|
Name |
Accession |
Description |
Interval |
E-value |
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-356 |
0e+00 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 709.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAM 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGSPAM 240
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFIGSPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 241 NLLEGRISNAGTHFELESGMALPINWYYRGYAGRKMTLGIRPEHIGLTSQAdGGVPLVMDTLEMLGADNLAHGRWGEQKM 320
Cdd:PRK11650 241 NLLDGRVSADGAAFELAGGIALPLGGGYRQYAGRKLTLGIRPEHIALSSAE-GGVPLTVDTVELLGADNLAHGRWGGQPL 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 578222446 321 VVRLAHQERPKAGSTLWLHLPENHLHLFDGETGQRV 356
Cdd:PRK11650 320 VVRLPHQERPAAGSTLWLHLPANQLHLFDADTGRRI 355
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-356 |
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 578222446 1 MAGLKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAM 80
Cdd:COG3839 1 MASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGSPAM 240
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 241 NLLEGRISNAGTHFElesGMALPINWYYRGYAGRKMTLGIRPEHIGLTSQADGGVPLVMDTLEMLGADNLAHGRWGEQKM 320
Cdd:COG3839 240 NLLPGTVEGGGVRLG---GVRLPLPAALAAAAGGEVTLGIRPEHLRLADEGDGGLEATVEVVEPLGSETLVHVRLGGQEL 316
|
330 340 350
....*....|....*....|....*....|....*.
gi 578222446 321 VVRLAHQERPKAGSTLWLHLPENHLHLFDGETGQRV 356
Cdd:COG3839 317 VARVPGDTRLRPGDTVRLAFDPERLHLFDAETGRRL 352
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-348 |
1.82e-149 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 425.28 E-value: 1.82e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAM 80
Cdd:COG3842 3 MPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGSpaM 240
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGE--A 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 241 NLLEGRI-SNAGTHFELEsGMALPINWYYRGYAGRKMTLGIRPEHIGLTSQA-DGGVPLVMDTLEMLGADNLAHGRWGE- 317
Cdd:COG3842 240 NLLPGTVlGDEGGGVRTG-GRTLEVPADAGLAAGGPVTVAIRPEDIRLSPEGpENGLPGTVEDVVFLGSHVRYRVRLGDg 318
|
330 340 350
....*....|....*....|....*....|...
gi 578222446 318 QKMVVRLAHQER--PKAGSTLWLHLPENHLHLF 348
Cdd:COG3842 319 QELVVRVPNRAAlpLEPGDRVGLSWDPEDVVVL 351
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-355 |
5.65e-146 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 417.12 E-value: 5.65e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAM 80
Cdd:PRK11000 1 MASVTLRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGSPAM 240
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 241 NLLEGRISNA---GTHFELESGMALPINWYYRGY-AGRKMTLGIRPEHIGLTSQADGGVPLVMDTLEMLGADNLAHGRW- 315
Cdd:PRK11000 240 NFLPVKVTATaieQVQVELPNRQQVWLPVEGRGVqVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGNETQIHIQIp 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 578222446 316 -GEQKMVVRLAHQERPKAGSTLWLHLPENHLHLF--DGETGQR 355
Cdd:PRK11000 320 aIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFreDGTACRR 362
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-217 |
1.39e-126 |
|
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: 361.96 E-value: 1.39e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQ 83
Cdd:cd03301 1 VELENVTKRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578222446 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIG 217
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-347 |
8.87e-114 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 334.42 E-value: 8.87e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 3 GLKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRV-TEMEPKDRGIAMV 81
Cdd:COG1118 2 SIEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 162 LSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGspAMN 241
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLG--CVN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 242 LLEGRISNAGTHFElesGMALPinwYYRGYAGRKMTLGIRPEHIGLTSQADG--GVPLVMDTLEMLGAD---NLAHGRWG 316
Cdd:COG1118 239 VLRGRVIGGQLEAD---GLTLP---VAEPLPDGPAVAGVRPHDIEVSREPEGenTFPATVARVSELGPEvrvELKLEDGE 312
|
330 340 350
....*....|....*....|....*....|....*
gi 578222446 317 EQKMVVRLAHQE----RPKAGSTLWLHLPENHLHL 347
Cdd:COG1118 313 GQPLEAEVTKEAwaelGLAPGDPVYLRPRPARVFL 347
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-236 |
2.10e-113 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 329.20 E-value: 2.10e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQ 83
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIG 236
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-217 |
6.35e-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: 319.47 E-value: 6.35e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQ 83
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578222446 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIG 217
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-247 |
1.20e-106 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 317.27 E-value: 1.20e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQ 83
Cdd:PRK09452 15 VELRGISKSFDGKE-VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGSpaMNLL 243
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGE--INIF 251
|
....
gi 578222446 244 EGRI 247
Cdd:PRK09452 252 DATV 255
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-348 |
9.78e-106 |
|
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: 314.28 E-value: 9.78e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAM 80
Cdd:TIGR03265 2 SPYLSIDNIRKRF-GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGSpaM 240
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGE--V 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 241 NLLEGRISNAGTHFELESGMALPINWYYRGYAGRkmtLGIRPEHI--GLTSQADGGVPLVMDTLEMLGA---DNLAHGRW 315
Cdd:TIGR03265 239 NWLPGTRGGGSRARVGGLTLACAPGLAQPGASVR---LAVRPEDIrvSPAGNAANLLLARVEDMEFLGAfyrLRLRLEGL 315
|
330 340 350
....*....|....*....|....*....|....*..
gi 578222446 316 GEQKMVVRLAHQERPK----AGSTLWLHLPENHLHLF 348
Cdd:TIGR03265 316 PGQALVADVSASEVERlgirAGQPIWIELPAERLRAF 352
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
5-297 |
1.08e-102 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 306.54 E-value: 1.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 5 KLQAVTKSW-DGKTQV--IQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTE-----MEPKDR 76
Cdd:NF040933 4 RVENVTKIFkKGKKEVvaLDNVNLEIKSGEFFGILGPSGHGKTTFLRIIAGLEVPTDGEIYFDDKLVASpgkiiVPPEDR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 77 GIAMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVF 156
Cdd:NF040933 84 NIGMVFQNWALYPNMTVFDNIAFPLKIKKVPKDEIEKKVKEVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 157 LFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIG 236
Cdd:NF040933 164 LLDEPFSNLDARIRDSARALVKKIQRELKITTIIVSHDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFVARLIG 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 237 SpaMNLLEGRISNAGthFELESGMALPINWYYRGyaGRKMTLGIRPEHIGLT----SQADGGVPL 297
Cdd:NF040933 244 D--INLLEGKVEEEG--LVDGNDLKIPLPNPKLE--AGEVIIGIRPEDIDISesdmRLPPGFVEV 302
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-340 |
3.32e-102 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 305.11 E-value: 3.32e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQ 83
Cdd:PRK11432 7 VVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGSPamNLL 243
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDA--NIF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 244 EGRISNA-----GTHFELESGMAlpinwyyRGYAGRKMTLGIRPEHIGLTSQADGGVPLVMDTLEMLGADNLAHGRWGEQ 318
Cdd:PRK11432 244 PATLSGDyvdiyGYRLPRPAAFA-------FNLPDGECTVGVRPEAITLSEQGEESQRCTIKHVAYMGPQYEVTVDWHGQ 316
|
330 340
....*....|....*....|...
gi 578222446 319 KMVVRL-AHQERPKAGSTLWLHL 340
Cdd:PRK11432 317 ELLLQVnATQLQPDLGEHYYLEI 339
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-237 |
1.98e-92 |
|
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: 276.14 E-value: 1.98e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 3 GLKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVF 82
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QNYALYPHMSVEENMAWGLKIR----GMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLF 158
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 159 DEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGS 237
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-292 |
3.08e-91 |
|
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: 276.30 E-value: 3.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 35 MVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDER 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 115 VKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHD 194
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 195 QVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGSpaMNLLEG-RISNAGTHFELESGMALPINWY--YRGY 271
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGE--INVFEAtVIERKSEQVVLAGVEGRRCDIYtdVPVE 238
|
250 260
....*....|....*....|.
gi 578222446 272 AGRKMTLGIRPEHIGLTSQAD 292
Cdd:TIGR01187 239 KDQPLHVVLRPEKIVIEEEDE 259
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
9-236 |
5.11e-89 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 267.44 E-value: 5.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQNYALY 88
Cdd:TIGR00968 6 ISKRF-GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQHYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 89 PHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 168
Cdd:TIGR00968 85 KHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 169 LRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIG 236
Cdd:TIGR00968 165 VRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLG 232
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
4-290 |
2.86e-85 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 261.55 E-value: 2.86e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdgKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQ 83
Cdd:NF040840 2 IRIENLSKDW--KEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:NF040840 80 NYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGspAMNLL 243
Cdd:NF040840 160 ALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVG--FENII 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 578222446 244 EGRISNAGTHFELESGmalPINWYYRGYAGRKMTLGIRPEHIGLTSQ 290
Cdd:NF040840 238 EGVAEKGGEGTILDTG---NIKIELPEEKKGKVRIGIRPEDITISTE 281
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-250 |
2.98e-85 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 258.48 E-value: 2.98e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSW---DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEmepKDRG 77
Cdd:COG1116 5 APALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG---PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 IAMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFL 157
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 158 FDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG---IAEQIgtPVDVyEKPATRfvaSF 234
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARpgrIVEEI--DVDL-PRPRDR---EL 235
|
250
....*....|....*.
gi 578222446 235 IGSPAMNLLEGRISNA 250
Cdd:COG1116 236 RTSPEFAALRAEILDL 251
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-303 |
3.91e-82 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 253.85 E-value: 3.91e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQNYALY 88
Cdd:PRK10851 8 IKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 89 PHMSVEENMAWGLKI----RGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 164
Cdd:PRK10851 87 RHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 165 LDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGSpaMNLLE 244
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGE--VNRLQ 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 245 GRISnaGTHFELeSGMALPINwYYRGYAGrKMTLGIRPEHIGLTSQADGGVPLVMDTLE 303
Cdd:PRK10851 245 GTIR--GGQFHV-GAHRWPLG-YTPAYQG-PVDLFLRPWEVDISRRTSLDSPLPVQVLE 298
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-337 |
1.28e-81 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 253.22 E-value: 1.28e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQViQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQ 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGSpaMNLL 243
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS--VNVF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 244 EGRISNAGTHFEL--ESGMALPI--NWYYRGYAGRKMTLGIRPEHIGLTSQ--ADG---GVPLVMDtLEMLGADNLAHGR 314
Cdd:PRK11607 257 EGVLKERQEDGLVidSPGLVHPLkvDADASVVDNVPVHVALRPEKIMLCEEppADGcnfAVGEVIH-IAYLGDLSIYHVR 335
|
330 340
....*....|....*....|....
gi 578222446 315 WGEQKMV-VRLAHQERPKAGSTLW 337
Cdd:PRK11607 336 LKSGQMIsAQLQNAHRYRKGLPTW 359
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-210 |
9.64e-81 |
|
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: 9.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGK---TQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKdrgIAM 80
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:cd03293 78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578222446 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNK 210
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-236 |
1.55e-80 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 245.71 E-value: 1.55e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdgKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQ 83
Cdd:cd03299 1 LKVENLSKDW--KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIG 236
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-237 |
1.51e-76 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 237.68 E-value: 1.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 5 KLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVF 82
Cdd:COG1125 3 EFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEaarILELDGL-----LKRRPRELSGGQRQRVAMGRAIVRDPAVFL 157
Cdd:COG1125 83 QQIGLFPHMTVAENIATVPRLLGWDKERIRARVDE---LLELVGLdpeeyRDRYPHELSGGQQQRVGVARALAADPPILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 158 FDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGS 237
Cdd:COG1125 160 MDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVGA 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-238 |
6.12e-73 |
|
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: 226.41 E-value: 6.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMV 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELD--GLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 160 EPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIGSP 238
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGAD 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-235 |
7.48e-68 |
|
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: 214.43 E-value: 7.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD------RGIAMVFQNYALY 88
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 89 PHMSVEENMAWGLKIRGMGKghiDERVKEAARILELDGL---LKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 165
Cdd:cd03294 115 PHRTVLENVAFGLEVQGVPR---AEREERAAEALELVGLegwEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 166 DAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFI 235
Cdd:cd03294 192 DPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-217 |
1.05e-67 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 212.16 E-value: 1.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 24 TLDVA---DGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDI------WIDRQRVTEMEPKDRGIAMVFQNYALYPHMSVE 94
Cdd:cd03297 14 TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 95 ENMAWGLKIRGMGKGHIdeRVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMR 174
Cdd:cd03297 94 ENLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578222446 175 LELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIG 217
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-211 |
1.06e-66 |
|
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: 208.20 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEME----PKDRGIA 79
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelpPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 80 MVFQNYALYPHMSVEENMAWGlkirgmgkghidervkeaarileldgllkrrpreLSGGQRQRVAMGRAIVRDPAVFLFD 159
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578222446 160 EPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-211 |
3.87e-66 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 208.36 E-value: 3.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSW---DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG--- 77
Cdd:COG1136 5 LELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 ---IAMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPA 154
Cdd:COG1136 85 rrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 155 VFLFDEPLSNLDAKLRVQ-MRLeLQQLHRRLKTTSLYVTHDQvEAMTLAQRVMVMNKG 211
Cdd:COG1136 165 LILADEPTGNLDSKTGEEvLEL-LRELNRELGTTIVMVTHDP-ELAARADRVIRLRDG 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-211 |
3.73e-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: 203.11 E-value: 3.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSW---DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG--- 77
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 ---IAMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPA 154
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 155 VFLFDEPLSNLDAKLRVQ-MRLeLQQLHRRLKTTSLYVTHDQVEAMtLAQRVMVMNKG 211
Cdd:cd03255 161 IILADEPTGNLDSETGKEvMEL-LRELNKEAGTTIVVVTHDPELAE-YADRIIELRDG 216
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-236 |
4.11e-62 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 202.77 E-value: 4.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEP------KDRGIAMVFQNYALY 88
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPvelrevRRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 89 PHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 168
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 169 LRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIG 236
Cdd:TIGR01186 164 IRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-226 |
7.43e-61 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 194.86 E-value: 7.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMV 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNyalyP-----HMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVF 156
Cdd:COG1122 81 FQN----PddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578222446 157 LFDEPLSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHDQVEAMTLAQRVMVMNKG--IAEqiGTPVDVYEKP 226
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTV-IIVTHDLDLVAELADRVIVLDDGriVAD--GTPREVFSDY 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-211 |
1.47e-60 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 194.12 E-value: 1.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-----RGI 78
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLF 158
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 159 DEPLSNLDAKLRVQ-MRLeLQQLHRRlKTTSLYVTHDQ--VEAMtlAQRVMVMNKG 211
Cdd:COG2884 162 DEPTGNLDPETSWEiMEL-LEEINRR-GTTVLIATHDLelVDRM--PKRVLELEDG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-247 |
1.74e-60 |
|
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: 198.02 E-value: 1.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVA----DGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDI------WIDRQRVTEMEPKDRGIAMVFQNYALYPHMS 92
Cdd:COG4148 14 FTLDVDftlpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggevLQDSARGIFLPPHRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 VEENMAWGLKIRGMGKGHIDerVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ 172
Cdd:COG4148 94 VRGNLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 173 MRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASfiGSPAMNLLEGRI 247
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAG--GEEAGSVLEATV 244
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-218 |
3.14e-60 |
|
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: 193.87 E-value: 3.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGK---TQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGI 78
Cdd:COG1124 2 LEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNY--ALYPHMSVEENMAWGLKIrgMGKGHIDERVKEAARILELD-GLLKRRPRELSGGQRQRVAMGRAIVRDPAV 155
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRI--HGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 156 FLFDEPLSNLDAKLRVQ-MRLeLQQLHRRLKTTSLYVTHDqVEAMT-LAQRVMVMNKG-IAEQIGT 218
Cdd:COG1124 160 LLLDEPTSALDVSVQAEiLNL-LKDLREERGLTYLFVSHD-LAVVAhLCDRVAVMQNGrIVEELTV 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-211 |
9.20e-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: 191.53 E-value: 9.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 5 KLQAVTKSW-DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG--IAMV 81
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNyalyP-HM----SVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVF 156
Cdd:cd03225 81 FQN----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 157 LFDEPLSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTI-IIVTHDLDLLLELADRVIVLEDG 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-236 |
2.10e-59 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 191.12 E-value: 2.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGktqviQPLTLD--VADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMV 81
Cdd:COG3840 2 LRLDDLTYRYGD-----FPLRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNYALYPHMSVEENMAWG----LKIRGMGKghidERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFL 157
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGlrpgLKLTAEQR----AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 158 FDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFIG 236
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-219 |
1.23e-57 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 187.11 E-value: 1.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-----RGI 78
Cdd:COG1127 6 IEVRNLTKSFGDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYPHMSVEENMAWGLKIR-GMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFL 157
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 158 FDEPLSNLDAK-LRVQMRLeLQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTP 219
Cdd:COG1127 165 YDEPTAGLDPItSAVIDEL-IRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
1.46e-57 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 194.74 E-value: 1.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWD----GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD---- 75
Cdd:COG1123 261 LEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 76 -RGIAMVFQN--YALYPHMSVEENMAWGLKIRGMGKGH-IDERVKEAARILELD-GLLKRRPRELSGGQRQRVAMGRAIV 150
Cdd:COG1123 341 rRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAeRRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 151 RDPAVFLFDEPLSNLDAKLRVQ-MRLeLQQLHRRLKTTSLYVTHD--QVEAMtlAQRVMVMNKG-IAEQiGTPVDVYEKP 226
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQiLNL-LRDLQRELGLTYLFISHDlaVVRYI--ADRVAVMYDGrIVED-GPTEEVFANP 496
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-228 |
1.11e-56 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 184.43 E-value: 1.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTeMEPKD-----RGI 78
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDinklrRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYPHMSVEENMAWGL-KIRGMGKghiDERVKEAARILELDGLLKRR---PRELSGGQRQRVAMGRAIVRDPA 154
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPiKVKKMSK---AEAEERAMELLERVGLADKAdayPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 155 VFLFDEPLSNLDAK-----LRVqMRlELqqlhRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQiGTPVDVYEKPAT 228
Cdd:COG1126 157 VMLFDEPTSALDPElvgevLDV-MR-DL----AKEGMTMVVVTHEMGFAREVADRVVFMDGGrIVEE-GPPEEFFENPQH 229
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-225 |
4.61e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 180.26 E-value: 4.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG-IAMVF 82
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPL 162
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 163 SNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVMVMNKG--IAEqiGTPVDVYEK 225
Cdd:COG1131 160 SGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGriVAD--GTPDELKAR 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-216 |
1.17e-54 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 180.06 E-value: 1.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSWDGKTQ---VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPkDRG 77
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 IamVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFL 157
Cdd:COG4525 80 V--VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578222446 158 FDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG---IAEQI 216
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGpgrIVERL 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-239 |
1.47e-54 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 182.20 E-value: 1.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPL---TLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD----- 75
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALddvSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 76 RGIAMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEaarILELDGLLKRR---PRELSGGQRQRVAMGRAIVRD 152
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAE---LLELVGLSDKAdayPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 153 PAVFLFDEPLSNLDAK-----LRVqmrleLQQLHRRLKTTSLYVTHDqveaM----TLAQRVMVMNKG-IAEQiGTPVDV 222
Cdd:COG1135 159 PKVLLCDEATSALDPEttrsiLDL-----LKDINRELGLTIVLITHE----MdvvrRICDRVAVLENGrIVEQ-GPVLDV 228
|
250
....*....|....*..
gi 578222446 223 YEKPATRFVASFIGSPA 239
Cdd:COG1135 229 FANPQSELTRRFLPTVL 245
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-211 |
2.65e-54 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 177.69 E-value: 2.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 21 QPLTLD--VADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQNYALYPHMSVEENMA 98
Cdd:cd03298 13 QPMHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 99 WGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQ 178
Cdd:cd03298 93 LGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|...
