.36e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 169.61 E-value: 3.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 22 DQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPhMTVAENMG 99
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVPQEPALWG-GTVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 100 FALKLAgtDKAEIRKRVGEAADMLDLGA-YLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQI 178
Cdd:COG4619 96 FPFQLR--ERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELL 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1423915573 179 AQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:COG4619 174 REYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
21-215 |
7.65e-51 |
|
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: 169.92 E-value: 7.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPkDRdiAMVFQNYALYPHMTVAENMGF 100
Cdd:NF040729 21 LKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGP-DR--GFVFQNYALFPWMTVKENIEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 101 ALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQ 180
Cdd:NF040729 98 PMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEPLGAVDFQMRQILQEELES 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1423915573 181 LQRRLGTTTVYVTHDQVEAMTMGDRVAVL---KGGVLQ 215
Cdd:NF040729 178 IWLKDKTTVLMVTHDVDEAVYLSDRVIVMsrdKGKILE 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-228 |
3.01e-50 |
|
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: 170.62 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 14 PGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLED---VDGGQILIGGRDVTHAEPKD------RDIAMVFQ 84
Cdd:COG0444 14 RRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElrkirgREIQMIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 85 N-Y-ALYPHMTVAENMGFALKL-AGTDKAEIRKRVGEAADMLDL---GAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFL 158
Cdd:COG0444 94 DpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 159 MDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHD--QVEAMTmgDRVAVLKGGVLQQCASPRELYRRPA 228
Cdd:COG0444 174 ADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDlgVVAEIA--DRVAVMYAGRIVEEGPVEELFENPR 243
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
17-239 |
1.05e-49 |
|
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: 167.14 E-value: 1.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPHMTV 94
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElaRRIAYVPQEPPAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AEN--MGFA--LKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKL 170
Cdd:COG1120 93 RELvaLGRYphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAH 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 171 RVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASP---------RELYRRPANVFVAGFMGSP 239
Cdd:COG1120 173 QLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPeevltpellEEVYGVEARVIEDPVTGRP 250
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-212 |
1.11e-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: 165.74 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAENMGFALK 103
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 104 LAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQR 183
Cdd:cd03298 97 PGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176
|
170 180
....*....|....*....|....*....
gi 1423915573 184 RLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:cd03298 177 ETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-214 |
1.10e-48 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 167.29 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGS--DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD----- 76
Cdd:PRK11153 2 IELKNISKVFPQGgrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 77 RDIAMVFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQV 156
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 157 FLMDEPLSNLDAklrvQTRTQI----AQLQRRLGTTTVYVTH--DQVEAMTmgDRVAVLKGGVL 214
Cdd:PRK11153 162 LLCDEATSALDP----ATTRSIlellKDINRELGLTIVLITHemDVVKRIC--DRVAVIDAGRL 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
17-195 |
3.60e-48 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 161.50 E-value: 3.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVD---GGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMT 93
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRRIGILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGFALKlAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQ 173
Cdd:COG4136 93 VGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQ 171
|
170 180
....*....|....*....|..
gi 1423915573 174 TRTQIAQLQRRLGTTTVYVTHD 195
Cdd:COG4136 172 FREFVFEQIRQRGIPALLVTHD 193
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
24-214 |
2.06e-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: 159.62 E-value: 2.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPK----DRDIAMVFQNYALYPHMTVAENMG 99
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVGMVFQQFNLFPHLTVLENIT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 100 FAL-KLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLR---VQTR 175
Cdd:cd03262 99 LAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVgevLDVM 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 1423915573 176 TQIAQlqrrLGTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:cd03262 179 KDLAE----EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
13-226 |
2.68e-47 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 161.06 E-value: 2.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAE--PKDRD-IAMVFQNyaly 89
Cdd:TIGR04520 10 YPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnlWEIRKkVGMVFQN---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PH-----MTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLS 164
Cdd:TIGR04520 86 PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 165 NLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAmTMGDRVAVLKGGVLQQCASPRELYRR 226
Cdd:TIGR04520 166 MLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-216 |
7.08e-47 |
|
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: 158.49 E-value: 7.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 23 QLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAENMGFAL 102
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 103 KLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQ 182
Cdd:TIGR01277 96 HPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLC 175
|
170 180 190
....*....|....*....|....*....|....
gi 1423915573 183 RRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQ 216
Cdd:TIGR01277 176 SERQRTLLMVTHHLSDARAIASQIAVVSQGKIKV 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-229 |
9.07e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 159.10 E-value: 9.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDI----AMVFQNYALYPHM 92
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVAENMGFA-LKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLR 171
Cdd:PRK09493 93 TALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 172 VQTRTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPAN 229
Cdd:PRK09493 173 HEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-214 |
4.55e-46 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 156.41 E-value: 4.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGsDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTH----AEPK-DRD 78
Cdd:cd03292 1 IEFINVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgrAIPYlRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 79 IAMVFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFL 158
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 159 MDEPLSNLDAklrvQTRTQIAQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:cd03292 160 ADEPTGNLDP----DTTWEIMNLLKKInkaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-223 |
5.52e-46 |
|
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: 156.57 E-value: 5.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 11 RLFPGsDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDV-----DGGQILIGGRDVTHAEPKD----RDIAM 81
Cdd:cd03260 7 NVYYG-DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlelrRRVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 82 VFQNYALYPhMTVAENMGFALKLAGT-DKAEIRKRVGEAADMLDLGAYLDRKPKA--LSGGQRQRVAMGRAIVRQPQVFL 158
Cdd:cd03260 86 VFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 159 MDEPLSNLD--AKLRVQTRtqIAQLQRRlgTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:cd03260 165 LDEPTSALDpiSTAKIEEL--IAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-223 |
1.21e-45 |
|
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: 155.36 E-value: 1.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVtHAEPKD--RDIAMVFQNYALYP 90
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAarQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKL 170
Cdd:cd03263 89 ELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 171 RVQTRTQIAQLQRrlGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:cd03263 169 RRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-235 |
1.22e-45 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 160.58 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHA------EPKDRDIAMVFQNYALYPHMT 93
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelrEVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQ 173
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 174 TRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGF 235
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
14-216 |
4.63e-45 |
|
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: 154.13 E-value: 4.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 14 PGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTH------AEPKDRDIAMVFQNYA 87
Cdd:COG4181 21 GAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedarARLRARHVGFVFQSFQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 88 LYPHMTVAENMGFALKLAGTDKAEIRkrvgeAADMLD---LGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLS 164
Cdd:COG4181 101 LLPTLTALENVMLPLELAGRRDARAR-----ARALLErvgLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1423915573 165 NLDAKlrvqTRTQIAQL----QRRLGTTTVYVTHDQVEAmTMGDRVAVLKGGVLQQ 216
Cdd:COG4181 176 NLDAA----TGEQIIDLlfelNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
17-199 |
5.15e-45 |
|
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: 153.40 E-value: 5.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHA-EPKDRDIAMVFQNYALYPHMTVA 95
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDArEDYRRRLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 96 ENMGFALKLAGTDKAEIRkrVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAklrvQTR 175
Cdd:COG4133 94 ENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDA----AGV 167
|
170 180
....*....|....*....|....*..
gi 1423915573 176 TQIAQL---QRRLGTTTVYVTHDQVEA 199
Cdd:COG4133 168 ALLAELiaaHLARGGAVLLTTHQPLEL 194
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-227 |
5.41e-45 |
|
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: 155.69 E-value: 5.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-----RDIAMVFQnyalYPHM-- 92
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrKKVGLVFQ----FPEHql 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 ---TVAENMGFALKLAGTDKAEIRKRVGEAADMLDLG-AYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDA 168
Cdd:TIGR04521 96 feeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 169 KLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRP 227
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
22-212 |
1.86e-44 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 153.68 E-value: 1.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 22 DQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEpkdRDIAMVFQNYALYPHMTVAENMGFA 101
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR---EDTRLMFQDARLLPWKKVIDNVGLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 102 LKLAGTDKAEirkrvgEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQL 181
Cdd:PRK11247 106 LKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESL 179
|
170 180 190
....*....|....*....|....*....|.
gi 1423915573 182 QRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK11247 180 WQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-164 |
4.90e-44 |
|
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: 148.95 E-value: 4.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPHMTVAENM 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 99 GFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRK----PKALSGGQRQRVAMGRAIVRQPQVFLMDEPLS 164
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
26-195 |
5.23e-44 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 152.09 E-value: 5.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 26 LHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDV---THAEPKD-----RDIAMVFQNYALYPHMTVAEN 97
Cdd:PRK11124 23 LDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAirelrRNVGMVFQQYNLWPHLTVQQN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 98 MGFA-LKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRT 176
Cdd:PRK11124 103 LIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVS 182
|
170
....*....|....*....
gi 1423915573 177 QIAQLQrRLGTTTVYVTHD 195
Cdd:PRK11124 183 IIRELA-ETGITQVIVTHE 200
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-212 |
7.35e-44 |
|
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: 151.08 E-value: 7.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPkdrDIAMVFQNYALYPHMTVAENMGF 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 101 ALK--LAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQI 178
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190
....*....|....*....|....*....|....
gi 1423915573 179 AQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-286 |
9.00e-44 |
|
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: 154.50 E-value: 9.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAE------PKDRDIAMVFQNYALYPHMTVAEN 97
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflpPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 98 MGFALKLAgtDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQ 177
Cdd:TIGR02142 96 LRYGMKRA--RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 178 IAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAgFMGSPSMNLFTVPVTD-----GG 252
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA-REDQGSLIEGVVAEHDqhyglTA 252
|
250 260 270
....*....|....*....|....*....|....
gi 1423915573 253 VQIGDQLVPVPRdVLTAAGSEVIFGIRPEHVEIA 286
Cdd:TIGR02142 253 LRLGGGHLWVPE-NLGPTGARLRLRVPARDVSLA 285
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-212 |
3.18e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 149.73 E-value: 3.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 23 QLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAENMGF-- 100
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 101 --ALKLagtdKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQI 178
Cdd:PRK10771 97 npGLKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|....
gi 1423915573 179 AQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-214 |
4.26e-43 |
|
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: 148.67 E-value: 4.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLF--PGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHaEPKD--RDI 79
Cdd:cd03266 2 ITADALTKRFrdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEarRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 80 AMVFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLM 159
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1423915573 160 DEPLSNLDAkLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:cd03266 161 DEPTTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
15-224 |
4.97e-43 |
|
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: 149.37 E-value: 4.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 15 GSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-----RDIAMVFQNYALY 89
Cdd:TIGR02315 12 PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRIGMIFQHYNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PHMTVAEN--------MGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:TIGR02315 92 ERLTVLENvlhgrlgyKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 162 PLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELY 224
Cdd:TIGR02315 172 PIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-212 |
7.46e-43 |
|
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: 146.37 E-value: 7.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYp 90
Cdd:cd03228 10 YPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAYVPQDPFLF- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HMTVAENMgfalklagtdkaeirkrvgeaadmldlgayldrkpkaLSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAkl 170
Cdd:cd03228 89 SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDP-- 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1423915573 171 rvQTRTQIAQ--LQRRLGTTTVYVTHDqVEAMTMGDRVAVLKGG 212
Cdd:cd03228 130 --ETEALILEalRALAKGKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
15-212 |
1.05e-42 |
|
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: 148.48 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 15 GSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-----RDIAMVFQNYALY 89
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQIGMIFQQFNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PHMTVAEN--------MGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:cd03256 91 ERLSVLENvlsgrlgrRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 162 PLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHdQVE-AMTMGDRVAVLKGG 212
Cdd:cd03256 171 PVASLDPASSRQVMDLLKRINREEGITVIVSLH-QVDlAREYADRIVGLKDG 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-216 |
1.36e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 148.24 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDvPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDV---THAEPKD-----RDIAMVFQ 84
Cdd:COG4161 11 FYGSH-QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAirllrQKVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 85 NYALYPHMTVAENMGFA-LKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPL 163
Cdd:COG4161 90 QYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1423915573 164 SNLDAKLRVQTRTQIAQLQrRLGTTTVYVTHdQVE-AMTMGDRVAVL-KGGVLQQ 216
Cdd:COG4161 170 AALDPEITAQVVEIIRELS-QTGITQVIVTH-EVEfARKVASQVVYMeKGRIIEQ 222
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
22-206 |
2.14e-42 |
|
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: 146.61 E-value: 2.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 22 DQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRD---VTHAEPKD--RD-IAMVFQNYALYPHMTVA 95
Cdd:TIGR03608 15 DDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtppLNSKKASKfrREkLGYLFQNFALIENETVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 96 ENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKlrvqTR 175
Cdd:TIGR03608 95 ENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPK----NR 170
|
170 180 190
....*....|....*....|....*....|....
gi 1423915573 176 TQIAQLQRRL---GTTTVYVTHDQvEAMTMGDRV 206
Cdd:TIGR03608 171 DEVLDLLLELndeGKTIIIVTHDP-EVAKQADRV 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
17-214 |
3.76e-42 |
|
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: 144.85 E-value: 3.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVtHAEPKD--RDIAMVFQNYALYPHMTV 94
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEvkRRIGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AENMgfalklagtdkaeirkrvgeaadmldlgayldrkpkALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQT 174
Cdd:cd03230 91 RENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREF 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1423915573 175 RTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:cd03230 135 WELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-226 |
4.84e-42 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 155.76 E-value: 4.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYp 90
Cdd:COG2274 483 YPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HMTVAENmgFALKLAGTDKAEIRkrvgEAADMLDLGAYLDRKPK-----------ALSGGQRQRVAMGRAIVRQPQVFLM 159
Cdd:COG2274 562 SGTIREN--ITLGDPDATDEEII----EAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILIL 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 160 DEPLSNLDAklrvQTRTQIAQ-LQRRL-GTTTVYVTHDqVEAMTMGDRVAVLKGG----------VLQQCASPRELYRR 226
Cdd:COG2274 636 DEATSALDA----ETEAIILEnLRRLLkGRTVIIIAHR-LSTIRLADRIIVLDKGrivedgtheeLLARKGLYAELVQQ 709
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-226 |
7.19e-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: 153.76 E-value: 7.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 15 GSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALyPHM 92
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWVPQNPYL-FAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVAENMGFALKLAgtDKAEIRkrvgEAADMLDLGAYLDRKPK-----------ALSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:COG4988 426 TIRENLRLGRPDA--SDEELE----AALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 162 PLSNLDAklrvQTRTQIAQLQRRL--GTTTVYVTHDQvEAMTMGDRVAVLKGGVLQQCASPRELYRR 226
Cdd:COG4988 500 PTAHLDA----ETEAEILQALRRLakGRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-214 |
1.37e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.62 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAepkDRDIAMVFQNYALYPH--MTV 94
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---RRRIGYVPQRAEVDWDfpITV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AE--NMGF--ALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKl 170
Cdd:COG1121 95 RDvvLMGRygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAA- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1423915573 171 rvqTRTQIAQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:COG1121 174 ---TEEALYELLRELrreGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-209 |
1.79e-41 |
|
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: 144.89 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDR---DIAMVFQNYALYPHMTVAE 96
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRTFQIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NM----------GFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:cd03219 95 NVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1423915573 167 DAKLRVQTRTQIAQLqRRLGTTTVYVTHDQVEAMTMGDRVAVL 209
Cdd:cd03219 175 NPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVL 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
16-226 |
5.16e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 145.26 E-value: 5.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNyalyPH-- 91
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDirHKIGMVFQN----PDnq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 ---MTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDA 168
Cdd:PRK13650 94 fvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 169 KLRVQTRTQIAQLQRRLGTTTVYVTHDqVEAMTMGDRVAVLKGGVLQQCASPRELYRR 226
Cdd:PRK13650 174 EGRLELIKTIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
21-238 |
7.01e-41 |
|
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: 144.20 E-value: 7.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD---------------RDIAMVFQN 85
Cdd:TIGR03005 16 LDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpadekhlrqmrNKIGMVFQS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 86 YALYPHMTVAENMGFA-LKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLS 164
Cdd:TIGR03005 96 FNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMRPKVMLFDEVTS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 165 NLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGS 238
Cdd:TIGR03005 176 ALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKEERTREFLSK 249
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
17-223 |
8.54e-41 |
|
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: 142.89 E-value: 8.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVThAEPKD--RDIAMVFQNYALYPHMTV 94
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV-REPREvrRRIGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQT 174
Cdd:cd03265 91 WENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1423915573 175 RTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:cd03265 171 WEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
17-212 |
1.52e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 140.07 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQnyalyphmtv 94
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 aenmgfalklagtdkaeirkrvgeaadmldlgayldrkpkaLSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQT 174
Cdd:cd00267 81 -----------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*...