gi 578222446 179 QLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
14-215 |
1.00e-53 |
|
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: 176.54 E-value: 1.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG-----IAMVFQNY--A 86
Cdd:cd03257 15 GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrkeIQMVFQDPmsS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 87 LYPHMSVEENMAWGLKIRGMGKGH--IDERVKEAARILELD-GLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:cd03257 95 LNPRMTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578222446 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQ 215
Cdd:cd03257 175 ALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGkIVEE 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-219 |
2.08e-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: 2.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 6 LQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-----RGIAM 80
Cdd:cd03261 3 LRGLTKSFGGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAWGLKIRG-MGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFD 159
Cdd:cd03261 82 LFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578222446 160 EPLSNLDAK-LRVQMRLeLQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTP 219
Cdd:cd03261 162 EPTAGLDPIaSGVIDDL-IRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-211 |
2.85e-52 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 173.32 E-value: 2.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-----RGI 78
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYPHMSVEENM------AWGLkIRGMGKGHIDERVKEAARILE---LDGLLKRRPRELSGGQRQRVAMGRAI 149
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVlagrlgRTST-WRSLLGLFPPEDRERALEALErvgLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578222446 150 VRDPAVFLFDEPLSNLDAKL-RVQMRLeLQQLHRRLKTTSLYVTHdQVE-AMTLAQRVMVMNKG 211
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTaRQVMDL-LRRIAREDGITVVVNLH-QVDlARRYADRIIGLRDG 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-211 |
3.26e-52 |
|
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: 171.94 E-value: 3.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPK----DRGIA 79
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 80 MVFQNYALYPHMSVEENMAWGL-KIRGMGKghiDERVKEAARILELDGLLKR---RPRELSGGQRQRVAMGRAIVRDPAV 155
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPiKVKGMSK---AEAEERALELLEKVGLADKadaYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 156 FLFDEPLSNLDAklrvQMRLELQQLHRRL---KTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03262 157 MLFDEPTSALDP----ELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-211 |
6.08e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.15 E-value: 6.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMV 81
Cdd:COG4619 1 LELEGLSFRVGGKP-ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNYALYPhMSVEENMAWGLKIRgmGKGHIDERVKEAARILELD-GLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:COG4619 80 PQEPALWG-GTVRDNLPFPFQLR--ERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578222446 161 PLSNLDAKLRVqmRLE--LQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:COG4619 157 PTSALDPENTR--RVEelLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-226 |
6.10e-50 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 166.99 E-value: 6.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPL---TLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD----- 75
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALkdvSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 76 RGIAMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEaarILELDGL---LKRRPRELSGGQRQRVAMGRAIVRD 152
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLE---LLELVGLedkADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 153 PAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHdQVEAM-TLAQRVMVMNKG-IAEQiGTPVDVYEKP 226
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITH-EMEVVkRICDRVAVMEKGeVVEE-GTVEEVFANP 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-227 |
9.31e-50 |
|
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: 173.94 E-value: 9.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVT---SGDIWIDRQRVTEMEPKDRG--IAMVFQN--YA 86
Cdd:COG1123 16 GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGrrIGMVFQDpmTQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 87 LYPhMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 166
Cdd:COG1123 96 LNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578222446 167 AKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQiGTPVDVYEKPA 227
Cdd:COG1123 175 VTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGrIVED-GPPEEILAAPQ 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-235 |
1.89e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 166.04 E-value: 1.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 6 LQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGI----AMV 81
Cdd:PRK09493 4 FKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNYALYPHMSVEENMAWG-LKIRGMGKGHIDERVKEaarILELDGLLKRR---PRELSGGQRQRVAMGRAIVRDPAVFL 157
Cdd:PRK09493 83 FQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARE---LLAKVGLAERAhhyPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 158 FDEPLSNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQiGTPVDVYEKPATRFVASFI 235
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGrIAED-GDPQVLIKNPPSQRLQEFL 236
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-217 |
2.89e-48 |
|
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: 161.95 E-value: 2.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 25 LDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQNYALYPHMSVEENMAWGLKIR 104
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 105 GMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRL 184
Cdd:TIGR01277 99 LKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSER 178
|
170 180 190
....*....|....*....|....*....|...
gi 578222446 185 KTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIG 217
Cdd:TIGR01277 179 QRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-222 |
5.27e-48 |
|
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: 162.52 E-value: 5.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG--IAMV 81
Cdd:COG1120 2 LEAENLSVGYGGRP-VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELArrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNYALYPHMSVEENMAWG----LKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFL 157
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 158 FDEPLSNLDAKLRVQ-MRLeLQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDV 222
Cdd:COG1120 161 LDEPTSHLDLAHQLEvLEL-LRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-225 |
5.32e-48 |
|
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: 162.33 E-value: 5.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG-IAMVF 82
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRqIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPL 162
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 163 SNLDAKLRVQMRLELQQLhRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEK 225
Cdd:COG4555 161 NGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-194 |
3.39e-47 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 159.18 E-value: 3.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 3 GLKLQAVTKSWDGKTQvIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAG-LERV--TSGDIWIDRQRVTEMEPKDRGIA 79
Cdd:COG4136 1 MLSLENLTITLGGRPL-LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 80 MVFQNYALYPHMSVEENMAWGLKiRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFD 159
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 578222446 160 EPLSNLDAKLRVQMR-LELQQLHRRlKTTSLYVTHD 194
Cdd:COG4136 159 EPFSKLDAALRAQFReFVFEQIRQR-GIPALLVTHD 193
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-219 |
5.56e-47 |
|
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: 158.88 E-value: 5.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKsWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERV-----TSGDIWIDRQRVTEMEPKD--- 75
Cdd:cd03260 1 IELRDLNV-YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 76 -RGIAMVFQNYALYPhMSVEENMAWGLKIRGM-GKGHIDERVKEAARILELDGLLKRR--PRELSGGQRQRVAMGRAIVR 151
Cdd:cd03260 80 rRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578222446 152 DPAVFLFDEPLSNLD--AKLRVqmrlelQQLHRRLK--TTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTP 219
Cdd:cd03260 159 EPEVLLLDEPTSALDpiSTAKI------EELIAELKkeYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
9-212 |
5.74e-47 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 158.57 E-value: 5.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-----RGIAMVFQ 83
Cdd:TIGR02673 7 VSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:TIGR02673 87 DFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578222446 164 NLDAKLRVQ-MRLeLQQLHRRlKTTSLYVTHDQVEAMTLAQRVMVMNKGI 212
Cdd:TIGR02673 167 NLDPDLSERiLDL-LKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
37-256 |
6.29e-47 |
|
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: 162.59 E-value: 6.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 37 GPSGCGKSTLLRMVAGLERVTSGDIWID-------RQRVtEMEPKDRGIAMVFQNYALYPHMSVEENMAWGLKiRGMGKg 109
Cdd:TIGR02142 30 GRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlfdsRKGI-FLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMK-RARPS- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 110 hiDERVKEAA--RILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTT 187
Cdd:TIGR02142 107 --ERRISFERviELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIP 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 188 SLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASfigSPAMNLLEGRISNAGTHFEL 256
Cdd:TIGR02142 185 ILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAR---EDQGSLIEGVVAEHDQHYGL 250
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-229 |
1.93e-45 |
|
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: 155.32 E-value: 1.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 20 IQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPkDRGIamVFQNYALYPHMSVEENMAW 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-DRMV--VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 100 GLK--IRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLEL 177
Cdd:TIGR01184 78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578222446 178 QQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDV-YEKPATR 229
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRDR 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-211 |
1.68e-44 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 153.11 E-value: 1.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-----RGI 78
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYPHMSVEENMAWGL-----KIRGMGKGHIDERVKEAARILELDGLLK---RRPRELSGGQRQRVAMGRAIV 150
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrsTWRSLFGLFPKEEKQRALAALERVGLLDkayQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 151 RDPAVFLFDEPLSNLDAKLRVQ-MRLeLQQLHRRLKTTSLYVTHdQVE-AMTLAQRVMVMNKG 211
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQvMDL-LKRINREEGITVIVSLH-QVDlAREYADRIVGLKDG 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-223 |
1.05e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 151.81 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSW-DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDrqrvtEMEPKD------- 75
Cdd:TIGR04520 1 IEVENVSFSYpESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-----GLDTLDeenlwei 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 76 -RGIAMVFQNyalyPH-----MSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAI 149
Cdd:TIGR04520 76 rKKVGMVFQN----PDnqfvgATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578222446 150 VRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAmTLAQRVMVMNKGIAEQIGTPVDVY 223
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-211 |
1.18e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 150.50 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 24 TLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQNYALYPHMSVEENMAWG--- 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 101 -LKIRGMGKghidERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQ 179
Cdd:PRK10771 99 gLKLNAAQR----EKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190
....*....|....*....|....*....|..
gi 578222446 180 LHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-211 |
1.57e-43 |
|
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: 150.28 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSW---DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDR---- 76
Cdd:COG4181 9 IELRGLTKTVgtgAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 77 --GIAMVFQNYALYPHMSVEENMAWGLKIRGMGKGHidervKEAARILELDGLLKR---RPRELSGGQRQRVAMGRAIVR 151
Cdd:COG4181 89 arHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR-----ARARALLERVGLGHRldhYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 152 DPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQveamTLA---QRVMVMNKG 211
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP----ALAarcDRVLRLRAG 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-163 |
3.43e-43 |
|
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: 146.64 E-value: 3.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 20 IQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALYPHMSVEENM 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 98 AWGLKIRGMGKGHIDERVKEAARILELDGLLKRR----PRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-227 |
3.60e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 152.19 E-value: 3.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 24 TLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVT-----EMEPKDRGIAMVFQN-YA-LYPHMSVEEN 96
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITglsgrELRPLRRRMQMVFQDpYAsLNPRMTVGDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 97 MAWGLKIRGMGKGhiDERVKEAARILELDGL----LKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ 172
Cdd:COG4608 118 IAEPLRIHGLASK--AERRERVAELLELVGLrpehADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQ 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 173 -MRLeLQQLHRRLKTTSLYVTHD--QVEAMtlAQRVMVMNKG-IAEqIGTPVDVYEKPA 227
Cdd:COG4608 196 vLNL-LEDLQDELGLTYLFISHDlsVVRHI--SDRVAVMYLGkIVE-IAPRDELYARPL 250
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-226 |
1.01e-42 |
|
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: 149.52 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 24 TLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-----RGIAMVFQnyalYPHM-----SV 93
Cdd:TIGR04521 25 SLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrKKVGLVFQ----FPEHqlfeeTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 94 EENMAWGLKIRGMGKGHIDERVKEAARILELD-GLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ 172
Cdd:TIGR04521 101 YKDIAFGPKNLGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578222446 173 MRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKP 226
Cdd:TIGR04521 181 ILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-235 |
1.33e-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: 1.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 3 GLKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWID------RQRVTEMEPKD- 75
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAghqfdfSQKPSEKAIRLl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 76 -RGIAMVFQNYALYPHMSVEENM-AWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDP 153
Cdd:COG4161 81 rQKVGMVFQQYNLWPHLTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 154 AVFLFDEPLSNLDAKLRVQMR---LELQQlhrrLKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQiGTpVDVYEKPATR 229
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVeiiRELSQ----TGITQVIVTHEVEFARKVASQVVYMEKGrIIEQ-GD-ASHFTQPQTE 234
|
....*.
gi 578222446 230 FVASFI 235
Cdd:COG4161 235 AFAHYL 240
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-211 |
1.47e-42 |
|
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: 147.50 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSW-DGK--TQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG--- 77
Cdd:TIGR02211 2 LKCENLGKRYqEGKldTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 ---IAMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPA 154
Cdd:TIGR02211 82 nkkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 155 VFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDqveaMTLA---QRVMVMNKG 211
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHD----LELAkklDRVLEMKDG 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-222 |
3.90e-42 |
|
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: 146.81 E-value: 3.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDR---GIAM 80
Cdd:cd03219 1 LEVRGLTKRFGGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAWGLKIRGMGKGH----------IDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIV 150
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSGLLlararreereARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578222446 151 RDPAVFLFDEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG--IAEqiGTPVDV 222
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGrvIAE--GTPDEV 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-223 |
4.18e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 148.27 E-value: 4.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGI----AMVFQ--NYALYPHmSVEEN 96
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrkkvGLVFQypEYQLFEE-TIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 97 MAWGLKIRGMGKGHIDERVKEAARI--LELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMR 174
Cdd:PRK13637 105 IAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEIL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578222446 175 LELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVY 223
Cdd:PRK13637 185 NKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-235 |
1.12e-41 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 145.93 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRV---TEMEPKD----- 75
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAirelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 76 RGIAMVFQNYALYPHMSVEENMAWG-LKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPA 154
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 155 VFLFDEPLSNLDAKLRVQMR---LELQQLHrrlkTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQiGTpVDVYEKPATRF 230
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVsiiRELAETG----ITQVIVTHEVEVARKTASRVVYMENGhIVEQ-GD-ASCFTQPQTEA 235
|
....*
gi 578222446 231 VASFI 235
Cdd:PRK11124 236 FKNYL 240
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-225 |
1.15e-41 |
|
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: 154.61 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALYpHM 91
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrRQIGVVLQDVFLF-SG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 92 SVEENMAwglkirgMGKGHI-DERVKEAARILELDGLLKRRP-----------RELSGGQRQRVAMGRAIVRDPAVFLFD 159
Cdd:COG2274 564 TIRENIT-------LGDPDAtDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 160 EPLSNLDAKLrvQMRLeLQQLHRRLK-TTSLYVTHDqVEAMTLAQRVMVMNKG-IAEQiGTPVDVYEK 225
Cdd:COG2274 637 EATSALDAET--EAII-LENLRRLLKgRTVIIIAHR-LSTIRLADRIIVLDKGrIVED-GTHEELLAR 699
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-227 |
1.38e-41 |
|
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: 147.51 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLER---VTSGDIWIDRQRVTEMEPKD------RGIAMVFQN 84
Cdd:COG0444 15 RGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElrkirgREIQMIFQD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 85 -Y-ALYPHMSVEENMAWGLKIRGMGKGhiDERVKEAARILELDGL------LKRRPRELSGGQRQRVAMGRAIVRDPAVF 156
Cdd:COG0444 95 pMtSLNPVMTVGDQIAEPLRIHGGLSK--AEARERAIELLERVGLpdperrLDRYPHELSGGMRQRVMIARALALEPKLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 157 LFDEPLSNLDAKLRVQ-MRLeLQQLHRRLKTTSLYVTHD--QVEAMtlAQRVMVMNKG-IAEqIGTPVDVYEKPA 227
Cdd:COG0444 173 IADEPTTALDVTIQAQiLNL-LKDLQRELGLAILFITHDlgVVAEI--ADRVAVMYAGrIVE-EGPVEELFENPR 243
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-211 |
1.74e-41 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 145.61 E-value: 1.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKtQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVtEMEPKDRGIamVFQ 83
Cdd:PRK11248 2 LQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAERGV--VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578222446 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-237 |
1.83e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 148.03 E-value: 1.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 5 KLQAVTKSWDGKTQVI---QPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-----R 76
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 77 GIAMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEaarILELDGLLKRR---PRELSGGQRQRVAMGRAIVRDP 153
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTE---LLELVGLSDKAdryPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 154 AVFLFDEPLSNLDAKLRVQMrLEL-QQLHRRLKTTSLYVTH--DQVEAmtLAQRVMVMNKG-IAEQiGTPVDVYEKPATR 229
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSI-LELlKDINRELGLTIVLITHemDVVKR--ICDRVAVIDAGrLVEQ-GTVSEVFSHPKHP 235
|
....*...
gi 578222446 230 FVASFIGS 237
Cdd:PRK11153 236 LTREFIQS 243
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-211 |
3.14e-41 |
|
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: 142.15 E-value: 3.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG-IAMVF 82
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRrIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QNYALYPHMSVEENMawglkirgmgkghidervkeaarileldgllkrrprELSGGQRQRVAMGRAIVRDPAVFLFDEPL 162
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578222446 163 SNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03230 124 SGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-211 |
3.21e-41 |
|
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: 143.70 E-value: 3.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-----RGI 78
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLF 158
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578222446 159 DEPLSNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-225 |
3.25e-41 |
|
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: 151.83 E-value: 3.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMV 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNYALyPHMSVEENMAwglkirgMGKGHI-DERVKEAARILELDGLLKRRP-----------RELSGGQRQRVAMGRAI 149
Cdd:COG4988 417 PQNPYL-FAGTIRENLR-------LGRPDAsDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARAL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 150 VRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRlKTTsLYVTHDQvEAMTLAQRVMVMNKGIAEQIGTPVDVYEK 225
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-RTV-ILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-222 |
4.16e-41 |
|
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: 144.80 E-value: 4.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDR---G 77
Cdd:COG0411 2 DPLLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 IAMVFQNYALYPHMSVEENMA----------WGLKIRGMGKGHIDER--VKEAARILE---LDGLLKRRPRELSGGQRQR 142
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLvaaharlgrgLLAALLRLPRARREEReaRERAEELLErvgLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 143 VAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDqVEA-MTLAQRVMVMNKG--IAEqiGTP 219
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD-MDLvMGLADRIVVLDFGrvIAE--GTP 237
|
...
gi 578222446 220 VDV 222
Cdd:COG0411 238 AEV 240
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-198 |
4.20e-41 |
|
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: 143.00 E-value: 4.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG-IAMVF 82
Cdd:COG4133 3 LEAENLSCRRGERL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QNYALYPHMSVEENMAWGLKIRGMGKGhiDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPL 162
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 578222446 163 SNLDAklrvQMRLELQQL---HRRLKTTSLYVTHDQVEA 198
Cdd:COG4133 160 TALDA----AGVALLAELiaaHLARGGAVLLTTHQPLEL 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
6.45e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 143.69 E-value: 6.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEmepKDRGIAM 80
Cdd:COG1121 4 MPAIELENLTVSYGGRP-VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPH--MSVEENMAWGLK-----IRGMGKGHiDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDP 153
Cdd:COG1121 80 VPQRAEVDWDfpITVRDVVLMGRYgrrglFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 154 AVFLFDEPLSNLDAKLRVQ-MRLeLQQLHRRlKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQiGTPVDV 222
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEAlYEL-LRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEV 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-234 |
1.07e-40 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 147.49 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 20 IQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEM------EPKDRGIAMVFQNYALYPHMSV 93
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaelrEVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 94 EENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQM 173
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578222446 174 RLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASF 234
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-222 |
5.54e-40 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 141.74 E-value: 5.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRgiaMVFQ 83
Cdd:PRK11247 13 LLLNAVSKRYGERT-VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---LMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMSVEENMAWGLKirgmgkGHIDERVKEAariLELDGLLKRR---PRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:PRK11247 89 DARLLPWKKVIDNVGLGLK------GQWRDAALQA---LAAVGLADRAnewPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578222446 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGiaeQIGTPVDV 222
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIGLDLTV 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-211 |
1.25e-39 |
|
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: 140.51 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-----RGI 78
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYPHMSVEENMAWGL--------KIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIV 150
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578222446 151 RDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAG 222
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-219 |
1.38e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 147.23 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 3 GLKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAM 80
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYpHMSVEENMAWglkirgmGKGHI-DERVKEAARILELDGLLKRRP-----------RELSGGQRQRVAMGRA 148
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRY-------GRPDAtDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578222446 149 IVRDPAVFLFDEPLSNLDAK--LRVQmrlelQQLHRRLK-TTSLYVTH--DQVEAmtlAQRVMVMNKG-IAEQiGTP 219
Cdd:COG1132 491 LLKDPPILILDEATSALDTEteALIQ-----EALERLMKgRTTIVIAHrlSTIRN---ADRILVLDDGrIVEQ-GTH 558
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-237 |
8.53e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 138.78 E-value: 8.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWID-------RQRVTEMEPKDR 76
Cdd:COG4598 9 LEVRDLHKSF-GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGgeeirlkPDRDGELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 77 --------GIAMVFQNYALYPHMSVEEN-MAWGLKIRGMGKghiDERVKEAARILELDGLLKRR---PRELSGGQRQRVA 144
Cdd:COG4598 88 rqlqrirtRLGMVFQSFNLWSHMTVLENvIEAPVHVLGRPK---AEAIERAEALLAKVGLADKRdayPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 145 MGRAIVRDPAVFLFDEPLSNLDAK-----LRVqMRlELQQLHRrlktTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTP 219
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPElvgevLKV-MR-DLAEEGR----TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPP 238
|
250
....*....|....*...
gi 578222446 220 VDVYEKPATRFVASFIGS 237
Cdd:COG4598 239 AEVFGNPKSERLRQFLSS 256
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-211 |
9.09e-39 |
|
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: 135.45 E-value: 9.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 5 KLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVF 82
Cdd:cd00267 1 EIENLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QnyalyphmsveenmawglkirgmgkghidervkeaarileldgllkrrpreLSGGQRQRVAMGRAIVRDPAVFLFDEPL 162
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578222446 163 SNLDAKLRVQMRLELQQLHRRLKTTsLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTV-IIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-219 |
1.25e-38 |
|
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: 136.87 E-value: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQ-VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWI-DRQRVTEMEPKDRGIAMV 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYInGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 162 LSNLDAKLRVQM-RLELQQLHRRlktTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTP 219
Cdd:cd03263 161 TSGLDPASRRAIwDLILEVRKGR---SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
1.32e-38 |
|
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: 135.20 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQ-VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAM 80
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYpHMSVEENMawglkirgmgkghidervkeaarileldgllkrrpreLSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:cd03228 81 VPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578222446 161 PLSNLDAKLRVQMRLELQQLHRrlKTTSLYVTHDqVEAMTLAQRVMVMNKG 211
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDG 170
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-195 |
1.61e-38 |
|
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: 136.21 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 6 LQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQ---RVTEMEP----KDRgI 78
Cdd:TIGR03608 1 LKNISKKFGDKV-ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKAskfrREK-L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLF 158
Cdd:TIGR03608 79 GYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 578222446 159 DEPLSNLDAKLR-VQMRLeLQQLHRRLKTTsLYVTHDQ 195
Cdd:TIGR03608 159 DEPTGSLDPKNRdEVLDL-LLELNDEGKTI-IIVTHDP 194
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-238 |
2.19e-37 |
|
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: 135.32 E-value: 2.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-----RGIAMVFQNY--AL 87
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrRDVQLVFQDSpsAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 88 YPHMSVEENMAWGLK-IRGMGKGHIDERVKEAARILELDG-LLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 165
Cdd:TIGR02769 102 NPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 166 DAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG--IAEQIGTPVDVYEKPATRFVASFIGSP 238
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGqiVEECDVAQLLSFKHPAGRNLQSAVLPE 256
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-211 |
6.24e-37 |
|
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: 132.49 E-value: 6.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWD---GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEmEPKD--RGI 78
Cdd:cd03266 2 ITADALTKRFRdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEarRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLF 158
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578222446 159 DEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-211 |
6.33e-37 |
|
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: 131.40 E-value: 6.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG--IAMVFQnyalyphms 92
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELArkIAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 veenmawglkirgmgkghidervkeAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ 172
Cdd:cd03214 81 -------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 578222446 173 MRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDG 174
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-211 |
6.52e-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: 132.56 E-value: 6.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDR---GIAMVFQNYALYPHM 91
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaraGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 92 SVEENMAWGLKIRgmGKGHIDERVkeaARILE----LDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDA 167
Cdd:cd03224 91 TVEENLLLGAYAR--RRAKRKARL---ERVYElfprLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578222446 168 KLRVQMRLELQQLhRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03224 166 KIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
4-237 |
2.34e-36 |
|
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: 132.26 E-value: 2.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-------- 75
Cdd:TIGR03005 1 VRFSDVTKRF-GILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpade 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 76 ------RG-IAMVFQNYALYPHMSVEENMAWG-LKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGR 147
Cdd:TIGR03005 80 khlrqmRNkIGMVFQSFNLFPHKTVLDNVTEApVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 148 AIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQiGTPVDVYEKP 226
Cdd:TIGR03005 160 ALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGrIVEQ-GKPDEIFRQP 238
|
250
....*....|.
gi 578222446 227 ATRFVASFIGS 237
Cdd:TIGR03005 239 KEERTREFLSK 249
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-215 |
3.65e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 131.41 E-value: 3.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLE-----RVTSGDIWID-----RQRVTE 70
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEqpeagTIRVGDITIDtarslSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 71 MEPKDRGIAMVFQNYALYPHMSVEENMAWG-LKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAI 149
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578222446 150 VRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQ 215
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGrIVEQ 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-224 |
5.92e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 131.65 E-value: 5.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 5 KLQAVTKSWDG-KTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWID-----RQRVTEMEPKdrgI 78
Cdd:PRK13632 9 KVENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDgitisKENLKEIRKK---I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNyalyPH-----MSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDP 153
Cdd:PRK13632 86 GIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578222446 154 AVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAmTLAQRVMVMNKGIAEQIGTPVDVYE 224
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-228 |
5.92e-36 |
|
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: 136.74 E-value: 5.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERvTSGDIWIDRQRVTEMEPKD-----RGIAMVFQN-YA-LYPHMSVEE 95
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpFGsLSPRMTVGQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 96 NMAWGLKI--RGMGKGHIDERVKEAARILELD-GLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ 172
Cdd:COG4172 384 IIAEGLRVhgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 173 MrLEL-QQLHRRLKTTSLYVTHDQ--VEAMtlAQRVMVMNKG-IAEQiGTPVDVYEKPAT 228
Cdd:COG4172 464 I-LDLlRDLQREHGLAYLFISHDLavVRAL--AHRVMVMKDGkVVEQ-GPTEQVFDAPQH 519
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-229 |
1.96e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 130.19 E-value: 1.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 18 QVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-----RGIAMVFQNY--ALYPH 90
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrRDIQMVFQDSisAVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 91 MSVEENMAWGLK-IRGMGKGHIDERVKEAARILELD-GLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 168
Cdd:PRK10419 106 KTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 169 LRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG--IAEQIGTPVDVYEKPATR 229
Cdd:PRK10419 186 LQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGqiVETQPVGDKLTFSSPAGR 248
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-227 |
3.04e-35 |
|
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: 135.28 E-value: 3.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 2 AGLKLQAVTKSWDGKTQ-VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGI 78
Cdd:COG4987 332 PSLELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYpHMSVEENmawgLKIrgmGKGHI-DERVKEAARILELDGLLKRRP-----------RELSGGQRQRVAMG 146
Cdd:COG4987 412 AVVPQRPHLF-DTTLREN----LRL---ARPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 147 RAIVRDPAVFLFDEPLSNLDAKLRVQMrleLQQLHRRLKT-TSLYVTHDQVeAMTLAQRVMVMNKG-IAEQiGTPVDVYE 224
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQAL---LADLLEALAGrTVLLITHRLA-GLERMDRILVLEDGrIVEQ-GTHEELLA 558
|
...
gi 578222446 225 KPA 227
Cdd:COG4987 559 QNG 561
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-211 |
5.57e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 128.62 E-value: 5.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLR-------MVAGLeRVTsGDIWIDRQRV--TEMEPKD--RGIAMVFQ 83
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGA-RVE-GEILLDGEDIydPDVDVVElrRRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPhMSVEENMAWGLKIRGM-GKGHIDERVKEAariLELDGL-------LKRRPRELSGGQRQRVAMGRAIVRDPAV 155
Cdd:COG1117 100 KPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEES---LRKAALwdevkdrLKKSALGLSGGQQQRLCIARALAVEPEV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 156 FLFDEPLSNLD--AKLRVqmrlelQQLHRRLKT--TSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:COG1117 176 LLMDEPTSALDpiSTAKI------EELILELKKdyTIVIVTHNMQQAARVSDYTAFFYLG 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-212 |
6.81e-35 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 126.88 E-value: 6.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEmepKDRGIAMVFQNYAL- 87
Cdd:cd03235 5 LTVSYGGHP-VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKRIGYVPQRRSId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 88 --YPhMSVEENMAWGL--KIRGMGK-GHID-ERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:cd03235 81 rdFP-ISVRDVVLMGLygHKGLFRRlSKADkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578222446 162 LSNLDAKLRVQ-MRLeLQQLHRRLKTTsLYVTHDQVEAMTLAQRVMVMNKGI 212
Cdd:cd03235 160 FAGVDPKTQEDiYEL-LRELRREGMTI-LVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-224 |
8.46e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.59 E-value: 8.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNyalyPH- 90
Cdd:PRK13635 17 DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvrRQVGMVFQN----PDn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 91 ----MSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 166
Cdd:PRK13635 93 qfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 167 AKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTlAQRVMVMNKGIAEQIGTPVDVYE 224
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-219 |
1.47e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 127.93 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNyalyPH-----MSVEE 95
Cdd:PRK13650 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDirHKIGMVFQN----PDnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 96 NMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRL 175
Cdd:PRK13650 102 DVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578222446 176 ELQQLHRRLKTTSLYVTHDqVEAMTLAQRVMVMNKGIAEQIGTP 219
Cdd:PRK13650 182 TIKGIRDDYQMTVISITHD-LDEVALSDRVLVMKNGQVESTSTP 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-229 |
2.29e-34 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 129.22 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 37 GPSGCGKSTLLRMVAGLERVTSGDIWI------DRQRVTEMEPKDRGIAMVFQNYALYPHMSVEENMAWGLKiRGMgKGH 110
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLngrvlfDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYGMA-KSM-VAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 111 IDERVKeaarILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLY 190
Cdd:PRK11144 109 FDKIVA----LLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILY 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 578222446 191 VTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATR 229
Cdd:PRK11144 185 VSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-211 |
2.42e-34 |
|
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: 125.41 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGIAMVFQ 83
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMSVEENmawgLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:cd03268 80 APGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578222446 164 NLDAKLRVQMRlELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03268 156 GLDPDGIKELR-ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-208 |
5.24e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.91 E-value: 5.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGkTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD---RGIAM 80
Cdd:COG1129 5 LEMRGISKSFGG-VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAWGLKIRGMGKghIDER--VKEAARILELDGL---LKRRPRELSGGQRQRVAMGRAIVRDPAV 155
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRGGL--IDWRamRRRARELLARLGLdidPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 156 FLFDEPLSNLDAKlrvqmrlELQQLH---RRLK---TTSLYVTHDQVEAMTLAQRVMVM 208
Cdd:COG1129 162 LILDEPTASLTER-------EVERLFriiRRLKaqgVAIIYISHRLDEVFEIADRVTVL 213
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-265 |
9.77e-34 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 127.13 E-value: 9.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 24 TLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDI-WIDrQRVTEMEPKDR-----GIAMVFQN--YALYPHMSVEE 95
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLG-KDLLGMKDDEWravrsDIQMIFQDplASLNPRMTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 96 NMAWGLKIR--GMGKGHIDERVKE-AARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ 172
Cdd:PRK15079 120 IIAEPLRTYhpKLSRQEVKDRVKAmMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 173 MRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPA---TRFVASFIGSP--------AMN 241
Cdd:PRK15079 200 VVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLhpyTKALMSAVPIPdpdlernkTIQ 279
|
250 260
....*....|....*....|....
gi 578222446 242 LLEGrisnagthfELESgmalPIN 265
Cdd:PRK15079 280 LLEG---------ELPS----PIN 290
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-205 |
2.38e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 123.77 E-value: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 17 TQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEM------EPKDRGIAMVFQNYALYPH 90
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaELRNQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 91 MSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLR 170
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190
....*....|....*....|....*....|....*
gi 578222446 171 VQMRLELQQLHRRLKTTSLYVTHDqveaMTLAQRV 205
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVTHD----LQLAKRM 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-211 |
3.35e-33 |
|
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: 122.30 E-value: 3.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGeFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG-IAMVF 82
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QNYALYPHMSVEE---NMAWglkIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFD 159
Cdd:cd03264 79 QEFGVYPNFTVREfldYIAW---LKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578222446 160 EPLSNLDAKLRVQMRLELQQLHRrlKTTSLYVTH--DQVEAMtlAQRVMVMNKG 211
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGE--DRIVILSTHivEDVESL--CNQVAVLNKG 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-211 |
6.06e-33 |
|
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: 121.62 E-value: 6.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEME-------PKDR 76
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 77 GiamvfqnyaLYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVF 156
Cdd:cd03269 80 G---------LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578222446 157 LFDEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTH--DQVEAMtlAQRVMVMNKG 211
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHqmELVEEL--CDRVLLLNKG 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
15-211 |
9.29e-33 |
|
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: 122.01 E-value: 9.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDR---GIAMVFQNYALYPHM 91
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 92 SVEENMAWGLKIRGmGKGHIDERVkeaARILELDGLLKRRPR----ELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDA 167
Cdd:COG0410 94 TVEENLLLGAYARR-DRAEVRADL---ERVYELFPRLKERRRqragTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578222446 168 KLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:COG0410 170 LIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERG 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-211 |
9.90e-33 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 121.52 E-value: 9.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIW-----IDRQRVTEMEPKDRGI 78
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWfsghdITRLKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAariLELDGLL---KRRPRELSGGQRQRVAMGRAIVRDPAV 155
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAA---LDKVGLLdkaKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 156 FLFDEPLSNLDAKLRVQMrLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK10908 159 LLADEPTGNLDDALSEGI-LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-219 |
9.92e-33 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 121.71 E-value: 9.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWDGKTQViQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEmEPKD--RGIAMVFQNYA 86
Cdd:cd03265 6 LVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREvrRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 87 LYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 166
Cdd:cd03265 84 VDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 167 AKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG--IAEqiGTP 219
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGriIAE--GTP 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-211 |
3.44e-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: 120.00 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 16 KTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALYpHMSV 93
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 94 EENMAwglkirgMGKGHI-DERVKEAARILELDGLLKRRP-----------RELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:cd03245 95 RDNIT-------LGAPLAdDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 578222446 162 LSNLDAKLRVQMRLELQQLHRrlKTTSLYVTHDQVeAMTLAQRVMVMNKG 211
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSG 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-229 |
3.48e-32 |
|
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: 120.34 E-value: 3.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDR---GIAM 80
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:cd03218 80 LPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578222446 161 PLSNLDAKlRVQmrlELQQLHRRLKTTSLYV---THDQVEAMTLAQRVMVMNKG--IAEqiGTPVDVYEKPATR 229
Cdd:cd03218 160 PFAGVDPI-AVQ---DIQKIIKILKDRGIGVlitDHNVRETLSITDRAYIIYEGkvLAE--GTPEEIAANELVR 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
15-235 |
5.84e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 120.46 E-value: 5.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD---------------RGIA 79
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrllrTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 80 MVFQNYALYPHMSVEEN-MAWGLKIRGMGKGHIDERvkeAARILELDGLLKRR----PRELSGGQRQRVAMGRAIVRDPA 154
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARER---AVKYLAKVGIDERAqgkyPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 155 VFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASF 234
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTM-VVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQF 251
|
.
gi 578222446 235 I 235
Cdd:PRK10619 252 L 252
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-211 |
8.34e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 120.19 E-value: 8.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKT----QVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG-- 77
Cdd:COG1101 2 LELKNLSKTFNPGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 IAMVFQNYAL--YPHMSVEENMA--------WGLKiRGMGKGHIdERVKEAARILELdGL---LKRRPRELSGGQRQRVA 144
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLR-RGLTKKRR-ELFRELLATLGL-GLenrLDTKVGLLSGGQRQALS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 145 MGRAIVRDPAVFLFDEPLSNLDAKlRVQMRLEL-QQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPK-TAALVLELtEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-208 |
3.12e-31 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 123.55 E-value: 3.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMV 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNYALYPHmSVEENMAWGLKirgmgkGHIDERVKEAARILELDGLLKRRP-----------RELSGGQRQRVAMGRAIV 150
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLARP------DASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 151 RDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRlkTTSLYVTHDqVEAMTLAQRVMVM 208
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHR-LALAALADRIVVL 529
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
16-211 |
4.41e-31 |
|
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: 124.21 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 16 KTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALYpHMSV 93
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlrRNIGYVPQDPRLF-YGTL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 94 EENMAwglkirgMGKGHI-DERVKEAARILELDGLLKRRP-----------RELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:TIGR03375 556 RDNIA-------LGAPYAdDEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILLLDEP 628
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 162 LSNLDaklrvqMRLElQQLHRRLK-----TTSLYVTHdQVEAMTLAQRVMVMNKG 211
Cdd:TIGR03375 629 TSAMD------NRSE-ERFKDRLKrwlagKTLVLVTH-RTSLLDLVDRIIVMDNG 675
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-225 |
1.93e-30 |
|
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: 115.79 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGK-TQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAM 80
Cdd:cd03251 1 VEFKNVTFRYPGDgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYpHMSVEENMAWGLKirgmgkGHIDERVKEAARILELDGLLKRRPR-----------ELSGGQRQRVAMGRAI 149
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGRP------GATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 150 VRDPAVFLFDEPLSNLD--AKLRVQMRLELQQLHRrlktTSLYVTHdQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEK 225
Cdd:cd03251 154 LKDPPILILDEATSALDteSERLVQAALERLMKNR----TTFVIAH-RLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-219 |
1.95e-30 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 115.79 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTE--MEPKDRGIAMVFQNYA 86
Cdd:cd03253 6 VTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtLDSLRRAIGVVPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 87 LYpHMSVEENMAWGlkirgmGKGHIDERVKEAARILELDGLLKRRPR-----------ELSGGQRQRVAMGRAIVRDPAV 155
Cdd:cd03253 86 LF-NDTIGYNIRYG------RPDATDEEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578222446 156 FLFDEPLSNLDaklrVQMRLELQQLHRRLKT--TSLYVTHDQVEAMTlAQRVMVMNKG-IAEQiGTP 219
Cdd:cd03253 159 LLLDEATSALD----THTEREIQAALRDVSKgrTTIVIAHRLSTIVN-ADKIIVLKDGrIVER-GTH 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-211 |
2.80e-30 |
|
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: 114.66 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEpKDRGIAMVFQN--YA 86
Cdd:cd03226 5 ISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-RRKSIGYVMQDvdYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 87 LYPHmSVEENMAWGLKIRGMGKGHIDERVKEaariLELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 166
Cdd:cd03226 84 LFTD-SVREELLLGLKELDAGNEQAETVLKD----LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578222446 167 AKlrvQMRlELQQLHRRL---KTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03226 159 YK---NME-RVGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-226 |
4.62e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 115.32 E-value: 4.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 13 WDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGL-----ERVTSGDIWIDRQRV--TEMEPKD--RGIAMVFQ 83
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIysPDVDPIEvrREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMSVEENMAWGLKIRGM--GKGHIDERV----KEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFL 157
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVewalKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 158 FDEPLSNLD----AKLRvQMRLELQQlhrrlKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKP 226
Cdd:PRK14267 173 MDEPTANIDpvgtAKIE-ELLFELKK-----EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-226 |
2.84e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.08 E-value: 2.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGL-----ERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYAL 87
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIElrRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 88 YPHMSVEENMAWGLKIRGM--GKGHIDERVKEAARILELDGLLKRR----PRELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:PRK14247 94 IPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 162 LSNLD----AKLRVQMrLELQQlhrrlKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKP 226
Cdd:PRK14247 174 TANLDpentAKIESLF-LELKK-----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-222 |
3.11e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 112.87 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 5 KLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVF 82
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QNYALYPHMSVEENMAWGlkiR-GMGKGHI---DER-VKEAARILELDGLLKRRPRELSGGQRQR--VAMgrAIVRDPAV 155
Cdd:COG4604 82 QENHINSRLTVRELVAFG---RfPYSKGRLtaeDREiIDEAIAYLDLEDLADRYLDELSGGQRQRafIAM--VLAQDTDY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 156 FLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQiGTPVDV 222
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGrVVAQ-GTPEEI 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-211 |
6.37e-29 |
|
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: 109.44 E-value: 6.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD---RGIAM 80
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDarrAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQnyalyphmsveenmawglkirgmgkghidervkeaarileldgllkrrpreLSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:cd03216 80 VYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578222446 161 PLSNLDAKlrvqmrlELQQLH---RRLK---TTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03216 109 PTAALTPA-------EVERLFkviRRLRaqgVAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-211 |
1.00e-28 |
|
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: 111.08 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDR---GIAM 80
Cdd:TIGR03410 1 LEVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaraGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILEldGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVLK--EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578222446 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERG 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-225 |
1.07e-28 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 111.16 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYA 86
Cdd:cd03254 8 VNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrSMIGVVLQDTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 87 LYPHmSVEENmawglkIRgMGKGHI-DERVKEAARILELDGLLKRRPR-----------ELSGGQRQRVAMGRAIVRDPA 154
Cdd:cd03254 88 LFSG-TIMEN------IR-LGRPNAtDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578222446 155 VFLFDEPLSNLDaklrVQMRLELQQLHRRL--KTTSLYVTHdQVEAMTLAQRVMVMNKG-IAEQiGTPVDVYEK 225
Cdd:cd03254 160 ILILDEATSNID----TETEKLIQEALEKLmkGRTSIIIAH-RLSTIKNADKILVLDDGkIIEE-GTHDELLAK 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
36-226 |
1.99e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 112.75 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 36 VGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-----RGIAMVFQN-YA-LYPHMSVEENMAWGLKIR-GMG 107
Cdd:PRK11308 47 VGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrQKIQIVFQNpYGsLNPRKKVGQILEEPLLINtSLS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 108 KghiDERVKEAARILELDGL----LKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRR 183
Cdd:PRK11308 127 A---AERREKALAMMAKVGLrpehYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578222446 184 LKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKP 226
Cdd:PRK11308 204 LGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-227 |
5.42e-28 |
|
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: 114.40 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTQVIQPLTLDVADGEFIVMVGPSGCGKS----TLLRMVAGLERVTSGDIWIDRQRVTEMEPKD----RG--IAMVFQ 83
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrriRGnrIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 N--YALYPHMSVEENMAWGLKI-RGMGKGHIDERVKEAariLELDGL------LKRRPRELSGGQRQRV--AMgrAIVRD 152
Cdd:COG4172 100 EpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALEL---LERVGIpdperrLDAYPHQLSGGQRQRVmiAM--ALANE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 153 PAVFLFDEPLSNLDAKLRVQMrLEL-QQLHRRLKTTSLYVTHDQ--VEAMtlAQRVMVMNKG-IAEQiGTPVDVYEKPA 227
Cdd:COG4172 175 PDLLIADEPTTALDVTVQAQI-LDLlKDLQRELGMALLLITHDLgvVRRF--ADRVAVMRQGeIVEQ-GPTAELFAAPQ 249
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-211 |
6.07e-28 |
|
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: 107.30 E-value: 6.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG--IAMVFQNYALYPHm 91
Cdd:cd03246 12 GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGdhVGYLPQDDELFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 92 SVEENMawglkirgmgkghidervkeaarileldgllkrrpreLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDaklrV 171
Cdd:cd03246 91 SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD----V 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578222446 172 QMRLELQQLHRRLK---TTSLYVTHdQVEAMTLAQRVMVMNKG 211
Cdd:cd03246 130 EGERALNQAIAALKaagATRIVIAH-RPETLASADRILVLEDG 171
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-211 |
7.17e-28 |
|
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: 109.40 E-value: 7.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSG-------------DIWIDRQRV-- 68
Cdd:COG1119 4 LELRNVTVRRGGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerrggeDVWELRKRIgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 69 --TEM----EPKDRGIAMV----FQNYALYPHMSVEEnmawglkirgmgkghiDERVKEAARILELDGLLKRRPRELSGG 138
Cdd:COG1119 83 vsPALqlrfPRDETVLDVVlsgfFDSIGLYREPTDEQ----------------RERARELLELLGLAHLADRPFGTLSQG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 139 QRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTH---DQVEAMTlaqRVMVMNKG 211
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhveEIPPGIT---HVLLLKDG 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-227 |
7.42e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.49 E-value: 7.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 27 VADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWI-DRQRVTEMEPKD-----RGIAMVFQnyalYP-HM----SVEE 95
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKlkplrKKVGIVFQ----FPeHQlfeeTVEK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 96 NMAWGLKIRGMGKghiDERVKEAARILELDGL----LKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRV 171
Cdd:PRK13634 106 DICFGPMNFGVSE---EDAKQKAREMIELVGLpeelLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 172 QMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPA 227
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-211 |
1.72e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.81 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 24 TLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD---RGIAMVFQNYALYPHMSVEENMAWG 100
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaiaLGIGMVHQHFMLVPNLTVAENIVLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 101 LKIRGMGKGHIDERVKEAARI-----LELDglLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAklrvQMRL 175
Cdd:COG3845 105 LEPTKGGRLDRKAARARIRELserygLDVD--PDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTP----QEAD 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 578222446 176 ELQQLHRRLK---TTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:COG3845 179 ELFEILRRLAaegKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-225 |
3.38e-27 |
|
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: 107.24 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 18 QVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMvagLER---VTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALYPhMS 92
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSL---LERfydPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 VEENMAWGLKIRgmgkghIDERVKEAAR-------ILEL----DGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:cd03249 93 IAENIRYGKPDA------TDEEVEEAAKkanihdfIMSLpdgyDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578222446 162 LSNLDAK--LRVQMRLElqqlHRRLKTTSLYVTHdQVEAMTLAQRVMVMNKG-IAEQiGTPVDVYEK 225
Cdd:cd03249 167 TSALDAEseKLVQEALD----RAMKGRTTIVIAH-RLSTIRNADLIAVLQNGqVVEQ-GTHDELMAQ 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-199 |
3.58e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.78 E-value: 3.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRqrvtemepkDRGIAMVFQNYALYPHM--S 92
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVPDSLplT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 VEENMAWGL-KIRGMGKGHIDERVKEAARILE---LDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 168
Cdd:NF040873 74 VRDLVAMGRwARRGLWRRLTRDDRAAVDDALErvgLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190
....*....|....*....|....*....|.