gi 1423915573 175 RTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:cd00267 120 LELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-226 |
1.97e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 149.93 E-value: 1.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 15 GSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYpHM 92
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGVVPQDTFLF-SG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVAENMGFALKLAgtDKAEIRkrvgEAADMLDLGAYLDRKPK-----------ALSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:COG1132 429 TIRENIRYGRPDA--TDEEVE----EAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 162 PLSNLDaklrvqTRTQiAQLQRRL-----GTTTVYVTH--DQVEAMtmgDRVAVLKGGVLQQCASPRELYRR 226
Cdd:COG1132 503 ATSALD------TETE-ALIQEALerlmkGRTTIVIAHrlSTIRNA---DRILVLDDGRIVEQGTHEELLAR 564
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-212 |
3.21e-40 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 142.53 E-value: 3.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSdvPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVT--HAEPkdrdiAMVFQNYALYP 90
Cdd:PRK11248 11 YGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpGAER-----GVVFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKL 170
Cdd:PRK11248 84 WRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1423915573 171 RVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK11248 164 REQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
18-209 |
5.70e-40 |
|
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: 141.71 E-value: 5.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 18 VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDR---DIAMVFQNYALYPHMTV 94
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlGIARTFQNPRLFPELTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AENM---------------GFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLM 159
Cdd:COG0411 97 LENVlvaaharlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 160 DEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDqVEA-MTMGDRVAVL 209
Cdd:COG0411 177 DEPAAGLNPEETEELAELIRRLRDERGITILLIEHD-MDLvMGLADRIVVL 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-228 |
9.16e-40 |
|
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: 147.99 E-value: 9.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYp 90
Cdd:COG4987 343 YPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRIAVVPQRPHLF- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HMTVAENmgfaLKLA--GTDKAEIRkrvgEAADMLDLGAYLDRKPK-----------ALSGGQRQRVAMGRAIVRQPQVF 157
Cdd:COG4987 422 DTTLREN----LRLArpDATDEELW----AALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPIL 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 158 LMDEPLSNLDAklrvQTRTQIAQLQRRL--GTTTVYVTHDQVeAMTMGDRVAVLKGGVLQQCASPRELYRRPA 228
Cdd:COG4987 494 LLDEPTEGLDA----ATEQALLADLLEAlaGRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
19-214 |
1.66e-39 |
|
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: 137.95 E-value: 1.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRdiamvfqnyalyphmtvAENM 98
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL-----------------ARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 99 GFalklagtdkaeirkrVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQI 178
Cdd:cd03214 76 AY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELL 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 1423915573 179 AQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:cd03214 141 RRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-228 |
6.66e-39 |
|
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: 139.17 E-value: 6.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-----RDIAMVFQNY--ALYPH 91
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQDSpsAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 MTVAENMGFALK-LAGTDKAEIRKRVGEAADMLDLGA-YLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAK 169
Cdd:TIGR02769 105 MTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 170 LRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG-VLQQCASPREL-YRRPA 228
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGqIVEECDVAQLLsFKHPA 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-212 |
8.02e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 144.39 E-value: 8.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGsdVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-RD--IAMVFQNYALY 89
Cdd:COG1129 14 FGG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAagIAIIHQELNLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PHMTVAEN--MGFALKLAGT-DKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:COG1129 92 PNLSVAENifLGREPRRGGLiDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 167 DAK-----LRVqtrtqIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:COG1129 172 TEReverlFRI-----IRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDG 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-227 |
1.40e-38 |
|
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: 144.06 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 18 VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDvDGGQILIGGRDVTHAEPKD-----RDIAMVFQN-YA-LYP 90
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HMTVAENMGFALKL--AGTDKAEIRKRVGEAadMLDLG---AYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:COG4172 378 RMTVGQIIAEGLRVhgPGLSAAERRARVAEA--LEEVGldpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 166 LDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQ--VEAMTmgDRVAVLKGGVLQQCASPRELYRRP 227
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHGLAYLFISHDLavVRALA--HRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-225 |
2.14e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 138.64 E-value: 2.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDI----AMVFQ--NYALYPHmT 93
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvGLVFQypEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGFALKLAGTDKAEIRKRVGEAADM--LDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLR 171
Cdd:PRK13637 101 IEKDIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 172 VQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYR 225
Cdd:PRK13637 181 DEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-271 |
4.45e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 137.45 E-value: 4.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNyalyP 90
Cdd:PRK13635 15 YPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGMVFQN----P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 H-----MTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:PRK13635 91 DnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 166 LDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTmGDRVAVLKGGVLQQCASPRELYRRPANVFVAGfMGSPsmnlFT 245
Cdd:PRK13635 171 LDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQEIG-LDVP----FS 244
|
250 260
....*....|....*....|....*.
gi 1423915573 246 VPVTDGGVQIGdqlVPVPRDVLTAAG 271
Cdd:PRK13635 245 VKLKELLKRNG---ILLPNTYLTMES 267
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-212 |
8.21e-38 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 136.36 E-value: 8.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTH---AEPKD--RDIAMVFQNY--ALYPHMT 93
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnrAQRKAfrRDIQMVFQDSisAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGFALK-LAGTDKAEIRKRVGEAADMLDLGA-YLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLR 171
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1423915573 172 VQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK10419 188 AGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-212 |
4.03e-37 |
|
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: 133.33 E-value: 4.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDR---DIAMVFQNYALYPHMT 93
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENmgfaLKLAGT--DKAEIRKRVGEAADML-DLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKL 170
Cdd:cd03224 92 VEEN----LLLGAYarRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1423915573 171 RVQTRTQIAQLqRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:cd03224 168 VEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-214 |
2.78e-36 |
|
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: 130.73 E-value: 2.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRdvtHAEPKDRDIAMVFQNYAL---YPhM 92
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK---PLEKERKRIGYVPQRRSIdrdFP-I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVAE--NMGFALK--LAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDA 168
Cdd:cd03235 86 SVRDvvLMGLYGHkgLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1423915573 169 KLRVQTRTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:cd03235 166 KTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-212 |
3.33e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 132.13 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGS--DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTH-AEPK-DRDIAMVFQNYAL 88
Cdd:COG1101 12 NPGTvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlPEYKrAKYIGRVFQDPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 89 --YPHMTVAENM----------GFALKLAGTDKAEIRKRVGEaadmLDLG--AYLDRKPKALSGGQRQRVAMGRAIVRQP 154
Cdd:COG1101 92 gtAPSMTIEENLalayrrgkrrGLRRGLTKKRRELFRELLAT----LGLGleNRLDTKVGLLSGGQRQALSLLMATLTKP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 155 QVFLMDEPLSNLDAKlrvqTRTQIAQLQRRL----GTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:COG1101 168 KLLLLDEHTAALDPK----TAALVLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
22-214 |
1.09e-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: 129.39 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 22 DQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTH------AEPKDRDIAMVFQNYALYPHMTVA 95
Cdd:TIGR02211 22 KGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKlssnerAKLRNKKLGFIYQFHHLLPDFTAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 96 ENMGFALKLAGTDKAEIRKRvgeAADMLD---LGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRV 172
Cdd:TIGR02211 102 ENVAMPLLIGKKSVKEAKER---AYEMLEkvgLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1423915573 173 QTRTQIAQLQRRLGTTTVYVTHDQVEAMTMgDRVAVLKGGVL 214
Cdd:TIGR02211 179 IIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
14-250 |
1.21e-35 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 132.52 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 14 PGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDR-----DIAMVFQN--Y 86
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsDIQMIFQDplA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 87 ALYPHMTVAENMGFALKL--AGTDKAEIRKRVgeAADMLDLGAY---LDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:PRK15079 110 SLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRV--KAMMLKVGLLpnlINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 162 PLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGSpsm 241
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSA--- 264
|
....*....
gi 1423915573 242 nlftVPVTD 250
Cdd:PRK15079 265 ----VPIPD 269
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
17-214 |
2.14e-35 |
|
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: 128.10 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVFQNYALYPHMTVAE 96
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEAPGFYPNLTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAGTDKaeirKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRT 176
Cdd:cd03268 92 NLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRE 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1423915573 177 QIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:cd03268 168 LILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
17-215 |
2.53e-35 |
|
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: 128.17 E-value: 2.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVThAEPKDRdIAMVFQNYALYPHMTVAE 96
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-IAARNR-IGYLPEERGLYPKMKVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRT 176
Cdd:cd03269 90 QLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1423915573 177 QIAQLQRRlGTTTVYVTH--DQVEAMTmgDRVAVLKGG--VLQ 215
Cdd:cd03269 170 VIRELARA-GKTVILSTHqmELVEELC--DRVLLLNKGraVLY 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-209 |
3.34e-35 |
|
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: 134.72 E-value: 3.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 3 TITYDRATRLFPGSDvPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIA 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 81 MVFQNYALYPHmTVAENMGFALKLAgtDKAEIR---KRVGeAADML-DLGAYLDRK----PKALSGGQRQRVAMGRAIVR 152
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDA--SDAEIRealERAG-LDEFVaALPQGLDTPigegGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 153 QPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRrlGTTTVYVTHDqVEAMTMGDRVAVL 209
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-217 |
4.71e-35 |
|
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: 127.31 E-value: 4.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGeFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRD-IAMVFQNYALYPHMTVAENM 98
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQEFGVYPNFTVREFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 99 GFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTqi 178
Cdd:cd03264 94 DYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRN-- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1423915573 179 aqLQRRLGTTTVYV--TH--DQVEAMTmgDRVAVLKGGVLQQC 217
Cdd:cd03264 172 --LLSELGEDRIVIlsTHivEDVESLC--NQVAVLNKGKLVFE 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-228 |
7.29e-35 |
|
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: 133.66 E-value: 7.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 14 PGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTS----LRMLAGLEDVDGGQILIGGRDVTHAEPKD------RDIAMVF 83
Cdd:COG4172 19 GGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERElrrirgNRIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 84 QN--YALYPHMTVAENMGFALKL-AGTDKAEIRKRvgeAADMLD----------LGAYldrkPKALSGGQRQRV--AMgr 148
Cdd:COG4172 99 QEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARAR---ALELLErvgipdperrLDAY----PHQLSGGQRQRVmiAM-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 149 AIVRQPQVFLMDEPLSNLDaklrVQTRTQI----AQLQRRLGTTTVYVTHDqveaMT----MGDRVAVLKGGVLQQCASP 220
Cdd:COG4172 170 ALANEPDLLIADEPTTALD----VTVQAQIldllKDLQRELGMALLLITHD----LGvvrrFADRVAVMRQGEIVEQGPT 241
|
....*...
gi 1423915573 221 RELYRRPA 228
Cdd:COG4172 242 AELFAAPQ 249
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-227 |
8.93e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 127.94 E-value: 8.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 1 MATITYDRATRLFPGSDVpaVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD---- 76
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 77 ------RDIAMVFQNYALYPHMTVAEN-MGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRA 149
Cdd:PRK11264 79 lirqlrQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 150 IVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQL--QRRlgtTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRP 227
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqEKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-212 |
7.10e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 127.84 E-value: 7.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGsdVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD---RDIAMVFQNYALY 89
Cdd:COG3845 15 FGG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIGMVHQHFMLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PHMTVAEN--MGF-ALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:COG3845 93 PNLTVAENivLGLePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 167 daklrvqTRTQIAQLQ---RRL---GTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:COG3845 173 -------TPQEADELFeilRRLaaeGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-212 |
8.07e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 124.07 E-value: 8.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAE-------PKDRdiamvfqnyALY 89
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEER---------GLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAk 169
Cdd:COG4152 84 PKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1423915573 170 LRVQT-RTQIAQLQRRlGTTTVYVTH--DQVEAMTmgDRVAVLKGG 212
Cdd:COG4152 163 VNVELlKDVIRELAAK-GTTVIFSSHqmELVEELC--DRIVIINKG 205
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
13-221 |
1.76e-32 |
|
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: 128.06 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYp 90
Cdd:TIGR03375 473 YPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HMTVAENMgfALKLAGTDKAEIRkrvgEAADMLDLGAYLDRKPK-----------ALSGGQRQRVAMGRAIVRQPQVFLM 159
Cdd:TIGR03375 552 YGTLRDNI--ALGAPYADDEEIL----RAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLL 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 160 DEPLSNLDAklrvQTRTQ-IAQLQRRL-GTTTVYVTHdQVEAMTMGDRVAVLKGG----------VLQQCASPR 221
Cdd:TIGR03375 626 DEPTSAMDN----RSEERfKDRLKRWLaGKTLVLVTH-RTSLLDLVDRIIVMDNGrivadgpkdqVLEALRKGR 694
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-214 |
1.81e-32 |
|
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: 119.07 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGsdVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD---RDIAMVFQnyaly 89
Cdd:cd03216 10 FGG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAMVYQ----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 phmtvaenmgfalklagtdkaeirkrvgeaadmldlgayldrkpkaLSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAK 169
Cdd:cd03216 83 ----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1423915573 170 LRVQTRTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:cd03216 117 EVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
17-228 |
4.72e-32 |
|
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: 120.09 E-value: 4.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDR---DIAMVFQNYALYPHMT 93
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPEGRRIFPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAEN--MGFAlklAGTDKAEIRKRVGEAADML-DLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKL 170
Cdd:COG0410 95 VEENllLGAY---ARRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 171 RVQTRTQIAQLqRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG--VLQqcASPRELYRRPA 228
Cdd:COG0410 172 VEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGriVLE--GTAAELLADPE 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-212 |
5.26e-32 |
|
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: 119.62 E-value: 5.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAM 81
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 82 VFQNYALYpHMTVAENMGFALKLAgTDkaeirKRVGEAADMLDLGAYLDRKPK-----------ALSGGQRQRVAMGRAI 150
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLGAPLA-DD-----ERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 151 VRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRrlGTTTVYVTHDQVeAMTMGDRVAVLKGG 212
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSG 214
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-195 |
2.35e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 120.84 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 6 YDRATRLFPGSD-VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-----RDI 79
Cdd:PRK11308 15 YPVKRGLFKPERlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 80 AMVFQN-YA-LYPHMTVAENMGFALKL-AGTDKAEIRKRVgeAADMLDLG---AYLDRKPKALSGGQRQRVAMGRAIVRQ 153
Cdd:PRK11308 95 QIVFQNpYGsLNPRKKVGQILEEPLLInTSLSAAERREKA--LAMMAKVGlrpEHYDRYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1423915573 154 PQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHD 195
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-212 |
2.61e-31 |
|
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: 117.36 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEpKDRDIAMVFQN--YALYPHmTVAENM 98
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-RRKSIGYVMQDvdYQLFTD-SVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 99 GFALKLAGTDKAEIRkrvgEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQI 178
Cdd:cd03226 94 LLGLKELDAGNEQAE----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELI 169
|
170 180 190
....*....|....*....|....*....|....
gi 1423915573 179 AQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:cd03226 170 RELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-195 |
4.05e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 117.28 E-value: 4.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-----RDIAMVFQNYALYPHMTV 94
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRvQT 174
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS-EG 175
|
170 180
....*....|....*....|.
gi 1423915573 175 RTQIAQLQRRLGTTTVYVTHD 195
Cdd:PRK10908 176 ILRLFEEFNRVGVTVLMATHD 196
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-227 |
6.04e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 118.75 E-value: 6.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGL---EDVDGGQILIGGRDVTHAEPKD-RD- 78
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDiREk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 79 IAMVFQNyalyPH-----MTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQ 153
Cdd:PRK13640 86 VGIVFQN----PDnqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 154 PQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAmTMGDRVAVLKGGVLQQCASPRELYRRP 227
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-229 |
9.91e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.45 E-value: 9.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLED-VDG----GQILIGGRDVTHaepKDRD-------IAMVFQ 84
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlIPGarveGEILLDGEDIYD---PDVDvvelrrrVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 85 NYALYPhMTVAENMGFALKLAG-TDKAEIRKRV----------GEAADMLDLGAYldrkpkALSGGQRQRVAMGRAIVRQ 153
Cdd:COG1117 100 KPNPFP-KSIYDNVAYGLRLHGiKSKSELDEIVeeslrkaalwDEVKDRLKKSAL------GLSGGQQQRLCIARALAVE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 154 PQVFLMDEPLSNLD--AKLRV-QTrtqIAQLQRRLgtTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPAN 229
Cdd:COG1117 173 PEVLLMDEPTSALDpiSTAKIeEL---ILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKD 246
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
13-223 |
1.01e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.78 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNyalyP 90
Cdd:PRK13632 17 YPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirKKIGIIFQN----P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 H-----MTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:PRK13632 93 DnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 166 LDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAmTMGDRVAVLKGGVLQQCASPREL 223
Cdd:PRK13632 173 LDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-227 |
2.26e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.17 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGL-----EDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALY 89
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIElrRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PHMTVAENMGFALKL--AGTDKAEIRKRVGEAADMLDL----GAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPL 163
Cdd:PRK14247 95 PNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 164 SNLDAKLRVQTRTQIAQLQRRLgtTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRP 227
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-211 |
2.62e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 115.26 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVT------HAEPKDRDIAMVFQNYALYPHMTVAEN 97
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdeeaRAKLRAKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 98 MGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAklrvQTRTQ 177
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR----QTGDK 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 1423915573 178 IA----QLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKG 211
Cdd:PRK10584 185 IAdllfSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-224 |
3.32e-30 |
|
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: 115.33 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPhMTV 94
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AENMGFALKLAGTDKAEIRKRVGEAADMLD---------LGAyldrKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:cd03249 94 AENIRYGKPDATDEEVEEAAKKANIHDFIMslpdgydtlVGE----RGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 166 LDAKlrVQTRTQIAQLQRRLGTTTVYVTHdQVEAMTMGDRVAVLKGGVLQQCASPRELY 224
Cdd:cd03249 170 LDAE--SEKLVQEALDRAMKGRTTIVIAH-RLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-228 |
4.17e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.66 E-value: 4.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVThAEPKDRD-------IAMVFQnyalYP-H 91
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVIT-AGKKNKKlkplrkkVGIVFQ----FPeH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 M----TVAENMGFALKLAGTDKAEIRKRVGEAADMLDLG-AYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:PRK13634 97 QlfeeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 167 DAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPA 228
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-237 |
4.89e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 115.32 E-value: 4.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDG-----GQILIGGRDVtHAEPKD-----RDIAMVFQNYALYPHMT 93
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNI-YSPDVDpievrREVGMVFQYPNPFPHLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGFALKLAG--TDKAEIRKRV----GEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD 167
Cdd:PRK14267 102 IYDNVAIGVKLNGlvKSKKELDERVewalKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANID 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 168 AKLRVQTRTQIAQLQRRLgtTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPAN----VFVAGFMG 237
Cdd:PRK14267 182 PVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHelteKYVTGALG 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
16-223 |
5.27e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 115.18 E-value: 5.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPHMT 93
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILRQENHINSRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGF--------ALKlagtdkAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQR--VAMgrAIVRQPQVFLMDEPL 163
Cdd:COG4604 92 VRELVAFgrfpyskgRLT------AEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRafIAM--VLAQDTDYVLLDEPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 164 SNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:COG4604 164 NNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
28-216 |
1.09e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 113.76 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 28 IEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTH------AEPKDRDIAMVFQNYALYPHMTVAENMGFA 101
Cdd:PRK11629 32 IGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakAELRNQKLGFIYQFHHLLPDFTALENVAMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 102 LKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQL 181
Cdd:PRK11629 112 LLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL 191
|
170 180 190
....*....|....*....|....*....|....*
gi 1423915573 182 QRRLGTTTVYVTHDQVEAMTMgDRVAVLKGGVLQQ 216
Cdd:PRK11629 192 NRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
25-238 |
1.26e-29 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 114.51 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 25 DLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVT-------HAEPKDRD--------IAMVFQNYALY 89
Cdd:COG4598 28 SLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgELVPADRRqlqrirtrLGMVFQSFNLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PHMTVAENMGFA-LKLAGTDKAEIRKRvgeAADMLD---LGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:COG4598 108 SHMTVLENVIEApVHVLGRPKAEAIER---AEALLAkvgLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 166 LDAK-----LRVqtrtqIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGS 238
Cdd:COG4598 185 LDPElvgevLKV-----MRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSS 256
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-203 |
1.36e-29 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 112.64 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 1 MATITYDRATRLFPGSDVPAVDQL----DLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDV--DGGQILIGGRDVTHAEP 74
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSGKQLlknvSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 75 KDRdIAMVFQNYALYPHMTVAENMGFALKLAGtdkaeirkrvgeaadmldlgayldrkpkaLSGGQRQRVAMGRAIVRQP 154
Cdd:cd03213 81 RKI-IGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 155 QVFLMDEPLSNLDAKlrvqTRTQIAQLQRRL---GTTTVYVTH----------DQVEAMTMG 203
Cdd:cd03213 131 SLLFLDEPTSGLDSS----SALQVMSLLRRLadtGRTIICSIHqpsseifelfDKLLLLSQG 188
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-214 |
1.40e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 111.92 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 14 PGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPH 91
Cdd:cd03246 11 PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgDHVGYLPQDDELFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 mTVAENMgfalklagtdkaeirkrvgeaadmldlgayldrkpkaLSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLR 171
Cdd:cd03246 91 -SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1423915573 172 VQTRTQIAQLQRRlGTTTVYVTHdQVEAMTMGDRVAVLKGGVL 214
Cdd:cd03246 133 RALNQAIAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-223 |
2.75e-29 |
|
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: 118.28 E-value: 2.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYP 90
Cdd:TIGR02203 340 YPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVALVSQDVVLFN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HmTVAENMGFAlKLAGTDKAEIRkRVGEAADMLDLgayLDRKPKA-----------LSGGQRQRVAMGRAIVRQPQVFLM 159
Cdd:TIGR02203 420 D-TIANNIAYG-RTEQADRAEIE-RALAAAYAQDF---VDKLPLGldtpigengvlLSGGQRQRLAIARALLKDAPILIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 160 DEPLSNLDAKLRVQTRTQIAQLQRrlGTTTVYVTHdQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:TIGR02203 494 DEATSALDNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-228 |
4.28e-29 |
|
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: 112.25 E-value: 4.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDR---DIAMVFQNYALYPHMTVA 95
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYLPQEASIFRKLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 96 ENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTR 175
Cdd:cd03218 94 ENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQ 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1423915573 176 TQIAQL-QRRLGtttVYVT-HDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPA 228
Cdd:cd03218 174 KIIKILkDRGIG---VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-216 |
4.40e-29 |
|
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: 112.32 E-value: 4.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAM 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 82 VFQNYALYpHMTVAENMGFalklaGTDKAEiRKRVGEAADMLDLGAYLDRKPKA-----------LSGGQRQRVAMGRAI 150
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAY-----GRPGAT-REEVEEAARAANAHEFIMELPEGydtvigergvkLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 151 VRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRrlGTTTVYVTHdQVEAMTMGDRVAVL-KGGVLQQ 216
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAH-RLSTIENADRIVVLeDGKIVER 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-225 |
6.89e-29 |
|
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: 116.83 E-value: 6.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 18 VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQ--ILIGGR--DVTHAEPKDRD-----IAMVFQNYAL 88
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEwvDMTKPGPDGRGrakryIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 89 YPHMTVAENMGFALKLAGTDKAEIRKRVG--EAADMLDLGA--YLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLS 164
Cdd:TIGR03269 377 YPHRTVLDNLTEAIGLELPDELARMKAVItlKMVGFDEEKAeeILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 165 NLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYR 225
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-215 |
7.75e-29 |
|
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: 111.66 E-value: 7.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD-RDIAMVF-QNYALYPHMTV 94
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFlRRIGVVFgQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQT 174
Cdd:cd03267 113 IDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1423915573 175 RTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQ 215
Cdd:cd03267 193 RNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-268 |
7.96e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.87 E-value: 7.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 15 GSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEP--KDRDIA-MVFQNyalyPH 91
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAgMVFQN----PD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 -----MTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:PRK13633 96 nqivaTIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 167 DAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTmGDRVAVLKGGVLQQCASPRELYRrpaNVFVAGFMGspsmnlFTV 246
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK---EVEMMKKIG------LDV 245
|
250 260
....*....|....*....|...
gi 1423915573 247 P-VTDGGVQIGDQLVPVPRDVLT 268
Cdd:PRK13633 246 PqVTELAYELKKEGVDIPSDILT 268
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-223 |
1.36e-28 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 110.78 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 15 GSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGG---RDVTHAEPKDRdIAMVFQNYALYPH 91
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDISRKSLRSM-IGVVLQDTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 mTVAENMGFALKLAgTDKAEIR--KRVGeAADML-----DLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLS 164
Cdd:cd03254 92 -TIMENIRLGRPNA-TDEEVIEaaKEAG-AHDFImklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 165 NLDAKlrVQTRTQIAQLQRRLGTTTVYVTHdQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:cd03254 169 NIDTE--TEKLIQEALEKLMKGRTSIIIAH-RLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
16-251 |
2.37e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 111.34 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNY-ALYPHM 92
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlrRKIGMVFQNPdNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRV 172
Cdd:PRK13642 98 TVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 173 QTRTQIAQLQRRLGTTTVYVTHDQVEAMTmGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFMGSPSMNLFTVPVTDG 251
Cdd:PRK13642 178 EIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDVPFSSNLMKDLRKNG 255
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-222 |
2.65e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 110.56 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 14 PGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEpkdrdIAMVFQnyalyPHMT 93
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLE-----LGAGFH-----PELT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQ 173
Cdd:COG1134 105 GRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 174 TRTQIAQLQRRlGTTTVYVTHD--QVEAMTmgDRVAVLKGGVLQQCASPRE 222
Cdd:COG1134 185 CLARIRELRES-GRTVIFVSHSmgAVRRLC--DRAIWLEKGRLVMDGDPEE 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
38-212 |
2.74e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 113.05 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 38 GPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAE------PKDRDIAMVFQNYALYPHMTVAENMGFALKlaGTDKAE 111
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclpPEKRRIGYVFQDARLFPHYKVRGNLRYGMA--KSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 112 IRKRVGeaadMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVY 191
Cdd:PRK11144 109 FDKIVA----LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170 180
....*....|....*....|.
gi 1423915573 192 VTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK11144 185 VSHSLDEILRLADRVVVLEQG 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-227 |
3.19e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.83 E-value: 3.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDI---------------AMVFQNYAL 88
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLkvadknqlrllrtrlTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 89 YPHMTVAEN-MGFALKLAGTDKAEIRKRVGEAADMLDL-GAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:PRK10619 104 WSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 167 DAKLrVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRP 227
Cdd:PRK10619 184 DPEL-VGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-229 |
1.08e-27 |
|
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: 108.61 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVD----GGQILIGGRDVTHAEPKDRDIAMVFQN--YALYPHMT 93
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGFALKLAGTDKAEIRKRVGEAADMLDL---GAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKL 170
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 171 RVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPAN 229
Cdd:TIGR02770 161 QARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-226 |
1.67e-27 |
|
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: 108.09 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYpHMTVAE 96
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrRAIGVVPQDTVLF-NDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFAlKLAGTDkAEIRkrvgEAADMLDLGAYLDRKPKA-----------LSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:cd03253 94 NIRYG-RPDATD-EEVI----EAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 166 LDaklrVQTRTQIAQLQRRL--GTTTVYVTHDQVEAMTmGDRVAVLKGGVLQQCASPRELYRR 226
Cdd:cd03253 168 LD----THTEREIQAALRDVskGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-229 |
2.28e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 108.21 E-value: 2.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDG------GQILIGGRDVTHAEPKD--RDIAMVFQNYA 87
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIDAIKlrKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 88 LYPHMTVAENMGFALKLAG-TDKAEIRKRVGEAADMLDLGA----YLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEP 162
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLWKevydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 163 LSNLDAKLRVQTRTQIAQLQRRLgtTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPAN 229
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-226 |
2.38e-27 |
|
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: 112.92 E-value: 2.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 2 ATITYDRATRLFPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDI 79
Cdd:COG4618 329 GRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 80 AMVFQNYALYPHmTVAENMGfalKLAGTDKAeirkRVGEAADMLDLGAYLDRKPK-----------ALSGGQRQRVAMGR 148
Cdd:COG4618 409 GYLPQDVELFDG-TIAENIA---RFGDADPE----KVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 149 AIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRlGTTTVYVTHDQvEAMTMGDRVAVLKGGVLQQCASPRELYRR 226
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-249 |
2.60e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.67 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNyalyPH-----M 92
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrSKVGLVFQD----PDdqvfsS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRV 172
Cdd:PRK13647 96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 173 QTRTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPrELYRRPANVFVAG---------FMGSPSMNL 243
Cdd:PRK13647 176 TLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQAGlrlplvaqiFEDLPELGQ 253
|
....*.
gi 1423915573 244 FTVPVT 249
Cdd:PRK13647 254 SKLPLT 259
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-228 |
5.16e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.77 E-value: 5.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDV---THAEPKDRDIAMVFQN-YALYPHMTV 94
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfSKLQGIRKLVGIVFQNpETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQT 174
Cdd:PRK13644 96 EEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 175 RTQIAQLQRRlGTTTVYVTHDqVEAMTMGDRVAVLKGGVLQQCASPRELYRRPA 228
Cdd:PRK13644 176 LERIKKLHEK-GKTIVYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
10-212 |
8.25e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 111.74 E-value: 8.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 10 TRLFPGSD--VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTH------AEPKDRDIAM 81
Cdd:PRK10535 11 RRSYPSGEeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadalAQLRREHFGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 82 VFQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:PRK10535 91 IFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 162 PLSNLDAKLRVQTRTQIAQLQRRlGTTTVYVTHD-QVEAmtMGDRVAVLKGG 212
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDpQVAA--QAERVIEIRDG 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-209 |
1.20e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.62 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGrdvthaepkDRDIAMVFQNYALYPHM--TV 94
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVPDSLplTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AE--NMGF--ALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKL 170
Cdd:NF040873 75 RDlvAMGRwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1423915573 171 RVQTRTQIAQLQRRlGTTTVYVTHDQVEAMTmGDRVAVL 209
Cdd:NF040873 155 RERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-207 |
1.21e-26 |
|
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: 105.59 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 15 GSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILI----GGRDVTHAEPKD------RDIAMVFQ 84
Cdd:COG4778 21 GKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPREilalrrRTIGYVSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 85 NYALYPHMT----VAEnmgfALKLAGTDKAEIRKRVGEAADMLDLGAYL-DRKPKALSGGQRQRVAMGRAIVRQPQVFLM 159
Cdd:COG4778 101 FLRVIPRVSaldvVAE----PLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1423915573 160 DEPLSNLDAKLRVQTRTQIAQLQRRlGTTTVYVTHDQvEAMtmgDRVA 207
Cdd:COG4778 177 DEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDE-EVR---EAVA 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-217 |
1.52e-26 |
|
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: 105.31 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVthaepkdrdiAMVFQNYALYPHMTVAE 96
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS----------SLLGLGGGFNPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRT 176
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1423915573 177 QIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQC 217
Cdd:cd03220 184 RLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-281 |
2.81e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.39 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPHMTV 94
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVPQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AE--NMG---FALKLAGTDKAEiRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAK 169
Cdd:PRK09536 95 RQvvEMGrtpHRSRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 170 LRVQTrtqiAQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRP-------ANVFVAGFMGSP 239
Cdd:PRK09536 174 HQVRT----LELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADtlraafdARTAVGTDPATG 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 240 SMNLFTVPVTDGGVQIGDQLV-------PVPRDV--LTAAGSEVIFGIRPE 281
Cdd:PRK09536 250 APTVTPLPDPDRTEAAADTRVhvvgggqPAARAVsrLVAAGASVSVGPVPE 300
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-252 |
3.51e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 109.56 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 6 YDRATRlfpgsDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDV-----THAEPKDRDIA 80
Cdd:PRK10261 330 LNRVTR-----EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspGKLQALRRDIQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 81 MVFQN-YA-LYPHMTVAENMGFALKLAGT-DKAEIRKRVGEAADMLDL-GAYLDRKPKALSGGQRQRVAMGRAIVRQPQV 156
Cdd:PRK10261 405 FIFQDpYAsLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKV 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 157 FLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGFM 236
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
250
....*....|....*.
gi 1423915573 237 GSpsmnlftVPVTDGG 252
Cdd:PRK10261 565 AA-------VPVADPS 573
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-222 |
3.82e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.81 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPHMTVAENM 98
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLAFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 99 GFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIV-------RQPQVFLMDEPLSNLDakLR 171
Cdd:COG4559 97 ALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD--LA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 172 VQTRT-QIA-QLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRE 222
Cdd:COG4559 175 HQHAVlRLArQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-212 |
5.89e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.94 E-value: 5.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 18 VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRD-----VTHAepkdRDIAMVF-QNYALYPH 91
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrrKEFA----RRIGVVFgQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 MTVAENmgFAL--KLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQR--VAMgrAIVRQPQVFLMDEPLSNLD 167
Cdd:COG4586 111 LPAIDS--FRLlkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRceLAA--ALLHRPKILFLDEPTIGLD 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1423915573 168 --AKLRVqtRTQIAQLQRRLGTTTVYVTHD--QVEAMTmgDRVAVLKGG 212
Cdd:COG4586 187 vvSKEAI--REFLKEYNRERGTTILLTSHDmdDIEALC--DRVIVIDHG 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-226 |
7.11e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 104.49 E-value: 7.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 5 TYDRATRLFPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRD--IAMV 82
Cdd:PRK15112 13 TFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 83 FQN--YALYPHMTVAENMGFALKL-AGTDKAEIRKRVGEAADMLDLGA-YLDRKPKALSGGQRQRVAMGRAIVRQPQVFL 158
Cdd:PRK15112 93 FQDpsTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 159 MDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTH---------DQVEAMTMGDrvAVLKGGVLQQCASP-RELYRR 226
Cdd:PRK15112 173 ADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQhlgmmkhisDQVLVMHQGE--VVERGSTADVLASPlHELTKR 248
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-222 |
9.79e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.70 E-value: 9.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPHMTVAENM 98
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLSFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 99 GFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVR------QPQVFLMDEPLSNLDakLRV 172
Cdd:PRK13548 98 AMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALD--LAH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 173 QTRT-QIA-QLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRE 222
Cdd:PRK13548 176 QHHVlRLArQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-263 |
9.96e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 105.58 E-value: 9.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 14 PGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDG---GQILIGGRDVTHAEPKD------RDIAMVFQ 84
Cdd:PRK09473 25 PDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKElnklraEQISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 85 N--YALYPHMTVAENMGFALKL-AGTDKAEIrkrVGEAADMLD----------LGAYldrkPKALSGGQRQRVAMGRAIV 151
Cdd:PRK09473 105 DpmTSLNPYMRVGEQLMEVLMLhKGMSKAEA---FEESVRMLDavkmpearkrMKMY----PHEFSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 152 RQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVF 231
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
|
250 260 270
....*....|....*....|....*....|..