gi 578222446 169 LRVQMRLELQQLHRRlKTTSLYVTHDQVEAM 199
Cdd:NF040873 154 SRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-225 |
8.42e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 107.14 E-value: 8.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 22 PLTLD-----VADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNyalyPH---- 90
Cdd:PRK13648 22 SFTLKdvsfnIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQN----PDnqfv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 91 -MSVEENMAWGLKIRGMGKGHIDERVKEAariLELDGLLKRR---PRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 166
Cdd:PRK13648 98 gSIVKYDVAFGLENHAVPYDEMHRRVSEA---LKQVDMLERAdyePNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 167 AklrvQMRLELQQLHRRLKT----TSLYVTHDQVEAMTlAQRVMVMNKGIAEQIGTPVDVYEK 225
Cdd:PRK13648 175 P----DARQNLLDLVRKVKSehniTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-258 |
1.28e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 106.61 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIW---IDRQRVTEMEPKDRGIAM 80
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQN-YALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFD 159
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 160 EPLSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHDqVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVAsfIGSPA 239
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTI-VYITHN-LEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLG--LTPPS 237
|
250
....*....|....*....
gi 578222446 240 MNLLEGRISNAGTHFELES 258
Cdd:PRK13644 238 LIELAENLKMHGVVIPWEN 256
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-211 |
1.43e-26 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 104.17 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 11 KSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERV--TSGDIWIDRQRVTEMEPKDRgIAMVFQNYALY 88
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKI-IGYVPQDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 89 PHMSVEENMAWGLKIRGmgkghidervkeaarileldgllkrrpreLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 168
Cdd:cd03213 95 PTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578222446 169 LRVQMRLELQQLHRRLKTTsLYVTHD-QVEAMTLAQRVMVMNKG 211
Cdd:cd03213 146 SALQVMSLLRRLADTGRTI-ICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-215 |
2.07e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 104.86 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLT---LDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG--- 77
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTgveLVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 ---IAMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPA 154
Cdd:PRK10584 87 akhVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578222446 155 VFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQ 215
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-235 |
2.67e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 105.62 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWID--------RQRVTEMEPKdrgIAMVFQNYA 86
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDgenipamsRSRLYTVRKR---MSMLFQSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 87 LYPHMSVEENMAWGLKirgmGKGHIDERVKEAARILELD-----GLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:PRK11831 95 LFTDMNVFDNVAYPLR----EHTQLPAPLLHSTVMMKLEavglrGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578222446 162 LSNLDA-KLRVQMRLeLQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVM--NKGIAEqiGTPVDVYEKPATRfVASFI 235
Cdd:PRK11831 171 FVGQDPiTMGVLVKL-ISELNSALGVTCVVVSHDVPEVLSIADHAYIVadKKIVAH--GSAQALQANPDPR-VRQFL 243
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-229 |
3.02e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 104.73 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSWdGKTQVIQPLTLDVADGEfIV-MVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMePKDR--- 76
Cdd:COG1137 1 MMTLEAENLVKSY-GKRTVVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-PMHKrar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 77 -GI------AMVFQNyalyphMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAI 149
Cdd:COG1137 78 lGIgylpqeASIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 150 VRDPAVFLFDEPLSNLDAkLRVQmrlELQQLHRRLKTTSLYV--T-HDQVEAMTLAQRVMVMNKG--IAEqiGTPVDVYE 224
Cdd:COG1137 152 ATNPKFILLDEPFAGVDP-IAVA---DIQKIIRHLKERGIGVliTdHNVRETLGICDRAYIISEGkvLAE--GTPEEILN 225
|
....*
gi 578222446 225 KPATR 229
Cdd:COG1137 226 NPLVR 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-215 |
3.35e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.02 E-value: 3.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKST----LLRMVAglervTSGDIWIDRQ-----RVTEMEPKDRGIAMVFQ-- 83
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQplhnlNRRQLLPVRHRIQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMSVEENMAWGLKI--RGMGKGHIDERVKEAARILELDGLLKRR-PRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 161 PLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQ 215
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGeVVEQ 507
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-225 |
3.52e-26 |
|
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: 109.36 E-value: 3.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG--IAMVFQNYALYPHmS 92
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGkhIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 VEENMAwglkiRgMGKGHIDERVKEAARILELDGLLKRRPR-----------ELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:TIGR01842 408 VAENIA-----R-FGENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578222446 162 LSNLDAKLRVQMRLELQQLHRRlKTTSLYVTHdQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEK 225
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKAR-GITVVVITH-RPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-211 |
4.08e-26 |
|
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: 104.34 E-value: 4.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIwidrqRVTEMEPKDRG------IAMVF-QNYALYPHM 91
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-----RVAGLVPWKRRkkflrrIGVVFgQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 92 SVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRV 171
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578222446 172 QMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
15-205 |
4.76e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.86 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLR-------MVAGLE---RVTSGDIWIDRQRVTEMEPKDRgIAMVFQN 84
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRvegKVTFHGKNLYAPDVDPVEVRRR-IGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 85 YALYPHmSVEENMAWGLKIRGMgKGHIDERV----KEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:PRK14243 100 PNPFPK-SIYDNIAYGARINGY-KGDMDELVerslRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578222446 161 PLSNLD--AKLRVQmrlEL-QQLHRRLktTSLYVTHDqveaMTLAQRV 205
Cdd:PRK14243 178 PCSALDpiSTLRIE---ELmHELKEQY--TIIIVTHN----MQQAARV 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-222 |
5.28e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 104.33 E-value: 5.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMV 81
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlaRRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNYALYPHMSVEENMAWG----LKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFL 157
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 158 FDEPLSNLDAKLRVqmrlELQQLHRRLKT---TSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDV 222
Cdd:PRK11231 162 LDEPTTYLDINHQV----ELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-226 |
7.83e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 108.40 E-value: 7.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 20 IQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRV-----TEMEPKDRGIAMVFQN-YA-LYPHMS 92
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspGKLQALRRDIQFIFQDpYAsLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 VEENMAWGLKIRGMGKGhiDERVKEAARILELDGLLK----RRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 168
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPG--KAAAARVAWLLERVGLLPehawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 169 LRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKP 226
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-211 |
8.25e-26 |
|
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: 103.32 E-value: 8.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGK--TQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPK--DRGIA 79
Cdd:cd03248 12 VKFQNVTFAYPTRpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 80 MVFQNYALYPHmSVEENMAWGLKirgmgkGHIDERVKEAARILELDGLLKRRPRE-----------LSGGQRQRVAMGRA 148
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYGLQ------SCSFECVKEAAQKAHAHSFISELASGydtevgekgsqLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 149 IVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRlkTTSLYVTHdQVEAMTLAQRVMVMNKG 211
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAH-RLSTVERADQILVLDGG 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-224 |
9.71e-26 |
|
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: 107.97 E-value: 9.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSW----DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSG-------DIWIDrqrVTEME 72
Cdd:TIGR03269 280 IKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvrvgDEWVD---MTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 73 PKDRG-----IAMVFQNYALYPHMSVEENM--AWGLKIR---GMGKGHIDERV-----KEAARILEldgllkRRPRELSG 137
Cdd:TIGR03269 357 PDGRGrakryIGILHQEYDLYPHRTVLDNLteAIGLELPdelARMKAVITLKMvgfdeEKAEEILD------KYPDELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 138 GQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIG 217
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
....*..
gi 578222446 218 TPVDVYE 224
Cdd:TIGR03269 511 DPEEIVE 517
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-211 |
1.55e-25 |
|
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: 102.35 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 11 KSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLER---VTSGDIWIDRQRVTEMEPKDRgIAMVFQNYAL 87
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQFQKC-VAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 88 YPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKR----RPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRiggnLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578222446 164 NLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSG 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-211 |
2.46e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 103.65 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWID--------RQRVTEMePKD 75
Cdd:COG4152 2 LELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDgepldpedRRRIGYL-PEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 76 RGiamvfqnyaLYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAV 155
Cdd:COG4152 80 RG---------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578222446 156 FLFDEPLSNLD---AKLrvqMRLELQQLHRRlKTTSLYVTH--DQVEAmtLAQRVMVMNKG 211
Cdd:COG4152 151 LILDEPFSGLDpvnVEL---LKDVIRELAAK-GTTVIFSSHqmELVEE--LCDRIVIINKG 205
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-225 |
2.47e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 103.66 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVT------EMEPKDRGIAMVFQnyalYPHM----- 91
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVRKKVGVVFQ----FPESqlfee 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 92 SVEENMAWGLKIRGMGKghiDERVKEAARILELDGLLK----RRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDA 167
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPK---EKAEKIAAEKLEMVGLADefweKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 168 KLRVQMRLELQQLHRRLKTTSLyVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEK 225
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVL-VTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
4-215 |
2.61e-25 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 102.58 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSW-DGKTQVI--QPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQR------VTEMEPK 74
Cdd:COG4107 9 LSVRGLSKRYgPGCGTVVacRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRDggprdlFALSEAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 75 DRGIA-----MVFQN--YALYPHMSVEENMAWGLKIRGMGK-GHIDERVKEAARILELD-GLLKRRPRELSGGQRQRVAM 145
Cdd:COG4107 89 RRRLRrtdwgMVYQNprDGLRMDVSAGGNIAERLMAAGERHyGDIRARALEWLERVEIPlERIDDLPRTFSGGMQQRVQI 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 146 GRAIVRDPAVFLFDEPLSNLDakLRVQMRL--ELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQ 215
Cdd:COG4107 169 ARALVTNPRLLFLDEPTTGLD--VSVQARLldLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGrVVES 239
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-222 |
6.19e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.77 E-value: 6.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALYPHMS 92
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElaRRRAVLPQHSSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 VEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVR------DPAVFLFDEPLSNLD 166
Cdd:PRK13548 93 VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 167 akLRVQ---MRLeLQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQiGTPVDV 222
Cdd:PRK13548 173 --LAHQhhvLRL-ARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGrLVAD-GTPAEV 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-207 |
7.08e-25 |
|
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: 101.33 E-value: 7.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 26 DVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVT----EMEPKdrgiamvfqnyalYPhMSVEENMAwgL 101
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKAD-------------YE-GTVRDLLS--S 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 102 KIRGMGkghIDERVK-EAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDaklrVQMRLELQQL 180
Cdd:cd03237 85 ITKDFY---THPYFKtEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD----VEQRLMASKV 157
|
170 180 190
....*....|....*....|....*....|.
gi 578222446 181 HRRL----KTTSLYVTHDQVEAMTLAQRVMV 207
Cdd:cd03237 158 IRRFaennEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-225 |
1.94e-24 |
|
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: 104.06 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG--IAMVFQNYALYPHmS 92
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGrhIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 VEENMAwglkirGMGKGHiDERVKEAAR-------ILEL----DGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:COG4618 422 IAENIA------RFGDAD-PEKVVAAAKlagvhemILRLpdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578222446 162 LSNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQvEAMTLAQRVMVMNKGIAEQIGTPVDVYEK 225
Cdd:COG4618 495 NSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-222 |
2.34e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 100.19 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALYPHMS 92
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElaRRRAVLPQHSSLAFPFT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 VEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAI------VRDPAVFLF-DEPLSNL 165
Cdd:COG4559 92 VEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepVDGGPRWLFlDEPTSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 166 DakLRVQ---MRLeLQQLHRRlKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDV 222
Cdd:COG4559 172 D--LAHQhavLRL-ARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEV 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
33-226 |
2.41e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.65 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 33 IVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQN---YALYPhmSVEENMAWGLKIRGMG 107
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLVFQNpddQIFSP--TVEQDIAFGPINLGLD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 108 KGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTT 187
Cdd:PRK13652 111 EETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMT 190
|
170 180 190
....*....|....*....|....*....|....*....
gi 578222446 188 SLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKP 226
Cdd:PRK13652 191 VIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
23-223 |
2.64e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.55 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNY-ALYPHMSVEENMAW 99
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlrRKIGMVFQNPdNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 100 GLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQ 179
Cdd:PRK13642 106 GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578222446 180 LHRRLKTTSLYVTHDQVEAMTlAQRVMVMNKGIAEQIGTPVDVY 223
Cdd:PRK13642 186 IKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
12-228 |
3.10e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.15 E-value: 3.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 12 SWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWID--------------RQRVtemepkdrG 77
Cdd:PRK13639 10 SYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepikydkksllevRKTV--------G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 IamVFQN-----YAlyPhmSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRD 152
Cdd:PRK13639 82 I--VFQNpddqlFA--P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578222446 153 PAVFLFDEPLSNLDAKLRVQ-MRLeLQQLHRRlKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPAT 228
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQiMKL-LYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-211 |
4.38e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 103.27 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 2 AGLKLQAVTKSW---DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGI 78
Cdd:PRK10535 3 ALLELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 ------AMVFQNYALYPHMSVEENMAWGLKIRGMGKghiDERVKEAARILELDGLLKR---RPRELSGGQRQRVAMGRAI 149
Cdd:PRK10535 83 lrrehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLER---KQRLLRAQELLQRLGLEDRveyQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 150 VRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHD-QVEAMtlAQRVMVMNKG 211
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTV-IIVTHDpQVAAQ--AERVIEIRDG 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-197 |
6.83e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.86 E-value: 6.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALYPHmS 92
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 VEENMAWGLKIRGMgkgHIDER--VKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLR 170
Cdd:PRK10247 97 VYDNLIFPWQIRNQ---QPDPAifLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180
....*....|....*....|....*..
gi 578222446 171 VQMRLELQQLHRRLKTTSLYVTHDQVE 197
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-226 |
1.10e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.49 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 18 QVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPK--DRGIAMVFQNYALYPHmSVEE 95
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHylHRQVALVGQEPVLFSG-SVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 96 NMAWGLKIRGMgkghidERVKEAARILELDGLLKRRPR-----------ELSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 164
Cdd:TIGR00958 574 NIAYGLTDTPD------EEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578222446 165 LDAklrvQMRLELQQLHRRLKTTSLYVTHdQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKP 226
Cdd:TIGR00958 648 LDA----ECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-211 |
1.89e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 98.62 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKT----QVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDI-WIDRQRVTEMEPKD--- 75
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 76 ----------------------RGIAMVFQ--NYALYpHMSVEENMAWGLKIRGMGKghiDERVKEAARILELDGL---- 127
Cdd:PRK13651 83 vleklviqktrfkkikkikeirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSK---EEAKKRAAKYIELVGLdesy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 128 LKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLyVTHDQVEAMTLAQRVMV 207
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIIL-VTHDLDNVLEWTKRTIF 237
|
....
gi 578222446 208 MNKG 211
Cdd:PRK13651 238 FKDG 241
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-211 |
2.41e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.50 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGkTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-RG-IAMVFQNyalyPH- 90
Cdd:PRK13647 16 DG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSkVGLVFQD----PDd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 91 ----MSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 166
Cdd:PRK13647 91 qvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578222446 167 AKLRVQMRLELQQLHRRLKTTsLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK13647 171 PRGQETLMEILDRLHNQGKTV-IVATHDVDLAAEWADQVIVLKEG 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-225 |
2.83e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.47 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEP--KDRGIA-MVFQNyalyPHMS--- 92
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAgMVFQN----PDNQiva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 --VEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLR 170
Cdd:PRK13633 101 tiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 171 VQMRLELQQLHRRLKTTSLYVTHDQVEAMTlAQRVMVMNKGIAEQIGTPVDVYEK 225
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
3.32e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.95 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 2 AGLKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDR---GI 78
Cdd:PRK13537 6 APIDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARqrvGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNyaLYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLF 158
Cdd:PRK13537 85 VPQFDN--LDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 159 DEPLSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHDQVEAMTLAQRVMVMNKG--IAEqiGTPVDVYE 224
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTI-LLTTHFMEEAERLCDRLCVIEEGrkIAE--GAPHALIE 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-194 |
9.15e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.98 E-value: 9.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 6 LQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIdrqrvtemePKDRGIAMVFQNY 85
Cdd:COG0488 1 LENLSKSFGGRP-LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 86 ALYPHMSVEENMAWGLK-IRGMGK---------GHIDERVKEAARILE-----------------LDGL------LKRRP 132
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAeLRALEAeleeleaklAEPDEDLERLAELQEefealggweaearaeeiLSGLgfpeedLDRPV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578222446 133 RELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAklrvQMRLELQQLHRRLKTTSLYVTHD 194
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEFLKNYPGTVLVVSHD 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-194 |
1.05e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.49 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSWDGKtQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTS-----GDIWIDRQRVTE----M 71
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrvnL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 72 EPKDRGIAMVFQNYALYPhMSVEENMAWGLKIRGM-GKGHIDERVKEAARILELDGLLKRR----PRELSGGQRQRVAMG 146
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRLCIA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578222446 147 RAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHD 194
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-215 |
1.24e-22 |
|
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: 99.05 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 18 QVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPK--DRGIAMVFQNYALYPHmSVEE 95
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAwlRRQMGVVLQENVLFSR-SIRD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 96 NMAWGlkirgmGKGHIDERVKEAAR-------ILEL----DGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 164
Cdd:TIGR01846 550 NIALC------NPGAPFEHVIHAAKlagahdfISELpqgyNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSA 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578222446 165 LDAKlrvQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQ 215
Cdd:TIGR01846 624 LDYE---SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGqIAES 672
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-222 |
1.80e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 95.05 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALYPHMS 92
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 VEENMAWG------LKIRgmGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 166
Cdd:PRK10253 98 VQELVARGryphqpLFTR--WRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 167 AKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDV 222
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-227 |
1.99e-22 |
|
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: 93.97 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 20 IQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGL----ERVTSGDIWIDRQRVTEMEPKDRGIAMVFQN--YALYPHMSV 93
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLlppgLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 94 EENMAWGLKIRGMGKGHIDERVKEAARILELDG---LLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLR 170
Cdd:TIGR02770 82 GNHAIETLRSLGKLSKQARALILEALEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 171 VQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQiGTPVDVYEKPA 227
Cdd:TIGR02770 162 ARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGrIVER-GTVKEIFYNPK 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-211 |
2.69e-22 |
|
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: 93.65 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSW-----DGKT-QVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQ-RVTEM---EP 73
Cdd:COG4778 5 LEVENLSKTFtlhlqGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDgGWVDLaqaSP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 74 KD------RGIAMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELdgllkrrPREL--------SGGQ 139
Cdd:COG4778 85 REilalrrRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNL-------PERLwdlppatfSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 140 RQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRlKTTSLYVTHDQvEAM-TLAQRVMVMNKG 211
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDE-EVReAVADRVVDVTPF 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-226 |
3.35e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.87 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGL---------------ERVTSGDIWIDRQRVtemepkdrGI 78
Cdd:PRK13640 17 DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnskitvdgITLTAKTVWDIREKV--------GI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 amVFQNyalyPH-----MSVEENMAWGLKIRGMGKghiDERVKEAARILELDGLL---KRRPRELSGGQRQRVAMGRAIV 150
Cdd:PRK13640 89 --VFQN----PDnqfvgATVGDDVAFGLENRAVPR---PEMIKIVRDVLADVGMLdyiDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 151 RDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAmTLAQRVMVMNKGIAEQIGTPVDVYEKP 226
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-220 |
3.58e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 95.67 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWI------DRQRVTEMepk 74
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvpARARLARA--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 75 drGIAMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPA 154
Cdd:PRK13536 115 --RIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578222446 155 VFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHDQVEAMTLAQRVMVMNKG-----------IAEQIGTPV 220
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTI-LLTTHFMEEAERLCDRLCVLEAGrkiaegrphalIDEHIGCQV 268
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-215 |
3.66e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.61 E-value: 3.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 2 AGLKLQA---VTKSWDGKtQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTsGDIWIDRQRVTEMEPKD--R 76
Cdd:PRK11174 346 DPVTIEAedlEILSPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESwrK 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 77 GIAMVFQNYALyPHMSVEENMAwglkirgMGKGHI-DERVKEA---ARILE--------LDGLLKRRPRELSGGQRQRVA 144
Cdd:PRK11174 424 HLSWVGQNPQL-PHGTLRDNVL-------LGNPDAsDEQLQQAlenAWVSEflpllpqgLDTPIGDQAAGLSVGQAQRLA 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578222446 145 MGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRlkTTSLYVTHdQVEAMTLAQRVMVMNKG-IAEQ 215
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRR--QTTLMVTH-QLEDLAQWDQIWVMQDGqIVQQ 564
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-183 |
3.68e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIwidrqrvtEMEPKDRGIAMVF--------QNyALYPHMSVE 94
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI--------KLDGGDIDDPDVAeachylghRN-AMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 95 ENMAWGLKIRGMGKGHIDErvkeAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKlRVQMR 174
Cdd:PRK13539 92 ENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALF 166
|
....*....