gi 1423915573 232 VAGFMGSpsmnlftVPVTDGGvqiGDQLVPVP 263
Cdd:PRK09473 258 SIGLLNA-------VPRLDAE---GESLLTIP 279
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-223 |
1.13e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 104.89 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRD-IAMVFQNYALYPHMTVAENMG 99
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrVGVVPQFDNLDPDFTVRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 100 FALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAklrvQTRTQIA 179
Cdd:PRK13537 103 VFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP----QARHLMW 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1423915573 180 QLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:PRK13537 179 ERLRSLlarGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
15-227 |
1.36e-25 |
|
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: 108.12 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 15 GSDVPAV-DQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPH 91
Cdd:TIGR03797 462 RPDGPLIlDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAvrRQLGVVLQNGRLMSG 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 mTVAENMGFALKLAGTDKAEIRKRVGEAADMLD----LGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD 167
Cdd:TIGR03797 542 -SIFENIAGGAPLTLDEAWEAARMAGLAEDIRAmpmgMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 168 -----------AKLRVqTRTQIAQlqrRLGTTtvyvthdqVEAmtmgDRVAVLKGGVLQQCASPRELYRRP 227
Cdd:TIGR03797 621 nrtqaivseslERLKV-TRIVIAH---RLSTI--------RNA----DRIYVLDAGRVVQQGTYDELMARE 675
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-235 |
2.21e-25 |
|
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: 107.79 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 11 RLFPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDV-THAEPKDRDIAMVFQNYALY 89
Cdd:TIGR01257 936 KIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PHMTVAENMGFALKLAGTDKAEIRKrvgEAADML-DLGAYLDRKPKA--LSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:TIGR01257 1016 HHLTVAEHILFYAQLKGRSWEEAQL---EMEAMLeDTGLHHKRNEEAqdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 167 DAKLRVQTRTQIaqLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELyrrpANVFVAGF 235
Cdd:TIGR01257 1093 DPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL----KNCFGTGF 1155
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-226 |
3.66e-25 |
|
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: 101.79 E-value: 3.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPK--DRDIAM 81
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 82 VFQNYALYpHMTVAENmgfalkLAGTDKAEIRKRVGEAADMLDLGAYLDRKPK-----------ALSGGQRQRVAMGRAI 150
Cdd:cd03252 81 VLQENVLF-NRSIRDN------IALADPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 151 VRQPQVFLMDEPLSNLDaklrVQTRTQIAQLQRRL--GTTTVYVTHdQVEAMTMGDRVAVLKGGVLQQCASPRELYRR 226
Cdd:cd03252 154 IHNPRILIFDEATSALD----YESEHAIMRNMHDIcaGRTVIIIAH-RLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
19-227 |
3.88e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 101.64 E-value: 3.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHA---------------EPKdrdiamVF 83
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhkrarlgigylpqEAS------IF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 84 QNyalyphMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPL 163
Cdd:COG1137 91 RK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 164 SNLD--AKLRVQtrTQIAQL-QRRLGtttVYVT-HDQVEAMTMGDRVAVLKGG-VLQQcASPRELYRRP 227
Cdd:COG1137 165 AGVDpiAVADIQ--KIIRHLkERGIG---VLITdHNVRETLGICDRAYIISEGkVLAE-GTPEEILNNP 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-227 |
4.10e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 102.57 E-value: 4.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQN---YALYP 90
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLVFQNpddQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 hmTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKL 170
Cdd:PRK13652 95 --TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 171 RVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRP 227
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-224 |
6.41e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.75 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVP-AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNyalyPH- 91
Cdd:PRK13648 19 SDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQN----PDn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 ----MTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD 167
Cdd:PRK13648 95 qfvgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 168 AKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTmGDRVAVLKGGVLQQCASPRELY 224
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-264 |
7.41e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.12 E-value: 7.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHA------EPKDRDIAMVFQnyalYPHM- 92
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkeiKPVRKKVGVVFQ----FPESq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 ----TVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGA-YLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD 167
Cdd:PRK13643 97 lfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 168 AKLRVQTRTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRpANVFVAGFMGSPSMNLFTVP 247
Cdd:PRK13643 177 PKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE-VDFLKAHELGVPKATHFADQ 254
|
250
....*....|....*..
gi 1423915573 248 VTDGGVQIGDQLvPVPR 264
Cdd:PRK13643 255 LQKTGAVTFEKL-PITR 270
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-212 |
1.02e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 104.61 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 1 MATITYDRATRLFPGsdVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD---R 77
Cdd:PRK11288 2 SPYLSFDGIGKTFPG--VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 78 DIAMVFQNYALYPHMTVAENM---GFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQP 154
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 155 QVFLMDEPLSNLDAKLRVQTRTQIAQLqRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
17-212 |
1.77e-24 |
|
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: 100.16 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLED-VDGGQILIGGRDVTHAEPKD--RDIAMV---FQNYaLYP 90
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPpTYGNDVRLFGERRGGEDVWElrKRIGLVspaLQLR-FPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HMTVaENM---GF--ALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:COG1119 94 DETV-LDVvlsGFfdSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1423915573 166 LDAKLRVQTRTQIAQLQRRLGTTTVYVTHdQVEAMTMG-DRVAVLKGG 212
Cdd:COG1119 173 LDLGARELLLALLDKLAAEGAPTLVLVTH-HVEEIPPGiTHVLLLKDG 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
20-227 |
1.81e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.92 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPK----DRDIAMVFQN-----YAlyP 90
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevRKTVGIVFQNpddqlFA--P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 hmTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAkl 170
Cdd:PRK13639 95 --TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP-- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 171 rvQTRTQIAQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRP 227
Cdd:PRK13639 171 --MGASQIMKLLYDLnkeGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-225 |
2.09e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.01 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHaEPKDR-------DIAMVFQnyalYPHM 92
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH-KTKDKyirpvrkRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 -----TVAENMGFALKLAGTDKAEIRKRvgeAADML-DLG---AYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPL 163
Cdd:PRK13646 97 qlfedTVEREIIFGPKNFKMNLDEVKNY---AHRLLmDLGfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 164 SNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYR 225
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-224 |
3.11e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.47 E-value: 3.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 5 TYDRATRLfpgsDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHA-----EPKD--R 77
Cdd:PRK13645 15 TYAKKTPF----EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkkikEVKRlrK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 78 DIAMVFQ--NYALYPHmTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGA-YLDRKPKALSGGQRQRVAMGRAIVRQP 154
Cdd:PRK13645 91 EIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 155 QVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELY 224
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-227 |
3.27e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.03 E-value: 3.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPK--DRDIAMVFQNYALYPHmT 93
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGFALKLagTDKAEIRKRVGEA-AD---MLDLGAY---LDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:TIGR00958 571 VRENIAYGLTD--TPDEEIMAAAKAAnAHdfiMEFPNGYdteVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 167 DAklrvQTRTQIAQLQRRLGTTTVYVTHdQVEAMTMGDRVAVLKGGVLQQCASPRELYRRP 227
Cdd:TIGR00958 649 DA----ECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-263 |
3.30e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.29 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 14 PGSDVPA--VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVT----HAEPKD--RDIAMVFQ- 84
Cdd:PRK13641 14 PGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKlrKKVSLVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 85 -------NYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDlgayldRKPKALSGGQRQRVAMGRAIVRQPQVF 157
Cdd:PRK13641 94 peaqlfeNTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLIS------KSPFELSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 158 LMDEPLSNLDAKLRVQTrTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPaNVFVAGFMG 237
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK-EWLKKHYLD 245
|
250 260
....*....|....*....|....*.
gi 1423915573 238 SPSMNLFTVPVTDGGVQIGDQLVPVP 263
Cdd:PRK13641 246 EPATSRFASKLEKGGFKFSEMPLTID 271
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
3-215 |
5.49e-24 |
|
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: 102.81 E-value: 5.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 3 TITYDRATRLFPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIA 80
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 81 MVFQNYALYPHmTVAENMG-F-----------ALKLAGTDKAEIRKRVGEAADMLDLGAyldrkpkALSGGQRQRVAMGR 148
Cdd:TIGR01842 396 YLPQDVELFPG-TVAENIArFgenadpekiieAAKLAGVHELILRLPDGYDTVIGPGGA-------TLSGGQRQRIALAR 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 149 AIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRlGTTTVYVTHdQVEAMTMGDRVAVLKGGVLQ 215
Cdd:TIGR01842 468 ALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIA 532
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-216 |
6.13e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.25 E-value: 6.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYP 90
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HmTVAENMGFALklagtdkaEIRKRVGEAADMLDLGAY-------LDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPL 163
Cdd:PRK10247 95 D-TVYDNLIFPW--------QIRNQQPDPAIFLDDLERfalpdtiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1423915573 164 SNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEaMTMGDRVAVLK--GGVLQQ 216
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQphAGEMQE 219
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-227 |
6.68e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 100.20 E-value: 6.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 1 MATITYDRATRLFPGSDVP--AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLED----VDGGQILIGGRDVTHAEP 74
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 75 KDR------DIAMVFQN--YALYPHMTVAENMGFALKL-AGTDKAEIRKRvgeAADML------DLGAYLDRKPKALSGG 139
Cdd:PRK11022 81 KERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQR---AIDLLnqvgipDPASRLDVYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 140 QRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCAS 219
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
....*...
gi 1423915573 220 PRELYRRP 227
Cdd:PRK11022 238 AHDIFRAP 245
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-229 |
2.19e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.15 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVD-----GGQILIGGRDV----THAEPKDRDIAMVFQNYALYP 90
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysprTDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 hMTVAENMGFALKLAGT-DKAEIRKRV----------GEAADMLDLGAYldrkpkALSGGQRQRVAMGRAIVRQPQVFLM 159
Cdd:PRK14239 100 -MSIYENVVYGLRLKGIkDKQVLDEAVekslkgasiwDEVKDRLHDSAL------GLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 160 DEPLSNLDAKLRVQTRTQIAQLQRRLgtTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPAN 229
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-168 |
2.62e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 96.10 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 23 QLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRdIAMVFQNYALYPHMTVAENMGFAL 102
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA-CHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1423915573 103 KLAGTDKAEIRkrvgEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDA 168
Cdd:PRK13539 99 AFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
21-222 |
2.77e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.01 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPHMTVAENM 98
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALLPQHHLTPEGITVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 99 GFA----LKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQT 174
Cdd:PRK11231 98 AYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVEL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1423915573 175 RTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRE 222
Cdd:PRK11231 178 MRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-214 |
3.11e-23 |
|
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: 96.39 E-value: 3.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPK--DRDIAMVFQNYALYPHmT 93
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGFALKLAGTDkaeirkRVGEAAD---------MLDLGAYLD--RKPKALSGGQRQRVAMGRAIVRQPQVFLMDEP 162
Cdd:cd03248 104 LQDNIAYGLQSCSFE------CVKEAAQkahahsfisELASGYDTEvgEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 163 LSNLDAKLRVQTRTQIAQLQRRlgtTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:cd03248 178 TSALDAESEQQVQQALYDWPER---RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-194 |
3.36e-23 |
|
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: 95.50 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDV-THAEPKDRDIAMVFQNYALYPHMTVAEN 97
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 98 MGFALKLAGTDkaeiRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQ 177
Cdd:TIGR01189 94 LHFWAAIHGGA----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGL 169
|
170
....*....|....*...
gi 1423915573 178 IAQ-LQRrlGTTTVYVTH 194
Cdd:TIGR01189 170 LRAhLAR--GGIVLLTTH 185
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-212 |
4.31e-23 |
|
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: 96.05 E-value: 4.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDR---DIAMVFQNYALYPHMTVAE 96
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAYVPQGREIFPRLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 N--MGFALKlagtdKAEIRKRVGEAADMLD-LGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQ 173
Cdd:TIGR03410 95 NllTGLAAL-----PRRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKD 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1423915573 174 TRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:TIGR03410 170 IGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERG 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-212 |
9.23e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.09 E-value: 9.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGsdVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDR---DIA 80
Cdd:PRK09700 6 ISMAGIGKSFGP--VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 81 MVFQNYALYPHMTVAENM--GFAL--KLAGT---DKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQ 153
Cdd:PRK09700 84 IIYQELSVIDELTVLENLyiGRHLtkKVCGVniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 154 PQVFLMDEPLSNLDAKLRVQTRTQIAQLqRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-211 |
1.18e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.49 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDG-----GQILIGGRDV----THAEPKDRDIAMVFQNYALYPh 91
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerrVNLNRLRRQVSMVHPKPNLFP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 MTVAENMGFALKLAG-TDKAEIRKRVGEA---ADMLD-LGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:PRK14258 102 MSVYDNVAYGVKIVGwRPKLEIDDIVESAlkdADLWDeIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1423915573 167 DAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKG 211
Cdd:PRK14258 182 DPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-195 |
1.26e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 22 DQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIggrdvthaePKDRDIAMVFQNYALYPHMTVAEN--MG 99
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEPPLDDDLTVLDTvlDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 100 F-----------ALKLAGTDKAEIRKRVGEA-ADMLDLGAY-------------------LDRKPKALSGGQRQRVAMGR 148
Cdd:COG0488 86 DaelraleaeleELEAKLAEPDEDLERLAELqEEFEALGGWeaearaeeilsglgfpeedLDRPVSELSGGWRRRVALAR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1423915573 149 AIVRQPQVFLMDEPLSNLDAklrvQTrtqIAQLQRRLGT---TTVYVTHD 195
Cdd:COG0488 166 ALLSEPDLLLLDEPTNHLDL----ES---IEWLEEFLKNypgTVLVVSHD 208
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-212 |
1.30e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 94.95 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 18 VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTH---AEPKDRDIAMVFQNYALYPHMTV 94
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtAKIMREAVAIVPEGRRVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AENMGFALKLAgtDKAEIRKRVGEAADMLD-LGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQ 173
Cdd:PRK11614 98 EENLAMGGFFA--ERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1423915573 174 TRTQIAQLqRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK11614 176 IFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-207 |
1.35e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 95.62 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLED-VDG----GQILIGGRDV--THAEPKD--RDIAMVFQNYALYP 90
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlIPGfrveGKVTFHGKNLyaPDVDPVEvrRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HmTVAENMGFALKLAG--TDKAEIRKRVGEAADMLD-LGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD 167
Cdd:PRK14243 105 K-SIYDNIAYGARINGykGDMDELVERSLRQAALWDeVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1423915573 168 --AKLRVQtrTQIAQLQRRLgtTTVYVTHDQVEAMTMGDRVA 207
Cdd:PRK14243 184 piSTLRIE--ELMHELKEQY--TIIIVTHNMQQAARVSDMTA 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-214 |
1.83e-22 |
|
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: 94.26 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDG---GQILIGGRDVTHAEPKDRdIAMVFQNYALYPHMTVAENMGF 100
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKC-VAYVRQDDILLPGLTVRETLTY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 101 ALKLAG---TDKAEIRKRV-----GEAADmLDLGaylDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRV 172
Cdd:cd03234 105 TAILRLprkSSDAIRKKRVedvllRDLAL-TRIG---GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1423915573 173 QTRTQIAQLQRRlgTTTVYVTHDQ--VEAMTMGDRVAVLKGGVL 214
Cdd:cd03234 181 NLVSTLSQLARR--NRIVILTIHQprSDLFRLFDRILLLSSGEI 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-229 |
1.96e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.39 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 18 VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQI-------------LIGGRDVTHAEPKD---RDIAM 81
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHvrgADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 82 VFQN--YALYPHMTVAENMGFALKL---AGTDKAeirkrVGEAADMLDL------GAYLDRKPKALSGGQRQRVAMGRAI 150
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRLhqgASREEA-----MVEAKRMLDQvripeaQTILSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 151 VRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPAN 229
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
20-212 |
2.09e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.08 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGL---EDVDGGQILIGGRDVTHAEPKDRDI-------AMVFQNYALY 89
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIrksrantGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PHMTVAENMGFAlKLAGTD---------KAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMD 160
Cdd:PRK09984 99 NRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1423915573 161 EPLSNLD---AKLRVQTRTQIAQLQrrlGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK09984 178 EPIASLDpesARIVMDTLRDINQND---GITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-214 |
3.15e-22 |
|
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: 93.38 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 26 LHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDvthAEPKDRDIAMVFQNYAL---YP----HMTVAENM 98
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS---PGKGWRHIGYVPQRHEFawdFPisvaHTVMSGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 99 GFALKLAGTDKAEIRKrVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDaklrVQTRTQI 178
Cdd:TIGR03771 78 GHIGWLRRPCVADFAA-VRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLD----MPTQELL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1423915573 179 AQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:TIGR03771 153 TELFIELagaGTAILMTTHDLAQAMATCDRVVLLNGRVI 191
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-226 |
3.34e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.81 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVThAEPKDRDI-------AMVFQnyalYPH 91
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT-STSKNKDIkqirkkvGLVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 M-----TVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYL-DRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:PRK13649 96 SqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 166 LDAKLRVQTRTQIAQLQrRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRR 226
Cdd:PRK13649 176 LDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-213 |
3.42e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 95.67 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDV-THAEPKDRDIAMVFQNYALYPHMTVA 95
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLARARIGVVPQFDNLDLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 96 ENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTR 175
Cdd:PRK13536 133 ENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIW 212
|
170 180 190
....*....|....*....|....*....|....*...
gi 1423915573 176 TQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGV 213
Cdd:PRK13536 213 ERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
17-229 |
1.22e-21 |
|
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: 96.35 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAV-DQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPK--DRDIAMVFQNYALY---- 89
Cdd:TIGR01846 468 DSPEVlSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFsrsi 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 --------PHMTVaENMGFALKLAGTDKAEIRKRVGEAADMLDLGAyldrkpkALSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:TIGR01846 548 rdnialcnPGAPF-EHVIHAAKLAGAHDFISELPQGYNTEVGEKGA-------NLSGGQRQRIAIARALVGNPRILIFDE 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 162 PLSNLDAKLRVQTRTQIAQLQRrlGTTTVYVTHdQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPAN 229
Cdd:TIGR01846 620 ATSALDYESEALIMRNMREICR--GRTVIIIAH-RLSTVRACDRIIVLEKGQIAESGRHEELLALQGL 684
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-223 |
1.25e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 96.07 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGgQILIGGRDVTHAEPKD--RDIAMVFQNYALyPHMTVAE 96
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG-SLKINGIELRELDPESwrKHLSWVGQNPQL-PHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAgtDKAEI-----RKRVGEAADMLDLGayLDRKPK----ALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD 167
Cdd:PRK11174 442 NVLLGNPDA--SDEQLqqaleNAWVSEFLPLLPQG--LDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 168 A---KLRVQTRTQIAQlqrrlGTTTVYVTHdQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:PRK11174 518 AhseQLVMQALNAASR-----RQTTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-167 |
1.36e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 95.86 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAM 81
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 82 VFQNYALYpHMTVAENMGFalklAGTDKAEiRKRVGEAADMLDLGAYLDRKPKA-----------LSGGQRQRVAMGRAI 150
Cdd:PRK11176 422 VSQNVHLF-NDTIANNIAY----ARTEQYS-REQIEEAARMAYAMDFINKMDNGldtvigengvlLSGGQRQRIAIARAL 495
|
170
....*....|....*..
gi 1423915573 151 VRQPQVFLMDEPLSNLD 167
Cdd:PRK11176 496 LRDSPILILDEATSALD 512
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
13-211 |
2.17e-21 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 91.06 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEpKDRDIAMVFQNYALYPHM 92
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLGHLPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVAENMGFALKLAGTdkaEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAK-LR 171
Cdd:PRK13543 98 STLENLHFLCGLHGR---RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEgIT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1423915573 172 VQTRTQIAQLqrRLGTTTVYVTHDQVEAMTMGDRVAVLKG 211
Cdd:PRK13543 175 LVNRMISAHL--RGGGAALVTTHGAYAAPPVRTRMLTLEA 212
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-235 |
2.18e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.38 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAE----PKDRDIAMVFQNYAL 88
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrgllALRQQVATVFQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 89 YPHMT-VAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD 167
Cdd:PRK13638 89 QIFYTdIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 168 AKlrvqTRTQIAQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVFVAGF 235
Cdd:PRK13638 169 PA----GRTQMIAIIRRIvaqGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQAGL 235
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-194 |
2.36e-21 |
|
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: 89.52 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATrLFPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIggrdvthaePKDRDIAMVF 83
Cdd:cd03223 1 IELENLS-LATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 84 QNyalyPHMTvaenmgfalklAGTDKAEIrkrvgeaadmldlgAYldrkP--KALSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:cd03223 71 QR----PYLP-----------LGTLREQL--------------IY----PwdDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|...
gi 1423915573 162 PLSNLDaklrVQTRTQIAQLQRRLGTTTVYVTH 194
Cdd:cd03223 118 ATSALD----EESEDRLYQLLKELGITVISVGH 146
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
17-194 |
2.66e-21 |
|
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: 95.40 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAePKDR---DIAMVFQNYALYpHMT 93
Cdd:TIGR03796 491 EPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVAMVDQDIFLF-EGT 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMG--------FALKLAGTDKA---EIRKRVGEAADMLDLGAyldrkpKALSGGQRQRVAMGRAIVRQPQVFLMDEP 162
Cdd:TIGR03796 569 VRDNLTlwdptipdADLVRACKDAAihdVITSRPGGYDAELAEGG------ANLSGGQRQRLEIARALVRNPSILILDEA 642
|
170 180 190
....*....|....*....|....*....|..
gi 1423915573 163 LSNLDAklrvQTRTQIAQLQRRLGTTTVYVTH 194
Cdd:TIGR03796 643 TSALDP----ETEKIIDDNLRRRGCTCIIVAH 670
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-228 |
2.80e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 15 GSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTS----LRMLAGLEDV-DGGQILIGGRDVTHA-EPKDR-----DIAMVF 83
Cdd:PRK15134 19 QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTalsiLRLLPSPPVVyPSGDIRFHGESLLHAsEQTLRgvrgnKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 84 QN--YALYPHMTVAENMGFALKL-AGTDKAEIRkrvGEAADMLD----------LGAYldrkPKALSGGQRQRVAMGRAI 150
Cdd:PRK15134 99 QEpmVSLNPLHTLEKQLYEVLSLhRGMRREAAR---GEILNCLDrvgirqaakrLTDY----PHQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 151 VRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPA 228
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-223 |
2.91e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.89 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTH-AEPKDRD-IAMVFQNYALYP 90
Cdd:PRK11160 348 YPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQaISVVSQRVHLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HmTVAENMGFALKLAGTDK-AEIRKRVG-----EAADMLDlgAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLS 164
Cdd:PRK11160 428 A-TLRDNLLLAAPNASDEAlIEVLQQVGlekllEDDKGLN--AWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 165 NLDAklrvQTRTQIAQLQRRL--GTTTVYVTHdQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:PRK11160 505 GLDA----ETERQILELLAEHaqNKTVLMITH-RLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-167 |
4.95e-21 |
|
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: 94.12 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYpHMTVAENMGFA 101
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIGIVPQDTVLF-NDTIAYNIAYG 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 102 lkLAGTDKAEIRkrvgEAADMLDLGAYLDRKPKA-----------LSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD 167
Cdd:COG5265 456 --RPDASEEEVE----AAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-195 |
7.53e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 93.58 E-value: 7.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYpHMTVAE 96
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVSVCAQDAHLF-DTTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAgTDKAeirkrVGEAADMLDLGAYLDRKP-----------KALSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:TIGR02868 428 NLRLARPDA-TDEE-----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180 190
....*....|....*....|....*....|
gi 1423915573 166 LDAKLRVQTRTQIAQLQRrlGTTTVYVTHD 195
Cdd:TIGR02868 502 LDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-226 |
8.47e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 94.04 E-value: 8.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGE---FLvlvGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVthaEPKDRDIAM----VFQNYALYPHM 92
Cdd:NF033858 281 AVDHVSFRIRRGEifgFL---GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIATRRrvgyMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRV 172
Cdd:NF033858 355 TVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1423915573 173 QTRTQIAQLQRRLGTTTVYVTHDQVEAMTMgDRVAVLKGG-VLqQCASPRELYRR 226
Cdd:NF033858 435 MFWRLLIELSREDGVTIFISTHFMNEAERC-DRISLMHAGrVL-ASDTPAALVAA 487
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-212 |
9.58e-21 |
|
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: 88.14 E-value: 9.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRD-IAMVFQNYALYpH 91
Cdd:cd03247 10 YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVLNQRPYLF-D 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 MTVAENMGfalklagtdkaeirkrvgeaadmldlgayldrkpKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLR 171
Cdd:cd03247 89 TTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1423915573 172 VQTRTQIAQLQRrlGTTTVYVTHdQVEAMTMGDRVAVLKGG 212
Cdd:cd03247 135 RQLLSLIFEVLK--DKTLIWITH-HLTGIEHMDKILFLENG 172
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-226 |
1.03e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.23 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTS----LRMLAGledvdGGQILIGGRDVTHAEPKD-----RDIAMVFQ--NYAL 88
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTglalLRLINS-----QGEIWFDGQPLHNLNRRQllpvrHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 89 YPHMTVAENM--GFALKLAGTDKAEIRKRVGEAadMLDLGayLD-----RKPKALSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:PRK15134 376 NPRLNVLQIIeeGLRVHQPTLSAAQREQQVIAV--MEEVG--LDpetrhRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 162 PLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG-VLQQ--C----ASPRELYRR 226
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGeVVEQgdCervfAAPQQEYTR 523
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-233 |
1.03e-20 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 89.77 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 28 IEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHaepKDRDIAMVFQnyalyphMTVAENMGFALKLAGT 107
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY---KPQYIKADYE-------GTVRDLLSSITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 108 D---KAEIrkrvgeaADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRR 184
Cdd:cd03237 92 HpyfKTEI-------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEN 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 185 LGTTTVYVTHDQVEAMTMGDRVAVLKG--GVLQQCASPRELyRRPANVFVA 233
Cdd:cd03237 165 NEKTAFVVEHDIIMIDYLADRLIVFEGepSVNGVANPPQSL-RSGMNRFLK 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-212 |
1.79e-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: 87.49 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRD---IAMV---FQNYALYPHMT 93
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGfalklagtdkaeirkrvgeaadmldLGAYLdrkpkalSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDaklrVQ 173
Cdd:cd03215 95 VAENIA-------------------------LSSLL-------SGGNQQKVVLARWLARDPRVLILDEPTRGVD----VG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1423915573 174 TRTQIAQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:cd03215 139 AKAEIYRLIRELadaGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-194 |
1.99e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.56 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIggrdvthaePKDRDIAMVFQ----------NYALYP 90
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFLPQrpylplgtlrEALLYP 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HMtvAENMgfalklagtDKAEIR---KRVG--EAADMLDLGAYLDRKpkaLSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:COG4178 450 AT--AEAF---------SDAELRealEAVGlgHLAERLDEEADWDQV---LSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180 190
....*....|....*....|....*....|
gi 1423915573 166 LDAKLRVQTrtqIAQLQRRL-GTTTVYVTH 194
Cdd:COG4178 516 LDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-215 |
3.15e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 92.38 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 10 TRLFPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVThaepkdRDIAMVFQNYALY 89
Cdd:TIGR01257 1944 TKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL------TNISDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PH-------MTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEP 162
Cdd:TIGR01257 2018 PQfdaiddlLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 163 LSNLDAKLRVQTRTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQ 215
Cdd:TIGR01257 2098 TTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-194 |
3.21e-20 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 87.55 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 23 QLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPK-DRDIAMVFQNYALYPHMTVAENMGFA 101
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 102 LKLAGTDKAEirkrvgEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQL 181
Cdd:cd03231 98 HADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170
....*....|...
gi 1423915573 182 QRRlGTTTVYVTH 194
Cdd:cd03231 172 CAR-GGMVVLTTH 183
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-224 |
4.91e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.75 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPK----DRDIAMVFQ--NYALYPhMT 93
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklRESVGMVFQdpDNQLFS-AS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQ 173
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 174 TRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELY 224
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-228 |
7.57e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 88.75 E-value: 7.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGL----------EDVDGGQILIGGRDVTHAEPKD--------RD 78
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGDKKNNHELITNPYSKKiknfkelrRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 79 IAMVFQ--NYALYPHmTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLG-AYLDRKPKALSGGQRQRVAMGRAIVRQPQ 155
Cdd:PRK13631 118 VSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 156 VFLMDEPLSNLDAKLRvQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPA 228
Cdd:PRK13631 197 ILIFDEPTAGLDPKGE-HEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-212 |
9.94e-20 |
|
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: 85.98 E-value: 9.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 2 ATITYDRAtrlfPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRdvthaepkdrdIAM 81
Cdd:cd03250 6 ASFTWDSG----EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IAY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 82 VFQNyALYPHMTVAENMGFALKLagtDKAEIRKrVGEAA------DMLDLGaylDR-----KPKALSGGQRQRVAMGRAI 150
Cdd:cd03250 71 VSQE-PWIQNGTIRENILFGKPF---DEERYEK-VIKACalepdlEILPDG---DLteigeKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1423915573 151 VRQPQVFLMDEPLSNLDAklrvQTRTQIAQ--LQRRL--GTTTVYVTHdQVEAMTMGDRVAVLKGG 212
Cdd:cd03250 143 YSDADIYLLDDPLSAVDA----HVGRHIFEncILGLLlnNKTRILVTH-QLQLLPHADQIVVLDNG 203
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-223 |
1.11e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.87 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 1 MATITYDRATRLFPGSDVpaVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVT----HAEPKd 76
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARAR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 77 RDIAMVFQNYALYPHMTVAENMGFALKLAGTDKAEIRK-RVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQ 155
Cdd:PRK10895 78 RGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 156 VFLMDEPLSNLDAkLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:PRK10895 158 FILLDEPFAGVDP-ISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-205 |
1.66e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 85.24 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 22 DQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVThaepKDRDiamVFQNYALY--------PHMT 93
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRD---EYHQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGFALKLAGTDKAEirkRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKlrvq 173
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ---- 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1423915573 174 trtQIAQLQRRL------GTTTVYVTHDQVEAMTMGDR 205
Cdd:PRK13538 164 ---GVARLEALLaqhaeqGGMVILTTHQDLPVASDKVR 198
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-237 |
2.36e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.69 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVpaVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLED-VDG----GQILIGGRDVTHAEPK---DRDIAMVFQ 84
Cdd:PRK14271 31 FAGKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkVSGyrysGDVLLGGRSIFNYRDVlefRRRVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 85 NYALYPhMTVAENMgfalkLAGTDKAEI--RK--RVGEAADMLDLGAY------LDRKPKALSGGQRQRVAMGRAIVRQP 154
Cdd:PRK14271 109 RPNPFP-MSIMDNV-----LAGVRAHKLvpRKefRGVAQARLTEVGLWdavkdrLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 155 QVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLgtTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANV---- 230
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAetar 260
|
....*..
gi 1423915573 231 FVAGFMG 237
Cdd:PRK14271 261 YVAGLSG 267
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-212 |
2.40e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.20 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVthAEPKDRDIA---MV--FQNYALYPHMTV 94
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI--EGLPGHQIArmgVVrtFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AENMGFA-------------LKLAGTDKAEiRKRVGEAADMLD---LGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFL 158
Cdd:PRK11300 98 IENLLVAqhqqlktglfsglLKTPAFRRAE-SEALDRAATWLErvgLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 159 MDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-220 |
2.72e-19 |
|
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: 85.24 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 14 PGSDvPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPH 91
Cdd:cd03244 14 PNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 mTVAENMGF-----------ALKLAGtdkaeIRKRVGEAADMLDlgAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMD 160
Cdd:cd03244 93 -TIRSNLDPfgeysdeelwqALERVG-----LKEFVESLPGGLD--TVVEEGGENLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 161 EPLSNLDaklrVQTRTQIAQLQRRL--GTTTVYVTHdQVEAMTMGDRVAVLKGGVLQQCASP 220
Cdd:cd03244 165 EATASVD----PETDALIQKTIREAfkDCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-214 |
2.98e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.54 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD---RDIAMVFQN---YALY 89
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVPEDrkgEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PHMTVAENMGFAL--KLAG---TDKAEIRKRVGEAADMLDL-GAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPL 163
Cdd:COG1129 343 LDLSIRENITLASldRLSRgglLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 164 SNLDaklrVQTRTQIAQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:COG1129 423 RGID----VGAKAEIYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-212 |
4.08e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.12 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLED--VDGGQILIGGRDVTHAEPKDR---DIAMVFQNYALYPHMTVAEnm 98
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERaraGIFLAFQYPVEIPGVSVSN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 99 gFaLKLAGT-------DKAEIRKRVGEAADMLDLGA-YLDRkpkAL----SGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:COG0396 97 -F-LRTALNarrgeelSAREFLKLLKEKMKELGLDEdFLDR---YVnegfSGGEKKRNEILQMLLLEPKLAILDETDSGL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 167 DA-KLRVQTRTqIAQLqRRLGTTTVYVTH-----DQVEAmtmgDRVAVLKGG 212
Cdd:COG0396 172 DIdALRIVAEG-VNKL-RSPDRGILIITHyqrilDYIKP----DFVHVLVDG 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
13-223 |
5.24e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 85.59 E-value: 5.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDV-----THAEPKDRDIAMVFQNYA 87
Cdd:PRK11831 15 FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrSRLYTVRKRMSMLFQSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 88 LYPHMTVAENMGFALKLAGTDKAEI-RKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:PRK11831 95 LFTDMNVFDNVAYPLREHTQLPAPLlHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 167 DAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:PRK11831 175 DPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-228 |
6.11e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.14 E-value: 6.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTS----LRML-AGLEDVdGGQILIGGRDVTHAEPKDRDIAMVFQN--YAL 88
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILpAGVRQT-AGRVLLDGKPVAPCALRGRKIATIMQNprSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 89 YPHMTVAENMGFALKLAG--TDKAEIRkRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:PRK10418 93 NPLHTMHTHARETCLALGkpADDATLT-AALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 167 DAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPA 228
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
17-195 |
9.18e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 9.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGgrdvTHAE----PKDRDiamvfqnyALYPHM 92
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETVKigyfDQHQE--------ELDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVAENMGFALKlaGTDKAEIRKRVGeaaDMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDaklrV 172
Cdd:COG0488 395 TVLDELRDGAP--GGTEQEVRGYLG---RFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD----I 465
|
170 180
....*....|....*....|...