gi 578222446 175 LELQQLHRR 183
Cdd:PRK13539 167 AELIRAHLA 175
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
15-204 |
4.64e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.69 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGL-----ERVTSG-------DIWIDRQRVTEMEpkdRGIAMVF 82
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGsivynghNIYSPRTDTVDLR---KEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QNYALYPhMSVEENMAWGLKIRGMGKGHI-DERV----KEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFL 157
Cdd:PRK14239 93 QQPNPFP-MSIYENVVYGLRLKGIKDKQVlDEAVekslKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578222446 158 FDEPLSNLDAKLRVQMRLELQQLhrRLKTTSLYVTHDQVEAMTLAQR 204
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDR 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-223 |
4.91e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 94.30 E-value: 4.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 6 LQAVTKSWDGKT----QVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGL-----ERVTSGDIWI--DRQRVTEMEPK 74
Cdd:PRK13645 9 LDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetGQTIVGDYAIpaNLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 75 DRGIAMVFQ--NYALYPHmSVEENMAWGLKIRGMGKGHIDERVKEAARILEL-DGLLKRRPRELSGGQRQRVAMGRAIVR 151
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578222446 152 DPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVY 223
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-264 |
4.92e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.04 E-value: 4.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVT------EMEPKDRGIAMVFQnyalYPHM----- 91
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDIKQIRKKVGLVFQ----FPESqlfee 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 92 SVEENMAWGLKIRGMGKGHIDERVKEAARILELD-GLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLR 170
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 171 VQMRLELQQLHRRLKTTSLyVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKpaTRFVASF-IGSPAMNLLEGRISN 249
Cdd:PRK13649 182 KELMTLFKKLHQSGMTIVL-VTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD--VDFLEEKqLGVPKITKFAQRLAD 258
|
250
....*....|....*
gi 578222446 250 AGTHFElesgmALPI 264
Cdd:PRK13649 259 RGISFS-----SLPI 268
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
21-219 |
6.43e-22 |
|
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: 96.95 E-value: 6.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 21 QPLTLD-----VADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALYPHmSV 93
Cdd:TIGR03797 465 GPLILDdvslqIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAvrRQLGVVLQNGRLMSG-SI 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 94 EENMAWGLKIRgmgkghIDErVKEAARILELDGLLKRRP-----------RELSGGQRQRVAMGRAIVRDPAVFLFDEPL 162
Cdd:TIGR03797 544 FENIAGGAPLT------LDE-AWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILLFDEAT 616
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 163 SNLDAKLR--VQMRLElqqlhrRLKTTSLYVTHDQVEAMTlAQRVMVMNKGIAEQIGTP 219
Cdd:TIGR03797 617 SALDNRTQaiVSESLE------RLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTY 668
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-215 |
6.97e-22 |
|
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: 92.93 E-value: 6.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPK--DRGIAMVFQNYALYpHMSVEEN 96
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 97 MAwgLKIRGMGKghidERVKEAAR-------ILEL----DGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 165
Cdd:cd03252 96 IA--LADPGMSM----ERVIEAAKlagahdfISELpegyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578222446 166 DAKlrvQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQ 215
Cdd:cd03252 170 DYE---SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGrIVEQ 217
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-211 |
7.94e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.38 E-value: 7.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIwidrqRVTEMEP-KDR-----GIAMVF-QNYALYPHMSVEE 95
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV-----RVLGYVPfKRRkefarRIGVVFgQRSQLWWDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 96 NMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQR--VAMgrAIVRDPAVFLFDEPLSNLDAKLRVQM 173
Cdd:COG4586 116 SFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRceLAA--ALLHRPKILFLDEPTIGLDVVSKEAI 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 578222446 174 RLELQQLHRRLKTTSLYVTHD--QVEAmtLAQRVMVMNKG 211
Cdd:COG4586 194 REFLKEYNRERGTTILLTSHDmdDIEA--LCDRVIVIDHG 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-217 |
9.13e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 92.21 E-value: 9.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRqRVTemepkdrgiAMVFQNYALYPHMSV 93
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVS---------SLLGLGGGFNPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 94 EENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQM 173
Cdd:cd03220 102 RENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 578222446 174 RLELQQLHRRLKtTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIG 217
Cdd:cd03220 182 QRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-211 |
1.77e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.41 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMvagLERV---TSGDIWIDRQRVTEMEPKD--RGIAMVFQ 83
Cdd:PRK13657 340 VSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINL---LQRVfdpQSGRILIDGTDIRTVTRASlrRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYpHMSVEENmawglkIRgMGK-GHIDERVKEAARILE-LDGLLKR----------RPRELSGGQRQRVAMGRAIVR 151
Cdd:PRK13657 417 DAGLF-NRSIEDN------IR-VGRpDATDEEMRAAAERAQaHDFIERKpdgydtvvgeRGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 152 DPAVFLFDEPLSNLDAKLRVQMRLELQQLhRRLKTTslYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDEL-MKGRTT--FIIAHRLSTVRNADRILVFDNG 545
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-222 |
2.17e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.49 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSWDGKtQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEM---EPKDRG 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 IAMVFQNYALYPHMSVEENMAWGLKIR-GMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVF 156
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 157 LFDEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDV 222
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-222 |
2.24e-21 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 91.07 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 25 LDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQrvtEMEPKDRGIAMVFQNYAL---YPhMSVEENMAWGl 101
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA---SPGKGWRHIGYVPQRHEFawdFP-ISVAHTVMSG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 102 KIRGMG----KGHIDER-VKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMrLE 176
Cdd:TIGR03771 76 RTGHIGwlrrPCVADFAaVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL-TE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 578222446 177 LQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQiGTPVDV 222
Cdd:TIGR03771 155 LFIELAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIAD-GTPQQL 199
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-211 |
3.63e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.71 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD---RG 77
Cdd:PRK11614 3 KVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimrEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 IAMVFQNYALYPHMSVEENMAWGlkirgmgkGHIDERVKEAARILELDGLLKR-------RPRELSGGQRQRVAMGRAIV 150
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMG--------GFFAERDQFQERIKWVYELFPRlherriqRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578222446 151 RDPAVFLFDEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-168 |
3.70e-21 |
|
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: 89.73 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPK-DRGIAMVF 82
Cdd:TIGR01189 1 LAARNLACSRGERM-LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAArileLDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPL 162
Cdd:TIGR01189 80 HLPGLKPELSALENLHFWAAIHGGAQRTIEDALAAVG----LTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
....*.
gi 578222446 163 SNLDAK 168
Cdd:TIGR01189 156 TALDKA 161
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-225 |
5.08e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.38 E-value: 5.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 18 QVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVT------EMEPKDRGIAMVFQnyalYPHM 91
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkYIRPVRKRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 92 -----SVEENMAWGLKIRGMgkgHIDErVKEAARILELD-----GLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:PRK13646 97 qlfedTVEREIIFGPKNFKM---NLDE-VKNYAHRLLMDlgfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578222446 162 LSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEK 225
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-211 |
6.07e-21 |
|
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: 88.64 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDR---GIAMV---FQNYALYPHMS 92
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYVpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 VEENMAWglkirgmgkghidervkeaarileldgllkrrPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDaklrVQ 172
Cdd:cd03215 95 VAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD----VG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578222446 173 MRLELQQLHRRLK---TTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:cd03215 139 AKAEIYRLIRELAdagKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-193 |
1.06e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.33 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIwidrQRvtemePKDRGIAMVFQ---------- 83
Cdd:COG4178 374 DGRP-LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI----AR-----PAGARVLFLPQrpylplgtlr 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYALYPHMsvEENMAwglkirgmgkghiDERVKEAARILELDGLLKR------RPRELSGGQRQRVAMGRAIVRDPAVFL 157
Cdd:COG4178 444 EALLYPAT--AEAFS-------------DAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLF 508
|
170 180 190
....*....|....*....|....*....|....*..
gi 578222446 158 FDEPLSNLDAKLRVQMrleLQQLHRRL-KTTSLYVTH 193
Cdd:COG4178 509 LDEATSALDEENEAAL---YQLLREELpGTTVISVGH 542
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-227 |
1.12e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.38 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKS----TLLRMV--AGLErVTSGDIWI---DRQRVTEMEPKD------RG-- 77
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGL-VQCDKMLLrrrSRQVIELSEQSAaqmrhvRGad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 IAMVFQN--YALYPHMSVEENMAWGLKI-RGMGKghiDERVKEAARILEL------DGLLKRRPRELSGGQRQRVAMGRA 148
Cdd:PRK10261 106 MAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASR---EEAMVEAKRMLDQvripeaQTILSRYPHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 149 IVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPA 227
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-211 |
1.25e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 89.36 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKtQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLE--RVTSGDIWIDRQRVTEMEPKDR---GI 78
Cdd:COG0396 1 LEIKNLHVSVEGK-EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaraGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYPHMSVEE--NMAWGlKIRG--MGKGHIDERVKEAARILELD-GLLKRRPRE-LSGGQRQRVAMGRAIVRD 152
Cdd:COG0396 80 FLAFQYPVEIPGVSVSNflRTALN-ARRGeeLSAREFLKLLKEKMKELGLDeDFLDRYVNEgFSGGEKKRNEILQMLLLE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 153 PAVFLFDEPLSNLDA-KLRVqMRLELQQLHRRlKTTSLYVTH-----DQVEamtlAQRVMVMNKG 211
Cdd:COG0396 159 PKLAILDETDSGLDIdALRI-VAEGVNKLRSP-DRGILIITHyqrilDYIK----PDFVHVLVDG 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-211 |
1.61e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 92.28 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLQAVTKSWDGkTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRV---TEMEPKDRG 77
Cdd:PRK11288 2 SPYLSFDGIGKTFPG-VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 IAMVFQNYALYPHMSVEENMAWG-LKIRGmgkGHIDER--VKEAARILELDGL---LKRRPRELSGGQRQRVAMGRAIVR 151
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGqLPHKG---GIVNRRllNYEAREQLEHLGVdidPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 152 DPAVFLFDEPLSNLDAKlrvqmrlELQQLHR---RLK---TTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK11288 158 NARVIAFDEPTSSLSAR-------EIEQLFRvirELRaegRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-194 |
1.62e-20 |
|
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: 92.42 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 2 AGLKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIA 79
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 80 MVFQNYALYpHMSVEENMAWGlkiRGMGKghiDERVKEAARILELDGLLKRRP-----------RELSGGQRQRVAMGRA 148
Cdd:TIGR02868 413 VCAQDAHLF-DTTVRENLRLA---RPDAT---DEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578222446 149 IVRDPAVFLFDEPLSNLDAKLRVQM-RLELQQLHRRlktTSLYVTHD 194
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELlEDLLAALSGR---TVVLITHH 529
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
19-218 |
2.81e-20 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 92.31 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMePKDR---GIAMVFQNYALYpHMSVEE 95
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI-PREVlanSVAMVDQDIFLF-EGTVRD 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 96 NMA-WGLKIRgmgkghiDERVKEAARILELDGLLKRRP-----------RELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:TIGR03796 572 NLTlWDPTIP-------DADLVRACKDAAIHDVITSRPggydaelaeggANLSGGQRQRLEIARALVRNPSILILDEATS 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 164 NLDAklrvQMRLELQQLHRRLKTTSLYVTHdQVEAMTLAQRVMVMNKGIAEQIGT 218
Cdd:TIGR03796 645 ALDP----ETEKIIDDNLRRRGCTCIIVAH-RLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-221 |
2.96e-20 |
|
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: 91.70 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALYPHmSVEEN 96
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVALVSQDVVLFND-TIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 97 MAWGlkirgMGKGHIDERVKEAARILELDGLLKRRPR-----------ELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 165
Cdd:TIGR02203 426 IAYG-----RTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578222446 166 DAKLRVQMRLELQQLHRrlKTTSLYVTHdQVEAMTLAQRVMVMNKG-IAEQiGTPVD 221
Cdd:TIGR02203 501 DNESERLVQAALERLMQ--GRTTLVIAH-RLSTIEKADRIVVMDDGrIVER-GTHNE 553
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-211 |
3.05e-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: 87.52 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQP----LTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRqrvtemepkdrGIA 79
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlkdINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 80 MVFQNyALYPHMSVEENMAWGLKIRgmgkghiDERVKEAARI--LELDglLKRRPR-------E----LSGGQRQRVAMG 146
Cdd:cd03250 70 YVSQE-PWIQNGTIRENILFGKPFD-------EERYEKVIKAcaLEPD--LEILPDgdlteigEkginLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 147 RAIVRDPAVFLFDEPLSNLDAKLRVQ-MRLELQQLHRRLKTTSLyVTHdQVEAMTLAQRVMVMNKG 211
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHiFENCILGLLLNNKTRIL-VTH-QLQLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-227 |
4.47e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.52 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQ----VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWI-----------DRQRV 68
Cdd:PRK13631 22 LRVKNLYCVFDEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 69 TEMEPK-------DRGIAMVFQ--NYALYPHmSVEENMAWGLKIRGMGKghiDERVKEAARILELDGL----LKRRPREL 135
Cdd:PRK13631 102 NPYSKKiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKK---SEAKKLAKFYLNKMGLddsyLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 136 SGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMrLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQ 215
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|..
gi 578222446 216 IGTPVDVYEKPA 227
Cdd:PRK13631 257 TGTPYEIFTDQH 268
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-225 |
6.03e-20 |
|
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: 90.63 E-value: 6.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKtQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLE--RVTSGDI-----------WIDRQRV-- 68
Cdd:TIGR03269 1 IEVKNLTKKFDGK-EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgYVERPSKvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 69 -------TEMEPKD---------------RGIAMVFQ-NYALYPHMSVEENMAWGLKIRGMgKGhiDERVKEAARILELD 125
Cdd:TIGR03269 80 epcpvcgGTLEPEEvdfwnlsdklrrrirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGY-EG--KEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 126 GLLKRR---PRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD---AKLRVQMRLELQqlhrRLKTTSLYVTHDQVEAM 199
Cdd:TIGR03269 157 QLSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHNALEEAV----KASGISMVLTSHWPEVI 232
|
250 260
....*....|....*....|....*..
gi 578222446 200 T-LAQRVMVMNKGIAEQIGTPVDVYEK 225
Cdd:TIGR03269 233 EdLSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-235 |
6.80e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.80 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQ---------RVTEMEPKdRGIAMVFQNYALYP 89
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifQIDAIKLR-KEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 90 HMSVEENMAWGLKIRGMG-KGHIDERVKEAARIL----ELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 164
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 165 LDaklrVQMRLELQQLHRRLKT--TSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASFI 235
Cdd:PRK14246 184 ID----IVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-211 |
1.40e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 18 QVIQPLTLDVADGEFIVMVGPSGCGKS----TLLRMVAGLERV-TSGDIWIDRQRVTEM-EPKDRG-----IAMVFQN-- 84
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHAsEQTLRGvrgnkIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 85 YALYPHMSVEENMAWGLKI-RGMGKghidervkEAARILELDGL-----------LKRRPRELSGGQRQRVAMGRAIVRD 152
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLhRGMRR--------EAARGEILNCLdrvgirqaakrLTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 153 PAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-227 |
1.49e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 88.24 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGL---ERVTSGDIWIDRQRVTEMEPKD------RGIAMVFQN 84
Cdd:PRK09473 26 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKElnklraEQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 85 --YALYPHMSVEENMAWGLKI-RGMGKGH-IDERVK--EAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLF 158
Cdd:PRK09473 106 pmTSLNPYMRVGEQLMEVLMLhKGMSKAEaFEESVRmlDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 159 DEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPA 227
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPS 254
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-218 |
2.20e-19 |
|
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: 89.11 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 2 AGLKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIA 79
Cdd:COG5265 356 GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlrAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 80 MVFQNYALYpHMSVEENMAWGlkiRgmgKGHIDERVKEAARILELDGLLKRRPR-----------ELSGGQRQRVAMGRA 148
Cdd:COG5265 436 IVPQDTVLF-NDTIAYNIAYG---R---PDASEEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIART 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578222446 149 IVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRlkTTSLYVTH------DqveamtlAQRVMVMNKG-IAEQiGT 218
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVARG--RTTLVIAHrlstivD-------ADEILVLEAGrIVER-GT 575
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
15-239 |
2.36e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALYPHMS 92
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVASVPQDTSLSFEFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 VEENMAWGL---KIRGMGKGHIDER-VKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 168
Cdd:PRK09536 94 VRQVVEMGRtphRSRFDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 169 LRVQMrLELQqlhRRL---KTTSLYVTHDqveaMTLAQR----VMVMNKGIAEQIGTPVDVYEKPATRfvASFIGSPA 239
Cdd:PRK09536 174 HQVRT-LELV---RRLvddGKTAVAAIHD----LDLAARycdeLVLLADGRVRAAGPPADVLTADTLR--AAFDARTA 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-238 |
2.49e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 86.38 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 18 QVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVT--EMEPKDRGIAMVFQN--YALYPHMSV 93
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 94 EENMAWGLKIRGMGKGhiDERVKEAARILELDGLLKRR----PRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKL 169
Cdd:PRK15112 107 SQILDFPLRLNTDLEP--EQREKQIIETLRQVGLLPDHasyyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 170 RVQ---MRLELQQLHrrlKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKP----ATRFVASFIGSP 238
Cdd:PRK15112 185 RSQlinLMLELQEKQ---GISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPlhelTKRLIAGHFGEA 257
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-225 |
4.76e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.13 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIdRQRVTEMepkdRGIAMVFQnyalyPHMSVEENMA 98
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV-NGRVSAL----LELGAGFH-----PELTGRENIY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 99 WGLKIRGMGKGHIDERVKEaarILELDGLLK--RRP-RELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDA--KLRVQM 173
Cdd:COG1134 111 LNGRLLGLSRKEIDEKFDE---IVEFAELGDfiDQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafQKKCLA 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578222446 174 RLElqQLHRRLKTTsLYVTHD--QVEamTLAQRVMVMNKGIAEQIGTPVDVYEK 225
Cdd:COG1134 188 RIR--ELRESGRTV-IFVSHSmgAVR--RLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-264 |
1.52e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.50 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 16 KTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVT-EMEPKD-----RGIAMVFQnyalYP 89
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNlkklrKKVSLVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 90 HMSVEENMAwgLKIRGMGK---GHIDERVKEAA-----RILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:PRK13641 95 EAQLFENTV--LKDVEFGPknfGFSEDEAKEKAlkwlkKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 162 LSNLDAKLRVQMrLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPaTRFVASFIGSPAMN 241
Cdd:PRK13641 173 AAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK-EWLKKHYLDEPATS 250
|
250 260
....*....|....*....|...