gi 1423915573 173 QTRTQIAQLQRRLGTTTVYVTHD 195
Cdd:COG0488 466 ETLEALEEALDDFPGTVLLVSHD 488
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-212 |
1.09e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.91 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 10 TRLFPGsdVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLE---DVDgGQILIGGRDVTHAEPKDRD---IAMVF 83
Cdd:PRK13549 12 TKTFGG--VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphgTYE-GEIIFEGEELQASNIRDTEragIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 84 QNYALYPHMTVAENM--GFALKLAG-TDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMD 160
Cdd:PRK13549 89 QELALVKELSVLENIflGNEITPGGiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1423915573 161 EPLSNLDAKlrvQTRTQ---IAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK13549 169 EPTASLTES---ETAVLldiIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
24-212 |
2.22e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.44 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHieDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRD------VTHAEPKDR-----DIAMVFQNYA--LYP 90
Cdd:PRK11701 27 FDLY--PGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlYALSEAERRrllrtEWGFVHQHPRdgLRM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HMTVAENMGFALKLAGTDK-AEIRKrvgEAADMLDL----GAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:PRK11701 105 QVSAGGNIGERLMAVGARHyGDIRA---TAGDWLERveidAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGG 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1423915573 166 LDakLRVQTR--TQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK11701 182 LD--VSVQARllDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-194 |
2.36e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.17 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 3 TITYDRATRLFPGSDvPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGG---RDVTHAEPKdRDI 79
Cdd:PRK13657 334 AVEFDDVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASLR-RNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 80 AMVFQNYALYpHMTVAENmgfaLKLAGTD--KAEIRkRVGEAADMLDlgaYLDRKPK-----------ALSGGQRQRVAM 146
Cdd:PRK13657 412 AVVFQDAGLF-NRSIEDN----IRVGRPDatDEEMR-AAAERAQAHD---FIERKPDgydtvvgergrQLSGGERQRLAI 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1423915573 147 GRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRrlGTTTVYVTH 194
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH 528
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-212 |
6.19e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 83.21 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRD----------------VTHAEPKDRDI---- 79
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekekvlekLVIQKTRFKKIkkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 80 ------AMVFQ--NYALYpHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLG-AYLDRKPKALSGGQRQRVAMGRAI 150
Cdd:PRK13651 102 eirrrvGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1423915573 151 VRQPQVFLMDEPLSNLDAklrvQTRTQIAQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDP----QGVKEILEIFDNLnkqGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
9-222 |
6.19e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.20 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 9 ATRLFPgsdvpavdqLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLedVDG-GQILIGGRDVTHAEPKD--RDIAMVFQN 85
Cdd:COG4138 9 AGRLGP---------ISAQVNAGELIHLIGPNGAGKSTLLARMAGL--LPGqGEILLNGRPLSDWSAAElaRHRAYLSQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 86 YALYPHMTVAENMGFALKlAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVR-------QPQVFL 158
Cdd:COG4138 78 QSPPFAMPVFQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 159 MDEPLSNLDAKLRVQTRTQIAQLqRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRE 222
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-223 |
7.94e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.34 E-value: 7.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 22 DQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPHMTVAENMG 99
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 100 FA----LKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTR 175
Cdd:PRK10253 104 RGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1423915573 176 TQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:PRK10253 184 ELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-225 |
9.29e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.76 E-value: 9.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPK--DRDIAMVFQNYALYPHMTVAENMGF- 100
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafARKVAYLPQQLPAAEGMTVRELVAIg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 101 ------ALklaGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQT 174
Cdd:PRK10575 110 rypwhgAL---GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 175 RTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYR 225
Cdd:PRK10575 187 LALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-216 |
2.87e-17 |
|
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: 83.25 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAepkDRDIAMVFQNY-ALYPHM---TV 94
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFINYlPQEPYIfsgSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AENMGFALK--------LAGTDKAEIRKRVGEAAdmLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:TIGR01193 565 LENLLLGAKenvsqdeiWAACEIAEIKDDIENMP--LGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 167 DAKLRVQTRTQIAQLQRRlgtTTVYVTHdQVEAMTMGDRVAVL-KGGVLQQ 216
Cdd:TIGR01193 643 DTITEKKIVNNLLNLQDK---TIIFVAH-RLSVAKQSDKIIVLdHGKIIEQ 689
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
16-214 |
3.70e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEP---KDRDIAMVFQNYALYPHM 92
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYLVPQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVAENMGFALKLAGTDKAEIRKRVGEAADMLDlgayLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAklrV 172
Cdd:PRK15439 102 SVKENILFGLPKRQASMQKMKQLLAALGCQLD----LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTP---A 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1423915573 173 QTRTQIAQLQ--RRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:PRK15439 175 ETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-226 |
7.63e-17 |
|
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: 77.95 E-value: 7.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLED--VDGGQILIGGRDVTHAEPKDR---DIAMVFQNYALYPHMTVAE-- 96
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERarlGIFLAFQYPPEIPGVKNADfl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 ---NMGFalklagtdkaeirkrvgeaadmldlgayldrkpkalSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAK-LRV 172
Cdd:cd03217 99 ryvNEGF------------------------------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDaLRL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 173 QTRTqIAQLqRRLGTTTVYVTH-----DQVEAmtmgDRVAVLKGGVLqQCASPRELYRR 226
Cdd:cd03217 143 VAEV-INKL-REEGKSVLIITHyqrllDYIKP----DRVHVLYDGRI-VKSGDKELALE 194
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
10-222 |
7.65e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.82 E-value: 7.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 10 TRLFPgsdvpavdqLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDvDGGQILIGGRDVTHAEPKDRD----------- 78
Cdd:PRK03695 10 TRLGP---------LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELArhraylsqqqt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 79 --IAM-VFQNYALYPHmtvaenmgfalklAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVR--- 152
Cdd:PRK03695 80 ppFAMpVFQYLTLHQP-------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 153 ----QPQVFLMDEPLSNLDAklrvqtrTQIAQLQR------RLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRE 222
Cdd:PRK03695 147 dinpAGQLLLLDEPMNSLDV-------AQQAALDRllselcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-266 |
8.22e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.39 E-value: 8.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGSDVpaVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDV--DGGQIL------------------ 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEV--LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 64 ------IGGR----DVTHAEPKD-------RDIAMVFQ-NYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDL 125
Cdd:TIGR03269 79 gepcpvCGGTlepeEVDFWNLSDklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 126 GAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDR 205
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 206 VAVLKGGVLQQCASPRELyrrpanvfVAGFMGSPSMnlftvPVTDGGVQIGDQLVPVpRDV 266
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEV--------VAVFMEGVSE-----VEKECEVEVGEPIIKV-RNV 285
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-212 |
1.17e-16 |
|
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: 81.02 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLE---DVDgGQILIGGRDVTHAEPKDRD---IAMVFQNYALYP 90
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgTWD-GEIYWSGSPLKASNIRDTEragIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HMTVAEN--MGFALKLAG--TDKAEIRKRVGEAADMLDLGAYLDRKPKA-LSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:TIGR02633 92 ELSVAENifLGNEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1423915573 166 LDAKLRVQTRTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-197 |
1.52e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 77.30 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVThaepKDR-----DIAMVFQNYA 87
Cdd:PRK13540 9 FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLctyqkQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 88 LYPHMTVAENMGFALKLAGTDKAeirkrVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD 167
Cdd:PRK13540 85 INPYLTLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180 190
....*....|....*....|....*....|
gi 1423915573 168 AKLRVQTRTQIaQLQRRLGTTTVYVTHDQV 197
Cdd:PRK13540 160 ELSLLTIITKI-QEHRAKGGAVLLTSHQDL 188
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-212 |
1.58e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 80.69 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 31 GEFLVLVGPSGCGKSTSLRMLAGLEDVDG--GQILIGGRDVThaEPKDRDIAMVFQNYALYPHMTVAENMGFA--LKLAG 106
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT--KQILKRTGFVTQDDILYPHLTVRETLVFCslLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 107 TDKAEIRKRVGEAAdMLDLGAYLDRKP-------KALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIA 179
Cdd:PLN03211 172 SLTKQEKILVAESV-ISELGLTKCENTiignsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLG 250
|
170 180 190
....*....|....*....|....*....|....
gi 1423915573 180 QLQRRlGTTTVYVTHD-QVEAMTMGDRVAVLKGG 212
Cdd:PLN03211 251 SLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
31-212 |
1.89e-16 |
|
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: 77.95 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 31 GEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRD------VTHAEPKDR-----DIAMVFQNYALYPHMTVAENMG 99
Cdd:TIGR02323 29 GEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelYQLSEAERRrlmrtEWGFVHQNPRDGLRMRVSAGAN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 100 FALKLAGTDKAEIRKRVGEAADMLDL----GAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTR 175
Cdd:TIGR02323 109 IGERLMAIGARHYGNIRATAQDWLEEveidPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLL 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 1423915573 176 TQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:TIGR02323 189 DLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQG 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-212 |
2.21e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 18 VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRDIAMVF------QNYALYPH 91
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAyipedrLGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 MTVAENMgfALKLAGT---------DKAEIRKRVGEAADMLDL-GAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:COG3845 351 MSVAENL--ILGRYRRppfsrggflDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 162 PLSNLDAKLRVQTRTQIAQLqRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-216 |
3.77e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 79.37 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYP 90
Cdd:PRK10789 323 YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrSRLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HmTVAENMgfALKLAGTDKAEIRkrvgEAADMLDLGAYLDRKPKA-----------LSGGQRQRVAMGRAIVRQPQVFLM 159
Cdd:PRK10789 403 D-TVANNI--ALGRPDATQQEIE----HVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 160 DEPLSNLDAklrvQTRTQIAQLQRRLGTT-TVYVTHDQVEAMTMGDRVAVLK-GGVLQQ 216
Cdd:PRK10789 476 DDALSAVDG----RTEHQILHNLRQWGEGrTVIISAHRLSALTEASEILVMQhGHIAQR 530
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-214 |
4.07e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.61 E-value: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 1 MATITYDRATRLFpgSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIgGRDVTHAE-PKD--R 77
Cdd:PRK11147 1 MSLISIHGAWLSF--SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDLIVARlQQDppR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 78 DIA-MVFqNYalyphmtVAENM---GFALK-------LAGTDKAE-IRKRVGEAADMLD-----------------LGAY 128
Cdd:PRK11147 78 NVEgTVY-DF-------VAEGIeeqAEYLKryhdishLVETDPSEkNLNELAKLQEQLDhhnlwqlenrinevlaqLGLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 129 LDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDaklrVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAV 208
Cdd:PRK11147 150 PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVD 225
|
....*.
gi 1423915573 209 LKGGVL 214
Cdd:PRK11147 226 LDRGKL 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-209 |
8.72e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 8.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 27 HIEDGEFLVLVGPSGCGKSTSLRMLAG--LEDVDG-GQILIGGRDVTHAEPKDRDiAMVFQNYALYPHMTVAENMGFA-- 101
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFrsPKGVKGsGSVLLNGMPIDAKEMRAIS-AYVQQDDLFIPTLTVREHLMFQah 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 102 LKL-AGTDKAEIRKRVGEAADMLDLGAYLDRK------PKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD---AKLR 171
Cdd:TIGR00955 126 LRMpRRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDsfmAYSV 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1423915573 172 VQTRTQIAQlqrrLGTTTVYVTH----------DQVEAMTMGdRVAVL 209
Cdd:TIGR00955 206 VQVLKGLAQ----KGKTIICTIHqpsselfelfDKIILMAEG-RVAYL 248
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-226 |
1.23e-15 |
|
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: 78.45 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 3 TITYDRATRLFPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGrdvthaepkdrDIAMV 82
Cdd:TIGR00957 636 SITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------SVAYV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 83 FQNyALYPHMTVAENMGFALKLagtdKAEIRKRVGEAADML-DL-------GAYLDRKPKALSGGQRQRVAMGRAIVRQP 154
Cdd:TIGR00957 705 PQQ-AWIQNDSLRENILFGKAL----NEKYYQQVLEACALLpDLeilpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 155 QVFLMDEPLSNLDAKLRVQTRTQIAQLQRRL-GTTTVYVTHDqVEAMTMGDRVAVLKGGVLQQCASPRELYRR 226
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-212 |
2.00e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.35 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGsdVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRD---IAMVFQNYALY 89
Cdd:PRK10762 14 FPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeagIGIIHQELNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PHMTVAEN--MG--FALKLAGTDkaeiRKRVGEAADMLDLGAYLDRKPKALSG----GQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:PRK10762 92 PQLTIAENifLGreFVNRFGRID----WKKMYAEADKLLARLNLRFSSDKLVGelsiGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 162 PLSNLdaklrvqTRTQIAQL------QRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK10762 168 PTDAL-------TDTETESLfrvireLKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-222 |
2.97e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 15 GSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD---RDIAMVFQNY---AL 88
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdnGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 89 YPHMTVAENMGFA--LKLAG-------TDKAEIRKRVGEAADMLDLG-AYLDRKPKALSGGQRQRVAMGRAIVRQPQVFL 158
Cdd:PRK09700 353 FPNFSIAQNMAISrsLKDGGykgamglFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1423915573 159 MDEPLSNLDaklrVQTRTQIAQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRE 222
Cdd:PRK09700 433 FDEPTRGID----VGAKAEIYKVMRQLaddGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
13-212 |
3.44e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 76.31 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGsdVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDV---THAEPKDRDIAMVFQNYALY 89
Cdd:PRK10982 8 FPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQELNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PHMTVAENM---GFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:PRK10982 86 LQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1423915573 167 DAKLRVQTRTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK10982 166 TEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
31-214 |
3.53e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.53 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 31 GEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDRdIAMVFQNYAL---YP-------HMTVAENMGF 100
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-VAYVPQSEEVdwsFPvlvedvvMMGRYGHMGW 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 101 aLKLAgtdKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDaklrVQTRTQIAQ 180
Cdd:PRK15056 112 -LRRA---KKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD----VKTEARIIS 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1423915573 181 LQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:PRK15056 184 LLRELrdeGKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-212 |
5.92e-15 |
|
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: 72.68 E-value: 5.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDG---GQILIGGRDVTH-AEPKDRDIAMVFQNYALYPHMTV 94
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEfAEKYPGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AENMGFALKLAGTDKaeIRKrvgeaadmldlgayldrkpkaLSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQT 174
Cdd:cd03233 101 RETLDFALRCKGNEF--VRG---------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1423915573 175 RTQIAQLQRRLGTTTVyVTHDQ--VEAMTMGDRVAVLKGG 212
Cdd:cd03233 158 LKCIRTMADVLKTTTF-VSLYQasDEIYDLFDKVLVLYEG 196
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
26-209 |
8.94e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.22 E-value: 8.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 26 LHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILiggrdvthAEPKDRdIAMVFQNYALYPHMTVAENMGFALKlA 105
Cdd:PRK09544 25 LELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLR-IGYVPQKLYLDTTLPLTVNRFLRLR-P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 106 GTDKAEIrkrvGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRL 185
Cdd:PRK09544 95 GTKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRREL 170
|
170 180
....*....|....*....|....
gi 1423915573 186 GTTTVYVTHDQVEAMTMGDRVAVL 209
Cdd:PRK09544 171 DCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-236 |
1.37e-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: 72.78 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 29 EDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQiliggrdvtHAEPKD-RDIAMVFQNYALYPHMT--VAENMGFALKLA 105
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---------FDDPPDwDEILDEFRGSELQNYFTklLEGDVKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 106 GTD---------------KAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKL 170
Cdd:cd03236 95 YVDlipkavkgkvgellkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 171 RVqtrtQIAQLQRRLGTTTVY---VTHDQVEAMTMGDRVAVLKG-----GVLQQCASPRElyrrPANVFVAGFM 236
Cdd:cd03236 175 RL----NAARLIRELAEDDNYvlvVEHDLAVLDYLSDYIHCLYGepgayGVVTLPKSVRE----GINEFLDGYL 240
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-196 |
3.50e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLedvdggqiliggrdvtHAEPKDRDIAMVFQNyALYPHMTVAENm 98
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA----------------LKGTPVAGCVDVPDN-QFGREASLIDA- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 99 gFALKLAGTDKAEIRKRVG--EAADMLdlgayldRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRT 176
Cdd:COG2401 106 -IGRKGDFKDAVELLNAVGlsDAVLWL-------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180
....*....|....*....|
gi 1423915573 177 QIAQLQRRLGTTTVYVTHDQ 196
Cdd:COG2401 178 NLQKLARRAGITLVVATHHY 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-231 |
3.76e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.30 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 28 IEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILiggrdvthaepKDRDIAMVFQNYALYPHMTVAENMGFALKLAGT 107
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-----------PELKISYKPQYIKPDYDGTVEDLLRSITDDLGS 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 108 D--KAEIRKRvgeaadmLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDaklrVQTRTQIAQLQRRL 185
Cdd:PRK13409 431 SyyKSEIIKP-------LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VEQRLAVAKAIRRI 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 186 ----GTTTVYVTHDQVEAMTMGDRVAVLKG--GVLQQCASPRELyRRPANVF 231
Cdd:PRK13409 500 aeerEATALVVDHDIYMIDYISDRLMVFEGepGKHGHASGPMDM-REGMNRF 550
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-227 |
4.71e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.25 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 18 VPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLED----VDGGQILIGGRDVTHAEPKDR------DIAMVFQN-- 85
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQEps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 86 YALYPHMTVAENMGFAL---KLAGT--DKAEIRKRvgEAADML------DLGAYLDRKPKALSGGQRQRVAMGRAIVRQP 154
Cdd:COG4170 100 SCLDPSAKIGDQLIEAIpswTFKGKwwQRFKWRKK--RAIELLhrvgikDHKDIMNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 155 QVFLMDEPLSNLDAKlrvqTRTQIAQLQRRL----GTTTVYVTHDqVEAMT-MGDRVAVLKGGVLQQCASPRELYRRP 227
Cdd:COG4170 178 RLLIADEPTNAMEST----TQAQIFRLLARLnqlqGTSILLISHD-LESISqWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
22-196 |
9.11e-14 |
|
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: 67.86 E-value: 9.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 22 DQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGgrdvthaepkdrdiamvfqnyalyphmtvaenmgfa 101
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------------------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 102 lklagtDKAEIrkrvgeaadmldlgAYLDRkpkaLSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDaklrVQTRTQIAQL 181
Cdd:cd03221 61 ------STVKI--------------GYFEQ----LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD----LESIEALEEA 112
|
170
....*....|....*
gi 1423915573 182 QRRLGTTTVYVTHDQ 196
Cdd:cd03221 113 LKEYPGTVILVSHDR 127
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-195 |
1.93e-13 |
|
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: 71.35 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 28 IEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQIliggrdvthaePKDRDIAMVFQnyalYP----HMTVAENMGFALK 103
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLKISYKPQ----YIspdyDGTVEEFLRSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 104 LAGTD---KAEIRKRvgeaadmLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDaklrVQTRTQIAQ 180
Cdd:COG1245 428 DDFGSsyyKTEIIKP-------LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VEQRLAVAK 496
|
170
....*....|....*....
gi 1423915573 181 LQRRL----GTTTVYVTHD 195
Cdd:COG1245 497 AIRRFaenrGKTAMVVDHD 515
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-192 |
2.84e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVthAEPKDRD-----IAMVFQ----Nya 87
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM--ADARHRRavcprIAYMPQglgkN-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 88 LYPHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD 167
Cdd:NF033858 89 LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
170 180
....*....|....*....|....*
gi 1423915573 168 AKLRVQTRTQIAQLQRRLGTTTVYV 192
Cdd:NF033858 169 PLSRRQFWELIDRIRAERPGMSVLV 193
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-195 |
3.33e-13 |
|
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: 70.58 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 29 EDGEFLVLVGPSGCGKSTSLRMLAG-----LEDVDggqiliggrdvthAEPKDRDIAMVFQNYALYPHMT--VAENMGFA 101
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGelkpnLGDYD-------------EEPSWDEVLKRFRGTELQDYFKklANGEIKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 102 LK----------LAGT-----DKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:COG1245 164 HKpqyvdlipkvFKGTvrellEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190
....*....|....*....|....*....|..
gi 1423915573 167 DaklrVQTRTQIAQLQRRL---GTTTVYVTHD 195
Cdd:COG1245 244 D----IYQRLNVARLIRELaeeGKYVLVVEHD 271
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4-212 |
5.09e-13 |
|
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: 66.88 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATrlfPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLED--VDGGQILIGGRDVTHAEPkdRDIAM 81
Cdd:cd03232 9 LNYTVPV---KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQ--RSTGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 82 VFQNYALYPHMTVAENMGFALKLAGtdkaeirkrvgeaadmldlgayldrkpkaLSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:cd03232 84 VEQQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1423915573 162 PLSNLDAklrvQTRTQIAQLQRRLGTT--TVYVTHDQVEAMTMG--DRVAVLKGG 212
Cdd:cd03232 135 PTSGLDS----QAAYNIVRFLKKLADSgqAILCTIHQPSASIFEkfDRLLLLKRG 185
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-212 |
7.44e-13 |
|
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: 66.97 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 15 GSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSL-RMLAGLEDVDG----GQILIGGRDVTHAEPKDR-DIAMVFQNYAL 88
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwSNKNESEPSFEATRSRNRySVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 89 YpHMTVAENMGFALKL------AGTDKAEIRKRVgeaaDMLDLG--AYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMD 160
Cdd:cd03290 91 L-NATVEENITFGSPFnkqrykAVTDACSLQPDI----DLLPFGdqTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 161 EPLSNLDAKLRVQTRTQ-IAQLQRRLGTTTVYVTHdQVEAMTMGDRVAVLKGG 212
Cdd:cd03290 166 DPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-216 |
1.11e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.85 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPHMTVAEn 97
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAVFTDFHLFDQLLGPE- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 98 mGFALKLAGTDKAEIRKRVGEAADMLDlGAYLDRKpkaLSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQ 177
Cdd:PRK10522 417 -GKPANPALVEKWLERLKMAHKLELED-GRISNLK---LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQV 491
|
170 180 190
....*....|....*....|....*....|....*....
gi 1423915573 178 IAQLQRRLGTTTVYVTHDQvEAMTMGDRVAVLKGGVLQQ 216
Cdd:PRK10522 492 LLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNGQLSE 529
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-227 |
3.96e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 66.36 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 14 PGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLED----VDGGQILIGGRDVTHAEPKDR------DIAMVF 83
Cdd:PRK15093 16 SDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERrklvghNVSMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 84 Q--NYALYPhmtvAENMGFALKLA---GTDKAEIRKRVG----EAADMLDLGAYLDRK------PKALSGGQRQRVAMGR 148
Cdd:PRK15093 96 QepQSCLDP----SERVGRQLMQNipgWTYKGRWWQRFGwrkrRAIELLHRVGIKDHKdamrsfPYELTEGECQKVMIAI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 149 AIVRQPQVFLMDEPLSNLDAklrvQTRTQIAQLQRRL----GTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELY 224
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEP----TTQAQIFRLLTRLnqnnNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV 247
|
...
gi 1423915573 225 RRP 227
Cdd:PRK15093 248 TTP 250
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
58-209 |
1.38e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 58 DGGQILIGGRDVTHAEPKD-RDIAMVFQNYALYPHMTVAENMGFalklaGTDKAeIRKRVGEAADMLDLGAYLDRKP--- 133
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKF-----GKEDA-TREDVKRACKFAAIDEFIESLPnky 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 134 --------KALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHdQVEAMTMGDR 205
Cdd:PTZ00265 1349 dtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDK 1427
|
....
gi 1423915573 206 VAVL 209
Cdd:PTZ00265 1428 IVVF 1431
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-225 |
1.70e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.77 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKsTSL--RMLAGLEDVDGGQILIGGrdvthaepkdrDIAMVFQNYALYpHMTVAE 96
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGK-TSLisAMLGELSHAETSSVVIRG-----------SVAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLAGtdkaeirKRVGEAADM------LDLGAYLDR-----KPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:PLN03232 698 NILFGSDFES-------ERYWRAIDVtalqhdLDLLPGRDLteigeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 166 LDAKLRVQTRTQIAQLQRRlGTTTVYVThDQVEAMTMGDRVAVLKGGVLQQCASPRELYR 225
Cdd:PLN03232 771 LDAHVAHQVFDSCMKDELK-GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-212 |
1.80e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.52 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 10 TRLFPGSDVPAVDQL---DLHIEDGEFLVLVGPSGCGKSTSLRMLAGleDVDGGQILIGGR----DVTHAEPKDR---DI 79
Cdd:TIGR00956 63 RKLKKFRDTKTFDILkpmDGLIKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGVitydGITPEEIKKHyrgDV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 80 AMVFQNYALYPHMTVAENMGFALKLA-------GTDKAEIRKRVGEAAdMLDLGAYLDRKPK-------ALSGGQRQRVA 145
Cdd:TIGR00956 141 VYNAETDVHFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKHIADVY-MATYGLSHTRNTKvgndfvrGVSGGERKRVS 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 146 MGRAIVRQPQVFLMDEPLSNLDAklrvQTRTQIA---QLQRRLGTTTVYVTHDQV--EAMTMGDRVAVLKGG 212
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDS----ATALEFIralKTSANILDTTPLVAIYQCsqDAYELFDKVIVLYEG 287
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-235 |
2.00e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 62.20 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 28 IEDGEFLVLVGPSGCGKSTSLRMLAGLEdvdggqiliggrdvthaEPKDRDIAmvfqnyalYPHMTVAenmgfalklagt 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQL-----------------IPNGDNDE--------WDGITPV------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 108 dkaeirkrvgeaadmldlgayldRKPK--ALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRL 185
Cdd:cd03222 65 -----------------------YKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 186 GTTTVYVTHDQVEAMTMGDRVAVLKG--GVLQQCASPRELyRRPANVFVAGF 235
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRIHVFEGepGVYGIASQPKGT-REGINRFLRGY 172
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-212 |
2.06e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.57 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 28 IEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILiggrdvthAEpkdRDIAMVFQNyALYPHMTVAENMGFalkLAGT 107
Cdd:PTZ00243 683 VPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------AE---RSIAYVPQQ-AWIMNATVRGNILF---FDEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 108 DKAEIRK--RVGE-AADMLDLGAYLD----RKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKL--RVqtrTQI 178
Cdd:PTZ00243 748 DAARLADavRVSQlEADLAQLGGGLEteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeRV---VEE 824
|
170 180 190
....*....|....*....|....*....|....
gi 1423915573 179 AQLQRRLGTTTVYVTHdQVEAMTMGDRVAVLKGG 212
Cdd:PTZ00243 825 CFLGALAGKTRVLATH-QVHVVPRADYVVALGDG 857
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
36-195 |
2.66e-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: 64.57 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 36 LVGPSGCGKSTSLRMLAGLE-DVDGGQILIGGRDVTH--AEPKDRDIAMVFQNYAlyphMTVAE-----------NMGFA 101
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDkDFNGEARPQPGIKVGYlpQEPQLDPTKTVRENVE----EGVAEikdaldrfneiSAKYA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 102 LKLAGTDK-----AEIRKRVgEAADMLDLGAYLDRKPKAL------------SGGQRQRVAMGRAIVRQPQVFLMDEPLS 164
Cdd:TIGR03719 112 EPDADFDKlaaeqAELQEII-DAADAWDLDSQLEIAMDALrcppwdadvtklSGGERRRVALCRLLLSKPDMLLLDEPTN 190
|
170 180 190
....*....|....*....|....*....|....
gi 1423915573 165 NLDAKlrvqtrtQIAQLQRRLGT---TTVYVTHD 195
Cdd:TIGR03719 191 HLDAE-------SVAWLERHLQEypgTVVAVTHD 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-220 |
3.19e-11 |
|
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: 62.04 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPHmTVAE 96
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKLagtDKAEIRK--RVGEAADmldlgayldrkpkALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDaklrVQT 174
Cdd:cd03369 101 NLDPFDEY---SDEEIYGalRVSEGGL-------------NLSQGQRQLLCLARALLKRPRVLVLDEATASID----YAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1423915573 175 RTQIAQLQRRL--GTTTVYVTHdQVEAMTMGDRVAVLKGGVLQQCASP 220
Cdd:cd03369 161 DALIQKTIREEftNSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-216 |
3.73e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.35 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDV---THAEPKdRDIAMVFQNYALyphm 92
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsslSHSVLR-QGVAMVQQDPVV---- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 tVAENMgFALKLAGTDKAEirKRVGEAADMLDLGAYLDRKPKA-----------LSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:PRK10790 427 -LADTF-LANVTLGRDISE--EQVWQALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 162 PLSNLDAKlrvqTRTQIAQLQR--RLGTTTVYVTHdQVEAMTMGDRVAVL-KGGVLQQ 216
Cdd:PRK10790 503 ATANIDSG----TEQAIQQALAavREHTTLVVIAH-RLSTIVEADTILVLhRGQAVEQ 555
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-195 |
3.78e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 28 IEDGEFLVLVGPSGCGKSTSLRMLAG-----LEDVDGgqiliggrDVTHAEPKDRDIAMVFQNY--ALYphmtvAENMGF 100
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGelipnLGDYEE--------EPSWDEVLKRFRGTELQNYfkKLY-----NGEIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 101 ALK----------LAGT-----DKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:PRK13409 163 VHKpqyvdlipkvFKGKvrellKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190
....*....|....*....|....*....|..
gi 1423915573 166 LDaklrVQTRTQIAQLQRRL--GTTTVYVTHD 195
Cdd:PRK13409 243 LD----IRQRLNVARLIRELaeGKYVLVVEHD 270
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-214 |
4.02e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKDR-DIAMVF-----QNYALYPHMTVAEN 97
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 98 --------MGFALKlAGTDKAeIRKRVGEAadmldLG---AYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:PRK15439 362 vcalthnrRGFWIK-PARENA-VLERYRRA-----LNikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 167 DaklrVQTRTQIAQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:PRK15439 435 D----VSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-231 |
5.84e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.03 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 28 IEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPHmTVAENMG------ 99
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQNVDpfleas 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 100 -----FALKLAGtdkaeIRKRVGEAADMLDlgayldrkPKALSG------GQRQRVAMGRAIVRQPQVF-LMDEPLSNLD 167
Cdd:PTZ00243 1412 saevwAALELVG-----LRERVASESEGID--------SRVLEGgsnysvGQRQLMCMARALLKKGSGFiLMDEATANID 1478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 168 AKLRVQTRtqiAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVF 231
Cdd:PTZ00243 1479 PALDRQIQ---ATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-215 |
1.02e-10 |
|
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: 62.92 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGL-EDVDGGQILIGGRDVTHAEPKD---RDIAMVFQN---YALYPHMT 93
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENmgfaLKLAGTDKAEIRKRVGEAADMLDLGAYLDR-KPKA---------LSGGQRQRVAMGRAIVRQPQVFLMDEPL 163
Cdd:TIGR02633 356 VGKN----ITLSVLKSFCFKMRIDAAAELQIIGSAIQRlKVKTaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 164 SNLDAKLRVQTRTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQ 215
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
237-283 |
1.03e-10 |
|
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: 56.44 E-value: 1.03e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 237 GSPSMNLFTVPVTDGGVQI--GDQLVPVPRDVLTA----AGSEVIFGIRPEHV 283
Cdd:pfam17912 1 GSPPMNFLPATVVEDGLLVlgGGVTLPLPEGQVLAlklyVGKEVILGIRPEHI 53
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-231 |
1.08e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQNYALYPHmTVAE 96
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFSG-TVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMG-FA-LKLAGTDKAEIRKRVGEAADMLDLG--AYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDaklrV 172
Cdd:PLN03232 1329 NIDpFSeHNDADLWEALERAHIKDVIDRNPFGldAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD----V 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 173 QTRTQIAQ-LQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVF 231
Cdd:PLN03232 1405 RTDSLIQRtIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-212 |
2.10e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.43 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 31 GEFLVLVGPSGCGKSTSLRMLAGLED---VDGGQILIGGRdvthaePKD----RDIAMVFQNYALYPHMTVAENMGFALK 103
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGR------PLDssfqRSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 104 L---AGTDKAEIRKRVGEAADMLDLGAYLDrkpkALSG--------GQRQRVAMGRAIVRQPQVFL-MDEPLSNLDAklr 171
Cdd:TIGR00956 863 LrqpKSVSKSEKMEYVEEVIKLLEMESYAD----AVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS--- 935
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1423915573 172 vQTRTQIAQLQRRLGTT--TVYVTHDQVEAMTMG--DRVAVL-KGG 212
Cdd:TIGR00956 936 -QTAWSICKLMRKLADHgqAILCTIHQPSAILFEefDRLLLLqKGG 980
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
24-167 |
2.38e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLED--VDGGQILIGGRDVTHAEPKDR---DIAMVFQnyalYPHMTVAENM 98
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRageGIFMAFQ----YPVEIPGVSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 99 GFALKlagTDKAEIRK-RVGEAADMLDLGAYLDRKPKAL---------------SGGQRQRVAMGRAIVRQPQVFLMDEP 162
Cdd:PRK09580 96 QFFLQ---TALNAVRSyRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCILDES 172
|
....*
gi 1423915573 163 LSNLD 167
Cdd:PRK09580 173 DSGLD 177
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-161 |
2.71e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 61.35 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVThaePKDRD-----IAMVFQNYALYPHmtvaenm 98
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREayrqlFSAVFSDFHLFDR------- 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 99 gfalkLAGTDKAEIRKRVGEAADMLDL--------GAYLDRkpkALSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:COG4615 421 -----LLGLDGEADPARARELLERLELdhkvsvedGRFSTT---DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-245 |
3.81e-10 |
|
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: 61.46 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRdvthaepkdrdIAMVFQNYALYPHmTVAENM 98
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------ISFSPQTSWIMPG-TIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 99 GFalklaGTDKAEIRKR-VGEAADMLDLGAYLDRKPK--------ALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDak 169
Cdd:TIGR01271 508 IF-----GLSYDEYRYTsVIKACQLEEDIALFPEKDKtvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD-- 580
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 170 lrVQTRTQIAQ--LQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELY-RRPAnvFVAGFMGSPSMNLFT 245
Cdd:TIGR01271 581 --VVTEKEIFEscLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQaKRPD--FSSLLLGLEAFDNFS 655
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-167 |
4.01e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.10 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGgrdvthaepKDRDIAMVFQNY-ALYPHMTVAEnmg 99
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG---------ETVKLAYVDQSRdALDPNKTVWE--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 100 falklagtdkaeirkRVGEAADMLDLG-------AYLDR----------KPKALSGGQRQRVAMGRAIVRQPQVFLMDEP 162
Cdd:TIGR03719 406 ---------------EISGGLDIIKLGkreipsrAYVGRfnfkgsdqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
....*
gi 1423915573 163 LSNLD 167
Cdd:TIGR03719 471 TNDLD 475
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-212 |
4.07e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD---RDIAMVFQNY---ALYPHM 92
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRkrdGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVAENMG------FALKLAGTDKAEIRKRVGEAADMLDLGA-YLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSN 165
Cdd:PRK10762 346 SVKENMSltalryFSRAGGSLKHADEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1423915573 166 LDaklrVQTRTQIAQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK10762 426 VD----VGAKKEIYQLINQFkaeGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-212 |
4.12e-10 |
|
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: 59.87 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRdvthaepkdrdIAMVFQNYALYPHm 92
Cdd:cd03291 45 LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------ISFSSQFSWIMPG- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVAENMgfalkLAGTDKAEIR-KRVGEAADM-LDLGAYLDRKPKA-------LSGGQRQRVAMGRAIVRQPQVFLMDEPL 163
Cdd:cd03291 113 TIKENI-----IFGVSYDEYRyKSVVKACQLeEDITKFPEKDNTVlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1423915573 164 SNLDaklrVQTRTQIAQ--LQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:cd03291 188 GYLD----VFTEKEIFEscVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-216 |
5.04e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.44 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQIliggrdvthaePKDRDIAMVFQNYALYPHMTVAENMG 99
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 100 FALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDaklrvQTRTQ-- 177
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD-----QTFAQkc 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1423915573 178 IAQLQ--RRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQ 216
Cdd:PRK13546 183 LDKIYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-223 |
5.42e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 16 SDVPAVDQLDLHIEDGEFLVLVGPSGCGKsTSL--RMLAGLEDVDGGQILIGGRdvthaepkdrdIAMVFQNYALYpHMT 93
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGK-TSLisAMLGELPPRSDASVVIRGT-----------VAYVPQVSWIF-NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VAENMGFALKLAgtdkaeiRKRVGEAADMLDLGAYLDRKPKA-----------LSGGQRQRVAMGRAIVRQPQVFLMDEP 162
Cdd:PLN03130 695 VRDNILFGSPFD-------PERYERAIDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1423915573 163 LSNLDAKLRVQTRTQIaqLQRRL-GTTTVYVThDQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:PLN03130 768 LSALDAHVGRQVFDKC--IKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
19-167 |
1.39e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.14 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQI------LIGGRDVTHAEPKDRDiamvfqnyalyphM 92
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenaNIGYYAQDHAYDFEND-------------L 399
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1423915573 93 TVAENMGfALKLAGTDKAEIRKRVGEaadMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD 167
Cdd:PRK15064 400 TLFDWMS-QWRQEGDDEQAVRGTLGR---LLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-194 |
1.51e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 59.38 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 14 PGSDVpAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIggrdvthaePKDRDIAMVFQNyalyPHMT 93
Cdd:TIGR00954 462 PNGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK---------PAKGKLFYVPQR----PYMT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 94 VaenmgfalklaGTDKAEI----------RKRVGEAA-----DMLDLGAYLDRK---------PKALSGGQRQRVAMGRA 149
Cdd:TIGR00954 528 L-----------GTLRDQIiypdssedmkRRGLSDKDleqilDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARL 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1423915573 150 IVRQPQVFLMDEPLSnldaKLRVQTRTQIAQLQRRLGTTTVYVTH 194
Cdd:TIGR00954 597 FYHKPQFAILDECTS----AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-171 |
3.03e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.03 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 38 GPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTH-AEPKdrdIAMVFQNYALYPHMTVAENMGFALKLagTDKAEIrkrV 116
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPY---CTYIGHNLGLKLEMTVFENLKFWSEI--YNSAET---L 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1423915573 117 GEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLR 171
Cdd:PRK13541 105 YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-223 |
3.72e-09 |
|
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: 58.42 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 7 DRATRLFPGSDVpAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD--RDIAMVFQ 84
Cdd:TIGR00957 1289 NYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrFKITIIPQ 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 85 NYALYP---HMTV-------AENMGFALKLAgtdkaEIRKRVGEAADMLDLGAylDRKPKALSGGQRQRVAMGRAIVRQP 154
Cdd:TIGR00957 1368 DPVLFSgslRMNLdpfsqysDEEVWWALELA-----HLKTFVSALPDKLDHEC--AEGGENLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 155 QVFLMDEPLSNLDaklrVQTRTQI-AQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPREL 223
Cdd:TIGR00957 1441 KILVLDEATAAVD----LETDNLIqSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
36-195 |
5.68e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 36 LVGPSGCGKSTSLRMLAGLE-DVDGGQILIGGRDVTH--AEPKdrdiamvfqnyaLYPHMTVAEN--------------- 97
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDkEFEGEARPAPGIKVGYlpQEPQ------------LDPEKTVRENveegvaevkaaldrf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 98 ----MGFALKLAGTDK-----AEIRKRVgEAADMLDLGAYLDRKPKAL------------SGGQRQRVAMGRAIVRQPQV 156
Cdd:PRK11819 106 neiyAAYAEPDADFDAlaaeqGELQEII-DAADAWDLDSQLEIAMDALrcppwdakvtklSGGERRRVALCRLLLEKPDM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1423915573 157 FLMDEPLSNLDAKlrvqtrtQIAQLQRRLGT---TTVYVTHD 195
Cdd:PRK11819 185 LLLDEPTNHLDAE-------SVAWLEQFLHDypgTVVAVTHD 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-194 |
7.08e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGG----RDVTHAEPKDRdIAMVFQNYALYPHm 92
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKWWRSK-IGVVSQDPLLFSN- 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVAENMGFAL--------------------------------KLAG-----------TDKAEIRK--RVGEAADMLDLG- 126
Cdd:PTZ00265 475 SIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscraKCAGdlndmsnttdsNELIEMRKnyQTIKDSEVVDVSk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 127 ---------AYLDR-------KPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTV 190
Cdd:PTZ00265 555 kvlihdfvsALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
....