gi 578222446 242 LLEGRISNAGTHFeleSGMALPI 264
Cdd:PRK13641 251 RFASKLEKGGFKF---SEMPLTI 270
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
2.27e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.13 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIW-----IDRQRVTEMEPKdRGI 78
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILfdgkpIDYSRKGLMKLR-ESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQ--NYALYPhMSVEENMAWGLKIRGMGKGHIDERVKeaaRILELDGL--LKRRPRE-LSGGQRQRVAMGRAIVRDP 153
Cdd:PRK13636 85 GMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVD---NALKRTGIehLKDKPTHcLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578222446 154 AVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEK 225
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-179 |
2.84e-18 |
|
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: 81.77 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPK-DRGIAMVFQNYALYPHMSVEENM 97
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 98 AWGLKIrgmgkgHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD----AKLRVQM 173
Cdd:cd03231 95 RFWHAD------HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARFAEAM 168
|
....*.
gi 578222446 174 RLELQQ 179
Cdd:cd03231 169 AGHCAR 174
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-211 |
3.83e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDR---GIAM 80
Cdd:PRK09700 6 ISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAWG-LKIRG-MGKGHID-ERVKEAARILELDGLLKRRPRE----LSGGQRQRVAMGRAIVRDP 153
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGrHLTKKvCGVNIIDwREMRVRAAMMLLRVGLKVDLDEkvanLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 154 AVFLFDEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
25-226 |
5.13e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.35 E-value: 5.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 25 LDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEM---EPKDRGIAMVFQNYALYPHMSVEENM---- 97
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghQIARMGVVRTFQHVRLFREMTVIENLlvaq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 98 ---------AWGLKIRGMGKGHiDERVKEAARILELDGLLKRRPRE---LSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 165
Cdd:PRK11300 106 hqqlktglfSGLLKTPAFRRAE-SEALDRAATWLERVGLLEHANRQagnLAYGQQRRLEIARCMVTQPEILMLDEPAAGL 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578222446 166 DAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKP 226
Cdd:PRK11300 185 NPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-195 |
5.57e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.54 E-value: 5.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDrqrvtemepkdrgiamvFQNYALYPHMSV 93
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----------------VPDNQFGREASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 94 EENMAwglkirgmgkghIDERVKEAARILELDGL-----LKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 168
Cdd:COG2401 103 IDAIG------------RKGDFKDAVELLNAVGLsdavlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*..
gi 578222446 169 LRVQMRLELQQLHRRLKTTSLYVTHDQ 195
Cdd:COG2401 171 TAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-211 |
5.63e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.68 E-value: 5.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEfIV-MVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD---RGIAMVFQN---YALYPHM 91
Cdd:COG1129 267 VVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairAGIAYVPEDrkgEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 92 SVEENMAWGLKIRGMGKGHIDERvKEAARILELDGLLKRRP-------RELSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 164
Cdd:COG1129 346 SIRENITLASLDRLSRGGLLDRR-RERALAEEYIKRLRIKTpspeqpvGNLSGGNQQKVVLAKWLATDPKVLILDEPTRG 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578222446 165 LD--AKlrvqmrLELQQLHRRLK---TTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:COG1129 425 IDvgAK------AEIYRLIRELAaegKAVIVISSELPELLGLSDRILVMREG 470
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-211 |
1.16e-17 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 81.42 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDI-WIDRQRVTEM-----EPKDRG 77
Cdd:TIGR02323 4 LQVSGLSKSY-GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYIMRSGAELElyqlsEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 IA-----MVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDeRVKEAA----RILELD-GLLKRRPRELSGGQRQRVAMGR 147
Cdd:TIGR02323 83 LMrtewgFVHQNPRDGLRMRVSAGANIGERLMAIGARHYG-NIRATAqdwlEEVEIDpTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 148 AIVRDPAVFLFDEPLSNLDakLRVQMRLE--LQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLD--VSVQARLLdlLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQG 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-215 |
1.31e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.72 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQ-VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAM 80
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlrQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHmSVEENMAwglkirgMGKGHI-DERVKEAARILELDGLLKRRP----------RELSGGQRQRVAMGRAI 149
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNLL-------LAAPNAsDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578222446 150 VRDPAVFLFDEPLSNLDAKLRVQMrLELQQLHRRLKTTsLYVTHdQVEAMTLAQRVMVMNKG-IAEQ 215
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQI-LELLAEHAQNKTV-LMITH-RLTGLEQFDRICVMDNGqIIEQ 554
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-211 |
1.44e-17 |
|
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: 79.28 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGK-TQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRG-IAMV 81
Cdd:cd03247 1 LSINNVSFSYPEQeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSlISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNYALYphmsveenmawglkirgmgkghidervkeAARILELDGllkrrpRELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:cd03247 81 NQRPYLF-----------------------------DTTLRNNLG------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578222446 162 LSNLDAKLRVQ-MRLELQQLHRRlktTSLYVTHdQVEAMTLAQRVMVMNKG 211
Cdd:cd03247 126 TVGLDPITERQlLSLIFEVLKDK---TLIWITH-HLTGIEHMDKILFLENG 172
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-215 |
5.00e-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: 82.48 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMepkDRGIAMVFQ 83
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NY-ALYPHM---SVEENMAWGLKirgmgKGHIDERVKEAARILELDGLLKRRPR-----------ELSGGQRQRVAMGRA 148
Cdd:TIGR01193 551 NYlPQEPYIfsgSILENLLLGAK-----ENVSQDEIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 149 IVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRlktTSLYVTHdQVEAMTLAQRVMVMNKG-IAEQ 215
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAH-RLSVAKQSDKIIVLDHGkIIEQ 689
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-223 |
5.49e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.67 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 18 QVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDI-WidrqrvtEMEPKD---RG-------IAMVFQNya 86
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlW-------QGKPLDyskRGllalrqqVATVFQD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 87 lyP-----HMSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:PRK13638 86 --PeqqifYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 162 LSNLDAKLRVQMrlelQQLHRRLKTTSLYV---THDQVEAMTLAQRVMVMNKGIAEQIGTPVDVY 223
Cdd:PRK13638 164 TAGLDPAGRTQM----IAIIRRIVAQGNHViisSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-195 |
5.79e-17 |
|
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: 76.72 E-value: 5.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRqrvtemepkdrgiamvfq 83
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 nyalyphmsveenmawGLKIrgmgkGHIDervkeaarileldgllkrrprELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:cd03221 62 ----------------TVKI-----GYFE---------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190
....*....|....*....|....*....|..
gi 578222446 164 NLDaklrVQMRLELQQLHRRLKTTSLYVTHDQ 195
Cdd:cd03221 100 HLD----LESIEALEEALKEYPGTVILVSHDR 127
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-211 |
2.40e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 77.66 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWdGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDI--------WIDRQRVTEMEPK- 74
Cdd:PRK11701 7 LSVRGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqLRDLYALSEAERRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 75 ----DRGIamVFQNYALYPHMSV-------EENMAWGLK----IRGMGkGHIDERVK-EAARILELdgllkrrPRELSGG 138
Cdd:PRK11701 86 llrtEWGF--VHQHPRDGLRMQVsaggnigERLMAVGARhygdIRATA-GDWLERVEiDAARIDDL-------PTTFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 139 QRQRVAMGRAIVRDPAVFLFDEPLSNLDakLRVQMRL--ELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLD--VSVQARLldLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-211 |
3.23e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.92 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 30 GEFIVMVGPSGCGKSTLLRMVAGleRVTS----GDIWIDRQRVTEmePKDRGIAMVFQNYALYPHMSVEENMAWGLKIRG 105
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAG--RIQGnnftGTILANNRKPTK--QILKRTGFVTQDDILYPHLTVRETLVFCSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 106 MGKGHIDERVKEAARILELDGLLKRRP--------RELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLEL 177
Cdd:PLN03211 170 PKSLTKQEKILVAESVISELGLTKCENtiignsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170 180 190
....*....|....*....|....*....|....*.
gi 578222446 178 QQLHRRLKT--TSLYVTHDQVEAMTlaQRVMVMNKG 211
Cdd:PLN03211 250 GSLAQKGKTivTSMHQPSSRVYQMF--DSVLVLSEG 283
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-194 |
3.45e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIdRQRVTemepkdrgIAMVFQ 83
Cdd:COG0488 316 LELEGLSKSYGDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--------IGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 NYA-LYPHMSVEENMAwglkirgmgkghideRVKEAARILELDGLLKR----------RPRELSGGQRQRVAMGRAIVRD 152
Cdd:COG0488 386 HQEeLDPDKTVLDELR---------------DGAPGGTEQEVRGYLGRflfsgddafkPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 578222446 153 PAVFLFDEPLSNLDaklrVQMRLELQQLhrrLKT---TSLYVTHD 194
Cdd:COG0488 451 PNVLLLDEPTNHLD----IETLEALEEA---LDDfpgTVLLVSHD 488
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-219 |
4.07e-16 |
|
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: 76.38 E-value: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKST----LLRMVagleRVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALY---- 88
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHDlrSRISIIPQDPVLFsgti 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 89 -----PHMSVEENMAWG-LKirgmgKGHIDERVKEAAriLELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPL 162
Cdd:cd03244 95 rsnldPFGEYSDEELWQaLE-----RVGLKEFVESLP--GGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 163 SNLDaklrVQMRLELQQ-LHRRLK-TTSLYVTHdQVEAMTLAQRVMVMNKGIAEQIGTP 219
Cdd:cd03244 168 ASVD----PETDALIQKtIREAFKdCTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-168 |
4.85e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.61 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDI-W----IDRQRvtemepKDRGIAMVF---QNyALYPHMSVE 94
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlWqgepIRRQR------DEYHQDLLYlghQP-GIKTELTAL 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578222446 95 ENMAWGLKIRGMGKghiDERVKEAariLELDGLLKRR--P-RELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 168
Cdd:PRK13538 93 ENLRFYQRLHGPGD---DEALWEA---LAQVGLAGFEdvPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-166 |
7.09e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 75.66 E-value: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 17 TQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEpKDRGIAMVFQNYALYPHMSVEEN 96
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-RSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 97 MAWglkIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 166
Cdd:PRK13543 103 LHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-222 |
8.05e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.36 E-value: 8.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 2 AGLKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIA 79
Cdd:PRK10575 10 TTFALRNVSFRVPGRT-LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 80 MVFQNYALYPHMSVEENMAWGlkiR-----GMGK-GHID-ERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRD 152
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAIG---RypwhgALGRfGAADrEKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578222446 153 PAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG--IAEqiGTPVDV 222
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGemIAQ--GTPAEL 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-211 |
1.24e-15 |
|
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: 74.49 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKtQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLE--RVTSGDIWIDRQRVTEMEPKDR---GI 78
Cdd:cd03217 1 LEIKDLHVSVGGK-EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYPHMSVEEnmawglKIRGMGKGhidervkeaarileldgllkrrpreLSGGQRQRVAMGRAIVRDPAVFLF 158
Cdd:cd03217 80 FLAFQYPPEIPGVKNAD------FLRYVNEG-------------------------FSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578222446 159 DEPLSNLDAklrVQMRL---ELQQLhRRLKTTSLYVTH-----DQVEamtlAQRVMVMNKG 211
Cdd:cd03217 129 DEPDSGLDI---DALRLvaeVINKL-REEGKSVLIITHyqrllDYIK----PDRVHVLYDG 181
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
27-226 |
3.54e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.55 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 27 VADGEFIVMVGPSGCGKSTLLRMVAGL----ERVTSGDIWIDRQRVTEMEPKDR------GIAMVFQN--YALYPHMSVE 94
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPCYTVG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 95 ENMAWGLKIRGMGKGHidERVKEAARILELDGL------LKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 168
Cdd:PRK11022 110 FQIMEAIKVHQGGNKK--TRRQRAIDLLNQVGIpdpasrLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 169 LRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKP 226
Cdd:PRK11022 188 IQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-211 |
3.86e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDgKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLervTSGDIWIDRQ------------RVTEM 71
Cdd:PRK09984 5 IRVEKLAKTFN-QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGSHiellgrtvqregRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 72 EPKDRG-IAMVFQNYALYPHMSVEENMAWGLK-----IRGMGKGHIDERVKEAARILELDGLLK---RRPRELSGGQRQR 142
Cdd:PRK09984 81 IRKSRAnTGYIFQQFNLVNRLSVLENVLIGALgstpfWRTCFSWFTREQKQRALQALTRVGMVHfahQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578222446 143 VAMGRAIVRDPAVFLFDEPLSNLDAKlrvQMRLELQQLHRRLKT--TSLYVTHDQVE-AMTLAQRVMVMNKG 211
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPE---SARIVMDTLRDINQNdgITVVVTLHQVDyALRYCERIVALRQG 229
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-194 |
3.98e-15 |
|
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: 74.33 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 27 VADGEFIVMVGPSGCGKSTLLRMVAG-----LERVTSGDIW---IDRQRVTEME-------PKDRGIAMVFQNYALYPHm 91
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGklkpnLGKFDDPPDWdeiLDEFRGSELQnyftkllEGDVKVIVKPQYVDLIPK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 92 SVEENMAWGLKiRGMGKGHIDERVKEaariLELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRV 171
Cdd:cd03236 102 AVKGKVGELLK-KKDERGKLDELVDQ----LELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|...
gi 578222446 172 QMRLELQQLHRRLKTTsLYVTHD 194
Cdd:cd03236 177 NAARLIRELAEDDNYV-LVVEHD 198
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-219 |
4.38e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.24 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 30 GEFIVMVGPSGCGKSTLL-----RMVAGLERvtSGDIWIDRQRVTEMEPKDRGiAMVFQNYALYPHMSVEENMAWG--LK 102
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMPIDAKEMRAIS-AYVQQDDLFIPTLTVREHLMFQahLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 103 I-RGMGKGHIDERVKEaarILELDGLLK---------RRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ 172
Cdd:TIGR00955 128 MpRRVTKKEKRERVDE---VLQALGLRKcantrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578222446 173 MRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTP 219
Cdd:TIGR00955 205 VVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSP 251
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-193 |
7.47e-15 |
|
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: 71.42 E-value: 7.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIdrqrvtemePKDRGIAMVFQNyalyPHMSv 93
Cdd:cd03223 12 DGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR----PYLP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 94 eenmawglkirgmgkghidervkeaarilelDGLLK---RRP--RELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 168
Cdd:cd03223 77 -------------------------------LGTLReqlIYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180
....*....|....*....|....*
gi 578222446 169 lrVQMRLeLQQLHRRLkTTSLYVTH 193
Cdd:cd03223 126 --SEDRL-YQLLKELG-ITVISVGH 146
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-207 |
1.10e-14 |
|
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: 71.45 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 26 DVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTemepkdrgiamvfqnyalyphmsveenmawglkirg 105
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 106 mgkghidervkeaarileldglLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLK 185
Cdd:cd03222 65 ----------------------YKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|..
gi 578222446 186 TTSLYVTHDQVEAMTLAQRVMV 207
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-194 |
1.24e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 2 AGLKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRgIAMV 81
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL-VAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNYAL---YPHMsVEENMAWGlKIRGMG-----KGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDP 153
Cdd:PRK15056 84 PQSEEVdwsFPVL-VEDVVMMG-RYGHMGwlrraKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578222446 154 AVFLFDEPLSNLDAKLRVQMRLELQQLhRRLKTTSLYVTHD 194
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHN 201
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-220 |
1.90e-14 |
|
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: 75.05 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRV-TEMEPKDRGIAMVFQNYALYPHMSVEENMAWGL 101
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQSLGMCPQHNILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 102 KIRGMGKghiDERVKEAARILELDGLLKRR---PRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELq 178
Cdd:TIGR01257 1029 QLKGRSW---EEAQLEMEAMLEDTGLHHKRneeAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL- 1104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578222446 179 qLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPV 220
Cdd:TIGR01257 1105 -LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL 1145
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-236 |
2.28e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.44 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKLqavTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGL-ERVT----SGDIWIDRQRV---TEME 72
Cdd:PRK14271 22 MAAVNL---TLGFAGKT-VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSIfnyRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 73 PKDRGIAMVFQNYALYPhMSVEENMAWGLKI-----RGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGR 147
Cdd:PRK14271 98 EFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAhklvpRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 148 AIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLktTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKP- 226
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPk 254
|
250
....*....|...
gi 578222446 227 ---ATRFVASFIG 236
Cdd:PRK14271 255 haeTARYVAGLSG 267
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-234 |
2.61e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIwidrqrvtEMEPKDRgIAMVFQNYALYPHM--S 92
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR-IGYVPQKLYLDTTLplT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 93 VEENMAWGLKIRGMGKGHIDERVKEAArileldgLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQ 172
Cdd:PRK09544 86 VNRFLRLRPGTKKEDILPALKRVQAGH-------LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578222446 173 MRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQiGTPVDVYEKPatRFVASF 234
Cdd:PRK09544 159 LYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCS-GTPEVVSLHP--EFISMF 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-218 |
2.87e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.81 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGkTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTS--GDIWIDRQRVTEMEPKD---RGI 78
Cdd:PRK13549 6 LEMKNITKTFGG-VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDterAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILE---LDGLLKRRPRELSGGQRQRVAMGRAIVRDPAV 155
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAqlkLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 156 FLFDEPLSNLDAKlRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGiaEQIGT 218
Cdd:PRK13549 165 LILDEPTASLTES-ETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG--RHIGT 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-221 |
3.04e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 20 IQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD---RGIAMVFQNY---ALYPHMSV 93
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkKGMAYITESRrdnGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 94 EENMAWG--LKIRGMGK--GHIDE----RVKEAAR-ILELD-GLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:PRK09700 359 AQNMAISrsLKDGGYKGamGLFHEvdeqRTAENQReLLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578222446 164 NLDaklrVQMRLELQQLHRRLK---TTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVD 221
Cdd:PRK09700 439 GID----VGAKAEIYKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
9-193 |
3.32e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 73.51 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWDGK-TQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNY 85
Cdd:PRK11176 347 VTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlrNQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 86 ALYpHMSVEENMAWGLKIRgmgkgHIDERVKEAARI---------LE--LDGLLKRRPRELSGGQRQRVAMGRAIVRDPA 154
Cdd:PRK11176 427 HLF-NDTIANNIAYARTEQ-----YSREQIEEAARMayamdfinkMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578222446 155 VFLFDEPLSNLD--AKLRVQMRLELQQLHRrlktTSLYVTH 193
Cdd:PRK11176 501 ILILDEATSALDteSERAIQAALDELQKNR----TSLVIAH 537
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-218 |
6.83e-14 |
|
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: 72.55 E-value: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGkTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGL--ERVTSGDIWIDRQRVTEMEPKD---RGI 78
Cdd:TIGR02633 2 LEMKGIVKTFGG-VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDterAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 79 AMVFQNYALYPHMSVEENMAWGLKIRGMG-KGHIDE---RVKEAARILELDGLLKRRP-RELSGGQRQRVAMGRAIVRDP 153
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGgRMAYNAmylRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 154 AVFLFDEPLSNLDAKlRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGiaEQIGT 218
Cdd:TIGR02633 161 RLLILDEPSSSLTEK-ETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG--QHVAT 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-216 |
9.66e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.46 E-value: 9.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 12 SWDGKTQ--VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGlervtsgdiwidrqrvtEMEPKDRGIAMVFQNYALYP 89
Cdd:PLN03130 623 SWDSKAErpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-----------------ELPPRSDASVVIRGTVAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 90 HMS------VEENMAWGLKIRGmgkghidERVKEAARILELDGLLK-----------RRPRELSGGQRQRVAMGRAIVRD 152
Cdd:PLN03130 686 QVSwifnatVRDNILFGSPFDP-------ERYERAIDVTALQHDLDllpggdlteigERGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 153 PAVFLFDEPLSNLDAKLRVQ-----MRLELQQLHRRLKTTSLYVThDQVEAMTLAQRVMVMNKGIAEQI 216
Cdd:PLN03130 759 SDVYIFDDPLSALDAHVGRQvfdkcIKDELRGKTRVLVTNQLHFL-SQVDRIILVHEGMIKEEGTYEEL 826
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-207 |
1.16e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.76 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 30 GEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWID------RQRVtemEPKdrgiamvfqnyalyPHMSVEENmawglkI 103
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykPQYI---KPD--------------YDGTVEDL------L 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 104 RGMGKGHIDERVK-EAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDaklrVQMRLELQQLHR 182
Cdd:PRK13409 422 RSITDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VEQRLAVAKAIR 497
|
170 180
....*....|....*....|....*....
gi 578222446 183 RL----KTTSLYVTHDQVEAMTLAQRVMV 207
Cdd:PRK13409 498 RIaeerEATALVVDHDIYMIDYISDRLMV 526
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-194 |
2.15e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.99 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 29 DGEFIVMVGPSGCGKSTLLRMVAG-----LERVTSGDIW---IDRQRVTEMepkdrgiamvfQNY-----------ALYP 89
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGelipnLGDYEEEPSWdevLKRFRGTEL-----------QNYfkklyngeikvVHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 90 HMsVEenmawglKIRGMGKG-------HIDER--VKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:PRK13409 167 QY-VD-------LIPKVFKGkvrellkKVDERgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*.