gi 1423915573 191 YVTH 194
Cdd:PTZ00265 635 IIAH 638
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-167 |
1.23e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLE--DVDGGQILIGGRDVTHAEPKDRD---IAMVFQnyalYP- 90
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAhlgIFLAFQ----YPi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 91 HMTVAENMGF----------ALKLAGTDKAEIRKRVGEAADMLDLGA-YLDRK-PKALSGGQRQRVAMGRAIVRQPQVFL 158
Cdd:CHL00131 95 EIPGVSNADFlrlaynskrkFQGLPELDPLEFLEIINEKLKLVGMDPsFLSRNvNEGFSGGEKKRNEILQMALLDSELAI 174
|
....*....
gi 1423915573 159 MDEPLSNLD 167
Cdd:CHL00131 175 LDETDSGLD 183
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-167 |
4.19e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 37 VGPSGCGKSTSLRMLAGLEDVDGGQILIGgrDVTHaepkdrdIAMVFQNY-ALYPHMTVAENmgfalklagtdkaeirkr 115
Cdd:PRK11819 356 IGPNGAGKSTLFKMITGQEQPDSGTIKIG--ETVK-------LAYVDQSRdALDPNKTVWEE------------------ 408
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 116 VGEAADMLDLG-------AYLDR----------KPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD 167
Cdd:PRK11819 409 ISGGLDIIKVGnreipsrAYVGRfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| CysA_C_terminal |
pfam17850 |
CysA C-terminal regulatory domain; ABC (ATP-binding cassette) transporters share a common ... |
242-285 |
4.86e-08 |
|
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: 48.59 E-value: 4.86e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1423915573 242 NLFTVPVTDGGVQIGDQLVPVPRDVLtAAGSEVIFGIRPEHVEI 285
Cdd:pfam17850 1 NLFHGRVEDGRVRIGGLALPLPELAG-AEGSEVVAYVRPHDLEI 43
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
60-215 |
6.02e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 60 GQILIGGRDVTHAEPKD---RDIAMVFQN---YALYPHMTVAENMgfalKLAGTDKAEIRKRVGEAADMLDLGAYLDR-K 132
Cdd:PRK13549 318 GEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVGKNI----TLAALDRFTGGSRIDDAAELKTILESIQRlK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 133 PKA---------LSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRlGTTTVYVTHDQVEAMTMG 203
Cdd:PRK13549 394 VKTaspelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLS 472
|
170
....*....|..
gi 1423915573 204 DRVAVLKGGVLQ 215
Cdd:PRK13549 473 DRVLVMHEGKLK 484
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-167 |
1.37e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 31 GEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGgrdvTHAEpkdrdIAMvFQNY--ALYPHMTVAENMgfalklaGTD 108
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLE-----VAY-FDQHraELDPEKTVMDNL-------AEG 407
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 109 KAEI----RKR-VgeaadmldLGaYLD---------RKP-KALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLD 167
Cdd:PRK11147 408 KQEVmvngRPRhV--------LG-YLQdflfhpkraMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-230 |
2.72e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.37 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 21 VDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAG--LEDVDGGQILIGGRDVTHAEPKDR-DIAMVFQNYALYPHmtvAEN 97
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDVTLNGEPLAAiDAPRLARLRAVLPQ---AAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 98 MGFAL--------------KLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAI---------VRQP 154
Cdd:PRK13547 94 PAFAFsareivllgryphaRRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1423915573 155 QVFLMDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYrRPANV 230
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL-TPAHI 248
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-205 |
3.00e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.29 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 31 GEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIggrdvthaepkdrdiamvfqnyalyphmtvaenmgfalkLAGTDKA 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------IDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 111 eirkrvgEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAK-----LRVQTRTQIAQLQRRL 185
Cdd:smart00382 43 -------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeallLLLEELRLLLLLKSEK 115
|
170 180
....*....|....*....|
gi 1423915573 186 GTTTVYVTHDQVEAMTMGDR 205
Cdd:smart00382 116 NLTVILTTNDEKDLGPALLR 135
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
19-231 |
4.14e-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: 50.68 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 19 PAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHA--EPKDRDIAMVFQNYALY------- 89
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplHTLRSRLSIILQDPILFsgsirfn 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 --PHMTVAEN-MGFALKLAgtdkaEIRKRVGEAADMLDlgAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNL 166
Cdd:cd03288 115 ldPECKCTDDrLWEALEIA-----QLKNMVKSLPGGLD--AVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1423915573 167 D-AKLRVQTRTQIAQLQRRlgtTTVYVTHdQVEAMTMGDRVAVLKGGVLQQCASPRELYRRPANVF 231
Cdd:cd03288 188 DmATENILQKVVMTAFADR---TVVTIAH-RVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-214 |
5.18e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 26 LHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHAEPKD---RDIAMVFQNY---ALYPHMTVAENMG 99
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairAGIMLCPEDRkaeGIIPVHSVADNIN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 100 FALKLAGTDKAEIRKRVGEAADMLDLGAYL-------DRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDaklrV 172
Cdd:PRK11288 354 ISARRHHLRAGCLINNRWEAENADRFIRSLniktpsrEQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID----V 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1423915573 173 QTRTQIAQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVLKGGVL 214
Cdd:PRK11288 430 GAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
17-199 |
8.39e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGledvDGGQ------ILIG---GRDVTHAEPKdRDIAMVFQNYA 87
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DHPQgysndlTLFGrrrGSGETIWDIK-KHIGYVSSSLH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 88 L-YPHMTVAENM---GF----ALKLAGTDKAeiRKRVGEAADMLDLGAYLDRKP-KALSGGQRQRVAMGRAIVRQPQVFL 158
Cdd:PRK10938 347 LdYRVSTSVRNVilsGFfdsiGIYQAVSDRQ--QKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLI 424
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1423915573 159 MDEPLSNLDAKLRVQTRTQIAQLQRRLGTTTVYVTHDQVEA 199
Cdd:PRK10938 425 LDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-209 |
8.85e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 8.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 25 DLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGRDVTHA--EPKDRDIAMVFQ---NYALYPH-----MTV 94
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLsfEQLQKLVSDEWQrnnTDMLSPGeddtgRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 95 AEnmgfaLKLAGTDKAEirkRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDaklrVQT 174
Cdd:PRK10938 103 AE-----IIQDEVKDPA---RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD----VAS 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1423915573 175 RTQIAQLQRRL---GTTTVYVTHDQVEAMTMGDRVAVL 209
Cdd:PRK10938 171 RQQLAELLASLhqsGITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
17-229 |
2.45e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 17 DVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSlRMLAGLEDVDGGQ-------ILIGGRDVTHAEPKDRDIamvfqNYALY 89
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRrpwrf*tWCANRRALRRTIG*HRPV-----R*GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 90 PHMTVAENMGFALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAK 169
Cdd:NF000106 99 ESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1423915573 170 LRVQTRTQIAQLQRRlGTTTVYVTHDQVEA------MTMGDRVAVLKGGVLQQCASP---RELYRRPAN 229
Cdd:NF000106 179 TRNEVWDEVRSMVRD-GATVLLTTQYMEEAeqlaheLTVIDRGRVIADGKVDELKTKvggRTLQIRPAH 246
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
277-348 |
3.40e-06 |
|
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.
Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 44.15 E-value: 3.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 277 GIRPEHVEIADSG-GLKLEIDVVEELGSEAFVFGRttVNGRTENLVAR-VDWRNPPEKGQVVHVRVDEAHAHIF 348
Cdd:pfam08402 2 AIRPEKIRLAAAAnGLSGTVTDVEYLGDHTRYHVE--LAGGEELVVRVpNAHARPPAPGDRVGLGWDPEDAHVL 73
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-98 |
3.58e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 10 TRLFPGsdVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGL------EdvdgGQILIGG-----RDVTHAEpkDRD 78
Cdd:NF040905 8 TKTFPG--VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyE----GEILFDGevcrfKDIRDSE--ALG 79
|
90 100
....*....|....*....|
gi 1423915573 79 IAMVFQNYALYPHMTVAENM 98
Cdd:NF040905 80 IVIIHQELALIPYLSIAENI 99
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-214 |
3.86e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 4 ITYDRATRLFPGSDVpAVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAG-LEDVDGgqiliggrdVTHAEPKDRdIAMV 82
Cdd:PLN03073 509 ISFSDASFGYPGGPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQPSSG---------TVFRSAKVR-MAVF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 83 FQNYALYPHMTVAENMGFALKLAGTDKAEIRKRVGEaadmLDLGAYLDRKPK-ALSGGQRQRVAMGRAIVRQPQVFLMDE 161
Cdd:PLN03073 578 SQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGS----FGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDE 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 162 PLSNLDAklrvqtrtqiaqlqrrlgtttvyvthDQVEAMTMGdrVAVLKGGVL 214
Cdd:PLN03073 654 PSNHLDL--------------------------DAVEALIQG--LVLFQGGVL 678
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-194 |
1.45e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.81 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 20 AVDQLDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGGQILIGGrdvthaepkdrDIAMVFQNYALYPHMTVAENMG 99
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------SAALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 100 FALKLAGTDKAEIRKRVGEAADMLDLGAYLDRKPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIA 179
Cdd:PRK13545 108 LKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMN 187
|
170
....*....|....*
gi 1423915573 180 QLQRRlGTTTVYVTH 194
Cdd:PRK13545 188 EFKEQ-GKTIFFISH 201
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-167 |
2.61e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 36 LVGPSGCGKSTSLRMLAgLEDVDG----GQIL-----IGGRDVTHAE-PKDRDI---------AMVFQNYALYPHMTVAE 96
Cdd:PLN03073 208 LVGRNGTGKTTFLRYMA-MHAIDGipknCQILhveqeVVGDDTTALQcVLNTDIertqlleeeAQLVAQQRELEFETETG 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 97 NMGFALKlAGTDKAEIRKRVGEAADMLDL-GAYL-------------------DRKPKALSGGQRQRVAMGRAIVRQPQV 156
Cdd:PLN03073 287 KGKGANK-DGVDKDAVSQRLEEIYKRLELiDAYTaearaasilaglsftpemqVKATKTFSGGWRMRIALARALFIEPDL 365
|
170
....*....|.
gi 1423915573 157 FLMDEPLSNLD 167
Cdd:PLN03073 366 LLLDEPTNHLD 376
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
92-230 |
4.79e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 MTVAENMGF--ALKLAGTDKA-------EIRKRVGEaadMLDLGA---YLDRKPKALSGGQRQRVAMGRAI------Vrq 153
Cdd:TIGR00630 436 LSIREAHEFfnQLTLTPEEKKiaeevlkEIRERLGF---LIDVGLdylSLSRAAGTLSGGEAQRIRLATQIgsgltgV-- 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 154 pqVFLMDEPLSNLDAKlrvQTRTQIAQLQ--RRLGTTTVYVTHDQvEAMTMGDRV------AVLKGGVLQQCASPRELYR 225
Cdd:TIGR00630 511 --LYVLDEPSIGLHQR---DNRRLINTLKrlRDLGNTLIVVEHDE-DTIRAADYVidigpgAGEHGGEVVASGTPEEILA 584
|
....*
gi 1423915573 226 RPANV 230
Cdd:TIGR00630 585 NPDSL 589
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
31-169 |
5.90e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 31 GEFLVLVGPSGCGKSTSLRMLAGlEDVDG---GQILIGG---RDVTHAepkdRDIAMVFQNYALYPHMTVAENMGFA--L 102
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG-RKTGGyieGDIRISGfpkKQETFA----RISGYCEQNDIHSPQVTVRESLIYSafL 980
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1423915573 103 KLAG-TDKAEIRKRVGEAADMLDLGAYLDR-----KPKALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAK 169
Cdd:PLN03140 981 RLPKeVSKEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
135-212 |
7.92e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 7.92e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423915573 135 ALSGGQRQRVAMGRAIVRQPQVFLMDEPLSNLDAKLRVQTRTQIAQLQRRlGTTTVYVTHDQVEAMTMGDRVAVLKGG 212
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-245 |
1.62e-04 |
|
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: 43.75 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKSTSLRMLAGLEDVDGgQILIGG-----------RDVTHAEPKDRDIAMVFQNYALYPH- 91
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEG-EIQIDGvswnsvtlqtwRKAFGVIPQKVFIFSGTFRKNLDPYe 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 92 -------MTVAENMGFalklagtdKAEIRKRVGEAADMLDLGAYLdrkpkaLSGGQRQRVAMGRAIVRQPQVFLMDEPLS 164
Cdd:TIGR01271 1317 qwsdeeiWKVAEEVGL--------KSVIEQFPDKLDFVLVDGGYV------LSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 165 NLD-AKLRVQTRTqiaqLQRRLGTTTVYVTHDQVEAMTMGDRVAVLKGGVLQQCASPRELYRRpANVFVAGFMGSPSMNL 243
Cdd:TIGR01271 1383 HLDpVTLQIIRKT----LKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE-TSLFKQAMSAADRLKL 1457
|
..
gi 1423915573 244 FT 245
Cdd:TIGR01271 1458 FP 1459
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
13-195 |
2.21e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.54 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 13 FPGSDVPAVDQLDLHIEDGEFLVLVGPSGCGKSTSLrmLAGLedvdggqiliggrdvthAEPKDRDIAMVFQNYalYPHM 92
Cdd:cd03238 3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGL-----------------YASGKARLISFLPKF--SRNK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 93 TVaenmgfalklagtdkaeirkRVGEAADMLDLG-AY--LDRKPKALSGGQRQRVAMGRAIVRQPQ--VFLMDEPLSNLD 167
Cdd:cd03238 62 LI--------------------FIDQLQFLIDVGlGYltLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH 121
|
170 180
....*....|....*....|....*...
gi 1423915573 168 AKLRVQTRTQIAQLqRRLGTTTVYVTHD 195
Cdd:cd03238 122 QQDINQLLEVIKGL-IDLGNTVILIEHN 148
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
33-64 |
7.17e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 36.17 E-value: 7.17e-03
10 20 30
....*....|....*....|....*....|...
gi 1423915573 33 FLVLVGPSGCGKSTSLRML-AGLEDVDGGQILI 64
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLlEQLPEVRDSVVFV 39
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-206 |
7.26e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 37.62 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 24 LDLHIEDGEFLVLVGPSGCGKST----------------SLRMLA----GLEDVDggqiliggrDVTHAEPKDRDIAMVF 83
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrryveSLSAYArqflGQMDKP---------DVDSIEGLSPAIAIDQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423915573 84 QNYALYPHMTVAENMG----FALKLAgtdKAEIRKRVGEaadMLDLG-AYL--DRKPKALSGGQRQRVAMGRAIVRQPQ- 155
Cdd:cd03270 85 KTTSRNPRSTVGTVTEiydyLRLLFA---RVGIRERLGF---LVDVGlGYLtlSRSAPTLSGGEAQRIRLATQIGSGLTg 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1423915573 156 -VFLMDEPLSNLDAKlrvQTRTQIAQLQ--RRLGTTTVYVTHDQvEAMTMGDRV 206
Cdd:cd03270 159 vLYVLDEPSIGLHPR---DNDRLIETLKrlRDLGNTVLVVEHDE-DTIRAADHV 208
|
|
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