gi 578222446 161 PLSNLDaklrVQMRLELQQLHRRL--KTTSLYVTHD 194
Cdd:PRK13409 239 PTSYLD----IRQRLNVARLIRELaeGKYVLVVEHD 270
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-216 |
2.68e-13 |
|
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: 68.06 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 16 KTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGL----ERVtSGDIWIDRQRVTEMEPKDRG-IAMVFQNYALYPH 90
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSV-EGDIHYNGIPYKEFAEKYPGeIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 91 MSVEENMAWGLKIRGmgkghiDERVkeaarileldgllkrrpRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLR 170
Cdd:cd03233 98 LTVRETLDFALRCKG------NEFV-----------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578222446 171 VQMRLELQQLHRRLKTT---SLYVTHDqvEAMTLAQRVMVMNKGiaEQI 216
Cdd:cd03233 155 LEILKCIRTMADVLKTTtfvSLYQASD--EIYDLFDKVLVLYEG--RQI 199
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-222 |
3.23e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 68.71 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 21 QPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERvTSGDIWIDRQRVTEMEPKD----RG---------IAM-VFQNYA 86
Cdd:COG4138 13 GPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElarhRAylsqqqsppFAMpVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 87 LY-PHMSVEEnmawglkirgmgkgHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVR-DPAV------FLF 158
Cdd:COG4138 92 LHqPAGASSE--------------AVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvWPTInpegqlLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 159 DEPLSNLDaklrVQMRLELQQLHRRLKTTSLYV---THDQVEAMTLAQRVMVMNKG--IAEqiGTPVDV 222
Cdd:COG4138 158 DEPMNSLD----VAQQAALDRLLRELCQQGITVvmsSHDLNHTLRHADRVWLLKQGklVAS--GETAEV 220
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-196 |
3.39e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 6 LQAVTKSWDGKTQ-VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTemepKDRG-----IA 79
Cdd:PRK13540 2 LDVIELDFDYHDQpLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCtyqkqLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 80 MVFQNYALYPHMSVEENMAWGLKIRGMGKGhIDERVkeaaRILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFD 159
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLYDIHFSPGAVG-ITELC----RLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 578222446 160 EPLSNLDaKLRVQMRLELQQLHRRLKTTSLYVTHDQV 196
Cdd:PRK13540 153 EPLVALD-ELSLLTIITKIQEHRAKGGAVLLTSHQDL 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-194 |
3.41e-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: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 30 GEFIVMVGPSGCGKSTLLRMVAGLERVTSGDI-----W---IDRQRVTEMepkdrgiamvfQNY-----------ALYPH 90
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepsWdevLKRFRGTEL-----------QDYfkklangeikvAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 91 MsVEenmawglKIRGMGKG-------HIDER--VKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEP 161
Cdd:COG1245 168 Y-VD-------LIPKVFKGtvrelleKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|...
gi 578222446 162 LSNLDAKLRVQMRLELQQLHRRLKTTsLYVTHD 194
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEEGKYV-LVVEHD 271
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-218 |
4.26e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.13 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPK--DRGIAMVFQNYA 86
Cdd:PRK10790 346 VSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlRQGVAMVQQDPV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 87 LYPHmSVEENMAWGLKIRGMGKGHIDERVKEAARILEL-DGL---LKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPL 162
Cdd:PRK10790 426 VLAD-TFLANVTLGRDISEEQVWQALETVQLAELARSLpDGLytpLGEQGNNLSVGQKQLLALARVLVQTPQILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 163 SNLDAKLRVQMRLELQQLhrRLKTTSLYVTHdQVEAMTLAQRVMVMNKGIAEQIGT 218
Cdd:PRK10790 505 ANIDSGTEQAIQQALAAV--REHTTLVVIAH-RLSTIVEADTILVLHRGQAVEQGT 557
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-211 |
7.15e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.31 E-value: 7.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGkTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEP---KDRGIAM 80
Cdd:PRK15439 12 LCARSISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPakaHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAWGLKIRGMGKGHIDERVKEAARILELD---GLLKRrprelsgGQRQRVAMGRAIVRDPAVFL 157
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDssaGSLEV-------ADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 158 FDEPLSNLD----AKLRVQMRlELQQLHRRLkttsLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK15439 164 LDEPTASLTpaetERLFSRIR-ELLAQGVGI----VFISHKLPEIRQLADRISVMRDG 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-243 |
8.14e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.04 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQ-VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEmepkdrGIAMVF 82
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT------NISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QNYALYPHMSVEENMAWG-------LKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAV 155
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLTGrehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 156 FLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLyVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFVASF- 234
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL-TSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMk 2170
|
....*....
gi 578222446 235 IGSPAMNLL 243
Cdd:TIGR01257 2171 IKSPKDDLL 2179
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-219 |
8.65e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 66.67 E-value: 8.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 18 QVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALYPHmSVEE 95
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrSSLTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 96 NmawgLKIRGMgkgHIDERVKEAARILElDGLlkrrprELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL----DAKLRV 171
Cdd:cd03369 101 N----LDPFDE---YSDEEIYGALRVSE-GGL------NLSQGQRQLLCLARALLKRPRVLVLDEATASIdyatDALIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578222446 172 QMRLELQqlhrrlKTTSLYVTHdQVEAMTLAQRVMVMNKGIAEQIGTP 219
Cdd:cd03369 167 TIREEFT------NSTILTIAH-RLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-207 |
9.81e-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: 69.04 E-value: 9.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 30 GEFIVMVGPSGCGKSTLLRMVAGLERVTSGdiwidrqrvtEMEPKDRgIAMVFQnY--ALYPhMSVEENMawglkirgmg 107
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEG----------EVDEDLK-ISYKPQ-YisPDYD-GTVEEFL---------- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 108 KGHIDERVK------EAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDaklrVQMRLELQQLH 181
Cdd:COG1245 423 RSANTDDFGssyyktEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VEQRLAVAKAI 498
|
170 180 190
....*....|....*....|....*....|.
gi 578222446 182 RRL----KTTSLYVTHD-QVEAMtLAQRVMV 207
Cdd:COG1245 499 RRFaenrGKTAMVVDHDiYLIDY-ISDRLMV 528
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-211 |
1.55e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.13 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEfIVMV-GPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDR---GIA 79
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSLEVRAGE-ILGIaGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 80 MV---FQNYALYPHMSVEENMAwgLKI---RGMGK-GHIDER-VKEAARileldGLLKR---RP-------RELSGGQRQ 141
Cdd:COG3845 337 YIpedRLGRGLVPDMSVAENLI--LGRyrrPPFSRgGFLDRKaIRAFAE-----ELIEEfdvRTpgpdtpaRSLSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578222446 142 RVAMGRAIVRDPAVFLFDEPLSNLDAKlrvqmrlELQQLHRRLK------TTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVG-------AIEFIHQRLLelrdagAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
22-211 |
2.28e-12 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 68.06 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 22 PLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALY---------PH 90
Cdd:TIGR01194 360 PIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDyrDLFSAIFADFHLFddligpdegEH 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 91 MSVEENMAWglkirgMGKGHIDERVKeaarileLDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLR 170
Cdd:TIGR01194 440 ASLDNAQQY------LQRLEIADKVK-------IEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFK 506
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578222446 171 VQMRLE-LQQLHRRLKTTsLYVTHDQvEAMTLAQRVMVMNKG 211
Cdd:TIGR01194 507 RFFYEElLPDLKRQGKTI-IIISHDD-QYFELADQIIKLAAG 546
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-227 |
2.38e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 66.26 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKS-----TLLRMVAGLERvTSGDIWIDRQRVTEMEPKDRGIAMVFQN--YALYPHMSVEE 95
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPVAPCALRGRKIATIMQNprSAFNPLHTMHT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 96 NMAWGLKIRGmgKGHIDERVKEAARILELDG---LLKRRPRELSGGQRQRVAMGRAIVRDpAVFLF-DEPLSNLDakLRV 171
Cdd:PRK10418 101 HARETCLALG--KPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCE-APFIIaDEPTTDLD--VVA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 172 QMR-LEL-QQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKG-IAEQiGTPVDVYEKPA 227
Cdd:PRK10418 176 QARiLDLlESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGrIVEQ-GDVETLFNAPK 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-194 |
2.68e-12 |
|
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: 67.65 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 6 LQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDrqrvtemepKDRGIAMVFQNY 85
Cdd:TIGR03719 7 MNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ---------PGIKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 86 ALYPHMSVEENMAWGL-KIRGMGK-------------GHIDERVKEAARILE---------LDGLLK------RRP---- 132
Cdd:TIGR03719 78 QLDPTKTVRENVEEGVaEIKDALDrfneisakyaepdADFDKLAAEQAELQEiidaadawdLDSQLEiamdalRCPpwda 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 133 --RELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAklrvqmrlE----LQQLHRRLKTTSLYVTHD 194
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA--------EsvawLERHLQEYPGTVVAVTHD 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-224 |
3.19e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.08 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 12 SWDGKTQ--VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGlervtsgdiwidrqrvtEMEPKDRGIAMVFQNYALYP 89
Cdd:PLN03232 623 SWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVVIRGSVAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 90 HMS------VEENMAWGLKIRgmgkghiDERVKEAARIL----ELDGLLKR-------RPRELSGGQRQRVAMGRAIVRD 152
Cdd:PLN03232 686 QVSwifnatVRENILFGSDFE-------SERYWRAIDVTalqhDLDLLPGRdlteigeRGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578222446 153 PAVFLFDEPLSNLDAKLRVQ-----MRLELQQLHRRLKTtslyvthDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYE 224
Cdd:PLN03232 759 SDIYIFDDPLSALDAHVAHQvfdscMKDELKGKTRVLVT-------NQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-211 |
3.33e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 21 QPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD---RGIAMVFQNY---ALYPHMSVE 94
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairAGIMLCPEDRkaeGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 95 ENMAWGLKIRGMGKGHIDERVKEAA----RILELDglLKRRPRE-----LSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 165
Cdd:PRK11288 350 DNINISARRHHLRAGCLINNRWEAEnadrFIRSLN--IKTPSREqlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578222446 166 DaklrVQMRLELQQLHRRL---KTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK11288 428 D----VGAKHEIYNVIYELaaqGVAVLFVSSDLPEVLGVADRIVVMREG 472
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-211 |
3.59e-12 |
|
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: 65.04 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 12 SWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDI-W----IDRQRVTEMEPKDRG-IAMVFQNY 85
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWsnknESEPSFEATRSRNRYsVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 86 ALYpHMSVEENMAWGlkiRGMGKGHIDERVKEAARILELDGL-------LKRRPRELSGGQRQRVAMGRAIVRDPAVFLF 158
Cdd:cd03290 89 WLL-NATVEENITFG---SPFNKQRYKAVTDACSLQPDIDLLpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 578222446 159 DEPLSNLDAKLRVQMRLE-LQQLHRRLKTTSLYVTHdQVEAMTLAQRVMVMNKG 211
Cdd:cd03290 165 DDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-211 |
7.73e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 7.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMV 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 82 FQNYALYPHMSVEENMA--------WgLKIRGMGkghidERVK-EAARILELDgllkrrpreLSGGQRQRVAMGRAIVRD 152
Cdd:PRK10522 403 FTDFHLFDQLLGPEGKPanpalvekW-LERLKMA-----HKLElEDGRISNLK---------LSKGQKKRLALLLALAEE 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 153 PAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQvEAMTLAQRVMVMNKG 211
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDD-HYFIHADRLLEMRNG 525
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-160 |
8.96e-12 |
|
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: 65.97 E-value: 8.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 20 IQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTemePKDRG-----IAMVFQNYALYPHMSve 94
Cdd:COG4615 348 LGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREayrqlFSAVFSDFHLFDRLL-- 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578222446 95 enmawglkirGMGKGHIDERVKEAARILELDGLLKRR-----PRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:COG4615 423 ----------GLDGEADPARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| OB_MalK |
pfam17912 |
MalK OB fold domain; This entry corresponds to one of two OB-fold domains found in the MalK ... |
236-285 |
1.50e-11 |
|
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: 58.75 E-value: 1.50e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 578222446 236 GSPAMNLLEGRISNAGtHFELESGMALPIN----WYYRGYAGRKMTLGIRPEHI 285
Cdd:pfam17912 1 GSPPMNFLPATVVEDG-LLVLGGGVTLPLPegqvLALKLYVGKEVILGIRPEHI 53
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-226 |
1.72e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.54 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLE----RVTSGDIWIDRQRVTEMEPKDR------GIAMVFQ 83
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 N--YALYPHMSV----EENM-AWGLKIRGMGKGHidERVKEAARILELDG------LLKRRPRELSGGQRQRVAMGRAIV 150
Cdd:COG4170 97 EpsSCLDPSAKIgdqlIEAIpSWTFKGKWWQRFK--WRKKRAIELLHRVGikdhkdIMNSYPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 151 RDPAVFLFDEPLSNLDAKLRVQM-RLeLQQLHRRLKTTSLYVTHDqVEAMT-LAQRVMVMNKGIAEQIGTPVDVYEKP 226
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIfRL-LARLNQLQGTSILLISHD-LESISqWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-193 |
1.85e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 65.16 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPK----DRGiamVFQNYALYPhMSVE 94
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQrpymTLG---TLRDQIIYP-DSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 95 EnmawgLKIRGMGkghiDERVKEAARILELDGLLKRR---------PRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSnl 165
Cdd:TIGR00954 543 D-----MKRRGLS----DKDLEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTS-- 611
|
170 180
....*....|....*....|....*...
gi 578222446 166 daKLRVQMRLELQQLHRRLKTTSLYVTH 193
Cdd:TIGR00954 612 --AVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-226 |
3.04e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.80 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDR------QRVTEMEPKDRGIAMVFQnyalyphmsvEEN 96
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERsiayvpQQAWIMNATVRGNILFFD----------EED 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 97 MAwglkirgmgkghideRVKEAARILELDGLLKRRPR-----------ELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 165
Cdd:PTZ00243 749 AA---------------RLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 166 DAKL--RVQMRLELQQLHRRlktTSLYVTHdQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKP 226
Cdd:PTZ00243 814 DAHVgeRVVEECFLGALAGK---TRVLATH-QVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-166 |
3.35e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.74 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLE--RVTSGDIWIDRQRVTEMEPKDR---GIAMVFQNYALYP 89
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERahlGIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 90 HMSVEE--NMAWGLKIRGMGKGHID-----ERVKEAARILELD-GLLKRRPRE-LSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:CHL00131 98 GVSNADflRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDpSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDE 177
|
....*.
gi 578222446 161 PLSNLD 166
Cdd:CHL00131 178 TDSGLD 183
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-222 |
3.90e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 22 PLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERvTSGDIWIDRQRVTEMEPKD----RG---------IAM-VFQNYAL 87
Cdd:PRK03695 14 PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAElarhRAylsqqqtppFAMpVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 88 YPHMSVEEnmawglkirgmgkGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVR-DPAV------FLFDE 160
Cdd:PRK03695 93 HQPDKTRT-------------EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 161 PLSNLDaklrVQMRLELQQLHRRLKTTSLYV---THDQVEAMTLAQRVMVMNKGIAEQIGTPVDV 222
Cdd:PRK03695 160 PMNSLD----VAQQAALDRLLSELCQQGIAVvmsSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-218 |
4.23e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.96 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD-RG-IAMVFQNYALYPHmSVEEN 96
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSrLAVVSQTPFLFSD-TVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 97 MAWGLKirgmgkGHIDERVKEAAR-------ILEL----DGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 165
Cdd:PRK10789 409 IALGRP------DATQQEIEHVARlasvhddILRLpqgyDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 578222446 166 DAKLRVQMrleLQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGT 218
Cdd:PRK10789 483 DGRTEHQI---LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-167 |
5.22e-11 |
|
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: 64.20 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKSTLLR-MVAGLERVtSGDIWIDRQrvtemepkdrgIAMVFQNyALYPHMSVEENMAWGl 101
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVHMKGS-----------VAYVPQQ-AWIQNDSLRENILFG- 722
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 102 kiRGMGKGHIDERVKEAARILELDGL-------LKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDA 167
Cdd:TIGR00957 723 --KALNEKYYQQVLEACALLPDLEILpsgdrteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
37-166 |
6.87e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.61 E-value: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 37 GPSGCGKSTLLRMVAGLERVTSGDIW-----ID------RQRVTEMEpkdrgiamvfQNYALYPHMSVEENMAWGLKIRG 105
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDagdiatRRRVGYMS----------QAFSLYGELTVRQNLELHARLFH 368
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578222446 106 MGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 166
Cdd:NF033858 369 LPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-161 |
8.81e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 8.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGkTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDR---GIAM 80
Cdd:PRK10762 5 LQLKGIDKAFPG-VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSqeaGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAWGLKIRGmGKGHIDERVKEAarilELDGLLKR-----RPR----ELSGGQRQRVAMGRAIVR 151
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGREFVN-RFGRIDWKKMYA----EADKLLARlnlrfSSDklvgELSIGEQQMVEIAKVLSF 158
|
170
....*....|
gi 578222446 152 DPAVFLFDEP 161
Cdd:PRK10762 159 ESKVIIMDEP 168
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-161 |
8.83e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.22 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWI------DRQRVTEMEPKdrgIAMVFQ----N 84
Cdd:NF033858 12 GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlggdmaDARHRRAVCPR---IAYMPQglgkN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 85 yaLYPHMSVEENMAWGLKIRGMGKGhidERvkeAARILEL---DGLL--KRRP-RELSGGQRQRVAMGRAIVRDPAVFLF 158
Cdd:NF033858 89 --LYPTLSVFENLDFFGRLFGQDAA---ER---RRRIDELlraTGLApfADRPaGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
...
gi 578222446 159 DEP 161
Cdd:NF033858 161 DEP 163
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-211 |
2.18e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 30 GEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD---RGIAMVFQNY---ALYPHMSVEENM---AWG 100
Cdd:PRK10762 278 GEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRkrdGLVLGMSVKENMsltALR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 101 LKIRGMGKGHIDERVKEAARILELDGLlKRRPRE-----LSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDaklrVQMRL 175
Cdd:PRK10762 358 YFSRAGGSLKHADEQQAVSDFIRLFNI-KTPSMEqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD----VGAKK 432
|
170 180 190
....*....|....*....|....*....|....*....
gi 578222446 176 ELQQLHRRLKTTSL---YVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK10762 433 EIYQLINQFKAEGLsiiLVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-170 |
2.20e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 59.50 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 37 GPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDRGiaMVFQNYALYPHMSVEENMAWGLKIRGMGkghidERVK 116
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCT--YIGHNLGLKLEMTVFENLKFWSEIYNSA-----ETLY 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 578222446 117 EAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLR 170
Cdd:PRK13541 106 AAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-211 |
6.37e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 6.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKDR-GIAMVF-----QNYALYphmsVEEN 96
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLY----LDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 97 MAW----------GLKIRGMGKGHIDERVKEAARILELDglLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 166
Cdd:PRK15439 358 LAWnvcalthnrrGFWIKPARENAVLERYRRALNIKFNH--AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 578222446 167 aklrVQMRLELQQLHRRL---KTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK15439 436 ----VSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-166 |
7.66e-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: 59.95 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIdrqrvtemepkdrG----IAMVFQN 84
Cdd:TIGR03719 328 LTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-------------GetvkLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 85 Y-ALYPHMSVEENMAWGLKIRGMGKGHIDERV-------KEAARileldgllKRRPRELSGGQRQRVAMGRAIVRDPAVF 156
Cdd:TIGR03719 394 RdALDPNKTVWEEISGGLDIIKLGKREIPSRAyvgrfnfKGSDQ--------QKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170
....*....|
gi 578222446 157 LFDEPLSNLD 166
Cdd:TIGR03719 466 LLDEPTNDLD 475
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-166 |
7.73e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 22 PLtLDVAD-----GEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQ-RVTEME---PKD----------RGIAMVF 82
Cdd:PRK11147 17 PL-LDNAElhiedNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlIVARLQqdpPRNvegtvydfvaEGIEEQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QNYALYPHMSV-------EENMAWGLKIRGM----GKGHIDERVKEAARILELDGllKRRPRELSGGQRQRVAMGRAIVR 151
Cdd:PRK11147 96 EYLKRYHDISHlvetdpsEKNLNELAKLQEQldhhNLWQLENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVS 173
|
170
....*....|....*
gi 578222446 152 DPAVFLFDEPLSNLD 166
Cdd:PRK11147 174 NPDVLLLDEPTNHLD 188
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-218 |
8.42e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.91 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDI-WIDRQRVTEMePKDRgiAMVF 82
Cdd:PRK15064 320 LEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYY-AQDH--AYDF 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QNyalypHMSVEENMA-WglkirgMGKGHIDERVKEA-ARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDE 160
Cdd:PRK15064 396 EN-----DLTLFDWMSqW------RQEGDDEQAVRGTlGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDE 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578222446 161 PLSNLD--AKLRVQMRLELqqlhrrLKTTSLYVTHDQVEAMTLAQRVM-VMNKGIAEQIGT 218
Cdd:PRK15064 465 PTNHMDmeSIESLNMALEK------YEGTLIFVSHDREFVSSLATRIIeITPDGVVDFSGT 519
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-211 |
1.18e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 30 GEFIVMVGPSGCGKSTLLRMVA----GLERVTSGDIWIDRQRVTEMEPKDRG-IAMVFQNYALYPHMSVEENMAWGLKI- 103
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGdVVYNAETDVHFPHLTVGETLDFAARCk 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 104 ----RGMGKGHIDERVKEAARILELDGLLKRRP--------RELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRV 171
Cdd:TIGR00956 167 tpqnRPDGVSREEYAKHIADVYMATYGLSHTRNtkvgndfvRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATAL 246
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 578222446 172 QMRLELQQLHRRLKTTSLyVTHDQV--EAMTLAQRVMVMNKG 211
Cdd:TIGR00956 247 EFIRALKTSANILDTTPL-VAIYQCsqDAYELFDKVIVLYEG 287
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
58-209 |
1.32e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 58 SGDIWIDRQRVTEMEPKD-RGIAMVFQNYALYPHMSVEENMAWGlkirgmGKGHIDERVKEAARILELDGLLKRRP---- 132
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPnkyd 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 133 -------RELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHdQVEAMTLAQRV 205
Cdd:PTZ00265 1350 tnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKI 1428
|
....
gi 578222446 206 MVMN 209
Cdd:PTZ00265 1429 VVFN 1432
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-168 |
1.35e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 18 QVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDI---------------WIDRQRVTEMEPkdrgiaMVF 82
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshnlkdinlkwWRSKIGVVSQDP------LLF 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 QN-------YALYPHMSVE--------------ENMAWGLKIRGMGKGHID------------------------ERVKE 117
Cdd:PTZ00265 473 SNsiknnikYSLYSLKDLEalsnyynedgndsqENKNKRNSCRAKCAGDLNdmsnttdsneliemrknyqtikdsEVVDV 552
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578222446 118 AARIL----------ELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 168
Cdd:PTZ00265 553 SKKVLihdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
14-226 |
1.44e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.66 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLE----RVTSGDIWIDRQRVTEMEPKDR------GIAMVFQ 83
Cdd:PRK15093 17 DGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 84 --NYALYPHMSVEENM-----AWGLKIRGMGKGHIDERvkeaaRILEL---------DGLLKRRPRELSGGQRQRVAMGR 147
Cdd:PRK15093 97 epQSCLDPSERVGRQLmqnipGWTYKGRWWQRFGWRKR-----RAIELlhrvgikdhKDAMRSFPYELTEGECQKVMIAI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 148 AIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKP 226
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
30-167 |
1.85e-09 |
|
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: 56.48 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 30 GEFIVMVGPSGCGKSTLLRMVAGleRVTS----GDIWIDRQRVTEMEPkdRGIAMVFQNYALYPHMSVEENMAWGLKIRG 105
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAG--RKTAgvitGEILINGRPLDKNFQ--RSTGYVEQQDVHSPNLTVREALRFSALLRG 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578222446 106 mgkghidervkeaarileldgllkrrpreLSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDA 167
Cdd:cd03232 109 -----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-194 |
3.22e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWID--------------------RQRV 68
Cdd:PRK11819 12 VSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApgikvgylpqepqldpektvRENV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 69 TE-----MEPKDR--GIAMvfqNYALyPHMSVEENMAwglkirGMGK---------GH-IDERVKEAArilelDGLlkRR 131
Cdd:PRK11819 92 EEgvaevKAALDRfnEIYA---AYAE-PDADFDALAA------EQGElqeiidaadAWdLDSQLEIAM-----DAL--RC 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 132 P------RELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAklrvqmrlE----LQQLHRRLKTTSLYVTHD 194
Cdd:PRK11819 155 PpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA--------EsvawLEQFLHDYPGTVVAVTHD 219
|
|
| TOBE_2 |
pfam08402 |
TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ... |
278-348 |
1.55e-08 |
|
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: 51.08 E-value: 1.55e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578222446 278 LGIRPEHIGLtSQADGGVPLVMDTLEMLGADNLAHGRWGEQKMVVRL---AHQERPKAGSTLWLHLPENHLHLF 348
Cdd:pfam08402 1 LAIRPEKIRL-AAAANGLSGTVTDVEYLGDHTRYHVELAGGEELVVRvpnAHARPPAPGDRVGLGWDPEDAHVL 73
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
17-166 |
2.23e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.41 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 17 TQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLE--RVTSGDIWIDRQRVTEMEPKDR---GIAMVFQNYALYPHM 91
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAFQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 92 SVEENMAWGL----KIRG---MGKGHIDERVKEAARILEL-DGLLKRRPRE-LSGGQRQRVAMGRAIVRDPAVFLFDEPL 162
Cdd:PRK09580 94 SNQFFLQTALnavrSYRGqepLDRFDFQDLMEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESD 173
|
....
gi 578222446 163 SNLD 166
Cdd:PRK09580 174 SGLD 177
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-166 |
2.48e-08 |
|
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: 54.48 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 17 TQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIwidrqrvtemepKDRG-IAMVFQNYALYPHmSVEE 95
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------------KHSGrISFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 96 NMAWGLKIrgmgkghiDE-RVKEAARILELDGLLKRRPRE-----------LSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:cd03291 117 NIIFGVSY--------DEyRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
...
gi 578222446 164 NLD 166
Cdd:cd03291 189 YLD 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-211 |
2.76e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWDGkTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRV---TEMEPKDRGIAMVFQNY 85
Cdd:PRK10982 4 ISKSFPG-VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 86 ALYPHMSVEENMAWG-LKIRGMGKGHiDERVKEAARIL-ELDglLKRRPRE----LSGGQRQRVAMGRAIVRDPAVFLFD 159
Cdd:PRK10982 83 NLVLQRSVMDNMWLGrYPTKGMFVDQ-DKMYRDTKAIFdELD--IDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 578222446 160 EPLSNLDAKlrvqmrlELQQLH---RRLKTTS---LYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK10982 160 EPTSSLTEK-------EVNHLFtiiRKLKERGcgiVYISHKMEEIFQLCDEITILRDG 210
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-222 |
3.35e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.06 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGL---------ERVTsGDIWID-------------RQRVTEMEPKDR 76
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggaprgARVT-GDVTLNgeplaaidaprlaRLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 77 GIAMVFQNYAL---YPHMSveenmawglkiRGMGKGHIDERVkeAARILEL---DGLLKRRPRELSGGQRQRVAMGRAI- 149
Cdd:PRK13547 95 AFAFSAREIVLlgrYPHAR-----------RAGALTHRDGEI--AWQALALagaTALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 150 --------VRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVD 221
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
.
gi 578222446 222 V 222
Cdd:PRK13547 242 V 242
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-211 |
4.49e-08 |
|
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: 54.45 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 23 LTLDVADGEFIVMVGPSGCGKSTLLRMVAGL-ERVTSGDIWIDRQRVTEMEPKD---RGIAMVFQN---YALYPHMSVEE 95
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQairAGIAMVPEDrkrHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 96 NMAWGLKIRGMGKGHIDErVKEAARILELDGLLKRRPRE-------LSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAK 168
Cdd:TIGR02633 359 NITLSVLKSFCFKMRIDA-AAELQIIGSAIQRLKVKTASpflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 578222446 169 LRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:TIGR02633 438 AKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-166 |
1.78e-07 |
|
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: 52.99 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 17 TQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGlervtsgdiwidrqrvtEMEPKDRGI------AMVFQNYALYPH 90
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG-----------------ELEPSEGKIkhsgriSFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 91 mSVEENMAWGLKIrgmgkghiDE-RVKEAARILELDGLLKRRPRE-----------LSGGQRQRVAMGRAIVRDPAVFLF 158
Cdd:TIGR01271 502 -TIKDNIIFGLSY--------DEyRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLL 572
|
....*...
gi 578222446 159 DEPLSNLD 166
Cdd:TIGR01271 573 DSPFTHLD 580
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-211 |
2.61e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 27 VADGEFIVMVGPSGCGKSTLLRMVAglERVTSGDIWIDrQRVTEMEPKD----RGIAMVFQNYALYPHMSVEENMAWGLK 102
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGG-DRLVNGRPLDssfqRSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 103 IR---GMGKGHIDERVKEAARILEL----DGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLF-DEPLSNLDAklrvQMR 174
Cdd:TIGR00956 863 LRqpkSVSKSEKMEYVEEVIKLLEMesyaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDS----QTA 938
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 578222446 175 LELQQLHRRLKTT--SLYVTHDQVEAMTLAQ--RVMVMNKG 211
Cdd:TIGR00956 939 WSICKLMRKLADHgqAILCTIHQPSAILFEEfdRLLLLQKG 979
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-183 |
2.75e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 1 MAGLKL-QAVTKSWDGKTQVIQPLTLdvADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEM--EPKDRG 77
Cdd:PRK10938 1 MSSLQIsQGTFRLSDTKTLQLPSLTL--NAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLsfEQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 78 IAMVFQ--NYALyphMSVEENmAWGLKIRGMgkghIDERVKEAARILEL------DGLLKRRPRELSGGQRQRVAMGRAI 149
Cdd:PRK10938 79 VSDEWQrnNTDM---LSPGED-DTGRTTAEI----IQDEVKDPARCEQLaqqfgiTALLDRRFKYLSTGETRKTLLCQAL 150
|
170 180 190
....*....|....*....|....*....|....
gi 578222446 150 VRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRR 183
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-204 |
3.92e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.91 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 30 GEFIVMVGPSGCGKSTLLRMVAGLERVTSGD-IWIDrqrvtemepkdrgiamvfqnyalyphmsveenmawglkirgmgk 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYID-------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 109 ghiDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLRVQMRLE-----LQQLHRR 183
Cdd:smart00382 38 ---GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSE 114
|
170 180
....*....|....*....|.
gi 578222446 184 LKTTSLYVTHDQVEAMTLAQR 204
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLR 135
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-230 |
4.88e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALY-------- 88
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrRVLSIIPQSPVLFsgtvrfni 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 89 -PHMSVEENMAWglkiRGMGKGHIDERVKEAAriLELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDA 167
Cdd:PLN03232 1331 dPFSEHNDADLW----EALERAHIKDVIDRNP--FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 168 KLRVQMRlelQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRF 230
Cdd:PLN03232 1405 RTDSLIQ---RTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-194 |
5.24e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIwidrqRV-TEMEpkdrgIAMvFQNY--ALYPH 90
Cdd:PRK11147 330 DGKQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----HCgTKLE-----VAY-FDQHraELDPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 91 MSVEENMAWGlKIRGMgkghIDERVKEAARILElDGLL--KR--RP-RELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNL 165
Cdd:PRK11147 398 KTVMDNLAEG-KQEVM----VNGRPRHVLGYLQ-DFLFhpKRamTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
170 180 190
....*....|....*....|....*....|
gi 578222446 166 DAKlrvqmRLE-LQQLHRRLKTTSLYVTHD 194
Cdd:PRK11147 472 DVE-----TLElLEELLDSYQGTVLLVSHD 496
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-222 |
1.15e-06 |
|
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: 50.71 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTllrMVAGLERV---TSGDIWIDRQRVTEMEPKD--RGIAMVFQNYALYP---H 90
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSS---LTLGLFRInesAEGEIIIDGLNIAKIGLHDlrFKITIIPQDPVLFSgslR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 91 MSV-------EENMAWGLKIrgmgkGHIDERVkeAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLS 163
Cdd:TIGR00957 1378 MNLdpfsqysDEEVWWALEL-----AHLKTFV--SALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578222446 164 NLDAK----LRVQMRLELQQlhrrlkTTSLYVTHDQVEAMTLAqRVMVMNKGIAEQIGTPVDV 222
Cdd:TIGR00957 1451 AVDLEtdnlIQSTIRTQFED------CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-166 |
1.44e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 33 IVMVGPSGCGKSTLLRMVAGLERVTSGDIWidrqrvteMEPKDRgIAMVFQNYALYPHMSVEENmawgLKIRGMGKGHID 112
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVF--------RSAKVR-MAVFSQHHVDGLDLSSNPL----LYMMRCFPGVPE 604
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 113 ERVKEAARILELDGLLKRRPR-ELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 166
Cdd:PLN03073 605 QKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
58-211 |
1.50e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 58 SGDIWIDRQRVTEMEPKD---RGIAMVFQN---YALYPHMSVEENMAWGLKIRGMGKGHIDErVKEAARILELDGLLKRR 131
Cdd:PRK13549 317 EGEIFIDGKPVKIRNPQQaiaQGIAMVPEDrkrDGIVPVMGVGKNITLAALDRFTGGSRIDD-AAELKTILESIQRLKVK 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 132 ---PR----ELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDaklrVQMRLELQQLHRRLKTTS---LYVTHDQVEAMTL 201
Cdd:PRK13549 396 tasPElaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGID----VGAKYEIYKLINQLVQQGvaiIVISSELPEVLGL 471
|
170
....*....|
gi 578222446 202 AQRVMVMNKG 211
Cdd:PRK13549 472 SDRVLVMHEG 481
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
4-168 |
3.12e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTkswDGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGleRVTSGDIWIDrQRVTEMEPKDRGIAMVF- 82
Cdd:PLN03140 883 MKEQGVT---EDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGD-IRISGFPKKQETFARISg 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 83 ---QNYALYPHMSVEENMAWGLKIRGMGKGHIDER---VKEAARILELDGL---LKRRP--RELSGGQRQRVAMGRAIVR 151
Cdd:PLN03140 957 yceQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKmmfVDEVMELVELDNLkdaIVGLPgvTGLSTEQRKRLTIAVELVA 1036
|
170
....*....|....*..
gi 578222446 152 DPAVFLFDEPLSNLDAK 168
Cdd:PLN03140 1037 NPSIIFMDEPTSGLDAR 1053
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-225 |
3.31e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.89 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 20 IQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIwidrqrvtemePKDRGIAMVFQNYALYPHMSVEENMAW 99
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAISAGLSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 100 GLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLDAKLrVQMRLELQQ 179
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF-AQKCLDKIY 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 578222446 180 LHRRLKTTSLYVTHDQVEAMTLAQRVMVMNKGIAEQIGTPVDV---YEK 225
Cdd:PRK13546 188 EFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVlpkYEA 236
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
19-198 |
4.97e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 19 VIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAG-----------L--ERVTSGD-IW-IDRQ------------RVTeM 71
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLfgRRRGSGEtIWdIKKHigyvssslhldyRVS-T 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 72 EPKDRGIAMVFQNYALYPHMSveenmawglkirgmgkghiDERVKEAARILELDGLLKR---RP-RELSGGQRQRVAMGR 147
Cdd:PRK10938 354 SVRNVILSGFFDSIGIYQAVS-------------------DRQQKLAQQWLDILGIDKRtadAPfHSLSWGQQRLALIVR 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578222446 148 AIVRDPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEA 198
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-165 |
6.24e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 4 LKLQAVTKSWDGkTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTS--GDIWIDRQrvtEMEPKD------ 75
Cdd:NF040905 2 LEMRGITKTFPG-VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGE---VCRFKDirdsea 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 76 RGIAMVFQNYALYPHMSVEENMAWGLKIRgmGKGHID--ERVKEAARILELDGlLKRRPRELSG----GQRQRVAMGRAI 149
Cdd:NF040905 78 LGIVIIHQELALIPYLSIAENIFLGNERA--KRGVIDwnETNRRARELLAKVG-LDESPDTLVTdigvGKQQLVEIAKAL 154
|
170
....*....|....*.
gi 578222446 150 VRDPAVFLFDEPLSNL 165
Cdd:NF040905 155 SKDVKLLILDEPTAAL 170
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-230 |
6.86e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 14 DGKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLL----RMV---AGLERVTSGDIWI----DRQRVTEMEPKDRGI--AM 80
Cdd:PTZ00243 1320 EGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMVevcGGEIRVNGREIGAyglrELRRQFSMIPQDPVLfdGT 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 81 VFQNYALYPHMSVEENMAwGLKIRGMGK------GHIDERVKEAArileldgllkrrpRELSGGQRQRVAMGRAIV-RDP 153
Cdd:PTZ00243 1400 VRQNVDPFLEASSAEVWA-ALELVGLRErvasesEGIDSRVLEGG-------------SNYSVGQRQLMCMARALLkKGS 1465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578222446 154 AVFLFDEPLSNLDAKLRVQMRLELQQLHRrlKTTSLYVTHdqvEAMTLAQ--RVMVMNKGIAEQIGTPVDVYEKPATRF 230
Cdd:PTZ00243 1466 GFILMDEATANIDPALDRQIQATVMSAFS--AYTVITIAH---RLHTVAQydKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
15-211 |
8.21e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCG--KSTLLRMVAGLE---RVTSGDIWIDRQR-----VTEMEPKDRGIAMVFqn 84
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrRPWRF*TWCANRRalrrtIG*HRPVR*GRRESF-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 85 yalyphmSVEENMAWGLKIRGMGKGHIDERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSN 164
Cdd:NF000106 102 -------SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 578222446 165 LDAKLRVQMRLELQQLHRRlKTTSLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:NF000106 175 LDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRG 220
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-166 |
1.56e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 9 VTKSWDGKTqVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIdrqrvtemepkdrG----IAMVFQN 84
Cdd:PRK11819 330 LSKSFGDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-------------GetvkLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 85 Y-ALYPHMSVEENMAWGLKIRGMGKGHIDERV-------------KEAArileldgllkrrprELSGGQRQRVAMGRAIV 150
Cdd:PRK11819 396 RdALDPNKTVWEEISGGLDIIKVGNREIPSRAyvgrfnfkggdqqKKVG--------------VLSGGERNRLHLAKTLK 461
|
170
....*....|....*.
gi 578222446 151 RDPAVFLFDEPLSNLD 166
Cdd:PRK11819 462 QGGNVLLLDEPTNDLD 477
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
30-235 |
1.66e-04 |
|
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: 42.59 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 30 GEFIVMVGPSGCGKSTL----LRMVAGLErvtsGDIWIDRQRVTEM---EPKDRgIAMVFQNYALYPHmSVEENMAWGLK 102
Cdd:cd03288 47 GQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLplhTLRSR-LSIILQDPILFSG-SIRFNLDPECK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 103 IrgmgkghIDERVKEAARILELDGLLKRRPREL-----------SGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD-AKLR 170
Cdd:cd03288 121 C-------TDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASIDmATEN 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 171 VQMRLELQQLHRRlktTSLYVTHdQVEAMTLAQRVMVMNKGIAEQIGTPVDVYEKPATRFvASFI 235
Cdd:cd03288 194 ILQKVVMTAFADR---TVVTIAH-RVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF-ASLV 253
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-166 |
2.65e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 15 GKTQVIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVA--------------------------GLERVTSGDIwiDRQRV 68
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilhveqevvgddttALQCVLNTDI--ERTQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 69 TEMEpkdrgIAMVFQNYALypHMSVEENMAWGLKIRGMGKGHIDERVKEAARILE--------------LDGL------L 128
Cdd:PLN03073 266 LEEE-----AQLVAQQREL--EFETETGKGKGANKDGVDKDAVSQRLEEIYKRLElidaytaearaasiLAGLsftpemQ 338
|
170 180 190
....*....|....*....|....*....|....*...
gi 578222446 129 KRRPRELSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD 166
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
32-123 |
8.21e-04 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 39.79 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 32 FIVMVGPSGCGKSTLLRMVA---GLERVTSGDIWidRqrvtEMePKDRGIAMV-FQNYAlyphmsvEENMAWGLKirgmg 107
Cdd:PRK04182 2 IITISGPPGSGKTTVARLLAeklGLKHVSAGEIF--R----EL-AKERGMSLEeFNKYA-------EEDPEIDKE----- 62
|
90 100
....*....|....*....|.
gi 578222446 108 kghIDERVKEAAR-----ILE 123
Cdd:PRK04182 63 ---IDRRQLEIAEkednvVLE 80
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
135-216 |
1.59e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.10 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578222446 135 LSGGQRQRVAMGRAIVRDPAVFLFDEPLSNLD--AKLRV-QMRLELQQLHRRLkttsLYVTHDQVEAMTLAQRVMVMNKG 211
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKFEIyQLIAELAKKDKGI----IIISSEMPELLGITDRILVMSNG 467
|
....*
gi 578222446 212 IAEQI 216
Cdd:PRK10982 468 LVAGI 472
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
33-76 |
1.60e-03 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 38.44 E-value: 1.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 578222446 33 IVMVGPSGCGKSTLLRMVA---GLERVTSgDIWIDRQRVTEMEPKDR 76
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLeelGAVRLSS-DDERKRLFGEGRPSISY 47
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
130-180 |
8.35e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 37.24 E-value: 8.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 578222446 130 RRPRELSGGQRQRVAMGR--AIVR-DPAVF-LFDEPLSNLDAKLRVQMRLELQQL 180
Cdd:cd03272 154 QEMQQLSGGQKSLVALALifAIQKcDPAPFyLFDEIDAALDAQYRTAVANMIKEL 208
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
37-61 |
8.67e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 36.31 E-value: 8.67e-03
10 20
....*....|....*....|....*...
gi 578222446 37 GPSGCGKSTLLRMVA---GLERVTSGDI 61
Cdd:cd02020 6 GPAGSGKSTVAKLLAkklGLPYLDTGGI 33
|
|
| |
